ID A0A1I5DYZ0_9BACT Unreviewed; 1082 AA.
AC A0A1I5DYZ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SAMN04488519_103212 {ECO:0000313|EMBL:SFO04494.1};
OS Algoriphagus ornithinivorans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=226506 {ECO:0000313|EMBL:SFO04494.1, ECO:0000313|Proteomes:UP000199564};
RN [1] {ECO:0000313|Proteomes:UP000199564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15282 {ECO:0000313|Proteomes:UP000199564};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Degrades oligopeptides. {ECO:0000256|PIRNR:PIRNR036421}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR036421}.
CC -!- SIMILARITY: Belongs to the peptidase S41B family.
CC {ECO:0000256|ARBA:ARBA00008524, ECO:0000256|PIRNR:PIRNR036421}.
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DR EMBL; FOVW01000003; SFO04494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5DYZ0; -.
DR STRING; 226506.SAMN04488519_103212; -.
DR Proteomes; UP000199564; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd07562; Peptidase_S41_TRI; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
DR InterPro; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43253; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR43253:SF1; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036421};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036421};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR036421};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1082
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011590003"
FT DOMAIN 843..1034
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 743
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 962
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1023
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 963
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1082 AA; 122084 MW; 1559137C85C64029 CRC64;
MYKATILSFL FISIFYNQSN AQEKPGYFMH PDLHENTMVF VAEGDIWTAP VSGGMATRLT
THPGDESDPK ISPDGKWVAY AASYEGPTEV YVMPISGGLP KRLTYEPSAS IPVAWRSSTE
LAYTTNQYST LPRLRTVVVD VNSRVKEVLP LEMAAEGSFD RESNTYFFVR PTYHNNVTKR
YQGGTARKLW KYSNGAAEAV KLTKDYAGED HHPIFHQGRV YFISSRDGIQ NVWSMKPDGS
DIQQHTKEVS YDVREYSLSG NTLVYRSGAD LFQMNLGQSE SRKIAINLVS DFDQLRENWV
DNPASYITNI SVSNDGEKVA LTARGRVFVF PAKDGRMIRL SRKDGVRYRD AVFTTDSKDI
LTFSDESGEF EIHQYSGLGL DQGKQLTDNG STLRFNLTPS PDGKWLAWID LNNDLWIRNL
GTGKAVKANL TDEDLHGSMS WSPDSQWLAY GQAASNTFTQ LFVFNPTTEK RVTLTSDRTN
SLNPQWSADG KWIYFLSDRN FETKVGSPWG QRQPEPFWEK QMKIYHIPLQ KGLISPFTPK
NELKAEEKKL EGPVSVKIDE EGLMERVQEV PVPAGNYKNL IVTDKALYYH RVGPGPGVYY
GGGASNEDEP ALMMTPISEK AEQKVFADKI NSYAVSANNK YALLRQGANH FLVELGASPV
SDLSKNKLDL NGWRFSIDPR EDWKQIYTDA WRMERDYFYD AGMHGVDWDK MYEKYLPLVD
RVTTRNELSD VIGELIGELS VLHTSVRGGD TRDGDDNIQF GMLGGLFTKT NQGYRIDYIF
QSDPDYPDEK SPLSHPAFGI QTGDVITHID GTSVLEVADM QVLLRDKARK QVRLAIAGKG
DFIIEPMSSG QESNLRYNDW EYTRRLETEA KSNGDIGYVH LRAMTSGDIG QWYRDFYPQF
KKKGLVIDVR HNRGGNIDSF ILEKLMREAF FYWKSRTGEP YWNMNYAFRG HLVLLVDEFT
ASDGEAFAEG FRRLGLGKAI GARTWGGEVW LSGVNTLSDN GIARAPMNGV YGETENGTEW
LIEGVGFIPD IEVINLPKAT FEGKDAQLDA AIEHLKELIQ KDPRPVPTPP AYPDLSFKNG
KN
//
