ID A0A1G2VNH3_9BACT Unreviewed; 401 AA.
AC A0A1G2VNH3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=A3I22_02020 {ECO:0000313|EMBL:OHB23181.1};
OS Parcubacteria group bacterium RIFCSPLOWO2_02_FULL_40_12.
OC Bacteria.
OX NCBI_TaxID=1817744 {ECO:0000313|EMBL:OHB23181.1, ECO:0000313|Proteomes:UP000177804};
RN [1] {ECO:0000313|EMBL:OHB23181.1, ECO:0000313|Proteomes:UP000177804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHB23181.1}.
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; MHXI01000012; OHB23181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2VNH3; -.
DR Proteomes; UP000177804; 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; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 100..168
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 401 AA; 44726 MW; 530185E516FF7F69 CRC64;
MKYRILIPVI LIFLVFGFLG GMEFQKFQEP SGGLRELINR DLGQPEAVDF SLFWDAWNLV
HERYVGRSEL DTRKMVFGAI EGMVDSIGDP FTVFLKAEES KRLQEDISGE FAGIGIEIGL
RDRVLTVISP LDDTPAAKAG IVAGDRILSI NGDLTGDITI DEAVSKIRGR RGSKVVLTIS
RDKDGEEETK DFELIRDKIK VPTVKWTKIE PNIGHIRLLS FNQIAKDEFD KALGELKKQD
VDKKLILDLR NNPGGLLNLA IDISSYFLEP GRVVVIEDFG DNLREELKSK PNGFLKDTKV
VILINKGSAS ASEIVAGALH DNKEVKLIGE TTFGKGSVQQ VEDLRFKTAL KVTVAKWLTP
KGRSISDEGI EPDIKVERTE EDIKNDRDPQ LEKAIEVIKN L
//
