ID A0A0M3Q9A7_9CORY Unreviewed; 430 AA.
AC A0A0M3Q9A7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|PROSITE:PS50106};
GN ORFNames=CDES_04390 {ECO:0000313|EMBL:ALC05323.1};
OS Corynebacterium deserti GIMN1.010.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=931089 {ECO:0000313|EMBL:ALC05323.1, ECO:0000313|Proteomes:UP000068067};
RN [1] {ECO:0000313|EMBL:ALC05323.1, ECO:0000313|Proteomes:UP000068067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMN1.010 {ECO:0000313|EMBL:ALC05323.1,
RC ECO:0000313|Proteomes:UP000068067};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium deserti GIMN1.010 (=DSM
RT 45689), isolated from desert sand in western China.";
RL Submitted (AUG-2014) 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; CP009220; ALC05323.1; -; Genomic_DNA.
DR RefSeq; WP_053544416.1; NZ_CP009220.1.
DR AlphaFoldDB; A0A0M3Q9A7; -.
DR STRING; 931089.CDES_04390; -.
DR KEGG; cdx:CDES_04390; -.
DR PATRIC; fig|931089.4.peg.887; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000068067; Chromosome.
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:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..416
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 43680 MW; A6FD5D3986B2525B CRC64;
MTNQFPTHNG DNADRSTGSS ETNSFDQVRS SYPQWGSTNS QNPHSNPYPQ TEQSPTWTSW
DQEPISSDVP KTKEKRKIGL GAALALMLVG SVASGSVVGI AASQMGSDSS TPVSALDQPS
VQRTTNAEPG SAEQVANAVL PSVVSIQAIS RSSASEGSGS IISSDGYVMT NNHVVSSVAE
SGVLQVTFSD GSTGEADFIA GDPSTDIAVI KIRNVQDLPV ISFGDSDSLA VGQEVMAVGS
PLGLSSTVTT GIVSALNRPV RASGDGGESS LIDAIQTDAA INPGNSGGPL VDMEGNLIGM
NSVIASISST SDTAGSIGLG FAIPSNFAKR VADQLISTGT VTQPMLGVQV GQDNSVSGAV
IASVQDGGPG AAAGLQPGDV VTKLNDRVID GADSLIAAVR SHDFGETVTL TITQPDTGQS
REVEVTLTSE
//
