ARP2_METAQ
ID ARP2_METAQ Reviewed; 267 AA.
AC E9EHG1;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Hydroxynaphthalene reductase-like protein Arp2 {ECO:0000303|PubMed:29958281};
DE EC=1.1.-.- {ECO:0000305|PubMed:29958281};
GN Name=Arp2 {ECO:0000303|PubMed:29958281}; ORFNames=MAC_09309;
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=29958281; DOI=10.1371/journal.pgen.1007472;
RA Zeng G., Zhang P., Zhang Q., Zhao H., Li Z., Zhang X., Wang C., Yin W.B.,
RA Fang W.;
RT "Duplication of a Pks gene cluster and subsequent functional
RT diversification facilitate environmental adaptation in Metarhizium
RT species.";
RL PLoS Genet. 14:E1007472-E1007472(2018).
CC -!- FUNCTION: Hydroxynaphthalene reductase-like protein; part of the Pks2
CC gene cluster that mediates the formation of infectious structures
CC (appressoria), enabling these fungi to kill insects faster
CC (PubMed:29958281). The product of the Pks2 gene cluster is different
CC from the one of Pks1 and has still not been identified
CC (PubMed:29958281). {ECO:0000269|PubMed:29958281}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; GL698613; EFY84644.1; -; Genomic_DNA.
DR RefSeq; XP_007815649.1; XM_007817458.1.
DR AlphaFoldDB; E9EHG1; -.
DR SMR; E9EHG1; -.
DR STRING; 92637.XP_007815649.1; -.
DR EnsemblFungi; EFY84644; EFY84644; MAC_09309.
DR GeneID; 19253620; -.
DR KEGG; maw:MAC_09309; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; E9EHG1; -.
DR OMA; KHMVDAG; -.
DR OrthoDB; 913128at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..267
FT /note="Hydroxynaphthalene reductase-like protein Arp2"
FT /id="PRO_0000445813"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 18..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P16544"
SQ SEQUENCE 267 AA; 28506 MW; F84AF5F1500998E2 CRC64;
MASTEEIPRS LAGKVALITG AGRGIGKGIA IELAKRGASV IVNYNSADKP AQEVVDEIAK
TGSRAIAIKA DITKVPEVSR LFQEALQHFG HLDIVVSNSG TEVFKPEEEV TEEDYDRVFN
LNTRAQFFVA QHAYIHLRNG GRIILMSSVA ANMSGIPNHA LYAGSKAAVE GFTRSFAVDA
GHKKITVNAI APGGVKTDMY DANAWHYVPG GKPGMPMEEI DKGLAAFCPL ERVAVPQDIG
RVVAFLAHPD SEWVNGQIIL LTGGSIT