ID   UBA5_DROWI              Reviewed;         406 AA.
AC   B4NDE5;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
GN   ORFNames=GK10218;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH964239; EDW82851.1; -; Genomic_DNA.
DR   RefSeq; XP_002071865.1; XM_002071829.2.
DR   AlphaFoldDB; B4NDE5; -.
DR   SMR; B4NDE5; -.
DR   STRING; 7260.FBpp0239361; -.
DR   EnsemblMetazoa; FBtr0240869; FBpp0239361; FBgn0212233.
DR   GeneID; 6648687; -.
DR   KEGG; dwi:6648687; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   HOGENOM; CLU_013325_0_1_1; -.
DR   InParanoid; B4NDE5; -.
DR   OMA; FTPDQAG; -.
DR   OrthoDB; 1092362at2759; -.
DR   PhylomeDB; B4NDE5; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
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   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..406
FT                   /note="Ubiquitin-like modifier-activating enzyme 5"
FT                   /id="PRO_0000391951"
FT   REGION          373..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        249
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  44758 MW;  59E20F3190505818 CRC64;
     MSAIDELQAL IVELKSELEA QKTETRQQQA QAQQARQRID RMSAEVVDSN PYSRLMALQR
     MNIVKDYERI REKTVAVVGV GGVGSVTADM LTRCGIGKLI LFDYDKVELA NMNRLFFTPD
     QAGLSKVEAA ARTLTFINPD VKIETHNYNI TTVDNFDNFL TTISQSGTEP GTPVDLILSC
     VDNFEARMAI NAACNEHSLN WFESGVSENA VSGHIQFIRP GDTACFACAP PLVVAENIDE
     RTLKREGVCA ASLPTTMGIT AGFLVQNALK YLLNFGEVSD YLGYNALNDF FPKMTLKPNP
     QCDDRHCLLR QKEFQTKPKP VKKEVEIVAE EPLHATNEWG IELVAEDAPA TEDADEPKPI
     VSDIGEGLRL AYEAPSKSTE TTSEATTTTT GDETSLDDLM AQMKSM