YL498_MIMIV
ID YL498_MIMIV Reviewed; 422 AA.
AC Q5UQG2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable zinc-type alcohol dehydrogenase-like protein L498;
DE EC=1.-.-.-;
GN OrderedLocusNames=MIMI_L498;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP LOCATION.
RX PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT "Mimivirus giant particles incorporate a large fraction of anonymous and
RT unique gene products.";
RL J. Virol. 80:11678-11685(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Virion
CC {ECO:0000269|PubMed:16971431}.
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DR EMBL; AY653733; AAV50763.1; -; Genomic_DNA.
DR RefSeq; YP_003987010.1; NC_014649.1.
DR SMR; Q5UQG2; -.
DR PRIDE; Q5UQG2; -.
DR GeneID; 9925129; -.
DR KEGG; vg:9925129; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Metal-binding; Oxidoreductase; Reference proteome; Virion;
KW Zinc.
FT CHAIN 1..422
FT /note="Probable zinc-type alcohol dehydrogenase-like
FT protein L498"
FT /id="PRO_0000160898"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 47285 MW; CB6953CDCFDAD6C6 CRC64;
MSLEEKLNKY SNKLSMTNNL NKIDVYNKKI NKYKERQIYS NLKKPQPIDE SVISLYSLKN
EYQKSPDKMT ALGFGVTDVG KPVELLVFDR KKPTNNEVSI EIYYTGICHS DWHFIVGEWK
ADFPLIPGHE LIGRVIDIGP NVDKYSIGDI VCVSPVIDSC GHCKMCTHHI EQHCMNGATE
IYNQKTRLPG DIKPSGPITY GGYSNIVIIK QHFVYKFPKN LDIERCAPLM CAGATTYSPL
RQAKVGPGMK VGIVGIGGLG HIAVKIAKAM GAHVVAITRT EWKFKDSVNN LGANESILST
NVWQMNQHKG SFDFILSTIP MAHDIVPYIE LLKYKATICT VGELFPTVIN GMDLAQHPCF
LQSSLIAGSD EIKEMLAFCS EHNIMPDVQI IKADKINDTR QKLLESKAKY RYVIDIRASL
NK