ID A0A1H3JPJ0_9FIRM Unreviewed; 565 AA.
AC A0A1H3JPJ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Serine protease Do {ECO:0000313|EMBL:SDY41821.1};
GN ORFNames=SAMN02910414_01521 {ECO:0000313|EMBL:SDY41821.1};
OS Lachnobacterium bovis DSM 14045.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnobacterium.
OX NCBI_TaxID=1122142 {ECO:0000313|EMBL:SDY41821.1, ECO:0000313|Proteomes:UP000183918};
RN [1] {ECO:0000313|EMBL:SDY41821.1, ECO:0000313|Proteomes:UP000183918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14045 {ECO:0000313|EMBL:SDY41821.1,
RC ECO:0000313|Proteomes:UP000183918};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNPG01000017; SDY41821.1; -; Genomic_DNA.
DR RefSeq; WP_074717674.1; NZ_FNPG01000017.1.
DR AlphaFoldDB; A0A1H3JPJ0; -.
DR STRING; 1122142.SAMN02910414_01521; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000183918; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDY41821.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDY41821.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183918};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 458..547
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 61677 MW; FD92C2F55120027C CRC64;
MDNNNNNSNN TFENGMNQNP NVNPYLNNRN MYQNNGGMNQ GQPMQQQPMN QQQMNQGHPT
QQQPMQQQQM KQGQPTQQQP MQQQQMKQGH PTQQQPMNQQ QMNQGYPTQQ QSMNQQQMNQ
GHPTQQQSMQ QQQMKQGHPA QQQLMNQQQM KQEQPTQQQQ LNQAQVVREK PKKKKGKKIA
AIIAVPITIG LITTGVLVGL DYTGFKFDSS SQNNSVKLST TSTKGKAKNL QDVSDVVDEV
MPSIVAITNL QEVQDDDDYY GYYSRRGSKQ QASAGSGIII KQNDTYIYIV TNNHVVADSK
SLKIKFCDKA VVKAEIQGQD ESNDLAVVRV KISDIKKSTY KKIKLAKLGD SKKLSVGEPT
IAIGNALGYG QSVTTGVVSA LGRSVQGKSE DGDKASASNL IQTDAAINPG NSGGALLNSK
GEVIGINSAK TAGQAIEGVG FAIPMEDVKP IVEDLISKEK IDESERGYLG INGNNVTEDY
SAMLDIPKGV YVTEVQPGSA AEAAGIQKDD VIVGVNGSSV STIQELQQKL SNCKVGDKVK
IKIARDDGTG YKETEVEVTL GAKNQ
//