ARP2_METBS
ID ARP2_METBS Reviewed; 267 AA.
AC A0A0B4FP77;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
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=MBR_03975;
OS Metarhizium brunneum (strain ARSEF 3297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276141;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 3297;
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; AZNG01000004; KID76040.1; -; Genomic_DNA.
DR RefSeq; XP_014545212.1; XM_014689726.1.
DR AlphaFoldDB; A0A0B4FP77; -.
DR SMR; A0A0B4FP77; -.
DR EnsemblFungi; KID76040; KID76040; MBR_03975.
DR GeneID; 26241245; -.
DR HOGENOM; CLU_010194_1_3_1; -.
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_0000445814"
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; 28481 MW; B955700E28F3153D CRC64;
MASSEETPRS LAGKVALVTG AGRGIGKGIA LELAKRGASL VVNYNSAEKP AQEVVDEISK
TGSRAVAIKA DITKVPEVSR LFQEALRHFG HLDIVVSNSG TEVFKPEEEV TEEDYDRVFN
LNTRAQFFIA QHAYVHLRDG GRIVLMSSVA ANMSGIPNHA LYAGSKAAVE GFTRSFAVDA
GHRKITVNAI APGGVKTDMY DANAWHYVPN GKPGMPMEEI DKGLAAFCPL GRVAVPQDIG
RVVAFLAHPD SEWVNGQVIL LTGGSVT