UBA5_DROER
ID UBA5_DROER Reviewed; 402 AA.
AC B3NUC9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GG18422;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH954180; EDV46044.1; -; Genomic_DNA.
DR RefSeq; XP_001977117.1; XM_001977081.2.
DR AlphaFoldDB; B3NUC9; -.
DR SMR; B3NUC9; -.
DR STRING; 7220.FBpp0136968; -.
DR EnsemblMetazoa; FBtr0138476; FBpp0136968; FBgn0110637.
DR GeneID; 6551372; -.
DR KEGG; der:6551372; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; B3NUC9; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:EnsemblMetazoa.
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 GO; GO:0050905; P:neuromuscular process; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Ubl conjugation pathway;
KW Zinc.
FT CHAIN 1..402
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391942"
FT REGION 369..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 43979 MW; C0B116EB7D896067 CRC64;
MPYAIDELQE IIGNLRTELV EPIDSGGVNN TRLGRDRVER MSAEVVDSNP YSRLMALQRM
NIVKDYERIR DKAVAIVGVG GVGSVTADML TRCGIGKLIL FDYDKVELAN MNRLFFTPNQ
AGLSKVAAAG ATLNFINPDV EIEMFNFNIT TVDNFDRFLN AISQGGRIAG QPVDLVLSCV
DNFEARMAIN AACNERNLNW FESGVSENAV SGHIQFIRPG DTACFACAPP LVVAENIDEK
TLKKEGVCAA SLPTTMGITA GFLVQNVLKY LLNFGEVSDY LGYNALSDFF PKMTLKPNPQ
CDDSNCLVRQ MEFQAKPKPV VVEEKADNEE PLHATNEWGI ELVAENAPEI NPTSTETPVV
GEGLKLAYEA PEKSSETSEE TVTTAPPDDA SLEDLMAQMK SM
