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Entry version 154 (12 Aug 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Propionyl-CoA carboxylase alpha chain, mitochondrial

Gene

pcca-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score:

Annotation score:4 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 is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).By similarity

<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

biotinPROSITE-ProRule annotation

<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: propanoyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.By similarity
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Propionyl-CoA carboxylase alpha chain, mitochondrial (pcca-1)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei163ATPBy similarity1
Binding sitei247ATPBy similarity1
Binding sitei282ATPBy similarity1
<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 bindingi322Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi335Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi335Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi337Magnesium or manganese 2PROSITE-ProRule annotation1
<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 sitei339By similarity1
Binding sitei395Biotin; via carbonyl oxygenBy 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 bindingi195 – 256ATPPROSITE-ProRule annotationAdd BLAST62

<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
Biological processLipid degradation, Lipid metabolism
LigandATP-binding, Biotin, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-196780, Biotin transport and metabolism
R-CEL-71032, Propionyl-CoA catabolism

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

More...
UniPathwayi
UPA00945;UER00908

<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:
Propionyl-CoA carboxylase alpha chain, mitochondrial1 Publication (EC:6.4.1.3By similarity)
Short name:
PCCase subunit alpha
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit alpha
<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:pcca-1
ORF Names:F27D9.5
<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 elegans
<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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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 X

Organism-specific databases

WormBase

More...
WormBasei
F27D9.5 ; CE04451 ; WBGene00017864 ; pcca-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

Keywords - Cellular componenti

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?MitochondrionSequence analysis
<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_0000234102? – 724Propionyl-CoA carboxylase alpha chain, mitochondrial

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 residuei690N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity.By similarity

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q19842

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

More...
PaxDbi
Q19842

PeptideAtlas

More...
PeptideAtlasi
Q19842

PRoteomics IDEntifications database

More...
PRIDEi
Q19842

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0011:Q19842

<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
WBGene00017864, 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

The holoenzyme is a dodecamer composed of 6 alpha subunits and 6 beta subunits (By similarity).

Interacts with sir-2.2 and sir-2.3 (PubMed:23438705).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
45950, 15 interactors

STRING: functional protein association networks

More...
STRINGi
6239.F27D9.5

<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
Q19842

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>Domaini48 – 495Biotin carboxylationPROSITE-ProRule annotationAdd BLAST448
Domaini167 – 364ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini649 – 724Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST76

<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

Consists of an N-terminal biotin carboxylation/carboxylase (BC) domain that catalyzes the transient carboxylation of the biotin covalently attached to the C-terminal biotinyl-binding/biotin carboxyl carrier (BCC) domain.By similarity

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0238, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156083

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000395_3_3_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q19842

KEGG Orthology (KO)

More...
KOi
K01965

Identification of Orthologs from Complete Genome Data

More...
OMAi
FVEICSH

Database of Orthologous Groups

More...
OrthoDBi
254436at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q19842

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR001882, Biotin_BS
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR000089, Biotin_lipoyl
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR041265, PCC_BT
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
IPR011053, Single_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF00364, Biotin_lipoyl, 1 hit
PF02786, CPSase_L_D2, 1 hit
PF18140, PCC_BT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00878, Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51230, SSF51230, 1 hit
SSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS00188, BIOTIN, 1 hit
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q19842-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRAASSIRA VANRGLATAA VARPGVPLDE REGKEIYTTV GIDYNEPKFD
60 70 80 90 100
KILIANRGEI ACRVIKTARA MGIKTVAVHS DVDSNSLHVK MADEAVCVGE
110 120 130 140 150
APTAKSYLRA DRILQAVEDT GAQAVHPGYG FLSENTKFAA ELEKAGAKFI
160 170 180 190 200
GPNSKAILDM GDKIHSKKIA TAARVSMIPG YDGEIADEDM CVKVSRDIGY
210 220 230 240 250
PVMIKASAGG GGKGMRVAWN DKQAREGYRL SKQEAASSFG DDRMLVEKFI
260 270 280 290 300
DNPRHIEMQV LCDKHGNALW LNERECSIQR RNQKVIEEAP SSFVPPEMRR
310 320 330 340 350
KMGEQAVQLA KAVGYDSAGT VEFLVDSQRN FYFLEMNTRL QVEHPITECI
360 370 380 390 400
TGIDIVQQML RVSYGHPLPI TQEQVPLNGW AFESRVYAED PYKGFGLPSV
410 420 430 440 450
GRLSRYVEPK HVDGVRCDSG IREGSEISIY YDPLICKLVT HGDNREQALN
460 470 480 490 500
RMQEALDNYV IRGVTHNIPL LRDIVQEKRF RTGDITTKYL PEVYPEGFQG
510 520 530 540 550
TSLSPKEQDV VIAFASALNA RKLARANQFL NQNKQRSTHV ASFSKTYKFV
560 570 580 590 600
SSLPVKEGER PTEHAVEVEF VEGSANKAQV RIGGKTVTIS GDLNLSHPVN
610 620 630 640 650
SIEVDGEHIT TQIVGKRAGE ITVLYKGTPF KVKVLPEQAV KYLQYMKEKA
660 670 680 690 700
KVDLSTVVLS PMPGAIKNVN VKPGDMVSEG QELVVMEAMK MQNSLHAGKT
710 720
GRVKAVNVKV GATVDEGEVL VELE
Length:724
Mass (Da):79,762
Last modified:November 1, 1996 - v1
<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:iE09832FB65AABA45
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
FO080935 Genomic DNA Translation: CCD67920.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T16187

NCBI Reference Sequences

More...
RefSeqi
NP_509293.1, NM_076892.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
F27D9.5.1; F27D9.5.1; WBGene00017864
F27D9.5.2; F27D9.5.2; WBGene00017864

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
181026

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cel:CELE_F27D9.5

UCSC genome browser

More...
UCSCi
F27D9.5, 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
FO080935 Genomic DNA Translation: CCD67920.1
PIRiT16187
RefSeqiNP_509293.1, NM_076892.4

3D structure databases

SMRiQ19842
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi45950, 15 interactors
STRINGi6239.F27D9.5

2D gel databases

World-2DPAGEi0011:Q19842

Proteomic databases

EPDiQ19842
PaxDbiQ19842
PeptideAtlasiQ19842
PRIDEiQ19842

Genome annotation databases

EnsemblMetazoaiF27D9.5.1; F27D9.5.1; WBGene00017864
F27D9.5.2; F27D9.5.2; WBGene00017864
GeneIDi181026
KEGGicel:CELE_F27D9.5
UCSCiF27D9.5, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
181026
WormBaseiF27D9.5 ; CE04451 ; WBGene00017864 ; pcca-1

Phylogenomic databases

eggNOGiKOG0238, Eukaryota
GeneTreeiENSGT00940000156083
HOGENOMiCLU_000395_3_3_1
InParanoidiQ19842
KOiK01965
OMAiFVEICSH
OrthoDBi254436at2759
PhylomeDBiQ19842

Enzyme and pathway databases

UniPathwayiUPA00945;UER00908
ReactomeiR-CEL-196780, Biotin transport and metabolism
R-CEL-71032, Propionyl-CoA catabolism

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q19842

Gene expression databases

BgeeiWBGene00017864, Expressed in multi-cellular organism and 5 other tissues

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR001882, Biotin_BS
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR000089, Biotin_lipoyl
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR041265, PCC_BT
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
IPR011053, Single_hybrid_motif
PfamiView protein in Pfam
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF00364, Biotin_lipoyl, 1 hit
PF02786, CPSase_L_D2, 1 hit
PF18140, PCC_BT, 1 hit
SMARTiView protein in SMART
SM00878, Biotin_carb_C, 1 hit
SUPFAMiSSF51230, SSF51230, 1 hit
SSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS00188, BIOTIN, 1 hit
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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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 nameiPCCA_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: Q19842
<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: May 2, 2006
Last sequence update: November 1, 1996
Last modified: August 12, 2020
This is version 154 of the entry and version 1 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

Direct protein sequencing, 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
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