ID A0A1M2W168_TRAPU Unreviewed; 413 AA.
AC A0A1M2W168;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Tripeptidyl-peptidase sed2 {ECO:0000313|EMBL:OJT13601.1};
GN ORFNames=TRAPUB_9852 {ECO:0000313|EMBL:OJT13601.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT13601.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT13601.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT13601.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJT13601.1}.
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DR EMBL; MNAD01000380; OJT13601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M2W168; -.
DR STRING; 154538.A0A1M2W168; -.
DR OMA; DISACFS; -.
DR OrthoDB; 5624639at2759; -.
DR Proteomes; UP000184267; 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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..413
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012228472"
FT DOMAIN 45..413
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 413 AA; 43532 MW; 29FEC05E23162153 CRC64;
MISTSLLIAS LFTLVFGAPT AYNLKLHESR TEIPAGFSLT GPAPPDTPLR LRIALVQNNF
TALEEILYNV STPSSANYGQ YLSEKDLEEY FNHTSNTFDS LLARVNMANS AKQYADAKGV
ALLDSWLTLE VPVREANEWL DADFSVFTHN ESGLQAIRTL SYSIPAELED HIDFVHPTIS
FPNPSPRLIS VGDNNHEGSL DLLNLLLKGR ALPQVLTISY SQNEDTLSPK LAAMYAQLAA
RGTSIIVPSG NGGVSGSRST NCGTFVPTFP ASCPLYAARP ATPLTPLTLI SNVTSVVATQ
GLCPETATAA PSSGGFSNIF PQPPWQAPAV SGYLSLLGDT HAGAFSRLGR ASPDVAHCAI
VVDGKTVRVD DAGCGGATFA AVIALLNARL VAAGRSPLGF LNPLLYSVAG AAA
//
