GenomeNet

Database: UniProt
Entry: Q6IVA4
LinkDB: Q6IVA4
Original site: Q6IVA4 
ID   UBA5_CHICK              Reviewed;         397 AA.
AC   Q6IVA4;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 90.
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-like protein;
DE   AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1;
GN   Name=UBA5; Synonyms=UBAL, UBE1DC1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xue P., Chen W., Zhang J., Ci H.L., Li Y.P.;
RT   "Expression pattern of UBAL in embryo development.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Localizes mainly in cytoplasm, while it mainly
CC       localizes to the nucleus in presence of SUMO2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000305}.
DR   EMBL; AY620963; AAT39515.1; -; mRNA.
DR   RefSeq; NP_001001765.1; NM_001001765.1.
DR   UniGene; Gga.14656; -.
DR   UniGene; Gga.28683; -.
DR   ProteinModelPortal; Q6IVA4; -.
DR   SMR; Q6IVA4; -.
DR   STRING; 9031.ENSGALP00000019110; -.
DR   PaxDb; Q6IVA4; -.
DR   PRIDE; Q6IVA4; -.
DR   GeneID; 414879; -.
DR   KEGG; gga:414879; -.
DR   CTD; 79876; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   HOGENOM; HOG000256352; -.
DR   HOVERGEN; HBG056496; -.
DR   InParanoid; Q6IVA4; -.
DR   KO; K12164; -.
DR   OrthoDB; 1092362at2759; -.
DR   PhylomeDB; Q6IVA4; -.
DR   PRO; PR:Q6IVA4; -.
DR   Proteomes; UP000000539; Unplaced.
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    397       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391932.
FT   ACT_SITE    243    243       Glycyl thioester intermediate.
FT                                {ECO:0000250}.
FT   METAL       219    219       Zinc. {ECO:0000250}.
FT   METAL       222    222       Zinc. {ECO:0000250}.
FT   METAL       296    296       Zinc. {ECO:0000250}.
FT   METAL       301    301       Zinc. {ECO:0000250}.
FT   BINDING      76     76       ATP; via amide nitrogen. {ECO:0000250}.
FT   BINDING      97     97       ATP. {ECO:0000250}.
FT   BINDING     120    120       ATP. {ECO:0000250}.
FT   BINDING     143    143       ATP. {ECO:0000250}.
FT   BINDING     177    177       ATP. {ECO:0000250}.
SQ   SEQUENCE   397 AA;  44178 MW;  E82183A7A53D3AA4 CRC64;
     MAERVELLER RVRELERELE LARGGRASAR ARIETMSPEV TDSNPYSRLM ALKRMGIVKD
     YEKIRTFTVA IVGVGGVGSV TAEMLTRCGI GKLLLFDYDK VELANMNRLF FQPHQAGLSK
     VQAAEHTLRN INPDVQFEVH NYNITTLDNF EHFMDRISNG ALEEGKPVDL VLSCVDNFEA
     RMAINTACNE LGQIWMESGV SENAVSGHIQ LIIPGESACF ACAPPLVVAA NIDEKTLKRE
     GVCAASLPTT MGVVAGILVQ NVLKYLLNFG TVSYYLGYNA MQDFFPTMAM KPNPQCSDQN
     CRKQQENYKI KEAAQPKQEE IHQEEEIVHE DNDWGIELVS ETTEDELKAA SGPVPDLPVG
     ITVAYTIPNK EENLTAEETV AESEESLEDL MAKMRNL
//
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