ID V2XHC0_MONRO Unreviewed; 580 AA.
AC V2XHC0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=Moror_10461 {ECO:0000313|EMBL:ESK91905.1};
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:ESK91905.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK91905.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK91905.1,
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 -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at
CC acidic pHs and is involved in virulence.
CC {ECO:0000256|ARBA:ARBA00002451}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01032}.
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:ESK91905.1}.
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DR EMBL; AWSO01000310; ESK91905.1; -; Genomic_DNA.
DR RefSeq; XP_007848800.1; XM_007850609.1.
DR AlphaFoldDB; V2XHC0; -.
DR KEGG; mrr:Moror_10461; -.
DR HOGENOM; CLU_013783_3_1_1; -.
DR OrthoDB; 2326650at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:ESK91905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..580
FT /note="tripeptidyl-peptidase II"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004713830"
FT DOMAIN 220..580
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 300
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 496
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 580 AA; 60736 MW; F9103BC421D1AD8B CRC64;
MARISCALAI LAVMASAVSA SVTPRQKAMS VLEQRPLPAG FARMSTATKL VAGNEDQLNL
RVALKPKDRD GLVKTLYETS TPGSASYGQH LSREEVKAFM APDAEAVSAV ARWLSENGVT
DIKPSGAFDD WLSFSVPASK ADSLFNAKFE KFQHISTGEQ IVRTLEYSVP QELLGHISLV
HPTTSFALRP PAEPRFIAPV VTETNVTARA NPAPTSCNNN VTPTCLQQLY GIPTTPASAS
SPTLGVTGFI QQWAQEADLS TFLSILRPDI DRNTSFTLQT FDGGENPQGS QFAGIEANLD
IQYTVGIATG VPVTFLSVGL DNSDDVSGFL DVYEQLTASE NPPPVLSTSY GFDEPDLGPA
LANRLCDAYA ALAARGVSNL YASGDGGVWG SRDNQCTTFV PTFPAGCPFV TAVGSTSGGA
AAGEEVASDF SSGGFSDVFA RPSYQDAAVS SYISAIGDEN AGLYNTSSRG YPDVSARGTP
VQIVNAGQRI LVQGTSCSCP IFASVIALIN DQLVAAGKPV LGFLNPFLYA NPDALFDTTK
GTNNGPDCQS KGFPAVKGWD ASTGLGTPNY EALLAAALAA
//
