ID   ARP2_METMF              Reviewed;         267 AA.
AC   A0A0B4HVU2;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   03-AUG-2022, entry version 25.
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=MAJ_07523;
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297;
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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; AZNE01000049; KID96467.1; -; Genomic_DNA.
DR   RefSeq; XP_014575461.1; XM_014719975.1.
DR   AlphaFoldDB; A0A0B4HVU2; -.
DR   SMR; A0A0B4HVU2; -.
DR   EnsemblFungi; KID96467; KID96467; MAJ_07523.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   OrthoDB; 913128at2759; -.
DR   Proteomes; UP000031176; 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.
FT   CHAIN           1..267
FT                   /note="Hydroxynaphthalene reductase-like protein Arp2"
FT                   /id="PRO_0000445816"
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;  28408 MW;  3C1BED0F6F242774 CRC64;
     MASSEETPRS LAGKVALVTG AGRGIGKGIA VELAKRGASV VVNYNSAEKP AQEVVDEIAK
     TGSRAVAIKA DITKVPEVSR LFQEALQHFG HLDIVVSNSG TEVFKPEEEV TEEDYDRVFN
     LNTRAQFFIA QHAYVHLRNG GRIVLMSSVA ANMSGIPNHA LYAGSKAAVE GFTRSFAVDA
     GHRKITVNAI APGGVKTDMY DANAWHYVPN GKPGMPMEEI DKGLAAFCPL GRVAVPQDIG
     RVVAFLAHPD SEWVNGQVIL LTGGSVT