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Database: UniProt
Entry: A0A0S8I7T9_9CHLR
LinkDB: A0A0S8I7T9_9CHLR
Original site: A0A0S8I7T9_9CHLR 
ID   A0A0S8I7T9_9CHLR        Unreviewed;       402 AA.
AC   A0A0S8I7T9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN   ORFNames=AMJ88_11780 {ECO:0000313|EMBL:KPK92090.1};
OS   Anaerolineae bacterium SM23_ 63.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK92090.1, ECO:0000313|Proteomes:UP000051685};
RN   [1] {ECO:0000313|EMBL:KPK92090.1, ECO:0000313|Proteomes:UP000051685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK92090.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK92090.1}.
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DR   EMBL; LJUS01000039; KPK92090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8I7T9; -.
DR   Proteomes; UP000051685; Unassembled WGS sequence.
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; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..402
FT                   /note="PDZ domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006648181"
FT   DOMAIN          281..362
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          26..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  42135 MW;  530D3FB300438B9D CRC64;
     MKSRFNTTVI VAVVLFVVTT SCSLSSAVSG NPTATSPPSP TTQQTRTPSQ PLAIPTTFGE
     QQILASDLAA LYQRVSPGVV TIWRFDTNGS PQDPNLPTGQ GSGFVIDYDG HIVTNQHVIN
     GADEIEVNFS SGLKAWAELI GSDTDSDLAV LKVDVLQEDL VPLPLADSDQ VRVGDFVVAI
     GNPFGLSGTM TIGIVSALDR TLASQNIAPG GGIFTSGDII QTDAAINPGN SGGPLINLRG
     EVIGVNQAIR TESFTLVGES VNSGVGFAIP VNTVQQVITS IIEYGRYRYP YLGIAMMGED
     LWNLKIIEAL GLPPDAAGVY LTDVTPGGPA EQAGLRGGNR RTVVGVNAGG DLIIALDGNP
     IRRNGDLLSY LINNTQVDQV VTLTILRDGE EIDISLTIGA RP
//
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