GenomeNet

Database: UniProt
Entry: B9VJ80
LinkDB: B9VJ80
Original site: B9VJ80 
ID   UBA5_BOMMO              Reviewed;         393 AA.
AC   B9VJ80;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 36.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Bombycoidea; Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wu P., Guo X.-J., Li M.-W.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1-like enzyme which activates UFM1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000305}.
DR   EMBL; FJ556993; ACL99855.1; -; mRNA.
DR   RefSeq; NP_001138805.1; NM_001145333.1.
DR   UniGene; Bmo.10321; -.
DR   SMR; B9VJ80; -.
DR   STRING; 7091.BGIBMGA013537-TA; -.
DR   PRIDE; B9VJ80; -.
DR   GeneID; 100270786; -.
DR   KEGG; bmor:100270786; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   KO; K12164; -.
DR   OrthoDB; 1092362at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
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; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Ubl conjugation pathway; Zinc.
FT   CHAIN         1    393       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391939.
FT   ACT_SITE    241    241       Glycyl thioester intermediate.
FT                                {ECO:0000250}.
FT   METAL       217    217       Zinc. {ECO:0000250}.
FT   METAL       220    220       Zinc. {ECO:0000250}.
FT   METAL       294    294       Zinc. {ECO:0000250}.
FT   METAL       299    299       Zinc. {ECO:0000250}.
FT   BINDING      75     75       ATP; via amide nitrogen. {ECO:0000250}.
FT   BINDING      96     96       ATP. {ECO:0000250}.
FT   BINDING     119    119       ATP. {ECO:0000250}.
FT   BINDING     142    142       ATP. {ECO:0000250}.
FT   BINDING     175    175       ATP. {ECO:0000250}.
SQ   SEQUENCE   393 AA;  42531 MW;  A8B2FE039515DEAB CRC64;
     MASVDELQKK IKELEAKLAA VEAKGGPMRQ KIEVMSSEVV DSNPYSRLMA LKRMGIVNNY
     EQIREKTVAV VGVGGVGSVT AEMLTRCGIG KLILFDYDKV ELANMNRLFF QPHQAGLSKV
     DAAAATLQNI NPDVTIDAYN YNITTVDNFQ KFCDTISKGS LTGGAVDLVL SCVDNFEARM
     AINTACNELD QKWFESGVSE NAVSGHIQFI SPGESACFAC APPLVVATKV DERTLKREGV
     CAASLPTTMG IVAGFLVQNS LKYLLEFGNV THYLGYSALT DFFPTMSLQP NPTCDDASCR
     ARQEQRRLQP RVELAAEVTE DCGPVHQDND WGISVLEENS PADEDCPGLK LVDGVQVAYS
     IPVDSSTPES STGGAVAASE LSLEDLMQQM KTM
//
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