GenomeNet

Database: UniProt
Entry: A8XEQ8
LinkDB: A8XEQ8
Original site: A8XEQ8 
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   16-JAN-2019, entry version 53.
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.,
RA   D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
RA   Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
RA   Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
RA   Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
RA   Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
RA   Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for
RT   comparative 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.
CC       {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}.
DR   EMBL; HE601540; CAP31026.2; -; Genomic_DNA.
DR   SMR; A8XEQ8; -.
DR   STRING; 6238.CBG11977; -.
DR   PRIDE; A8XEQ8; -.
DR   EnsemblMetazoa; CBG11977; CBG11977; WBGene00032994.
DR   WormBase; CBG11977; CBP25964; WBGene00032994; Cbr-uba-5.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   InParanoid; A8XEQ8; -.
DR   OMA; HANICKD; -.
DR   OrthoDB; 1092362at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
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; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Ubl conjugation pathway; Zinc.
FT   CHAIN         1    432       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391936.
FT   ACT_SITE    262    262       Glycyl thioester intermediate.
FT                                {ECO:0000250}.
FT   METAL       238    238       Zinc. {ECO:0000250}.
FT   METAL       241    241       Zinc. {ECO:0000250}.
FT   METAL       315    315       Zinc. {ECO:0000250}.
FT   METAL       320    320       Zinc. {ECO:0000250}.
FT   BINDING      96     96       ATP; via amide nitrogen. {ECO:0000250}.
FT   BINDING     117    117       ATP. {ECO:0000250}.
FT   BINDING     140    140       ATP. {ECO:0000250}.
FT   BINDING     163    163       ATP. {ECO:0000250}.
FT   BINDING     196    196       ATP. {ECO:0000250}.
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
//
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