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Database: UniProt
Entry: A0A101IDJ8_9BACT
LinkDB: A0A101IDJ8_9BACT
Original site: A0A101IDJ8_9BACT 
ID   A0A101IDJ8_9BACT        Unreviewed;       462 AA.
AC   A0A101IDJ8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Protease Do {ECO:0000313|EMBL:KUK93320.1};
GN   ORFNames=XE05_1076 {ECO:0000313|EMBL:KUK93320.1};
OS   Thermotogales bacterium 46_20.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales.
OX   NCBI_TaxID=1635293 {ECO:0000313|EMBL:KUK93320.1, ECO:0000313|Proteomes:UP000054930};
RN   [1] {ECO:0000313|Proteomes:UP000054930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(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:KUK93320.1}.
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DR   EMBL; LGGZ01000058; KUK93320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101IDJ8; -.
DR   PATRIC; fig|1635293.3.peg.127; -.
DR   Proteomes; UP000054930; 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; 2.40.10.10; 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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF13180; PDZ_2; 1.
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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KUK93320.1}.
FT   DOMAIN          244..333
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   462 AA;  49683 MW;  32AD743101B19AE4 CRC64;
     MKRILVSVVV VVLALTTFAI VNPDYENPIV NVVEVAAPAV VRVEVQVRDS FGGLDPFLDE
     FFRRFFGDIP PREGIGSGFI FDEEGYIMTN DHVVQNATRI QVTLLDGSTY PAEYIGGDRE
     LDLAVIKINA EDKKLPTIKI GSSSMLRIGE WAIAIGNPLG FQQTVTVGVV SAVERQIPKP
     DGSGYYSNLI QTDAAINPGN SGGPLLNIHG EVIGINTALV APQVGTALGF AIPIDVAMRF
     VDALIESGVA EKAFLGVYHR TVNENLVKSL NLQTNTGALI TDVVPGGPAD RAGIRPLDVV
     KKVDNQDITS AESLGAAIRN YPPGATVTIT VNRMGEVLQI EVILGHEREL LSSEQPPEET
     LADDKLGLVV AALTAEDIER LGIKREIDGV IVKEVKSGKP ASIVGIRADD IITKVSIMGE
     FFSVKSLEDY EFAVGSIMKG DHVSLFVARE SVTFIASFEY QE
//
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