ID V2WK32_MONRO Unreviewed; 917 AA.
AC V2WK32;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=Moror_15392 {ECO:0000313|EMBL:ESK81957.1};
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:ESK81957.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK81957.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK81957.1,
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 -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:ESK81957.1}.
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DR EMBL; AWSO01002138; ESK81957.1; -; Genomic_DNA.
DR RefSeq; XP_007858736.1; XM_007860545.1.
DR AlphaFoldDB; V2WK32; -.
DR KEGG; mrr:Moror_15392; -.
DR HOGENOM; CLU_003559_3_1_1; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02124; PA_PoS1_like; 1.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034187; Peptidases_S8_5.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..917
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004711031"
FT DOMAIN 166..601
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 407..461
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 633..741
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 175
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 555
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 917 AA; 96450 MW; 469CBAE50D28B795 CRC64;
MSPRHFFLSF LSFLSFLSVV HLTLAVVPLS SVKKTTNLPI LPNRYIVEVN EASSVAQLSS
RSEESVHKRL YHSLKSRDVG FDVNKEFNSP GVFVGVSLTL ENADDVSKLE ETEGVKAIRP
VRKFGRPQPL NEHIVTDPSD PNIPPDSQST HILTGVDKLH AEGVFGKGIK IGIIDTGIDY
THPALGNGFG PGFKIEGGFD LVGDDYDGEN GPIPDPDPLD QCAGHGTHVA GIIGADPGNP
FNISGVAYES NLYAYRVFGC EGFTTDDVII DALLLGLKDG QDILTLSLGE TDGWSESSSA
VVASRIAGAG KVVTIAAGNG RFQLLSSQEN VFSQLFYADG ASGSWYTSSP ANGINVISVA
SLDNTVINLQ AATVNGVEHD PIVYYELFPF PIPEPIPIYA TSNSTTVVDD ACNPLPDDIP
DLSGFLTVIR RGTCTFTQKA TNAAAKGANF IFIYDNGNGF GAIDVGDFNA TLIRAPDGEF
LVNQFAAGAP ITITFPQTGG GVEFPDPDGG LISSFTSWGP TNEAGFRPAF AAPGGNILST
LPVAQGSYGV ESGTSMATPF AAGSAALLLQ VKGKSANIAR GARTLFETTA SVVPSSHTDA
DPLQSLTQAG AGLINVYNAL HTTTFVSPGE LVLNDTAHFV GEHTISVTNA GTEDKAYRVS
HVPAGTAITV QPGTIFPANG PVPQTSDAAT VQISSESFSL APGESTTLTV NIKPPSGLDP
STFPVYSGFI EISAESESLH VSYLGIAASL IDKQVLDDTD VYFGVPLPLI VDAAGNVQVS
PTNYTFDEST GDFPTLLYRL VFGTALFRLD LVEATAEVTA SLNGRDVVPL ITFPHAKVGA
VKVVGPLAEV TYTERNDEST EAGYFSIALD SPTFANGTAI PAGSYRLLAR ALRVTGNPAN
EEDYDSWLSP IVGFFPA
//
