ID V2WRY6_MONRO Unreviewed; 648 AA.
AC V2WRY6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Peptidase prolyl oligopeptidase active site region {ECO:0000313|EMBL:ESK84332.1};
GN ORFNames=Moror_10215 {ECO:0000313|EMBL:ESK84332.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK84332.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK84332.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84332.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK84332.1}.
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DR EMBL; AWSO01001323; ESK84332.1; -; Genomic_DNA.
DR RefSeq; XP_007856365.1; XM_007858174.1.
DR AlphaFoldDB; V2WRY6; -.
DR KEGG; mrr:Moror_10215; -.
DR HOGENOM; CLU_012236_1_0_1; -.
DR OrthoDB; 2785676at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR43056:SF5; ACYL-PEPTIDE HYDROLASE; 1.
DR PANTHER; PTHR43056; PEPTIDASE S9 PROLYL OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 432..642
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 648 AA; 71130 MW; 7765679F1BA7CCDB CRC64;
MSPQIAPYGT WDTPITADAI TGNSTSLIDI VVDPITSNIY HLELRPSEDG RTVLVDTRAK
RDIFGPEWNA ADGVHEYGGG AATVYDGIAY FSNFKDGRIY RVSVKDDGAA PEAVTPDNLP
YRYANFAIHP KYTNLIVAIL EDHTHDIPSE VVNTLCLIDT NTKTVSPKFV SGNDFYSHPV
FSTDGNYLAW QEWSFPDMPW EGGELYVAKV QVDGGKLTLK SEAKVAGEKE TYSAGYPLWA
SSETLIFISD ISGFSNPWKY TVSDGKASPI LPRTVEEDFS NCMWSLSMFP FAVIAGGKQG
IFSSWKDGKN FLNLIDIDSG SRSDVPGPYV LIDSVRAVGE NGIAFIGSAP NKGDSVVLYT
TDGDYNVLKP NPNSDKFDPS IVSVAQGITL PGPLYVVYYP PHNPGYQGLV GEKPPCIVSV
HGGPTGMAYQ GLSWTIQYYT SRGFAWMDVN YGGSFGYGSE YRNRLNGEWG IVDVEDCILA
VQAMSQGDEI DPQRVVIRGG SAGGFTTLLS LCHSSNPKTY AGGTSLYGIS NLLKLTEDTH
KFESQYAFKL VGGTPEQVPK NYKDRSAINH IDDFNRPLLL LQGTEDRVVP PEQSQAIYDG
IKARGGDVEL KLYPGEGHGF KQKEHQIDAL ERELAFYTRI LNLKKRPY
//
