ID   E1GWT6_9BACT            Unreviewed;       489 AA.
AC   E1GWT6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Peptidase Do {ECO:0000313|EMBL:EFN90873.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:EFN90873.1};
GN   ORFNames=HMPREF9018_0393 {ECO:0000313|EMBL:EFN90873.1};
OS   Prevotella amnii CRIS 21A-A.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=679191 {ECO:0000313|EMBL:EFN90873.1, ECO:0000313|Proteomes:UP000016016};
RN   [1] {ECO:0000313|EMBL:EFN90873.1, ECO:0000313|Proteomes:UP000016016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIS 21A-A {ECO:0000313|EMBL:EFN90873.1,
RC   ECO:0000313|Proteomes:UP000016016};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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:EFN90873.1}.
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DR   EMBL; ADFQ01000079; EFN90873.1; -; Genomic_DNA.
DR   RefSeq; WP_008449818.1; NZ_ADFQ01000079.1.
DR   AlphaFoldDB; E1GWT6; -.
DR   MEROPS; S01.453; -.
DR   eggNOG; COG0265; Bacteria.
DR   Proteomes; UP000016016; 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; -; 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; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
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, ECO:0000313|EMBL:EFN90873.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..489
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003146228"
FT   DOMAIN          302..371
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   489 AA;  52339 MW;  FFF5225B5B016920 CRC64;
     MKNLSKLLVG ASCFSALALS TGAFIKVCAA PTTVAAYGQP VDLTYASEKA LPAVVHIKYV
     QNSKTKTVEV DEDPFGGFFD PFGFFDQRQG DGNRRRQQIQ TPKKEATGSG VIISSDGYIV
     TNNHVVEGAD ELTVTLNDNR EFSAKIVGTD KQTDLALLKV NAKNLPVLPI GDSEKLKVGE
     WVIAVGNPYN LSSTVTAGIV SAKARGLGAT QGGIESFIQT DAAINPGNSG GALVNTKGEL
     VGINAMLYSR TGSYSGYGFA IPTSIMIKVV DDIKKYGSVQ RVMLGIQGGD VLDYINAQKD
     DGKTVDLGTN EGVYVDKITN DDGNGAAAGL QKGDVITQFD GTKVTKMSEL QQAINAKRPG
     DKVYITYMRN KKVIKKLITL KNAQGTTKLL EQADIDVLGG QFRPVSKSMK QQLGINYGLE
     VIKVNNGALK KAGIPRDYII QNVNDTPVKT IDDLQSIVKK ASTSKYPVLY IQGIYPTGKK
     GYFAVPLSE
//