UBA5_DROPE
ID UBA5_DROPE Reviewed; 384 AA.
AC B4GYC7;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
GN ORFNames=GL19893;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479197; EDW27783.1; -; Genomic_DNA.
DR RefSeq; XP_002023606.1; XM_002023570.1.
DR AlphaFoldDB; B4GYC7; -.
DR SMR; B4GYC7; -.
DR STRING; 7234.FBpp0184000; -.
DR PRIDE; B4GYC7; -.
DR EnsemblMetazoa; FBtr0185508; FBpp0184000; FBgn0157491.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR OMA; FTPDQAG; -.
DR PhylomeDB; B4GYC7; -.
DR Proteomes; UP000008744; 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..384
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000391946"
FT REGION 352..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 42079 MW; 55048415F41F4FAC CRC64;
MTNAIDELQA IIAELKTEVE EQRAVIRQSR DRIEHMSAEV RMNIVKNYER IRDKTVAIVG
VGGVGSVTAD MLTRCGIGKL ILFDYDKVEL ANMNRLFFTP DQAGLSKVEA AARTLTFINP
DVRIETHNYN ITTIDNFDNF LNTITGDGTV AGEPVDLVLS CVDNFEARMA INAACNEKCL
NWFESGVSEN AVSGHIQFLR PGDTACFACA PPLVVAENID EKTLKREGVC AASLPTTMGI
TAGFLVQNAL KYLLNFGEVS DYLGYNALND FFPKMTLKPN PQCDDRNCLL RQKEFQARPK
PVVVQEEAPT DEPLHASNDW GIELVAEDAP SNAPTDLSQS TDVGQGLRLA YEAPEKSSAE
ATQAATAPVD DTSLEDLMAQ MKSM
