ID   A0A0K1FD90_9MICO        Unreviewed;       474 AA.
AC   A0A0K1FD90;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN   ORFNames=ADJ73_00930 {ECO:0000313|EMBL:AKT52488.1};
OS   Arsenicicoccus sp. oral taxon 190.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Arsenicicoccus.
OX   NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT52488.1, ECO:0000313|Proteomes:UP000065578};
RN   [1] {ECO:0000313|Proteomes:UP000065578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; CP012070; AKT52488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K1FD90; -.
DR   STRING; 1658671.ADJ73_00930; -.
DR   KEGG; ars:ADJ73_00930; -.
DR   PATRIC; fig|1658671.3.peg.186; -.
DR   Proteomes; UP000065578; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
FT   DOMAIN          372..459
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  46702 MW;  75A555CE9C423836 CRC64;
     MEHTQEIRRD EPTREIPATN ASAPAAASGS SSGSPYAAPA AYPTAVGGGS GYGGGSGGSG
     EGSSGGGASP QGPQGGPAYG TATQPKARRA GWWQVPTAAL AAALLASGGT AALLHNSSDG
     TSTGVVNRSQ PSVSTARNTQ APLNQGNATA PDWKATASAV SPSVVSISVQ AGSGSGEGSG
     VILDTEGRIV TNNHVVGDAA QGGQIVVTLD DQRAYQAKIV GLDPSTDLAV IKLQGDVKDL
     KPIAVGNSDD LKVGAPVMAV GNPLGLSGTV TTGIVSALNR PVSTQPSQQQ DPSGGLFGSQ
     SSGNEVITNA IQTSAPINPG NSGGALVNAD GQLVGINSSI ASMGSGSSGQ SGSIGIGFAI
     PVNEVTSIAD QLIKNGKAEH AFMGVTSKPG MVKDGDGQRV AAVIGSVVSG SPADAAGLRA
     GDAIIAIDGE PVTGSTSLVA QVRERKVGDK ATMTYLRGGE RHDVQVTFAQ RSNQ
//