UBA5_CAEBR
ID UBA5_CAEBR Reviewed; 432 AA.
AC A8XEQ8;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN Name=uba-5 {ECO:0000312|WormBase:CBG11977};
GN ORFNames=CBG11977 {ECO:0000312|WormBase:CBG11977};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: E1-like enzyme which activates ufm-1. Required for
CC interaction between ufm-1 and ufc-1. {ECO:0000250|UniProtKB:P91430}.
CC -!- SUBUNIT: Interacts with ufc-1. {ECO:0000250|UniProtKB:P91430}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
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DR EMBL; HE601540; CAP31026.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XEQ8; -.
DR SMR; A8XEQ8; -.
DR STRING; 6238.CBG11977; -.
DR EnsemblMetazoa; CBG11977.1; CBG11977.1; WBGene00032994.
DR WormBase; CBG11977; CBP25964; WBGene00032994; Cbr-uba-5.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; A8XEQ8; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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; IEA:EnsemblMetazoa.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
DR GO; GO:0097501; P:stress response to metal ion; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..432
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391936"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ9"
SQ SEQUENCE 432 AA; 48009 MW; 61E84516B88425B4 CRC64;
MTESDVAESI GDIVSRLNNA LDDLETKKNQ TPSVLKGPTV SQERPSAPYR QKIEKLSAEV
VDSNPYSRLM ALQRMGIVRD YEQIRDKTVA VVGVGGVGSV VAEMLTRCGI GKLILFDYDK
VEIANMNRLF YQPNQAGLSK VEAARDTLIH VNPDVQIEVH NFNITTMDNF DVFVGRIRNG
SLKSGKIDLV LSCVDNFEAR MAVNMACNEE NQIWMESGVS ENAVSGHIQY IEPGKTACFA
CVPPLVVASN IDERTLKREG VCAASLPTTM AVVAGFLVMN TLKYLLNFGE VSHYVGYNAL
ADFFPRESIK PNPSCDDRHC QIRQKEYEEK ISSEPITLDI QAPEDEPIIH EENDWGIEVV
DSDTTEAPSS SAATEVAPGL KFAYEPTQTP KKNSSDNLKL SPSQAVTKEW MENIRDALLE
EDRLKKEQNK RK
