ID A0A010QYZ5_9PEZI Unreviewed; 941 AA.
AC A0A010QYZ5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EXF85432.1};
GN ORFNames=CFIO01_04440 {ECO:0000313|EMBL:EXF85432.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF85432.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF85432.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF85432.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF85432.1}.
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DR EMBL; JARH01000104; EXF85432.1; -; Genomic_DNA.
DR RefSeq; XP_007590969.1; XM_007590907.1.
DR AlphaFoldDB; A0A010QYZ5; -.
DR KEGG; cfj:CFIO01_04440; -.
DR eggNOG; KOG4266; Eukaryota.
DR HOGENOM; CLU_003559_1_0_1; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000020467; 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; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR010435; Fn3_5.
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; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
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:UP000020467};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..941
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001455348"
FT DOMAIN 167..599
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 643..744
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 99..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 561
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 941 AA; 99867 MW; A7B8949C9D5090F4 CRC64;
MRLIAHFAAA AACCLAIDTS QAVPKTYFIE LSKDSTAEGL SISPYDLASK AAEASIPLRV
RYEYTDKSVF YGVSVSLDSD SDSEKLRALP GVENVIPVQS VAHPHRPSSN VKRSPSSGKG
SGKLATRNYE GSRDQSKYSL SRRAHVDWNS PHAMTGVDRV HAKGVLGEGV RVAVIDTGID
YLHPALGGCF GKGCKVEFGY DFVGDDYGFS NSTPNPSPDP RPGCFDSFHG THVAGIIGME
VSSNASMFAG LVGVAPRATL GMYRVFGCDG SASDDAIVAA MQRAVEEGAH VVSISIGEFG
TWSGYPGSIL PAAVTALRAK GVAVIAAAGN SGTQGMFSIN LPGGADDGLG VASVENAKFP
TYPVRDSNGA EFHYGALYPF PEGEYPVAWA GRNTSTYKFG CSASDYPPAS SLQRPISEYI
VAVKRGPSCS PTQVQTYASA ANFTRVITYP DPTIDDVFIE GHAVPTPSLN ADGYVYSMGS
VIDETLSNAA KSTGQYKLLV ESQTPLLVDQ LGGGSPNNFT SLGPNADFVF KPQIAAPGGV
ILATFPLMEN SGGFGIISGT SMATPYISGV YALIKSQNPD LSVEEIFERM QTTAKQVNMA
DYDLMSPAIQ QGAGLVQAHK AVFPGTVVSP GEFKLVDVEE AIFTIDNPSD TDVAYSFYNV
PAVGAAPFAE GSSRTAQVGY IPSVFSARID FASGSQLTVP AGGSANVSFS VTPPPSPDAS
IVPIFSGFIS ISSSANETFT VPYMGPAYDY SSTPVIGTKN ITAEQRANAL TPTRDPLSAP
QVFANGDKAD IGNYRAFSFQ YPDYPVALFT SLQPVRKFRF DIVRASTNFT PTWYGFDPNV
EFDNLTETSM KENATVAGVP ILGSNMIQNG WLPQTSQQAG WSYSILDATA TIGLGLKKGS
YRILLRWLKF YKDEEDPASW DSWMSGVVDV LEDVFEPTVP S
//
