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Entry version 215 (02 Dec 2020)
Sequence version 3 (25 Oct 2005)
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Protein

CAD protein

Gene

r

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) together form the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. CAD protein (r)
  2. CAD protein, CAD protein (r)
  3. Aspartate carbamoyltransferase (r), CAD protein (r)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei269Nucleophile; for GATase activityPROSITE-ProRule annotation1
Active sitei353For GATase activityPROSITE-ProRule annotation1
Active sitei355For GATase activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi678Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi692Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi692Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi694Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1228Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1228Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1230Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1486Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1486Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1488Zinc 1; via tele nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1490N-carbamoyl-L-aspartateBy similarity1
Binding sitei1520N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1571Zinc 1; via carbamate groupBy similarity1
Metal bindingi1571Zinc 3; via carbamate groupBy similarity1
Metal bindingi1605Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1628Zinc 2By similarity1
Metal bindingi1629Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1652Zinc 2By similarity1
Binding sitei1676N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1701Zinc 1By similarity1
Binding sitei1701N-carbamoyl-L-aspartateBy similarity1
Binding sitei1705N-carbamoyl-L-aspartateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi555 – 610ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi1092 – 1149ATPPROSITE-ProRule annotationAdd BLAST58

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Ligase, Multifunctional enzyme, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.5.5, 1994

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-500753, Pyrimidine biosynthesis

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00070;UER00115
UPA00070;UER00116
UPA00070;UER00117

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M38.972

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CAD protein
Alternative name(s):
Protein rudimentary
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.51 Publication)
Aspartate carbamoyltransferase (EC:2.1.3.2By similarity)
Dihydroorotase (EC:3.5.2.3By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:r
ORF Names:CG18572
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0003189, r

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1167E → K: Severely diminishes UTP inhibition of CPSase; in Su(b). 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001995051 – 2224CAD proteinAdd BLAST2224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1571N6-carboxylysineBy similarity1
Modified residuei1883Phosphoserine1 Publication1
Modified residuei1885Phosphoserine1 Publication1
Modified residuei1892Phosphoserine1 Publication1
Modified residuei1894Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P05990

PRoteomics IDEntifications database

More...
PRIDEi
P05990

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P05990

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0003189, Expressed in embryo and 19 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P05990, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P05990, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
58976, 39 interactors

Protein interaction database and analysis system

More...
IntActi
P05990, 8 interactors

Molecular INTeraction database

More...
MINTi
P05990

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0088675

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P05990

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini195 – 380Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST186
Domaini529 – 721ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini1066 – 1257ATP-grasp 2PROSITE-ProRule annotationAdd BLAST192
Domaini1322 – 1477MGS-likePROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 369GATase (Glutamine amidotransferase)By similarityAdd BLAST369
Regioni370 – 415LinkerBy similarityAdd BLAST46
Regioni416 – 1470CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1055
Regioni1471 – 1484LinkerBy similarityAdd BLAST14
Regioni1485 – 1800DHOase (dihydroorotase)By similarityAdd BLAST316
Regioni1801 – 1912LinkerBy similarityAdd BLAST112
Regioni1913 – 2224ATCase (Aspartate transcarbamylase)By similarityAdd BLAST312

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0370, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000513_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05990

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADKCYFL

Database of Orthologous Groups

More...
OrthoDBi
273358at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P05990

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01744, GATase1_CPSase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 2 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00001, Asp_carb_tr, 1 hit
MF_01209, CPSase_S_chain, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006680, Amidohydro-rel
IPR006132, Asp/Orn_carbamoyltranf_P-bd
IPR006130, Asp/Orn_carbamoylTrfase
IPR036901, Asp/Orn_carbamoylTrfase_sf
IPR002082, Asp_carbamoyltransf
IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR006275, CarbamoylP_synth_lsu
IPR005480, CarbamoylP_synth_lsu_oligo
IPR036897, CarbamoylP_synth_lsu_oligo_sf
IPR006274, CarbamoylP_synth_ssu
IPR002474, CarbamoylP_synth_ssu_N
IPR036480, CarbP_synth_ssu_N_sf
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR005483, CbamoylP_synth_lsu_CPSase_dom
IPR029062, Class_I_gatase-like
IPR035686, CPSase_GATase1
IPR002195, Dihydroorotase_CS
IPR017926, GATASE
IPR011059, Metal-dep_hydrolase_composite
IPR032466, Metal_Hydrolase
IPR011607, MGS-like_dom
IPR036914, MGS-like_dom_sf
IPR016185, PreATP-grasp_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01979, Amidohydro_1, 1 hit
PF02786, CPSase_L_D2, 2 hits
PF02787, CPSase_L_D3, 1 hit
PF00988, CPSase_sm_chain, 1 hit
PF00117, GATase, 1 hit
PF02142, MGS, 1 hit
PF00185, OTCace, 1 hit
PF02729, OTCace_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00100, AOTCASE
PR00098, CPSASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01096, CPSase_L_D3, 1 hit
SM01097, CPSase_sm_chain, 1 hit
SM00851, MGS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48108, SSF48108, 1 hit
SSF51338, SSF51338, 1 hit
SSF51556, SSF51556, 1 hit
SSF52021, SSF52021, 1 hit
SSF52317, SSF52317, 1 hit
SSF52335, SSF52335, 1 hit
SSF52440, SSF52440, 2 hits
SSF53671, SSF53671, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00670, asp_carb_tr, 1 hit
TIGR01369, CPSaseII_lrg, 1 hit
TIGR01368, CPSaseIIsmall, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975, ATP_GRASP, 2 hits
PS00097, CARBAMOYLTRANSFERASE, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 2 hits
PS00482, DIHYDROOROTASE_1, 1 hit
PS00483, DIHYDROOROTASE_2, 1 hit
PS51273, GATASE_TYPE_1, 1 hit
PS51855, MGS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P05990-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGFGGEVVF QTGMVGYTEA
60 70 80 90 100
LTDRSYSGQI LVLTYPLIGN YGVPAPDEDE HGLPLHFEWM KGVVQATALV
110 120 130 140 150
VGEVAEEAFH WRKWKTLPDW LKQHKVPGIQ DIDTRALTKK LREQGSMLGK
160 170 180 190 200
IVYEKPPVEG LPKSSFVDPN VRNLAKECSV KERQVYGNPN GKGPRIAILD
210 220 230 240 250
CGLKLNQLRC LLQRGASVTL LPWSARLEDE QFDALFLSNG PGNPESCDQI
260 270 280 290 300
VQQVRKVIEE GQKPVFGICL GHQLLAKAIG CSTYKMKYGN RGHNLPCLHR
310 320 330 340 350
ATGRCLMTSQ NHGYAVDLEQ LPDGWSELFV NANDGTNEGI VHASKPYFSV
360 370 380 390 400
QFHPEHHAGP QDTEFLFDVF MESIQQKDLT IPQLIEQRLR PTTPAIDSAP
410 420 430 440 450
VMPRKVLILG SGGLSIGQAG EFDYSGSQAI KAMRESNIQT VLINPNIATV
460 470 480 490 500
QTSKGMADKC YFLPLTPHYV EQVIKSERPN GVLLTFGGQT ALNCGVQLER
510 520 530 540 550
AGVFSKYNVR ILGTPIQSII ETEDRKLFAE RVNEIGEQVA PSEAVYSVAQ
560 570 580 590 600
ALDAASRLGY PVMARAAFSL GGLGSGFANN EEELQSLAQQ ALAHSSQLIV
610 620 630 640 650
DKSLKGWKEV EYEVVRDAYN NCITVCNMEN FDPLGIHTGE SIVVAPSQTL
660 670 680 690 700
SDREYQMLRS TALKVIRHFG VVGECNIQYA LCPHSEQYYI IEVNARLSRS
710 720 730 740 750
SALASKATGY PLAYVAAKLA LGLPLPDIKN SVTGNTTACF EPSLDYCVVK
760 770 780 790 800
IPRWDLAKFV RVSKHIGSSM KSVGEVMAIG RNFEEAFQKA LRMVDSDVLG
810 820 830 840 850
FDPDVVPLNK EQLAEQLSEP TDRRPFVIAA ALQLGMSLRE LHQLTNIDYW
860 870 880 890 900
FLEKLERIIL LQSLLTRNGS RTDAALLLKA KRFGFSDKQI AKYIKSTELA
910 920 930 940 950
VRHQRQEFGI RPHVKQIDTV AGEWPASTNY LYHTYNGSEH DVDFPGGHTI
960 970 980 990 1000
VVGSGVYRIG SSVEFDWCAV GCLRELRKLQ RPTIMINYNP ETVSTDYDMC
1010 1020 1030 1040 1050
DRLYFEEISF EVVMDIYEME NSEGIILSMG GQLPNNIAMD LHRQQAKVLG
1060 1070 1080 1090 1100
TSPESIDCAE NRFKFSRMLD RKGILQPRWK ELTNLQSAIE FCEEVGYPCL
1110 1120 1130 1140 1150
VRPSYVLSGA AMNVAYSNQD LETYLNAASE VSREHPVVIS KFLTEAKEID
1160 1170 1180 1190 1200
VDAVASDGRI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNA ETLEAIKRIT
1210 1220 1230 1240 1250
CDLASVLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLDHDFVA
1260 1270 1280 1290 1300
TATRAIVGLD VEPLDVLHGV GKVGVKVPQF SFSRLAGADV QLGVEMASTG
1310 1320 1330 1340 1350
EVACFGDNRY EAYLKAMMST GFQIPKNAVL LSIGSFKHKM ELLPSIRDLA
1360 1370 1380 1390 1400
KMGYKLYASM GTGDFYAEHG VNVESVQWTF DKTTPDDING ELRHLAEFLA
1410 1420 1430 1440 1450
NKQFDLVINL PMSGGGARRV SSFMTHGYRT RRLAVDYSIP LVTDVKCTKL
1460 1470 1480 1490 1500
LVESMRMNGG KPPMKTHTDC MTSRRIVKLP GFIDVHVHLR EPGATHKEDF
1510 1520 1530 1540 1550
ASGTAAALAG GVTLVCAMPN TNPSIVDRET FTQFQELAKA GARCDYALYV
1560 1570 1580 1590 1600
GASDDNWAQV NELASHACGL KMYLNDTFGT LKLSDMTSWQ RHLSHWPKRS
1610 1620 1630 1640 1650
PIVCHAERQS TAAVIMLAHL LDRSVHICHV ARKEEIQLIR SAKEKGVKVT
1660 1670 1680 1690 1700
CEVCPHHLFL STKDVERLGH GMSEVRPLLC SPEDQEALWE NIDYIDVFAT
1710 1720 1730 1740 1750
DHAPHTLAEK RSERPPPGFP GVETILPLLL QAVHEGRLTM EDIKRKFHRN
1760 1770 1780 1790 1800
PKIIFNLPDQ AQTYVEVDLD EEWTITGNEM KSKSGWTPFE GTKVKGRVHR
1810 1820 1830 1840 1850
VVLRGEVAFV DGQVLVQPGF GQNVRPKQSP LASEASQDLL PSDNDANDTF
1860 1870 1880 1890 1900
TRLLTSEGPG GGVHGISTKV HFVDGANFLR PNSPSPRIRL DSASNTTLRE
1910 1920 1930 1940 1950
YLQRTTNSNP VAHSLMGKHI LAVDMFNKDH LNDIFNLAQL LKLRGTKDRP
1960 1970 1980 1990 2000
VDELLPGKIM ASVFYEVSTR TQCSFAAAML RLGGRVISMD NITSSVKKGE
2010 2020 2030 2040 2050
SLEDSIKVVS SYADVVVLRH PSPGAVARAA TFSRKPLINA GDGVGEHPTQ
2060 2070 2080 2090 2100
ALLDIFTIRE EFGTVNGLTI TMVGDLKNGR TVHSLARLLT LYNVNLQYVA
2110 2120 2130 2140 2150
PNSLQMPDEV VQFVHQRGVK QLFARDLKNV LPDTDVLYMT RIQRERFDNV
2160 2170 2180 2190 2200
EDYEKCCGHL VLTPEHMMRA KKRSIVLHPL PRLNEISREI DSDPRAAYFR
2210 2220
QAEYGMYIRM ALLAMVVGGR NTAL
Length:2,224
Mass (Da):246,672
Last modified:October 25, 2005 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF89DEAD44FEFAEC6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
X2JFG0X2JFG0_DROME
Aspartate carbamoyltransferase
r ACT, CAD, CG4601, CPS, csp2
2,224Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA28873 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence AAL90298 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAA27509 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA27510 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA27511 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA27513 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA28502 differs from that shown. Various problems, including DNA not present in the genome.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti34F → V in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti58G → A in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti172 – 173RN → QD in CAA27509 (PubMed:3023623).Curated2
Sequence conflicti220 – 221LL → FV in CAA27509 (PubMed:3023623).Curated2
Sequence conflicti288Y → I in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti394P → L in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti2192S → L in CAA27513 (PubMed:3023623).Curated1
Sequence conflicti2222 – 2224TAL → RRS in CAA27513 (PubMed:3023623).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04813 Genomic DNA Translation: CAA28502.1 Sequence problems.
X03875 Genomic DNA Translation: CAA27509.1 Sequence problems.
X03876 Genomic DNA Translation: CAA27510.1 Sequence problems.
X03877 Genomic DNA Translation: CAA27511.1 Sequence problems.
X03878 Genomic DNA Translation: CAA27512.1
X03879 Genomic DNA Translation: CAA27513.1 Sequence problems.
AE014298 Genomic DNA Translation: AAF48639.3
AE014298 Genomic DNA Translation: AAS65389.2
BT046159 mRNA Translation: ACI46547.1
M37783 Genomic DNA Translation: AAA28873.1 Sequence problems.
AY089560 mRNA Translation: AAL90298.1 Different initiation.
AF129814 mRNA Translation: AAD18071.1
S74010 mRNA Translation: AAB32204.1

Protein sequence database of the Protein Information Resource

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PIRi
A29106, QZFF

NCBI Reference Sequences

More...
RefSeqi
NP_001285343.1, NM_001298414.1
NP_523377.1, NM_078653.2
NP_996488.2, NM_206765.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0089734; FBpp0088675; FBgn0003189
FBtr0340155; FBpp0309141; FBgn0003189
FBtr0340156; FBpp0309142; FBgn0003189

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
32640

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG18572

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04813 Genomic DNA Translation: CAA28502.1 Sequence problems.
X03875 Genomic DNA Translation: CAA27509.1 Sequence problems.
X03876 Genomic DNA Translation: CAA27510.1 Sequence problems.
X03877 Genomic DNA Translation: CAA27511.1 Sequence problems.
X03878 Genomic DNA Translation: CAA27512.1
X03879 Genomic DNA Translation: CAA27513.1 Sequence problems.
AE014298 Genomic DNA Translation: AAF48639.3
AE014298 Genomic DNA Translation: AAS65389.2
BT046159 mRNA Translation: ACI46547.1
M37783 Genomic DNA Translation: AAA28873.1 Sequence problems.
AY089560 mRNA Translation: AAL90298.1 Different initiation.
AF129814 mRNA Translation: AAD18071.1
S74010 mRNA Translation: AAB32204.1
PIRiA29106, QZFF
RefSeqiNP_001285343.1, NM_001298414.1
NP_523377.1, NM_078653.2
NP_996488.2, NM_206765.3

3D structure databases

SMRiP05990
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi58976, 39 interactors
IntActiP05990, 8 interactors
MINTiP05990
STRINGi7227.FBpp0088675

Protein family/group databases

MEROPSiM38.972

PTM databases

iPTMnetiP05990

Proteomic databases

PaxDbiP05990
PRIDEiP05990

Genome annotation databases

EnsemblMetazoaiFBtr0089734; FBpp0088675; FBgn0003189
FBtr0340155; FBpp0309141; FBgn0003189
FBtr0340156; FBpp0309142; FBgn0003189
GeneIDi32640
KEGGidme:Dmel_CG18572

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
32640
FlyBaseiFBgn0003189, r

Phylogenomic databases

eggNOGiKOG0370, Eukaryota
HOGENOMiCLU_000513_2_1_1
InParanoidiP05990
OMAiADKCYFL
OrthoDBi273358at2759
PhylomeDBiP05990

Enzyme and pathway databases

UniPathwayiUPA00070;UER00115
UPA00070;UER00116
UPA00070;UER00117
BRENDAi6.3.5.5, 1994
ReactomeiR-DME-500753, Pyrimidine biosynthesis

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
32640, 1 hit in 3 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
r, fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
32640

Protein Ontology

More...
PROi
PR:P05990

Gene expression databases

BgeeiFBgn0003189, Expressed in embryo and 19 other tissues
ExpressionAtlasiP05990, baseline and differential
GenevisibleiP05990, DM

Family and domain databases

CDDicd01744, GATase1_CPSase, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 2 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit
HAMAPiMF_00001, Asp_carb_tr, 1 hit
MF_01209, CPSase_S_chain, 1 hit
InterProiView protein in InterPro
IPR006680, Amidohydro-rel
IPR006132, Asp/Orn_carbamoyltranf_P-bd
IPR006130, Asp/Orn_carbamoylTrfase
IPR036901, Asp/Orn_carbamoylTrfase_sf
IPR002082, Asp_carbamoyltransf
IPR006131, Asp_carbamoyltransf_Asp/Orn-bd
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR006275, CarbamoylP_synth_lsu
IPR005480, CarbamoylP_synth_lsu_oligo
IPR036897, CarbamoylP_synth_lsu_oligo_sf
IPR006274, CarbamoylP_synth_ssu
IPR002474, CarbamoylP_synth_ssu_N
IPR036480, CarbP_synth_ssu_N_sf
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR005483, CbamoylP_synth_lsu_CPSase_dom
IPR029062, Class_I_gatase-like
IPR035686, CPSase_GATase1
IPR002195, Dihydroorotase_CS
IPR017926, GATASE
IPR011059, Metal-dep_hydrolase_composite
IPR032466, Metal_Hydrolase
IPR011607, MGS-like_dom
IPR036914, MGS-like_dom_sf
IPR016185, PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF01979, Amidohydro_1, 1 hit
PF02786, CPSase_L_D2, 2 hits
PF02787, CPSase_L_D3, 1 hit
PF00988, CPSase_sm_chain, 1 hit
PF00117, GATase, 1 hit
PF02142, MGS, 1 hit
PF00185, OTCace, 1 hit
PF02729, OTCace_N, 1 hit
PRINTSiPR00100, AOTCASE
PR00098, CPSASE
SMARTiView protein in SMART
SM01096, CPSase_L_D3, 1 hit
SM01097, CPSase_sm_chain, 1 hit
SM00851, MGS, 1 hit
SUPFAMiSSF48108, SSF48108, 1 hit
SSF51338, SSF51338, 1 hit
SSF51556, SSF51556, 1 hit
SSF52021, SSF52021, 1 hit
SSF52317, SSF52317, 1 hit
SSF52335, SSF52335, 1 hit
SSF52440, SSF52440, 2 hits
SSF53671, SSF53671, 1 hit
TIGRFAMsiTIGR00670, asp_carb_tr, 1 hit
TIGR01369, CPSaseII_lrg, 1 hit
TIGR01368, CPSaseIIsmall, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 2 hits
PS00097, CARBAMOYLTRANSFERASE, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 2 hits
PS00482, DIHYDROOROTASE_1, 1 hit
PS00483, DIHYDROOROTASE_2, 1 hit
PS51273, GATASE_TYPE_1, 1 hit
PS51855, MGS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPYR1_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05990
Secondary accession number(s): B5X540
, O97163, Q26376, Q7KUX4, Q8SXM0, Q9VXD5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 25, 2005
Last modified: December 2, 2020
This is version 215 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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