ID A0A2N1DF23_9ALTE Unreviewed; 1093 AA.
AC A0A2N1DF23;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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=CXF95_05840 {ECO:0000313|EMBL:PKH00143.1};
OS Paraglaciecola sp. MB-3u-78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=2058332 {ECO:0000313|EMBL:PKH00143.1, ECO:0000313|Proteomes:UP000233828};
RN [1] {ECO:0000313|EMBL:PKH00143.1, ECO:0000313|Proteomes:UP000233828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-78 {ECO:0000313|EMBL:PKH00143.1,
RC ECO:0000313|Proteomes:UP000233828};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) 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}.
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:PKH00143.1}.
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DR EMBL; PJCF01000003; PKH00143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1DF23; -.
DR OrthoDB; 9758793at2; -.
DR Proteomes; UP000233828; 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; 5.
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.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000233828};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 854..1048
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 537..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 978
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1037
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1093 AA; 122157 MW; EB091D5449715B0C CRC64;
MIKFVPWLLV VASMFILPRS IAQQTRLLRQ PSISDSHLAF VYAGDIWITD LLGQNSKRLT
STAAIESNPH FSPDGQRLAF SSNRSGTNSV YVMPSSGGQA NRLSWHAASG SVRGWTPDGQ
RVLFASGRDT APRPINRLWT ISVDGGPAEL VLHQWAYNGA YSGDGKHMVI DRMSRWDGEW
RNYRGGQNTP LVVVDLASLE ETMINSDSTI DIEPVWVDDT VYFLSDRDWV SNIWSYSVKR
KKLKQITEFK NADIKQLATN GKQLVFEQNG DLFTFDLASE ELQKLSIAVT GDFPWAETQW
QDVGEKADSA SLSPTGKRAI MASRGEIFTV PIEHGSVRNL TQTSDAADRA PIWSPKGDQI
AWFSDKGEQG YQLLLKSQDG LSELQAIAIG ESKMAWEPTW SPDGKYIAFV DDDVRIRLLE
LATKNIITVD TGGNNLERGR NDLAWAPDSN ALAYVKTADN GFQQIKIYSV NSQDTHFLTN
KFANSMSPAW DQNSKYLYFL ASTDYGLNSG WANTSSMAAD SEYAPYIVSL LADETSPFAP
RSDEEGTEED EPKNDDEKDS EVADETQDKD AKATEKETVE AIKIDFKEIE RRILPLPMPA
GEYAFTLTAP QGTVFFAKRQ CENRDLALLK FDLKSRKAES FMEGIQLASI SADHKKLLVK
KGPKWFVVDA DKSTAKTDKP LETKLMMNLN RQQEWRQIFV EAWRYQRDYF YDKNMHGRDW
DEVFGRYESL VKHIKHRADL TYLLDMVNGE LSVGHSFVFG GDYPKTPKAS AALLGADLIV
KEGRWQLDRI FTAESWNPKL KGPLDQPGLK LAQGQYLVGV NGKELTSADN PYKFLDGTVD
QQTVLHINDK PSFSEAWQIT VKPTGNETAL RQRAWVEDNR RLVDKLSDGK LAYVWVPNTS
SPGFVSFNRY FFAQQDKLGA VIDERFNGGG LLDDYMVDLM NRKLRAALTN EVPNGKPLLL
PAGIKGPKVL LINELAGSGG DYFPWAFRQQ KVGKLIGART WGGLVKSSVH YALVDGGALT
APDNAVFDPV NNKWVGENIG IAPDIEVYQD AQSLAKGDDP QLLTGVKELM KQLKQIETKQ
VTPPKYSTPA IQN
//
