UBA5_DROVI
ID UBA5_DROVI Reviewed; 400 AA.
AC B4M357;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GJ19153;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940651; EDW65232.1; -; Genomic_DNA.
DR RefSeq; XP_002055031.1; XM_002054995.2.
DR AlphaFoldDB; B4M357; -.
DR SMR; B4M357; -.
DR STRING; 7244.FBpp0233570; -.
DR EnsemblMetazoa; FBtr0235078; FBpp0233570; FBgn0206298.
DR GeneID; 6631874; -.
DR KEGG; dvi:6631874; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; B4M357; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; B4M357; -.
DR Proteomes; UP000008792; 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; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..400
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391950"
FT ACT_SITE 243
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 296
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"
SQ SEQUENCE 400 AA; 43994 MW; F54C7F3150C94B95 CRC64;
MSNAIDELQA IIAELKSELE EQKTCTRNAR ERIERMSAEV VDSNPYSRLM ALQRMNIVKD
YERIRDKAVA IVGVGGVGSV TADMLTRCGI GKLILFDYDK VELANMNRLF FTPDQAGLSK
VEAAARTLSF INPDVRIETH NYNITTVDNF DKFLSTISES GMQQGQPVDL VLSCVDNFEA
RMAINAACNE NNLNWFESGV SENAVSGHIQ FIRPGDTACF ACAPPLVVAE NIDERTLKRE
GVCAASLPTT MGITAGLLVQ NALKYLLNFG EVSDYLGYNA LNDFFPKMTL KPNTQCDDRH
CLQRQKEFQE RPKPVLQQVE EVSDEPLHAS NDWGIELVAD DAPVAEQAPK ATDTANVASG
LRLAYEAPEK EAVDQAGHAA AGDGMPETSL EDLMAQMKSM
