ID A0A1Y4FD47_9FIRM Unreviewed; 432 AA.
AC A0A1Y4FD47;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=B5F53_03615 {ECO:0000313|EMBL:OUO80802.1};
OS Blautia sp. An249.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965603 {ECO:0000313|EMBL:OUO80802.1, ECO:0000313|Proteomes:UP000195974};
RN [1] {ECO:0000313|Proteomes:UP000195974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An249 {ECO:0000313|Proteomes:UP000195974};
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:OUO80802.1}.
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DR EMBL; NFJL01000002; OUO80802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4FD47; -.
DR OrthoDB; 1765023at2; -.
DR Proteomes; UP000195974; 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; IPR041489; PDZ_6.
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:SF125; PROTEASE DO-LIKE 14-RELATED; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF17820; PDZ_6; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000195974};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..414
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 72..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47777 MW; 98A86217CA73EB69 CRC64;
MQWKKKKEGN ENPENYYFIK ETIKKNGKKE RILKTGYLLG AGILFGLAAA AAFTLAAPQF
LQINEENAEK TQKVQIPVDS PQEQEETEEN AQVQEQEKPE AASSAQTEKN ALEQYESAYQ
EILTIAEKPQ KALVTVYGES EDENLLDKTR LTYGLASGII YMENENEYYI LTETKAVENA
ETLWVTFQDG KTVKGNPRKS DPRTGLAVMT VEKEKIPQDT RAGLYVASLG NSYSLFRGKG
VIALGNPSAY SDLVSYGVIT SVANEYQSID ARYNLLMTDI LGEEQSSGVL LNNQGEIIGL
IVQPQEGQNA SSSMVKALAV SQLKPLLEIL SNGETIMYLG IKGEEVDESS QSRGIPQGIY
VDSVERDSPA MKAGVQSGDI ICSLNGEPVA TMQEYSTYLQ KCKEGQKIKV VLKRRGTENY
EKMEYTMIVE GI
//