ID   A0A1Q7SZJ1_9BACT        Unreviewed;       488 AA.
AC   A0A1Q7SZJ1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN   ORFNames=AUF67_07200 {ECO:0000313|EMBL:OLD81663.1};
OS   Acidobacteria bacterium 13_1_20CM_58_21.
OC   Bacteria; Acidobacteriota.
OX   NCBI_TaxID=1803438 {ECO:0000313|EMBL:OLD81663.1, ECO:0000313|Proteomes:UP000186215};
RN   [1] {ECO:0000313|EMBL:OLD81663.1, ECO:0000313|Proteomes:UP000186215}
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   -!- 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:OLD81663.1}.
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DR   EMBL; MNIJ01000106; OLD81663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7SZJ1; -.
DR   Proteomes; UP000186215; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 2.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF13180; PDZ_2; 2.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..488
FT                   /note="PDZ domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010341347"
FT   DOMAIN          266..363
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   488 AA;  51135 MW;  A851698C3671D988 CRC64;
     MSEFSSRPMI SPRLALRLFR ALSSALFLLV HLPAANGQAQ DHSTDALRKF NESVDALIKK
     VTPSVVQILV TGYGPLEEGE HGNTNTLIGR QRAIGSGFVI DPSGYIVTNA HVVKGAQRVQ
     VVLPSANADG SVDAALSTRT KVVPARIVGA SSEIDLAVIK VDAGTLPALP LASYRKLGQG
     EIVFAFGSPG GLRNTVTMGV VSAVARQTDL DSPMVYIQTD APINPGNSGG PLVTVNGEVA
     GVNTFILSQS GGNEGLGFAI PSGVVSVAFQ QLRKFGHLHR AEIGIGIQTI TPSMAEALML
     PRTYGVVVSD VLPGSPAEAA GVEIGDVLAS VDGKAADSLP LVAFHFYLLE TGDKVHLDVL
     RGKDRLVFNV SVMEPPRDMD QVTGLADPEK NLVPTLGILG VEIDKKIASM AADLRDPFGI
     IVAARSAGAG VEVPLNAGDV IRTLNGQPMT TLDRLRVALK ALPPGAPVAL QIQRDQKLLF
     VSFTLDQP
//