ID C6H4M3_AJECH Unreviewed; 619 AA.
AC C6H4M3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=HCDG_00224 {ECO:0000313|EMBL:EER44645.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER44645.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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}.
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DR EMBL; GG692419; EER44645.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H4M3; -.
DR STRING; 544712.C6H4M3; -.
DR MEROPS; S53.010; -.
DR VEuPathDB; FungiDB:HCDG_00224; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR HOGENOM; CLU_013783_3_0_1; -.
DR OMA; SGWGTPW; -.
DR Proteomes; UP000002624; 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:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
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:SF39; 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.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW 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:UP000002624};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 213..605
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 298
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 522
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 564
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"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 619 AA; 68257 MW; F4D16C71B62FBDD5 CRC64;
MDSRMRRASI DEYLSSNWSC AGPIKGAGKE ASRRSDALAS SIWSHSLTEI LPVSNPLHKR
YGKFLTRIEA AKLLHPGQDA INRTQAWLEN HGISIHRHRF NAAGDWLRVT VSIAEAERLL
DTKYYIYRYG NQTAARAMEW SLPQSLHDVI DTIQPTTSFI RLPVHVKARQ NENHEVTDLN
QLAEDVAPGT GTAVDLSNIP PHLTPQQACN ASAVTPLCLR TLYGTLYYKA SAKRGTRMAL
VNYLGEFNNR SDISQFLKVY RPDALAGAES FENISINGGI NQQSLVTDEQ YTHGSGREGN
LDAEVMIGIA HPIPLTTYTV GESEPPFKPD SFTPTNTNEP FLTWLNWILD QPDSELPSVV
STSYGDIEHT VPISYARRVC NGFAQLGARG VSVIMGSGDH GVGHPGDCYS NDGLFTPEFL
VSFPDSCPWV TSVGATKGIQ PEVVAVNSRN GFSSGGGFSN YFPRPDYQTN NPHSVARYLS
KIGALHSGMF NPYGRAIPDV SAQGYRYVTI WNGETKLVDG TSASTPIFAA IVALVNDALA
AEDRPPLGFL NPWLYAEGYR AFRDINEGTN GGCNTTGFPA LQGWDAASGW GTPWFPKFKE
LALKRRSRET RPWYIQWFL
//
