ID   UBA5_DROSI              Reviewed;         404 AA.
AC   B4R345; B4F5T5;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
GN   ORFNames=GD17028;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-111.
RC   STRAIN=S1;
RX   PubMed=18477586; DOI=10.1093/molbev/msn111;
RA   Baines J.F., Sawyer S.A., Hartl D.L., Parsch J.;
RT   "Effects of X-linkage and sex-biased gene expression on the rate of
RT   adaptive protein evolution in Drosophila.";
RL   Mol. Biol. Evol. 25:1639-1650(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDX17647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM999171; CAQ53533.1; -; Genomic_DNA.
DR   EMBL; CM000366; EDX17647.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_016038940.1; XM_016173754.1.
DR   AlphaFoldDB; B4R345; -.
DR   SMR; B4R345; -.
DR   STRING; 7240.B4R345; -.
DR   GeneID; 6725682; -.
DR   Proteomes; UP000000304; Chromosome x.
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..404
FT                   /note="Ubiquitin-like modifier-activating enzyme 5"
FT                   /id="PRO_0000391949"
FT   REGION          372..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        250
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   VARIANT         111
FT                   /note="D -> A (in strain: S1)"
FT                   /evidence="ECO:0000269|PubMed:18477586"
SQ   SEQUENCE   404 AA;  44200 MW;  48FC21AD03557EA9 CRC64;
     MSHAIDELQA IIADLKTELE TEPKSSVGVA SNSRLARDRI DRMSAEVVDS NPYSRLMALQ
     RMNIVKDYER IRDKAVAIVG VGGVGSVTAD MLTRCGIGKL ILFDYDKVEL DNMNRLFFTP
     DQAGLSKVAA AAATLSFINP DVEIETHNYN ITTVENFDRF LDTISQGGRI AGQPVDLVLS
     CVDNFEARMA INAACNERNL NWFESGVSEN AVSGHIQFIR PGDTACFACA PPLVVAENID
     EKTLKREGVC AASLPTTMGI TAGFLVQNAL KYLLNFGEVS DYLGYNALSD FFPKMTLKPN
     PQCDDRNCIV RQKEFQARPK PVVIEEKAVS EEPLHATNEW GIELVAEDAP QSNPTPAETP
     VMGEGLRLAY EAPEKSSETS EETVTAATAD ETSLEDLMAQ MKSM