ID I4CAU9_DESTA Unreviewed; 335 AA.
AC I4CAU9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:AFM26690.1};
GN OrderedLocusNames=Desti_4051 {ECO:0000313|EMBL:AFM26690.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM26690.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003360; AFM26690.1; -; Genomic_DNA.
DR RefSeq; WP_014811816.1; NC_018025.1.
DR AlphaFoldDB; I4CAU9; -.
DR STRING; 706587.Desti_4051; -.
DR KEGG; dti:Desti_4051; -.
DR PATRIC; fig|706587.4.peg.4592; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_828277_0_0_7; -.
DR OrthoDB; 8581982at2; -.
DR Proteomes; UP000006055; 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:UniProtKB-KW.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR025241; DUF4190.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR Pfam; PF13828; DUF4190; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AFM26690.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AFM26690.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..89
FT /note="DUF4190"
FT /evidence="ECO:0000259|Pfam:PF13828"
SQ SEQUENCE 335 AA; 36650 MW; CFCDE9A8E2844B5A CRC64;
MDDYTSETLP GKGTDSVRNL ATRLHPFALW SLILALLGIP LMGLITGVIA VILAGIAITQ
IAANPYLHGR KLAIAGLAIG LADVVLWVFL LGFAFPRSVH TAYKSVEQFT FPSANFLERA
PESIRRAMEL NVFFVVERRG WPAFLHNESL TGSGIILGQN EGEYVILTNR HVVDPAFNGD
QTSKLDQRAF ITIYFHDGTN KKGYVWWTAP EGLDLALVAT GPNPHGIPFP ELQSTPDFEI
GDRVFTVGNP HELSWSYAEG AISGIRESSK GSIQLKIIQT QTPINQGNSG GGLYLEDGTL
IGIVSWTKDK SQAEGISFAI TYEDFLAVYN REKAE
//