ID A0A498CNG9_9FIRM Unreviewed; 604 AA.
AC A0A498CNG9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=PDZ domain-containing protein {ECO:0000313|EMBL:RLL09058.1};
GN ORFNames=D4A47_10815 {ECO:0000313|EMBL:RLL09058.1};
OS Anaerotruncus massiliensis (ex Liu et al. 2021).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=2321404 {ECO:0000313|EMBL:RLL09058.1, ECO:0000313|Proteomes:UP000276301};
RN [1] {ECO:0000313|EMBL:RLL09058.1, ECO:0000313|Proteomes:UP000276301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22A2-44 {ECO:0000313|EMBL:RLL09058.1,
RC ECO:0000313|Proteomes:UP000276301};
RA Wang Y.-J.;
RT "Anaerotruncus faecis sp. nov., isolated from human feces.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
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:RLL09058.1}.
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DR EMBL; RCHT01000024; RLL09058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498CNG9; -.
DR Proteomes; UP000276301; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000276301};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..178
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 412..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 63994 MW; 85811388AACED766 CRC64;
MSKKISLGAA IAFTVIVITA TITMTWLFAR RSFDETAYNL SEREAMYSKL AEVDDYVRQN
YTGAIGEGEL VNQLVTGYLN GTGDAYARYY DAAAYARLKQ SYNDQRVQIG IVPRMDESGY
IVVDEVYPDS PAQAAGLQEG DLIVRIDETD ITAENYSEAV SMLYGAAGTK MNIVVRRGVE
DSTLPDMTRR FVEVPSVYSS MLENQIGLVV IKDFADNTPD QFTKQVDRLI DEGAQGLVFD
VRGVSITSSG TSALDSVSEA LDKLLPSGVL ASTVDKTGRV ENTKISDARE VTLPMAVLIN
EKTSGESELF AAVIRDYNKG KLIGQKTAGK GTMQRIFPLT DGSAVEITTA VYNPPTSPSF
DGEGVRPDFE VKMNDDSMPG NLLTDPQLQK AVDSIIATIR MNMTVIDLEP EESGGAASAT
SLPDAAYASS SEEEPSAAES SETASSGEES SDMEEPRDVS SEASSEEEEA SSSEPEPEAE
PEPAREPLDL TEFSAAIDLL AGLTFEVPAP PAPPVQSEAP AASEPVVSEP PASQPAESQP
AESGAPAESQ AESQPPAESS GTESGPEGSS SEGTATSGEE ETESSSEASS APPARLGAFS
SGRR
//
