ID A0A2S0WD37_9CORY Unreviewed; 377 AA.
AC A0A2S0WD37;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=PDZ domain-containing protein {ECO:0000313|EMBL:PWB99520.1};
DE SubName: Full=Serine protease {ECO:0000313|EMBL:AWB83670.1};
GN ORFNames=C3E79_03525 {ECO:0000313|EMBL:AWB83670.1}, DF219_06270
GN {ECO:0000313|EMBL:PWB99520.1};
OS Corynebacterium liangguodongii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2079535 {ECO:0000313|EMBL:AWB83670.1, ECO:0000313|Proteomes:UP000244754};
RN [1] {ECO:0000313|EMBL:AWB83670.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2184 {ECO:0000313|EMBL:AWB83670.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWB99520.1, ECO:0000313|Proteomes:UP000245180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2185 {ECO:0000313|EMBL:PWB99520.1,
RC ECO:0000313|Proteomes:UP000245180};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP026948; AWB83670.1; -; Genomic_DNA.
DR EMBL; QEEY01000005; PWB99520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0WD37; -.
DR KEGG; clia:C3E79_03525; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000244754; Chromosome.
DR Proteomes; UP000245180; 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:AWB83670.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 282..363
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 37721 MW; 896D14859DA481A6 CRC64;
MPEQQPPFVT QVQSQPEKKR TGGVGAAVAL ALVGSLVVGG GAGYFAGNAA GGSNHGYVNE
ALDQKPASDP APAPEGSVEQ VAATVLPAVV SIAVNGAQGR AEGSGSIISS DGYVLTNHHV
IAEAEKGARV EVTLNDGSSH PASFVASDVN TDVGVLKIEG ASNLPVIRFG DSNELHVGQE
VVAIGSPLGF SATVTSGIVS ALNRPVRASQ GGGESSLMDG IQTDAAINPG NSGGPLVDMN
GNLVGMNSVI ASMSASPQGG AGSIGLGFAI PSNFAQRVAK QLIDTGEAKQ PMLGVQVSIA
DPTRGAVVAG VEPGSPADKA GLKVGDVVTR LNERPIDSAD ALIAATRSQD FGATVKLEVR
SRGNDQPRAV DVTLSSE
//
