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Database: UniProt
Entry: Q5R8X4
LinkDB: Q5R8X4
Original site: Q5R8X4 
ID   UBA5_PONAB              Reviewed;         404 AA.
AC   Q5R8X4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 71.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000312|EMBL:CAH91786.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex {ECO:0000312|EMBL:CAH91786.1};
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with UFC1. Interacts with
CC       UFM1. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}.
CC       Nucleus {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9GZZ9}. Note=Localizes mainly in the
CC       cytoplasm, while it localizes to the nucleus in presence of SUMO2.
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000255}.
DR   EMBL; CR859624; CAH91786.1; -; mRNA.
DR   RefSeq; NP_001126036.1; NM_001132564.1.
DR   ProteinModelPortal; Q5R8X4; -.
DR   SMR; Q5R8X4; -.
DR   STRING; 9601.ENSPPYP00000015785; -.
DR   GeneID; 100172985; -.
DR   KEGG; pon:100172985; -.
DR   CTD; 79876; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   HOVERGEN; HBG056496; -.
DR   InParanoid; Q5R8X4; -.
DR   KO; K12164; -.
DR   OrthoDB; 1092362at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; 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   GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; 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; Golgi apparatus;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway; Zinc.
FT   CHAIN         1    404       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000194972.
FT   ACT_SITE    250    250       Glycyl thioester intermediate.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       226    226       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       229    229       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       303    303       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       308    308       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING      83     83       ATP; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     104    104       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     127    127       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     150    150       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     184    184       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   MOD_RES      45     45       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   MOD_RES     358    358       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8VE47}.
SQ   SEQUENCE   404 AA;  44774 MW;  7424DBC3173F4E95 CRC64;
     MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS NPYSRLMALK
     RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
     HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFQHF MDRISNGGLE EGKPVDLVLS
     CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID
     EKSLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
     PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE KEEIIHEDNE WGIELVSEVS EEELKNSSGP
     VPDLPEGITV AYTIPKKQED SVTEVTVEDS GESLEDLMAK MKNM
//
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