ID A0A1Y3YLE3_9FIRM Unreviewed; 523 AA.
AC A0A1Y3YLE3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:OUN95090.1};
GN ORFNames=B5G00_00120 {ECO:0000313|EMBL:OUN95090.1};
OS Blautia sp. An46.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965636 {ECO:0000313|EMBL:OUN95090.1, ECO:0000313|Proteomes:UP000196301};
RN [1] {ECO:0000313|Proteomes:UP000196301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An46 {ECO:0000313|Proteomes:UP000196301};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUN95090.1}.
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DR EMBL; NFIF01000001; OUN95090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3YLE3; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000196301; 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; 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; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OUN95090.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196301};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..493
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 54975 MW; FE50410C31C6470F CRC64;
MRNSQESETD SQQQNMQEPQ EAPSEENPYY ARTYRKASEP RTENRSTEET ADNTAREPAG
EKKNSYSSYQ FATPVPPEKK AKKKKNTSGA ARKLGFAAAC AAVFGLVAGV VFQGVNYVGD
QLTPEENTQI AQAQLTNSST ASSDSSSQGS VAQVAANVMP SVVAITSISV QEIPNYYGYF
FNYGGGTQEQ ETESSGSGII VGQNDTELLI ATNNHVVEGA TSLSVCFTNQ DGTAASSQSD
VENTSSDSGS STDLEGGTAV TAQVKGTDVD NDLAVVSVNL SDIPEDVLNE IAIANLGSSD
DLVVGEQVVA IGNALGYGQS VTSGYVSALN KQVSSDDVDG TFIQTDAAIN PGNSGGALLN
MNGEVVGINS SKIASSSVEG MGFAIPISRA EPILDELMNR ETRQKVEDES QAAYLGITCI
NVTSNTEEMY NMPVGVFVSS VEEGGPAAEA GIQQGDIIQK FDGTTVQTYD NLTNQLSYYQ
AGEQVEIVIS RAEGGQYQEQ TVTVTLGARS DAQSSAQDSQ NGQ
//
