ID C1D0U5_DEIDV Unreviewed; 417 AA.
AC C1D0U5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative trypsin-like serine protease {ECO:0000313|EMBL:ACO45469.1};
GN OrderedLocusNames=Deide_06250 {ECO:0000313|EMBL:ACO45469.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45469.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO45469.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP001114; ACO45469.1; -; Genomic_DNA.
DR RefSeq; WP_012692592.1; NC_012526.1.
DR AlphaFoldDB; C1D0U5; -.
DR STRING; 546414.Deide_06250; -.
DR PaxDb; 546414-Deide_06250; -.
DR KEGG; ddr:Deide_06250; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_2_0; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000002208; Chromosome.
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; 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 Hydrolase {ECO:0000313|EMBL:ACO45469.1};
KW Protease {ECO:0000313|EMBL:ACO45469.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 300..402
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 417 AA; 43266 MW; 3C79B779D2988CD7 CRC64;
MKRPLFATTL VLVGLGLGAT LLRDQVPPGT AQAPAVPQAE RSARLQNEQN TMDIVRRYEP
GLVFISTEQQ VVRQDPLGWM FGGGQETQVQ QGVGSGFFVN KAGDILTNYH VIAAESPTGA
ADRITIRLMG REESITARVI GLAPQYDLAL IRAEKLDPKL ITPIPLGNSD TLAVGQKAVA
MGAPFGLDFS VTEGIVSNAA RTIPIGFSAS GEGIMQRAIQ TDAAINPGNS GGPLLDSSGK
VIGINTQIIS PGVQAGGVGQ NAGIGFAIPV NAARNLLPRL QEARGGVVSA PRLGLAAGLV
VQSARGTVPA GLSLLSSEAK QQLKLPETGL VIGEVVPGSP AARAGLRGAQ QEQRFPGGKI
ALGSDVIVKA DGRAVDALED LQAALLNKRE GDQVTLQVVR GGERREVKVT LDASAFK
//
