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Database: UniProt
Entry: A0A3M0CLD8_9PROT
LinkDB: A0A3M0CLD8_9PROT
Original site: A0A3M0CLD8_9PROT 
ID   A0A3M0CLD8_9PROT        Unreviewed;       458 AA.
AC   A0A3M0CLD8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:RMB07889.1};
GN   ORFNames=BXY39_1982 {ECO:0000313|EMBL:RMB07889.1};
OS   Eilatimonas milleporae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Eilatimonas.
OX   NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB07889.1, ECO:0000313|Proteomes:UP000271227};
RN   [1] {ECO:0000313|EMBL:RMB07889.1, ECO:0000313|Proteomes:UP000271227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB07889.1,
RC   ECO:0000313|Proteomes:UP000271227};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:RMB07889.1}.
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DR   EMBL; REFR01000011; RMB07889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0CLD8; -.
DR   InParanoid; A0A3M0CLD8; -.
DR   Proteomes; UP000271227; Unassembled WGS sequence.
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; 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; PF13180; PDZ_2; 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:RMB07889.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271227};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}.
FT   DOMAIN          92..158
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          375..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  50423 MW;  1018B0C2EA200CE5 CRC64;
     MRIWKTARQT ALGMAVTLAL TTGLSIPSGP PAAAAEDDLY EHLNLLMRVF QRVQSEYVDE
     VDDREVIEAA IQGMLRSLDP HSTYLNPDVY QQVRVQMEGE YGGLGIEVQM EDGLVKVVSP
     IDDTPAAEAG IEGGDLISHI DGQAVMGQTL TEAVKKMRGP VGSPINITVI REGESDPFDV
     EIVRDRILVR SVRHRVEAET IGYIRVTTFN MQSGEGVEQA VTALKEELGG RMDGVILDLR
     NNPGGLLDEA VRISDAFVER GEIVSTRGRR RQNNNRWFAT EGDMLDGLPM VVLVNAYSAS
     ASEIVAGALQ DQRRALVIGD QTFGKGTVQS EIRLGRAGDQ AIRLTTARYY TPSGRSIQER
     GIEPDIEVLF PRDKARKARK PRREKDLQNS IDNDTQDVDR AGEVDAMSEE EIAHIEALIE
     AQNDSDTAPA DIQLQYAIKL LKNISMLPIP QIAEARPE
//
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