ID A0A0C1R0Q1_9CYAN Unreviewed; 1098 AA.
AC A0A0C1R0Q1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=DA73_0234390 {ECO:0000313|EMBL:KIE09423.1}, DA73_0400004520
GN {ECO:0000313|EMBL:KAF3884796.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE09423.1};
RN [1] {ECO:0000313|EMBL:KIE09423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE09423.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3884796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3884796.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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:KIE09423.1}.
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DR EMBL; JHEG04000001; KAF3884796.1; -; Genomic_DNA.
DR EMBL; JHEG02000058; KIE09423.1; -; Genomic_DNA.
DR RefSeq; WP_050046431.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1R0Q1; -.
DR STRING; 1479485.DA73_0234390; -.
DR OrthoDB; 499686at2; -.
DR Proteomes; UP000029738; 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; IPR024977; Apc4-like_WD40_dom.
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; PF12894; ANAPC4_WD40; 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.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000029738};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 863..1053
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 513..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 751
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 984
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1042
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 985
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1098 AA; 125105 MW; C25BEE8FF5113EB9 CRC64;
MNKQSGYYRF PTIHGINVVF ACEDDLWSVP LQGGYAVRLT SNLGEVSHPF LSPDGTSLAF
VGREEGHSEV YVMPSDGGIA KRLTFLGAAT AVVGWSLDGK FILFSSNAAQ PFRRIHNLYR
IPPEGGTPER LPVGLAHHIS YGANGGAVLG KNTSDIAYWK RYRGGRTGVL WIDPSGTGTF
QKLINLPGNM SVPMWVGERI YFISDHEGIG NLYSCTLNGE DLQRHTYSRE YYVRNATTDG
KRIVYHAGAE LFCFDPTLEE NYQIEVDFHS PQIQRHRKFV DAANYLEEYN LHPEGHSTLI
TCRGKSFWFG NWEGAVNQIG LPDGVRYRLT RWLNDKKRFV TISDSGGVEA IEIHSTNLNA
QPERLNGVDL GQAVAIDVSP VEDLVVLSNH RLELILVNLN TQESRIIDRS NHNRIAGLCW
SPDGKWIAYS FSIKPKISVI KLYSVEDGTT HCLTEPVFWD FSPSFDPEGK FLYFLSYREF
NPVYDRLYFD LGFPRAVRPF LISLKKDTPS PFVPVPKQLT KQSQNSTEKS SGENGDREEN
GEAKNNLASE NKKTPKFEID FDGITHRIVA FPVPEGNYKK IWGLKGKVLF SSFPIQGSLD
NDEGWFHQKE EKASLLVYDF DKQKQETVAK EISSFNVARD KETIIYRSKN RLRVCTANPQ
TNHKLEDEPG RKTGWLDLKR VRISVVPTQE FQQMMREAWR LQKEHFWVEN MSGVDWERVW
LRYRPLLDKV STRSEFSDLI WEMQGELGTS HAYEMGGDYR KSPVYRLGFL GADFSYDTDA
DAYRVERIVR GDSWNDKADS PLNRLGANVR VGDLLLAVNG QRVSRDREAQ AVPSYRPLQE
MLVHQAECEV SLTFADSSSP EEYRTITVKT LKDESKARYR EWVEHNRQIV HEKTNHQVGY
VHIPDMGPTG YAEFHRYYSM EAQYEGLIVD VRYNSGGHVS QLLLEKLSRQ RIGYKVPRWN
QPQPYPHDSV AGPIVAIANE YCGSDGDIFS HSFKLMKLGT LVGKRTWGGV IGIRSRHFLV
DGSILTQPEN SSWFADVGWK VENYGTDPDI EVEMTPQDWV RGKDSQLERA LELILEQLVQ
NPVQLPNFGD RPQLRLPD
//
