ID A0A094E273_9PEZI Unreviewed; 609 AA.
AC A0A094E273;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-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=V497_01284 {ECO:0000313|EMBL:KFY65780.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY65780.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY65780.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFY65780.1}.
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DR EMBL; JPJZ01000168; KFY65780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094E273; -.
DR STRING; 1420910.A0A094E273; -.
DR HOGENOM; CLU_013783_3_0_1; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000029268; 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; IPR023828; Peptidase_S8_Ser-AS.
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.
DR PROSITE; PS00138; SUBTILASE_SER; 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:UP000029268};
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..609
FT /note="tripeptidyl-peptidase II"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001894375"
FT DOMAIN 210..599
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 500
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 609 AA; 66026 MW; CB283C748E44A81E CRC64;
MFVINSVVQA LLLSASVVVA IKPFEQLNEV PRGWELVGAA KDATAIKLRL SLKQQNVDKF
YEEMLAVSTP DNAKYGQHYE GLELRSLLAP TAETSGTVIS WLQDNNITSI ADDGDYIVLQ
TNVGAANKLL STEFQWFRNA DEKTPVLRTL QYSVPDEIAS HINFVQPTTR FGGIQKLKST
VKIVEDGEAV SALKWTPSTS SKVDPACNTS ITPTCLLQLY NVHYKGDPKS GSRVGYASFL
EEYARYSDLE KFEAAYAPYA AGQNFTVIKF NGGLDNQTST DDSGEANLDN QYALSLGYPN
PVTEFSVGGR GLLIPDGDSP TPDDNTNEPY LDFLLALLKL PNSKIPQVIS ISYGENEQEI
PVSYAEQVCQ LFAQLGARGT SVLFSSGDSG TGDFCLSNDG KNTVKFQPQF PASCPWITSV
GGTRNIEPEE ATYFSSGGFS NLWPRPLYQE LAVRGYLAQI GKKNDGYFNK KGRGFPDIAA
QSYRYHVYDS GKDVQYQGTS CASPAAAGII SLLNSARLSS KLPPFGFLNP WLYTIGQIGF
NDIVHGAGTG CNGLSRFNSE PNGSPVIPGA SWNATKGWDP VTGLGTPDFG KLLKLSTPWV
KNEGGQVPA
//
