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Entry version 137 (02 Dec 2020)
Sequence version 2 (26 May 2009)
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Protein

Protein pyrABCN

Gene

pyrABCN

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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>
-Protein inferred from homologyi <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 three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase).By similarity

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).Curated
In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.

<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 <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 and 2 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. Protein pyrABCN (pyrABCN)
  2. Protein pyrABCN (pyrABCN)
  3. Dihydroorotase (AN0961.2), Dihydroorotase (ANIA_10131)
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 sitei342For GATase activityBy similarity1
Active sitei426For GATase activityBy similarity1
Active sitei428For GATase activityBy similarity1

<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 functionLigase, Multifunctional enzyme, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00070;UER00115
UPA00070;UER00116

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C26.956

<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:
Protein pyrABCN
Including the following 2 domains:
Glutamine-dependent carbamoyl-phosphate (EC:6.3.5.5)
Aspartate carbamoyltransferase (EC:2.1.3.2)
<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:pyrABCNImported
ORF Names:AN0565
<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>OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
<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 identifieri227321 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Nidulantes
<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
  • UP000000560 <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 VIII
  • UP000005890 Componenti: Unassembled WGS sequence

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<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_00001995091 – 2275Protein pyrABCNAdd BLAST2275

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O93937

<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

STRING: functional protein association networks

More...
STRINGi
162425.CADANIAP00002113

<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
O93937

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>Domaini265 – 453Glutamine amidotransferase type-1Add BLAST189
Domaini604 – 796ATP-grasp 1Sequence analysisAdd BLAST193
Domaini1139 – 1330ATP-grasp 2Sequence analysisAdd BLAST192
Domaini1396 – 1575MGS-likePROSITE-ProRule annotationAdd BLAST180

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 – 440GATase (Glutamine amidotransferase)By similarityAdd BLAST440
Regioni441 – 482LinkerBy similarityAdd BLAST42
Regioni483 – 1522CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1040
Regioni1523 – 1532LinkerBy similarity10
Regioni1533 – 1862Defective DHOase domainBy similarityAdd BLAST330
Regioni1863 – 1953LinkerBy similarityAdd BLAST91
Regioni1954 – 2258ATCase (Aspartate transcarbamylase)By similarityAdd BLAST305

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The DHOase domain is defective.

<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

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
O93937

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADKCYFL

Database of Orthologous Groups

More...
OrthoDBi
273358at2759

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_01209, CPSase_S_chain, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
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
IPR017926, GATASE
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
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
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, 2 hits
PS00867, CPSASE_2, 2 hits
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>Sequencei

<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.

O93937-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPETVGHEEP ALPSSPQAGG AVAYNAISKE LQPLPPTETA NGGIIPPASS
60 70 80 90 100
RIEGSTGRLC ALELEDGTVY QGYNFGAEKS VAGELVFQTG MVGYPESITD
110 120 130 140 150
PSYRGQILVI TFPLVGNYGV PSRETMDELL KTLPKHFEST EIHIAALVVA
160 170 180 190 200
TYAGENYSHF LAESSLGQWL KEQGVPAIHG VDTRALTKRI RQKGSMLGRL
210 220 230 240 250
LLHKADVAET DAALAQDTWK SSFEQIDWVD PNTKNLVSEV SIREPKLFSP
260 270 280 290 300
PENVALKHPS SRPIRVLCLD VGLKFNQLRC LVARGVEVLV VPWDYDFPTL
310 320 330 340 350
AGKDYDGLFV SNGPGDPATM TTTVNNLAKT MQEARTPIFG ICLGHQLIAR
360 370 380 390 400
SVGAQTLKMK FGNRGHNIPC TSLVTGKCHI TSQNHGYAVD SSTLPSDWQE
410 420 430 440 450
LFVNANDGSN EGIRHVSRPY FSVQFHPEST PGPRDTEYLF DVFINAIKDT
460 470 480 490 500
IASPEALQKP VNFPGGAVAE NIKASPRVSV KKVLILGSGG LSIGQAGEFD
510 520 530 540 550
YSGSQAIKAL KEEGIYTILI NPNIATIQTS KGLADKVYFL PVNADFVRKV
560 570 580 590 600
IKHERPDAIY VTFGGQTALQ VGIQLKDEFE SLGVKVLGTP IDTIITTEDR
610 620 630 640 650
ELFARSMDSI GEKCAKSASA SSLEEALQVV ESIGFPVIVR AAYALGGLGS
660 670 680 690 700
GFADNLDELK DLCAKAFAAS PQVLIERSMK GWKEIEYEVV RDARDNCITV
710 720 730 740 750
CNMENFDPLG IHTGDSIVVA PSQTLSDEDY NMLRTTAVNV IRHLGVVGEC
760 770 780 790 800
NIQYALNPYS KEYCIIEVNA RLSRSSALAS KATGYPLAFI AAKLGLNIPL
810 820 830 840 850
NEIKNSVTKV TCACFEPSLD YCVVKIPRWD LKKFTRVSTQ LGSSMKSVGE
860 870 880 890 900
VMAIGRTFEE AIQKAIRSVD FHNLGFNETN ALMSIKTELQ TPSDQRLFAI
910 920 930 940 950
ANAMAAGYSV DDIWKLTNID KWFLTRLKGL SDFGKLMTNY NASTVTAPLL
960 970 980 990 1000
RQAKQLGFSD RQLAKFLSSN ELAIRRLRVE AGIIPIVKQI DTVAAEFPSV
1010 1020 1030 1040 1050
TNYLYLTYNA SEHDVRFDDN GIMVLGSGVY RIGSSVEFDW CSVRTIRTLR
1060 1070 1080 1090 1100
EQGHKTVMVN YNPETVSTDY DEADRLYFEN INLETVLDIY QLESSSGVIM
1110 1120 1130 1140 1150
SMGGQTPNNI ALPLHRLNVR ILGTSPEMID GAENRYKFSR MLDRIGVDQP
1160 1170 1180 1190 1200
AWKELTSIEE AREFCDKVGY PVLVRPSYVL SGAAMNTVYS EHDLASYLNQ
1210 1220 1230 1240 1250
AADVSREHPV VITKYIENAK EIEMDAVARN GVMVGHFISE HVENAGVHSG
1260 1270 1280 1290 1300
DATLILPPQD LDPETVRRIE EATRKIGNAL NVTGPFNIQF IAKDNDIKVI
1310 1320 1330 1340 1350
ECNVRASRSF PFVSKVMGVD LIEMATKAMI GAPFAEYPPV TIPKDYVGVK
1360 1370 1380 1390 1400
VPQFSFSRLA GADPVLGVEM ASTGEVASFG RDKYEAYLKA LLSTGFKLPK
1410 1420 1430 1440 1450
RNILLSIGSY KEKMEMLPSI IKLRDVGFEL FATSGTADFL KENGVPVKYL
1460 1470 1480 1490 1500
EILPGEDEDI KSEYSLTQHL ANNLIDLYIN LPSSNRFRRP ANYMSKGYRT
1510 1520 1530 1540 1550
RRMAVDYQTP LVTNVKNAKI LIEAIARHYA LNVQTIDYQT SHRSIILPGL
1560 1570 1580 1590 1600
INVGAFVPGL GSADSKDFEA VTKASIAAGF SMIRVMPVGV DSSITDARTL
1610 1620 1630 1640 1650
KLVQQNAGKA SFCDYNFSVV ATSSNSAEVG QLTGEVGSLF IPFNHLSGNI
1660 1670 1680 1690 1700
SKVAAVTSHF GAWPSSKPII TDAKSTDLAS VLLLASLHSR NIHVMSVTSK
1710 1720 1730 1740 1750
EDIGLIALSK EKGLKVTCDV SIYCLFLSRD DYPEAAFLPT AEDQKALWEH
1760 1770 1780 1790 1800
LSTIDIFSIG SIPYQLAGEK GSPAAGIAEA LPLLFTAVSE GRLTVEDIIA
1810 1820 1830 1840 1850
RLYENPKKIF ELHDQSDSSV EVEIDRPYLF QSAQAWSPFS GKSVKGLVQR
1860 1870 1880 1890 1900
VIFQGKTSCL DSEITPDAPK GSDMSGHRIV PASPSLKAMS PRVDGALDRR
1910 1920 1930 1940 1950
QSISIAGTPA RLGRKPVDHF PAATGAELGP PLYTPVPRAS SPLLQMLSRS
1960 1970 1980 1990 2000
PFKQKHVLSV NQFNRADLHL LFTVAQEMRL GVQREGVLDI LKGRLLCTLF
2010 2020 2030 2040 2050
YEPSTRTSAS FDAAMQRLGG RTIAISTEHS STKKGETLQD TLRTLGCYGD
2060 2070 2080 2090 2100
AVVLRHPEPS STEVAAKFSP VPVINGGNGS VEHPTQAFLD LFTIREELGT
2110 2120 2130 2140 2150
VGGLTITFTG DLKYGRPVHS LIKLLQFYDV RVQLVAPKDL SLPADIRQQL
2160 2170 2180 2190 2200
LATGQLLTES EELTPEIVAR SDVLYSTRVQ KERFADLEQY ERLKNSFIID
2210 2220 2230 2240 2250
NALLKHAKSH MVVMHPLPRN AEVSEEVDFD QRAAYFRQVS LQSRGPSSEF
2260 2270
DMLMWMQMRY GLYCRMALLA LIMAP
Length:2,275
Mass (Da):249,540
Last modified:May 26, 2009 - v2
<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:i25F581F3A50BB5CC
GO

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 conflicti19G → R in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti169 – 170WL → CV in AAD09129 (PubMed:10417650).Curated2
Sequence conflicti403V → D in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti454P → A in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti909 – 910SV → RL in AAD09129 (PubMed:10417650).Curated2
Sequence conflicti1007T → A in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti1741A → R in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti2013A → V in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti2238Q → L in AAD09129 (PubMed:10417650).Curated1
Sequence conflicti2269 – 2270LA → IE in AAD09129 (PubMed:10417650).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF112473 Genomic DNA Translation: AAD09129.1
AACD01000007 Genomic DNA Translation: EAA66664.1
BN001308 Genomic DNA Translation: CBF89223.1

NCBI Reference Sequences

More...
RefSeqi
XP_658169.1, XM_653077.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CBF89223; CBF89223; ANIA_00565
EAA66664; EAA66664; AN0565.2

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2876339

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ani:AN0565.2

<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
AF112473 Genomic DNA Translation: AAD09129.1
AACD01000007 Genomic DNA Translation: EAA66664.1
BN001308 Genomic DNA Translation: CBF89223.1
RefSeqiXP_658169.1, XM_653077.1

3D structure databases

SMRiO93937
ModBaseiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00002113

Protein family/group databases

MEROPSiC26.956

Proteomic databases

PRIDEiO93937

Genome annotation databases

EnsemblFungiiCBF89223; CBF89223; ANIA_00565
EAA66664; EAA66664; AN0565.2
GeneIDi2876339
KEGGiani:AN0565.2

Phylogenomic databases

eggNOGiKOG0370, Eukaryota
HOGENOMiCLU_000513_2_1_1
InParanoidiO93937
OMAiADKCYFL
OrthoDBi273358at2759

Enzyme and pathway databases

UniPathwayiUPA00070;UER00115
UPA00070;UER00116

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_01209, CPSase_S_chain, 1 hit
InterProiView protein in InterPro
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
IPR017926, GATASE
IPR032466, Metal_Hydrolase
IPR011607, MGS-like_dom
IPR036914, MGS-like_dom_sf
IPR016185, PreATP-grasp_dom_sf
PfamiView protein in Pfam
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
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, 2 hits
PS00867, CPSASE_2, 2 hits
PS51273, GATASE_TYPE_1, 1 hit
PS51855, MGS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_EMENI
<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: O93937
Secondary accession number(s): C8VSK1, Q5BFW5
<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: July 19, 2004
Last sequence update: May 26, 2009
Last modified: December 2, 2020
This is version 137 of the entry and version 2 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 programFungal Protein Annotation Program

<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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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