ID C6RB86_9CORY Unreviewed; 488 AA.
AC C6RB86;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:EET76862.1};
GN ORFNames=CORTU0001_0331 {ECO:0000313|EMBL:EET76862.1};
OS Corynebacterium tuberculostearicum SK141.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=553206 {ECO:0000313|EMBL:EET76862.1, ECO:0000313|Proteomes:UP000004384};
RN [1] {ECO:0000313|EMBL:EET76862.1, ECO:0000313|Proteomes:UP000004384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK141 {ECO:0000313|EMBL:EET76862.1,
RC ECO:0000313|Proteomes:UP000004384};
RA Dodson R., Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA Sutton G.G., Strausberg R.L., Nelson K.E.;
RL Submitted (JUN-2009) 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:EET76862.1}.
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DR EMBL; ACVP01000025; EET76862.1; -; Genomic_DNA.
DR RefSeq; WP_005329141.1; NZ_ACVP01000025.1.
DR AlphaFoldDB; C6RB86; -.
DR MEROPS; S01.494; -.
DR Proteomes; UP000004384; 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: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 129..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 393..474
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 49218 MW; 7F77FF2769BE49DD CRC64;
MNMRNDDYRG FDGNSPEGAS QEGPGRAEPV QGGPNFGETG QPNAGAGNAG PYSDSTGPYS
GAGAQAYETG SYSQGWNQPR GGAQGDDPRT LGSLGPYPNG PQTQSFSGQG QEGPMVTPLP
PQPEQKKKIG LGAATALAAV AAIAAGSIAG AVVGMSSGGG NNDTSVVNEA LKAEPANNST
GKEPEQGSVE EVASKVLPAV VSIQTMTRTG GAEGSGSVIS PDGYVLTNHH VVAGAEHGGM
MQVTMNDGSK HEADVVASDA NTDVAIVKIK DVKDLPFLQF GDSDSVAVGQ EVVAVGSPLG
LNATVTSGIV SAKNRPVRAS QEGGESSLID AIQTDAAVNP GNSGGPLVDR DGNIVGMNSM
IASLSNDSSG EGGSIGLGFA IPSNFAKRMA DELINDGKVS HPTLGVKVLA RDDGNGARIA
EVEPGGPADK AGLKDGDIVT RVNDRLIENA DALIAAARSQ DFGATVTLEV TREDSDDSRQ
VEVTLSGE
//
