ID A0A1Z4RSJ8_9CHRO Unreviewed; 431 AA.
AC A0A1Z4RSJ8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:BAZ45436.1};
GN ORFNames=NIES4102_24590 {ECO:0000313|EMBL:BAZ45436.1};
OS Chondrocystis sp. NIES-4102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Chondrocystis.
OX NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ45436.1, ECO:0000313|Proteomes:UP000217698};
RN [1] {ECO:0000313|EMBL:BAZ45436.1, ECO:0000313|Proteomes:UP000217698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ45436.1,
RC ECO:0000313|Proteomes:UP000217698};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; AP018281; BAZ45436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RSJ8; -.
DR KEGG; chon:NIES4102_24590; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000217698; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:BAZ45436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217698};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013142681"
FT DOMAIN 110..178
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 431 AA; 47266 MW; AE67BF905A299F4E CRC64;
MASKKKGLVL GATAIALSTV AVTGAGIHLS QSQALIQNGP KETVDEVWQI INYQYVDDDF
NHHDWSKIRQ KYVKDANYSN KEDAYKAIRQ MLNQLGDPYT RFMNPEEFQN MRIDTSGELT
GVGIQIAKDE KTDRLIVIAP IEDSPAFEAG ILAQDIILKI DNQDTKGMDV NDAVKLIRGE
RGTQVNLTIK RNEDQQEYTI VREQIAIHPV RAFVRDTNIG KVGYIRLTTF NEHAAEDMKK
AIKDQEKANV VGYVLDLRSN PGGLLYSSIN IARMWLDEGV IVSTVDRQGI SDRSIAKNKA
LTDKPLVVLV NEGSASASEI LSGALQDNKR ATLLGTKTFG KGLVQSVRPL RDGSGLAVTI
AKYLTPSGKD INKAGIAPDI VIKLSEEQLK ELYGGDSSAL GTSKDPQFTK AIDVLNENIQ
AQQGSEPQAA K
//
