ID   A0A0G0GNR2_9BACT        Unreviewed;       548 AA.
AC   A0A0G0GNR2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   SubName: Full=Protease Do {ECO:0000313|EMBL:KKQ32708.1};
GN   ORFNames=US49_C0006G0159 {ECO:0000313|EMBL:KKQ32708.1};
OS   candidate division TM6 bacterium GW2011_GWF2_37_49.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619083 {ECO:0000313|EMBL:KKQ32708.1, ECO:0000313|Proteomes:UP000033926};
RN   [1] {ECO:0000313|EMBL:KKQ32708.1, ECO:0000313|Proteomes:UP000033926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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:KKQ32708.1}.
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DR   EMBL; LBTE01000006; KKQ32708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0GNR2; -.
DR   Proteomes; UP000033926; 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; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.20.190.20; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR041517; DEGP_PDZ.
DR   InterPro; IPR046449; DEGP_PDZ_sf.
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; PTHR45980; -; 1.
DR   PANTHER; PTHR45980:SF9; PROTEASE DO-LIKE 10, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF17815; PDZ_3; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
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;
KW   Hydrolase {ECO:0000313|EMBL:KKQ32708.1};
KW   Protease {ECO:0000313|EMBL:KKQ32708.1}.
FT   DOMAIN          283..332
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   548 AA;  61313 MW;  64A6B01A8E0F05D3 CRC64;
     MIKKLLSTML LLSISGQLQC KRTKHTDDLI QQRVPTHETT PDLKKQSAPI AESVLDTKIK
     WPDICSKYKN SVVQIYSYVN VFNLSDPSKT GSEQYIVAGT GFFISDDGYL LTNFHVISEA
     PVVEVRFPAL GDQSFEVKIV GCFPEKDFAL LKIKDSSLQS LKDLLKVNNI TPLELGDSDK
     LKESQKVMCM GYPLGQRNLK ISLGNISGRE SMGEIGECAQ TTTPINHGNS GGPFLDENGK
     VVGIATLKVE NSDGIGYFIP INTVKTSLDT LFTKKIIKKV LLGVDLQPTT AETLKFLGNP
     TDGGVYVVEV ELKSLAEKAK IQKGDVIYEI DGFKIDRYGY INPSWRDAKI AVSDYISQLK
     IESTVSLTIY RDGEKLSLQI QLKNEDEFAV KEFHPWLQEA PDFERIGGIV VAQLTLNHLQ
     HFINEGHCKQ KMLKYTKIKH QQEPRVIVSC IYPGSVALDY QPQFFNPIIN MVNDIEVKTV
     QDFRDAVLAG NKKNPDYLTI ETEDGFFAAI PLKDLLDEEQ SISQTNYLQE SNLVKQLCEK
     YSTSSIES
//