GenomeNet

Database: UniProt
Entry: Q3KQ23
LinkDB: Q3KQ23
Original site: Q3KQ23 
ID   UBA5_XENLA              Reviewed;         397 AA.
AC   Q3KQ23;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JAN-2019, entry version 67.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) 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; BC106418; AAI06419.1; -; mRNA.
DR   RefSeq; NP_001089728.1; NM_001096259.1.
DR   UniGene; Xl.42315; -.
DR   ProteinModelPortal; Q3KQ23; -.
DR   SMR; Q3KQ23; -.
DR   BioGrid; 592572; 1.
DR   IntAct; Q3KQ23; 1.
DR   MaxQB; Q3KQ23; -.
DR   GeneID; 734791; -.
DR   KEGG; xla:734791; -.
DR   CTD; 734791; -.
DR   Xenbase; XB-GENE-955667; uba5.
DR   HOVERGEN; HBG056496; -.
DR   KO; K12164; -.
DR   OrthoDB; 1092362at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; Cytoplasm; Metal-binding; Nucleotide-binding; Nucleus;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN         1    397       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391933.
FT   ACT_SITE    244    244       Glycyl thioester intermediate.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       220    220       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       223    223       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       297    297       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       302    302       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING      77     77       ATP; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING      98     98       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     121    121       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     144    144       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     178    178       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
SQ   SEQUENCE   397 AA;  44169 MW;  20E22E83D6F1608A CRC64;
     MEGLIEELRS RVRELEEELD RVRNGQHEGH RTKIEKMSAE VVDSNPYSRL MALKRMGIVE
     NYEKIRTFTV AVVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS
     KVEAAEHTLR NINPDVQFEV HNYNITTLDN FQHFMDRISK GGLKEGSPVD LVLSCVDNFE
     ARMAINTACN ELGQVWMESG VSENAVSGHI QLIKPGETAC FACAPPLVVA ANIDEKTLKR
     EGVCAASLPT TMGVVAGILV QNVLKYLLNF GTVSFYLGYN AMQDFFPTMA MKPNPQCDDK
     YCRKQQEEFK LKEAAKPKQE TVVVEEEEVV HEDNDWGIEL VSEVSEEELK AASGPVPDLP
     EGIKVAYTIP ITKPTSGFTV EDSEQSLDEL MAQMKNL
//
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