ID A0A067NX81_PLEOS Unreviewed; 656 AA.
AC A0A067NX81;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=PLEOSDRAFT_1110226 {ECO:0000313|EMBL:KDQ32678.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ32678.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(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|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; KL198004; KDQ32678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067NX81; -.
DR STRING; 1137138.A0A067NX81; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1110226; -.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; A0A067NX81; -.
DR OrthoDB; 2326650at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 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, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..656
FT /note="tripeptidyl-peptidase II"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012836472"
FT DOMAIN 235..655
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 321
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 571
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 614
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 635
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 656 AA; 70620 MW; 2C0B082B482D3B6D CRC64;
MKLLLLASLF LAAQAAIITH PHATVLHEKR DLLPSGWAHA RRHDPSAIIP LKFALTQSNM
HRLEEFLNEV SHPKSPQYGN HWTAGKIAET FAPSEETIST VHNWLVGSGI PAERIKISST
KGWINVDASV AEANDLLRTE YNVYVHESGK SHVGCNEYHL PAHVAPHVEL VLPSVHFDAR
VEKRGPSTAP VTISNLGQPG FGITPKTTGK VPTEVLKFHN AKQDAAAAAD YCWLILTPDC
LRTLYGLNYT TQAAAKNSFG VVEYTPQAFL QSDIDMFHFN YSREIMGKTP NVISIDGGKS
TLTTQRSVLQ TQVQNFAYNG ESDLDLEYAM NLVGVQQNIT LYQVGDLVQG ASFNNFLDAI
DGSYCTFEGG DDIYQDPHYP NTQTGGWKGA AECGTVKPTN VISTSYGYNE ADLNPTYTAR
QCAEYAKLGL MGITMLFSSG DSGVGGNNGV CMSEFGFPDA YGPVFNPGFP ASCPFVTVVG
ATQINKNAPV TAPEAAIDQV IFSGGGFSNH FAMPDYQKDH VNNYLTNFPP SHPDDIWNST
GVARAFPDIA ANGANFVAAV NGQFILVYGT SASTPVIGAL ITLINDARLA AGKKTVGFIN
PTIYSPDFSD AFNDIVAGNN SGCGSSGFNA TSGWDPVTGL GTPRFGKLLE KWLSLP
//
