UBA5_BOMMO
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 03-AUG-2022, entry version 46.
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; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC 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}.
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DR EMBL; FJ556993; ACL99855.1; -; mRNA.
DR RefSeq; NP_001138805.1; NM_001145333.1.
DR AlphaFoldDB; B9VJ80; -.
DR SMR; B9VJ80; -.
DR STRING; 7091.BGIBMGA013537-TA; -.
DR PRIDE; B9VJ80; -.
DR GeneID; 100270786; -.
DR KEGG; bmor:100270786; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_0_1; -.
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; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..393
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391939"
FT ACT_SITE 241
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="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