UBA5_DROAN
ID UBA5_DROAN Reviewed; 396 AA.
AC D1GY43; B3MAM7; D1GY50;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GF23479;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-373 AND GLY-373.
RC STRAIN=BKK11, BKK13, BKK16, BKK4, BKK5, BKK7, BKK8, and BKK9;
RX PubMed=20015359; DOI=10.1186/1471-2148-9-291;
RA Grath S., Baines J.F., Parsch J.;
RT "Molecular evolution of sex-biased genes in the Drosophila ananassae
RT subgroup.";
RL BMC Evol. Biol. 9:291-291(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN546432; CBE66731.1; -; Genomic_DNA.
DR EMBL; FN546433; CBE66732.1; -; Genomic_DNA.
DR EMBL; FN546434; CBE66733.1; -; Genomic_DNA.
DR EMBL; FN546435; CBE66734.1; -; Genomic_DNA.
DR EMBL; FN546436; CBE66735.1; -; Genomic_DNA.
DR EMBL; FN546437; CBE66736.1; -; Genomic_DNA.
DR EMBL; FN546438; CBE66737.1; -; Genomic_DNA.
DR EMBL; FN546439; CBE66738.1; -; Genomic_DNA.
DR EMBL; CH902618; EDV41314.1; -; Genomic_DNA.
DR RefSeq; XP_001958508.1; XM_001958472.2.
DR AlphaFoldDB; D1GY43; -.
DR SMR; D1GY43; -.
DR STRING; 7217.FBpp0126671; -.
DR EnsemblMetazoa; FBtr0128179; FBpp0126671; FBgn0100473.
DR GeneID; 6506120; -.
DR KEGG; dan:6506120; -.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; D1GY43; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; D1GY43; -.
DR Proteomes; UP000007801; 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..396
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391941"
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"
FT VARIANT 373
FT /note="E -> A (in strain: BKK11, BKK13, BKK16, BKK4, BKK5,
FT BKK7 and BKK8)"
FT /evidence="ECO:0000269|PubMed:20015359"
FT VARIANT 373
FT /note="E -> G (in strain: BKK9)"
FT /evidence="ECO:0000269|PubMed:20015359"
SQ SEQUENCE 396 AA; 43896 MW; 39DBC40209A837CA CRC64;
MSHAIDELQA IIAELKVELE EQKTSNRQAR SRIDRMSAEV VDSNPYSRLM ALQRMNIVKE
YERIRDKAVA VVGVGGVGSV TADMLTRCGI GKLILFDYDK VELANMNRLF FTPDQAGLSK
VEAAARTLNF INPDVQIETH NYNITTVDNF DRFLATITES GKELGQPVDL VLSCVDNFEA
RMAINAACNE RNLNWFESGV SENAVSGHIQ FIRPGDTACF ACAPPLVVAE NIDEKTLKRE
GVCAASLPTT MGITAGFLVQ NALKYLLNFG EVSDYLGYNA LNDFFPRMTL KPNPQCDDRN
CLLRQKEFQA RPKPIEVKED VSSSDEPLHA TNEWGIELVA DDEPVNCPEP AKSSAVVQGL
KLAYEAPEKE KVEEENVATV SDETSLEDLM AQMKSM
