ID A0A1J4NQY5_9ACTN Unreviewed; 1064 AA.
AC A0A1J4NQY5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=WN71_027310 {ECO:0000313|EMBL:OIJ64739.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ64739.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ64739.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
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}.
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:OIJ64739.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAVA02000072; OIJ64739.1; -; Genomic_DNA.
DR RefSeq; WP_046581825.1; NZ_LAVA02000072.1.
DR AlphaFoldDB; A0A1J4NQY5; -.
DR STRING; 1428628.WN71_027310; -.
DR OrthoDB; 9758793at2; -.
DR Proteomes; UP000034196; 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; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 2.
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:UP000034196};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 821..1026
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 514..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 737
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 957
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1015
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 958
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1064 AA; 115648 MW; 3E01A7C742D65100 CRC64;
MPPEQPAYLR FPHLRGDTVV FTAEDDVWLA PLDGGRAWRV SADNMPVTHP RLSPDGTLVA
WTSTRDGAPE VHLASVAGGP SKRLTYWGSS RTQVRGWTPD GQILAVSAAG QASLRRSWAR
AVPLDGGPAT TLPYGPVGDV AFGPHTVLLS APMGREAAWW KRYRGGTAGK LWIDRDEPGE
FVRLHEDLDG NLEQPLWVGD RVAFLSDHEG TGALYSSLAD GSDLRRHTPL DAFYARHAAT
DGTRVVYASA GELWLLDDLD GAEPRRLDIR LGGPRVDQQP YPVDAARWFG SASPDHTGRG
SAVCVRGGVH WVTHRSGPAR ALAVRPGVRA RLPRAFRADG EEWVVWVTDA EGDDALEFAP
ATGLAPGATP RRLAAGRLGR VLGLAMAPDG SRAAVAAHDG RLLLVERETG EVREVDRSED
GDVTGLVFSP DSAWLAWSHP GPRPLRQLRL ANTTDLSVTE ATPLRFQDYA PAFTADGKHL
AFLSTRSFDP VYDEHVFDLA FVVGDRPHLI TLAATTPSPF GPQRHGRPFE APDKDETPDS
EGTPATRVDL EGLADRIVPF PVEAGRYSGL RAAKDGVLWL RHPVHGVLGA SRARPDDPDP
RSELQRYDLV QQRLEHLADD ADHFRVSGDG KRVLLWSDGR LRVVPSDRRA SSDEDGDTAF
TIDLGRVRQS VDPAAEWRQM YDENGRIMRD NFWRADLSGV DWDGVLDRYR PVLDRVATHD
DLVDLLWEVH GELGTSHAYV TPRGSGGGPR QGLLGADLSR HDDGSWRIDR VLPAETSDPD
ARSPLAAPGV AVRAGDAILA VAGQGVDPVT GPGPLLVGTA GKPVELTVSP SGGGDPRHAV
VVPIADEEPL RYHAWVADRR AYVHERSGGR LGYLHVPDMQ APGWAQIHRD LRVEVAREGL
VVDVRENRGG HTSQLVVEKL ARRIVGWANP RGMRPYSYPM DAPRGPVVAV ANEFSGSDGD
IVNAAIRALG IGPVVGTRTW GGVIGIDSRY RLVDGTLVTQ PKYAFWLEGY GWDVENHGVD
PDIEVLHRPQ DWAAGRDPQL DEAIRLALET LETSPAKTPP SPPS
//
