UBA5_DROSE
ID UBA5_DROSE Reviewed; 404 AA.
AC B4IK21;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GM13085;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480851; EDW51393.1; -; Genomic_DNA.
DR RefSeq; XP_002044081.1; XM_002044045.1.
DR AlphaFoldDB; B4IK21; -.
DR SMR; B4IK21; -.
DR STRING; 7238.B4IK21; -.
DR EnsemblMetazoa; FBtr0196070; FBpp0194562; FBgn0168016.
DR GeneID; 6619868; -.
DR KEGG; dse:6619868; -.
DR HOGENOM; CLU_013325_0_1_1; -.
DR OMA; FTPDQAG; -.
DR PhylomeDB; B4IK21; -.
DR Proteomes; UP000001292; 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..404
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391948"
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"
SQ SEQUENCE 404 AA; 44156 MW; ACFBE84A9FE4A46F CRC64;
MSHAIDELQA IIADLKTELE TEPKSSVGVA SNSRLARDRI DRMSAEVVDS NPYSRLMALQ
RMNIVKDYER IRDKAVAIVG VGGVGSVTAD MLTRCGIGKL ILFDYDKVEL ANMNRLFFTP
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
