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UniProtKB - Q18990 (PYR1_CAEEL)

Entry version 162 (02 Dec 2020)
Sequence version 2 (05 Feb 2008)
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Protein

CAD protein

Gene

pyr-1

Organism
Caenorhabditis elegans
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) (By similarity). Involved in the elongation of the pharyngeal isthmus during development, probably by providing precursors of UDP-sugars required for heparan sulfate proteoglycan biosynthesis (PubMed:16828468). Regulates the organization of the actin and intermediate filaments cytoskeleton in the pharyngeal muscles (PubMed:16828468).By similarity1 Publication

Miscellaneous

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

<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.By similarity
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. CAD protein (pyr-1)
  2. CAD protein (pyr-1)
  3. CAD protein (pyr-1)
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 sitei255Nucleophile; for GATase activityPROSITE-ProRule annotation1
Active sitei339For GATase activityPROSITE-ProRule annotation1
Active sitei341For 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 bindingi665Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi679Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi679Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi681Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi1204Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1218Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1483Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1483Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1485Zinc 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 sitei1487N-carbamoyl-L-aspartateBy similarity1
Binding sitei1517N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1568Zinc 1; via carbamate groupBy similarity1
Metal bindingi1568Zinc 3; via carbamate groupBy similarity1
Metal bindingi1602Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1626Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1649Zinc 2By similarity1
Binding sitei1670N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1695Zinc 1By similarity1
Binding sitei1695N-carbamoyl-L-aspartateBy similarity1
Binding sitei1699N-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 bindingi542 – 597ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi1080 – 1137ATPPROSITE-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Reactome - a knowledgebase of biological pathways and processes

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

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

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

<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 proteinBy similarity
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthaseBy similarity (EC:6.3.5.5By similarity)
Aspartate carbamoyltransferaseBy similarity (EC:2.1.3.2By similarity)
DihydroorotaseBy similarity (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:pyr-11 PublicationImported
ORF Names:D2085.1Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 lineageiEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditina › Rhabditomorpha › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis
<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
  • UP000001940 <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 II

Organism-specific databases

WormBase

More...WormBasei		D2085.1 ; CE41886 ; WBGene00004259 ; pyr-1

<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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown causes an arrest at the embryonic stage or at the L1 larval stage (PubMed:16828468). The few surviving animals grow more slowly (PubMed:16828468). L1 larvae have incomplete pharyngeal isthmus elongation, 36 percent of which have the pharynx detached from the buccal cavity (PubMed:16828468). In an umps-1 zu456 mutant background embryo, prevents the formation of abnormally enlarged gut granules (PubMed:20148972).2 Publications

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>Mutagenesisi1602H → Q in cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background. 3 Publications1

<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_00004387711 – 2198CAD proteinCuratedAdd BLAST2198

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 residuei1568N6-carboxylysineBy similarity1

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q18990

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

More...PaxDbi		Q18990

PeptideAtlas

More...PeptideAtlasi		Q18990

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the intestine.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed predominantly in gut precursor cells from the 4E embryonic stage until the bean stage. Expression resumes at the L1 larval stage and continues into adulthood.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		WBGene00004259, Expressed in multi-cellular organism and 5 other tissues

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		6239.D2085.1

<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		Q18990

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>Domaini180 – 366Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST187
Domaini516 – 708ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini1054 – 1245ATP-grasp 2PROSITE-ProRule annotationAdd BLAST192
Domaini1318 – 1474MGS-likePROSITE-ProRule annotationAdd BLAST157

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>Regioni3 – 368GATase (Glutamine amidotransferase)By similarityAdd BLAST366
Regioni392 – 1467CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1076
Regioni392 – 934CPSase ABy similarityAdd BLAST543
Regioni935 – 1467CPSase BBy similarityAdd BLAST533
Regioni1468 – 1799DHOase (dihydroorotase)By similarityAdd BLAST332
Regioni1800 – 1870LinkerBy similarityAdd BLAST71
Regioni1871 – 2196ATCase (Aspartate transcarbamylase)By similarityAdd BLAST326

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157241

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000513_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q18990

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		Q18990

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, 2 hits
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>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.

Q18990-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRATLHLEDG STFVGSIYGA TKSVVGEIVF QTGMVGYVES LTDPSYAKQL 
        60         70         80         90        100
LTLTYPLIGN YGVPSAEILD QFKLPAEFES DRIWPAALIV EKICVDGEHS 
       110        120        130        140        150
HWQAVQSLSE WLRKADVPCL SGIDVRQLVK KIRETGTMKA KLVIESDNAQ 
       160        170        180        190        200
NFDYVDVNAE NLVDFVSRKE PVVYGSGDQT ILAVDCGLKN NQIRCLAKRG 
       210        220        230        240        250
FRVKVVPWNH PIDTESDYDG LFLSNGPGDP EICAPLVDRL AKVIARGDKP 
       260        270        280        290        300
IFGICLGHQI LSRAIGAKTY KLKYGNRGHN QPCTHYATGR CYITSQNHGY 
       310        320        330        340        350
AVDPDSLPAD WKALFTNEND KTNEGIVHSS KPFFSVQFHP EHTAGPTDCE 
       360        370        380        390        400
FLFDVFADSV RQAKSGTFMN VDQELTRLMT FTPIYHAKEQ RKVLVLGSGG 
       410        420        430        440        450
LTIGQAGEFD YSGAQALKAL REEGIRTVLI NPNIATVQTS KGFADFTYFL 
       460        470        480        490        500
PITKEYVTDV IKKERPTGIL CTFGGQTALN CAIDLYKDGI FEQYDVQVLG 
       510        520        530        540        550
TQINTIMKTE DRDLFNQEIS AIGEKVAPSK AATTMEGAIE AAEELGYPVL 
       560        570        580        590        600
VRAAYALGGL GSGFADNREE LIAIAQQALA HSNQVLVDKS LKGWKEVEYE 
       610        620        630        640        650
VVRDAYDNCI TVCNMENVDP LGIHTGESVV VAPSQTLSDR EYNALRTCAI 
       660        670        680        690        700
KVIRHLGIIG ECNIQYALDP YSLTYYIIEV NARLSRSSAL ASKATGYPLA 
       710        720        730        740        750
YVAAKLALGQ HLPVIRNSVT GTTTACFEPS LDYCVVKIPR WDLGKFARVS 
       760        770        780        790        800
TQIGSSMKSV GEVMGIGRCF EEALQKALRM VSDHADGFSP YTFSRPTTAD 
       810        820        830        840        850
DLSKPTDKRM FALARGMYYG DFDVEKAHEL TRIDRWFLFR MQNIVDIYHR 
       860        870        880        890        900
LEKTDVNTVS AELLLEAKQA GFSDRQIAKK IGSNEYTVRE ARFVKGITPC 
       910        920        930        940        950
VKQIDTVAGE WPAQTNYLYT TFNGIENDVS FNMKNAVMVL GSGVYRIGSS 
       960        970        980        990       1000
VEFDSSCVGC IRELKALGYS TITVNCNPET VSTDYDICDR LYFEEISFET 
      1010       1020       1030       1040       1050
VLDVYHLEKP KGVILAFGGQ APNNIAMSLS RAQVKIFGTS PNDIDNAEDR 
      1060       1070       1080       1090       1100
FKFSRKLESL KISQPQWKKS ENMEDAKNFC AQVGYPCLIR PSYVLSGAAM 
      1110       1120       1130       1140       1150
NVAHNAEDLE VFLKQAAVVA KEHPVVVSKF INEAKELDVD AVALDGKLVV 
      1160       1170       1180       1190       1200
MAVSEHIENA GVHSGDATLV TPAQDMNKLT LDRIKDITFR IAEAFNVNGP 
      1210       1220       1230       1240       1250
FNMQLIAKNN ELKVIECNLR VSRSFPFVSK TLDYDFVALA TRAMMASDSP 
      1260       1270       1280       1290       1300
AIRATIKPTA TLLKGKGRVG VKVPQFSFSR LAGADVMLGV EMASTGEVAC 
      1310       1320       1330       1340       1350
FGTSRCDAYL KALLSTGFVV PKQNIFISIG GYHAKAEMLK SVEALLKLGY 
      1360       1370       1380       1390       1400
ELYGSKGTAD YFQSNKINVK PVDWPFEEGS SDEKTASGTR SVVEFLENKE 
      1410       1420       1430       1440       1450
FHLVINLPIR GSGAYRVSAF RTHGYKTRRM AIDNGIPLIT DIKCAKTFIQ 
      1460       1470       1480       1490       1500
ALEMVGKRPT MNSLVDCVTS KSLKRLPGMV DIHVHVREPG ATHKEDWATC 
      1510       1520       1530       1540       1550
SKAALAGGVT TILAMPNTSP VLVDTDSFYQ TEQLASAKSV VDYALYIGAT 
      1560       1570       1580       1590       1600
PNNSKFAAEF ADKAAGLKMY LNETFSTLKM DNISDWAKHL SAFPANRPIV 
      1610       1620       1630       1640       1650
CHAEKQTLAA ILCMAQMANR AVHIAHVATA DEINLVKEAK QRGWNVTCEV 
      1660       1670       1680       1690       1700
CPHHLFLIEE DLPDGIREVR PRLVKPEDRQ ALWDNMEYID CFATDHAPHT 
      1710       1720       1730       1740       1750
WAEKTGKDGK IPPGFPGVEY MLPLLLTAVH DGKLTMKELT DRMSTNPRRI 
      1760       1770       1780       1790       1800
FNLPPQDDTY IEVDLNEEWT IPENGGQSKA GWTPFAGRKV FGKVHNVIIR 
      1810       1820       1830       1840       1850
GEEAVIDGRI VAIPGFGKNV RLYPHSGTAH RGDSDFDQIL EPIPQQMIES 
      1860       1870       1880       1890       1900
SSDEQSPLHT PPRAHTPIAF PGELLAKNCI SVKHLDKGQI NRIFELADRY 
      1910       1920       1930       1940       1950
KHDVEKGHPL THILNGKVLV NLFYEVSTRT SCSFSAAMQR LGGSVISVDS 
      1960       1970       1980       1990       2000
QSSSVQKGET LEDTVQVLGS YGDILVLRSN ENGAADRAAR VCDQPVINGG 
      2010       2020       2030       2040       2050
DGTGEHPTQA LLDVYTIRQE MGTVNGLTIA LVGDLKNGRT VHSLAKLLCL 
      2060       2070       2080       2090       2100
YKDITLHYVA PSTELEMPQE VLDYVSSKSN FVQKKFTSLA EGINHVDVVY 
      2110       2120       2130       2140       2150
VTRIQKERFS SPDEYNKVKG SYVINAKLLN EAARDVEEPS SLLVPARSLP 
      2160       2170       2180       2190 
IVMHPLPRVD EIAVELDHDE RAAYFRQAKN GVFVRMSILS LLLGRGHL
Length:2,198
Mass (Da):242,582
Last modified:February 5, 2008 - 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:i31CFC62E64D21B1E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
BX284602 Genomic DNA Translation: CAA91059.2

NCBI Reference Sequences

More...RefSeqi		NP_495838.2, NM_063437.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		D2085.1.1; D2085.1.1; WBGene00004259

Database of genes from NCBI RefSeq genomes

More...GeneIDi		174385

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cel:CELE_D2085.1

UCSC genome browser

More...UCSCi		D2085.1, c. elegans

<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
BX284602 Genomic DNA Translation: CAA91059.2
RefSeqiNP_495838.2, NM_063437.4

3D structure databases

SMRiQ18990
ModBaseiSearch...

Protein-protein interaction databases

STRINGi6239.D2085.1

Proteomic databases

EPDiQ18990
PaxDbiQ18990
PeptideAtlasiQ18990

Genome annotation databases

EnsemblMetazoaiD2085.1.1; D2085.1.1; WBGene00004259
GeneIDi174385
KEGGicel:CELE_D2085.1
UCSCiD2085.1, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		174385
WormBaseiD2085.1 ; CE41886 ; WBGene00004259 ; pyr-1

Phylogenomic databases

eggNOGiKOG0370, Eukaryota
GeneTreeiENSGT00940000157241
HOGENOMiCLU_000513_2_0_1
InParanoidiQ18990
OMAiADKCYFL
OrthoDBi273358at2759
PhylomeDBiQ18990

Enzyme and pathway databases

UniPathwayiUPA00070;UER00115
UPA00070;UER00116
UPA00070;UER00117
ReactomeiR-CEL-500753, Pyrimidine biosynthesis

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q18990

Gene expression databases

BgeeiWBGene00004259, Expressed in multi-cellular organism and 5 other tissues

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, 2 hits
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_CAEEL
<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: Q18990
<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: January 18, 2017
Last sequence update: February 5, 2008
Last modified: December 2, 2020
This is version 162 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 programCaenorhabditis 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. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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