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Database: UniProt
Entry: M5FV78_DACPD
LinkDB: M5FV78_DACPD
Original site: M5FV78_DACPD 
ID   M5FV78_DACPD            Unreviewed;       586 AA.
AC   M5FV78;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE            EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN   ORFNames=DACRYDRAFT_23637 {ECO:0000313|EMBL:EJT99514.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT99514.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJT99514.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT99514.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH795869; EJT99514.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FV78; -.
DR   STRING; 1858805.M5FV78; -.
DR   HOGENOM; CLU_013783_3_0_1; -.
DR   OMA; EKHAWVE; -.
DR   OrthoDB; 2326650at2759; -.
DR   Proteomes; UP000030653; 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; 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, 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:UP000030653};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..586
FT                   /note="tripeptidyl-peptidase II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004067340"
FT   DOMAIN          204..585
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        282
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        286
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        502
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         544
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         545
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         563
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         565
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   586 AA;  63179 MW;  F5B9CE6733402664 CRC64;
     MIFIQLLFWA LTFSGSALAW QSFLVKESVS VIPRGWTTSS RAPPDHLLRL QIGLRQADPT
     SLYDALANIS DPRHVQYGQH LEKEQVEALV RPHPDASESI EAWLSHHGIP AGSVSRNGAG
     DWLSIEVPVH KAEHMLDAEY RIFEHEDGSS IVRCSSWSLP ADLYEHVEFI QPTTMFARLK
     PQRSFVHSVS PGIVLANPID CSHYVTPDCI KELYGIGSYR PNSSAPNHLG IAGYLESYAN
     VNDTTFFYQE FAPKAFADDF TFSVELINNG FNDQSEMAAS LEGNLDVQYG GSLSFPIPNT
     YYSTGGSPPF NPSSGTPQNT NEPYAEFLSY ILNKSNSELP TVLSTSYGDE EQTVPYSYAV
     SVCNLFAQLG ARGVSVLFSS GDGGVGDGKG PGQDSLTCIS IDGNYTPMFL PFFPATCPYV
     TAVGATSGVP ETAASFSGGG FSNYFSRPYW QEGAVNAYTP QIPSSYSGFY NASGRAYPDV
     SAQGDNFIIR QSGNLTTGFG TSCSAPTLSS IIALLNDFLM ARGKAPLGFL NPWLYIIGST
     GFNDIVTGTN PGCGKNGFSA AVGWDPITGV GTPNVTRLMS LLSLSL
//
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