ID   UBA5_DROPS              Reviewed;         397 AA.
AC   Q29HT0;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
GN   ORFNames=GA14526;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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; CH379064; EAL31677.1; -; Genomic_DNA.
DR   RefSeq; XP_001354623.1; XM_001354587.3.
DR   RefSeq; XP_015041519.1; XM_015186033.1.
DR   AlphaFoldDB; Q29HT0; -.
DR   SMR; Q29HT0; -.
DR   STRING; 7237.FBpp0286306; -.
DR   EnsemblMetazoa; FBtr0287868; FBpp0286306; FBgn0074554.
DR   EnsemblMetazoa; FBtr0365778; FBpp0329057; FBgn0074554.
DR   GeneID; 4814656; -.
DR   KEGG; dpo:Dpse_GA14526; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   HOGENOM; CLU_013325_0_1_1; -.
DR   InParanoid; Q29HT0; -.
DR   OMA; FTPDQAG; -.
DR   PhylomeDB; Q29HT0; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0074554; Expressed in male reproductive system and 3 other tissues.
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..397
FT                   /note="Ubiquitin-like modifier-activating enzyme 5"
FT                   /id="PRO_0000391947"
FT   REGION          343..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   397 AA;  43528 MW;  410636D88DFB3A8D CRC64;
     MTNAIDELQA IIAELKTEVE EQRAVIRQSR DRIEHMSAEV VDSNPYSRLM ALQRMNIVKN
     YERIRDKTVA IVGVGGVGSV TADMLTRCGI GKLILFDYDK VELANMNRLF FTPDQAGLSK
     VEAAARTLTF INPDVRIETH NYNITTIDNF DNFLSTITGD GTVAGEPVDL VLSCVDNFEA
     RMAINAACNE KCLNWFESGV SENAVSGHIQ FLRPGDTACF ACAPPLVVAE NIDEKTLKRE
     GVCAASLPTT MGITAGFLVQ NALKYLLNFG EVSDYLGYNA LNDFFPKMTL KPNPQCDDRN
     CLLRQKEFQA RPKPVVVQEE APTDEPLHAS NDWGIELVAE DAPSDAPTDL SQSTDVGQGL
     RLAYEAPEKS SAEATQAATA PVDDTSLEDL MAQMKSM