UBA5_CAEEL
ID UBA5_CAEEL Reviewed; 419 AA.
AC P91430;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN Name=uba-5 {ECO:0000312|WormBase:T03F1.1};
GN ORFNames=T03F1.1 {ECO:0000312|WormBase:T03F1.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, INTERACTION WITH UFC-1, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23449979; DOI=10.1074/jbc.m113.458000;
RA Hertel P., Daniel J., Stegehake D., Vaupel H., Kailayangiri S., Gruel C.,
RA Woltersdorf C., Liebau E.;
RT "The ubiquitin-fold modifier 1 (Ufm1) cascade of Caenorhabditis elegans.";
RL J. Biol. Chem. 288:10661-10671(2013).
CC -!- FUNCTION: E1-like enzyme which activates ufm-1. Required for
CC interaction between ufm-1 and ufc-1. {ECO:0000269|PubMed:23449979}.
CC -!- SUBUNIT: Interacts with ufc-1. {ECO:0000269|PubMed:23449979}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine.
CC {ECO:0000269|PubMed:23449979}.
CC -!- DISRUPTION PHENOTYPE: Reduced egg laying and lifespan. Delayed larval
CC development. Enhanced resistance to pathogens, heat and oxidative
CC stress. Reduced survival in the presence of cadmium. Inactivation of
CC the ufm-1 cascade. {ECO:0000269|PubMed:23449979}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
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DR EMBL; FO080917; CCD67786.1; -; Genomic_DNA.
DR PIR; T29201; T29201.
DR RefSeq; NP_491248.1; NM_058847.7.
DR AlphaFoldDB; P91430; -.
DR SMR; P91430; -.
DR BioGRID; 37442; 5.
DR DIP; DIP-24997N; -.
DR IntAct; P91430; 2.
DR STRING; 6239.T03F1.1.2; -.
DR EPD; P91430; -.
DR PaxDb; P91430; -.
DR PeptideAtlas; P91430; -.
DR EnsemblMetazoa; T03F1.1.1; T03F1.1.1; WBGene00020184.
DR EnsemblMetazoa; T03F1.1.2; T03F1.1.2; WBGene00020184.
DR EnsemblMetazoa; T03F1.1.3; T03F1.1.3; WBGene00020184.
DR GeneID; 171968; -.
DR UCSC; T03F1.1.1; c. elegans.
DR CTD; 171968; -.
DR WormBase; T03F1.1; CE13096; WBGene00020184; uba-5.
DR eggNOG; KOG2336; Eukaryota.
DR GeneTree; ENSGT00940000156177; -.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; P91430; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; P91430; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P91430; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020184; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IMP:UniProtKB.
DR GO; GO:0097501; P:stress response to metal ion; IMP:UniProtKB.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..419
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391937"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 260
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
SQ SEQUENCE 419 AA; 46512 MW; BA61B08DB8AC8F4C CRC64;
MSDEQIDKLV SRLDGALNRL GNVKKDHPLE SSSNSKPTHQ PKSPAPYRQK IEKLSAEVVD
SNPYSRLMAL QRMGIVNEYE RIREKTVAVV GVGGVGSVVA EMLTRCGIGK LILFDYDKVE
IANMNRLFYQ PNQAGLSKVE AARDTLIHVN PDVQIEVHNF NITTMDNFDT FVNRIRKGSL
TDGKIDLVLS CVDNFEARMA VNMACNEENQ IWMESGVSEN AVSGHIQYIE PGKTACFACV
PPLVVASGID ERTLKRDGVC AASLPTTMAV VAGFLVMNTL KYLLNFGEVS QYVGYNALSD
FFPRDSIKPN PYCDDSHCLQ RQKEYEEKVA NQPVDLEVEV PEEETVVHED NEWGIELVNE
SEPSAEQSSS LNAGTGLKFA YEPIKRDAQT ELSPAQAATH DFMKSIKDKL VEEAQNKGK
