UBA5_DROYA
ID UBA5_DROYA Reviewed; 403 AA.
AC B4PYA4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GE15940;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000162; EDX01966.1; -; Genomic_DNA.
DR RefSeq; XP_002100858.1; XM_002100822.2.
DR AlphaFoldDB; B4PYA4; -.
DR SMR; B4PYA4; -.
DR STRING; 7245.FBpp0260950; -.
DR EnsemblMetazoa; FBtr0262458; FBpp0260950; FBgn0233497.
DR GeneID; 6525019; -.
DR KEGG; dya:Dyak_GE15940; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; B4PYA4; -.
DR Proteomes; UP000002282; 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; Ubl conjugation pathway;
KW Zinc.
FT CHAIN 1..403
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391952"
FT REGION 371..403
FT /note="Disordered"
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 403 AA; 44120 MW; 95B66CDDD7944702 CRC64;
MSHAIDELQA IIAELKTELE EPKATGGVAT NSRLARDRID RMSAEVVDSN PYSRLMALQR
MNIVKDYERI RDKAVAIVGV GGVGSVTADM LTRCGIGKLI LFDYDKVELA NMNRLFFTPD
QAGLSKVEAA AATLSFINPD VEIETHNYNI TTVENFDRFL DTISQGGRIA GQPVDLVLSC
VDNFEARMAI NAACNERNLN WFESGVSENA VSGHIQFIRP GDTACFACAP PLVVAENIDE
KTLKREGVCA ASLPTTMGIT AGFLVQNALK YLLNFGEVSD YLGYNALSDF FPKMTLKPNP
QCDDRNCIVR QKEFQARPKP VVIEEKAVSE EPLHATNEWG IELVAEDAPE SNPTPTEAPV
VGEGLRLAYE APERSSETSE ETVTTAPADE TSLEDLMAQM KSM
