UBA5_DROGR
ID UBA5_DROGR Reviewed; 398 AA.
AC B4JIY0;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GH12371;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916370; EDV99544.1; -; Genomic_DNA.
DR RefSeq; XP_001990920.1; XM_001990884.1.
DR AlphaFoldDB; B4JIY0; -.
DR SMR; B4JIY0; -.
DR STRING; 7222.FBpp0146277; -.
DR EnsemblMetazoa; FBtr0147785; FBpp0146277; FBgn0119850.
DR GeneID; 6564884; -.
DR KEGG; dgr:6564884; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; B4JIY0; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; B4JIY0; -.
DR Proteomes; UP000001070; 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..398
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391943"
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 398 AA; 43718 MW; A738B3646A2D72EE CRC64;
MSAAIDELQA IIAELKSELE EQKTTTRNAR ERIERMSAEV VDSNPYSRLM ALQRMNIVKD
YERIRDKAVA IVGVGGVGSV TADMLTRCGI GKLILFDYDK VELANMNRLF FTPDQAGLSK
VEAAARTLSF INPDVCIETH NYNITTVDNF DQFLSTISAS GIAVGQPVDL VLSCVDNFEA
RMAINAACNE KNMNWFESGV SENAVSGHIQ FVRPGDTACF ACAPPLVVAE NIDERTLKRE
GVCAASLPTT MGITASLLVQ NALKYLLNFG EVSDYLGYNA LSDFFPKMTL RPNTQCDDRN
CLVRQKEFHL RPKPVEKLVE VEVSDEPLHA CNDWGIELVA DNVPTTTTKS PENTNVAFGL
RLAYEAPDKS EKSETTATAG DGVSEASLEE LMAQMKSM
