ID A0A1Q7HRH2_9CHLR Unreviewed; 441 AA.
AC A0A1Q7HRH2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=AUH85_12900 {ECO:0000313|EMBL:OLC54014.1};
OS Chloroflexi bacterium 13_1_40CM_4_68_4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC54014.1, ECO:0000313|Proteomes:UP000185706};
RN [1] {ECO:0000313|EMBL:OLC54014.1, ECO:0000313|Proteomes:UP000185706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
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:OLC54014.1}.
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DR EMBL; MNFM01000135; OLC54014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7HRH2; -.
DR Proteomes; UP000185706; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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 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|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 102..180
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 441 AA; 46592 MW; 5D8C34476DF6D032 CRC64;
MRHPLRFAAG ALLLALIVVA SATGGFLIGR DNPGLLGPFR SANADPSLDL TAFWEAWNYL
RQEYYQPLDR QTLVRGATRG LLAATGDDNT GYLAPQDFQL FSSQLQGSFE GIGAEVDLRD
GQLLIISPLP DSPAEKAGVR AGDQILKIDG EDAGKFTLLD AISKVRGPKG TTVTLTIRRP
ADPSSLDATS RQRLLDTLPQ LEAALAANDA ERAKSAAAPV GDALKALAGA TVELEMKIVR
DVIAQPKVET RLLDNGVGYI KLSQFSRGVS TEFDTALAST LGAGARSLVL DLRGDSGGFV
NEAVAIASQF LREGTVVFTE QRADGKRDYT ATAGGRALAT PLVLLVDRGT ASASEILSAA
LHDNGRAKLV GEKTYGKGTE QLQQTLDDGG GARITVARWL TPKGVWVHHQ GIEPDVAVSD
PDPAPPDLVL QKAVETLGQT P
//
