ID A0A218UH03_9PASE Unreviewed; 610 AA.
AC A0A218UH03;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Tripeptidyl-peptidase 1 {ECO:0000256|ARBA:ARBA00020254};
DE EC=3.4.14.9 {ECO:0000256|ARBA:ARBA00012067};
DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
DE AltName: Full=Tripeptidyl-peptidase I {ECO:0000256|ARBA:ARBA00032661};
GN Name=TPP1 {ECO:0000313|EMBL:OWK53005.1};
GN ORFNames=RLOC_00005034 {ECO:0000313|EMBL:OWK53005.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK53005.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK53005.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK53005.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide, but
CC also has endopeptidase activity.; EC=3.4.14.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000884};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OWK53005.1}.
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DR EMBL; MUZQ01000308; OWK53005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218UH03; -.
DR STRING; 299123.ENSLSDP00000012646; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..610
FT /note="Tripeptidyl-peptidase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012126204"
FT DOMAIN 242..610
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 518
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 610 AA; 66029 MW; 3D8A397AD6EB3129 CRC64;
MARGCWGIPA VLALCAAAWS CAPGLALQLE RDQPFRVPPG WAHAGRVDPG QPVLLTFALR
QRGAARLARL VQAVSDPRSP QYGQYLSLEQ VRDLVQPSPA TLMTVLKWLQ GHGVEDCRSV
TTLDFLECYL PASAAEHLLP GAEFHRYVQG QRSLLRSPLP YSVPAELAEH LDFGTSHLGE
LRLRNAGLCP ALPGLCALTA SPIPLGSAAV GGLHRFPTEH KAISRARARK DAKLARASFH
LGVTPAVLRQ RYNMTGGDVG LLPNNSQACA QFLEQYFHQA DLAEFMQLFG SGFAHRTQVD
RVVGHQGRGK AGLEASLDVE YIMSTGANVS TWVFSNAGRH ESQEPFLAWL LLLSNMSALP
WVHSVSYGDD EDSLSYAYME RVNTEFMKAA ARGLTILFAS GDDGAGCRRE HGGNHTFRPS
FPASSPYVTT VGGTSFKNPF LVTEEVTDYI SGGGFSNVFP MPEYQAAAVG HFLHSASKLP
PSSYYNSSGR AYPDLAALSD NYWVVTNRIP LPWVSGTSAS TPVVAGMVAL INDRRLQRGL
APLGFLNPAL YQLQKQGLGD AFYDVIQGCH LSCLDGTVQG QGFCATPAWD PVTGWGTPNF
PRLLRALGPR
//
