ID   ARP1_METBS              Reviewed;         744 AA.
AC   A0A0B4GDU5;
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=Scytalone dehydratase-like protein Arp1 {ECO:0000305|PubMed:29958281};
DE            EC=4.2.1.- {ECO:0000305|PubMed:29958281};
GN   Name=Arp1 {ECO:0000303|PubMed:29958281}; ORFNames=MBR_03976;
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: Scytalone dehydratase-like protein; part of the Pks2 gene
CC       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   -!- SUBUNIT: Homotrimer. Each subunit contains an active site, located in
CC       the central part of the hydrophobic core of the monomer, which
CC       functions independently. {ECO:0000250|UniProtKB:P56221}.
CC   -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
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DR   EMBL; AZNG01000004; KID76041.1; -; Genomic_DNA.
DR   RefSeq; XP_014545213.1; XM_014689727.1.
DR   AlphaFoldDB; A0A0B4GDU5; -.
DR   SMR; A0A0B4GDU5; -.
DR   EnsemblFungi; KID76041; KID76041; MBR_03976.
DR   GeneID; 26241246; -.
DR   HOGENOM; CLU_020129_1_0_1; -.
DR   GO; GO:0030411; F:scytalone dehydratase activity; IEA:InterPro.
DR   GO; GO:0006582; P:melanin metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR004235; Scytalone_dehydratase.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF02982; Scytalone_dh; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..744
FT                   /note="Scytalone dehydratase-like protein Arp1"
FT                   /id="PRO_5002089388"
FT   ACT_SITE        656
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
FT   ACT_SITE        681
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
FT   BINDING         621
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
FT   BINDING         702
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P56221"
SQ   SEQUENCE   744 AA;  81966 MW;  FF3470A58C6FF713 CRC64;
     MGWNQTFLFL AFAATAASSL VGSGTSLQLN GIDYFVSPFS QGKVTNGSVA INTRQNQLGF
     VPATVIAGDL YTESTLQSLF LNWSTVDDVW QPAFLETIFV FNFAKLTNKN HNYHDGVSSS
     VFPLQVTHKI PSGPYFLNVH TGEVHPAYRL YDDFAGAFTQ SLLQRPDGRF QTLSAQVPAA
     ASITIGVPSR LYFTKTEAKP LAGVRIGVKD IFSLAGVKKG CGNRAWYHLY PVANSTGTAM
     QNLIDKGAII VGVQKTSQFA NGETPTADWV DYHSPFNPRG DGYQDPATSS AGAGSSIASY
     EWLDLAVGSD TGGSIRGPAT VQGIFGNRPS HGLVSLDNVM PLSPKLDTPG FLARDPCLWN
     AANAALYRDK YTFFGHQAPR YPKKLYLLDF PAGNTSHAPI LQNFVTKLAK FLDTSPTNID
     LNKEWERTRP TSAGDQSLAQ LLNTTYAAII SKDQAKLVRE PFYRDYAAVH DGRLPFVNPV
     PLARWTWGDS QPSSLLSDAV RNKTLFMDWF NGNILPPSSD PLTCSSGLLL HVNGSADFVS
     RNRYINPPVP PFGFSNSQIS LFAETPDSVF PLGQVPVFSS ITNNTEYLPV TIDVVAAKGF
     QLQRDWARLR AILAPALYVD YTKIGKEKWD AMSADDFMAM VSNDDFLGDP CVKTQHLIGA
     TYWERVSESK VIGHHQLRAA HQVYTSPDLK TVKLRGHSHA TNEHYYVKSN GVWKFAGLKP
     EVRWNEYKFE EVFKGSYTQS EKHS