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Database: UniProt
Entry: Q6GLG7
LinkDB: Q6GLG7
Original site: Q6GLG7 
ID   UBA5_XENTR              Reviewed;         399 AA.
AC   Q6GLG7;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
DE   AltName: Full=UFM1-activating enzyme;
DE   AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1;
GN   Name=uba5; Synonyms=ube1dc1; ORFNames=TNeu098a04.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}.
CC       Nucleus {ECO:0000250|UniProtKB:Q9GZZ9}. Note=Localizes mainly in
CC       cytoplasm, while it mainly localizes to the nucleus in presence of
CC       SUMO2. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR760171; CAJ82881.1; -; mRNA.
DR   EMBL; BC074525; AAH74525.1; -; mRNA.
DR   RefSeq; NP_001004790.1; NM_001004790.1.
DR   UniGene; Str.11058; -.
DR   ProteinModelPortal; Q6GLG7; -.
DR   SMR; Q6GLG7; -.
DR   STRING; 8364.ENSXETP00000054036; -.
DR   PaxDb; Q6GLG7; -.
DR   Ensembl; ENSXETT00000054036; ENSXETP00000054036; ENSXETG00000025266.
DR   GeneID; 448010; -.
DR   KEGG; xtr:448010; -.
DR   CTD; 79876; -.
DR   Xenbase; XB-GENE-955661; uba5.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   GeneTree; ENSGT00940000156177; -.
DR   HOGENOM; HOG000256352; -.
DR   HOVERGEN; HBG056496; -.
DR   InParanoid; Q6GLG7; -.
DR   KO; K12164; -.
DR   OMA; ETHNYNI; -.
DR   OrthoDB; 1092362at2759; -.
DR   TreeFam; TF314168; -.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000025266; Expressed in 17 organ(s), highest expression level in embryo.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071566; F:UFM1 activating enzyme activity; ISS:UniProtKB.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN         1    399       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391934.
FT   ACT_SITE    246    246       Glycyl thioester intermediate.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       222    222       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       225    225       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       299    299       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       304    304       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING      79     79       ATP; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     100    100       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     123    123       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     146    146       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     180    180       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
SQ   SEQUENCE   399 AA;  44463 MW;  14DE1F439061102E CRC64;
     MEKLIEELRS RVSELEEELH RVRNGEQVHE GHRAKINTMS AEVVDSNPYS RLMALKRMGI
     VEDYEKIRTF TVAVVGVGGV GSVTAEMLTR CGIGKLLLFD YDKVEMANMN RLFFQPHQAG
     LSKVEAAEHT LRNINPDVQF EVHNYNITTL DNFQHFMDRI SKGGLKEGTP VDLVLSCVDN
     FEARMAINTA CNELVQIWME SGVSENAVSG HIQLIKPGET ACFACAPPLV VAANIDEKTL
     KREGVCAASL PTTMGVVAGM LVQNVLKYLL NFGTVSFYLG YNAMQDFFPT MAMKPNPQCG
     DKYCRKQQEE FKLKEAARPK QEPIVVKEEE IVHEDNDWGI ELVSEVSEEE LKAASGPVPE
     LPEGIKVAYT VPITEPTSGF IVEDSEQSLD ELMAQMKNL
//
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