ID D0MJS5_RHOM4 Unreviewed; 535 AA.
AC D0MJS5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:ACY48733.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ACY48733.1};
GN OrderedLocusNames=Rmar_1850 {ECO:0000313|EMBL:ACY48733.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48733.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY48733.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
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DR EMBL; CP001807; ACY48733.1; -; Genomic_DNA.
DR RefSeq; WP_012844344.1; NC_013501.1.
DR AlphaFoldDB; D0MJS5; -.
DR STRING; 518766.Rmar_1850; -.
DR MEROPS; S01.453; -.
DR KEGG; rmr:Rmar_1850; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_10; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000002221; Chromosome.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
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; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000313|EMBL:ACY48733.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ACY48733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002221};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 301..392
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 535 AA; 58024 MW; 5C2A81D2BDB9A3DE CRC64;
MAEKGRSRVL LILGGIGLLL VGLLAGVLLM EWRFQQVQMA AAPARIVERV QLGGGERVGA
VTLPEGDGRR LALDPVVLNQ VFREVAARVT PAVVYIEVTA GSRSFSGDFF HRFDPNQERF
FREFTPRQSV GSGVIISPDG YLVTNYHVVE DAREIRVTLA DKRQFEARLI GFDRSTDLAV
LKIDPPEGET FPVIAFGNSD ELKVGEWVLA VGNPFRLTST VTAGIVSALG RQVNIIDDFF
RVEDFIQTDA AINPGNSGGA LVNLRGELVG INTAIATESG AYEGYGFAVP VNLVARVVED
LIAYGEVQRG YLGVSIQEID AQQARELGLP GVQGVLISEV RAGGAADQAG VRAGDVVLRV
NGRAVNAPNE LQSVVARYRP GDRLTLEIWR KGRRLQVQVE LMGRDAPAYR EWFSELTQEA
PPQMPELTPE APRGSVYNLE AWGLGLRDLT ASERTAFDVD GGVYVAYVAR GSVAEEAGLP
RDVVILQIEG IDVAALEDAL MLLGELSEAE TVLFRVKKRD GTIAFYEVPV PALSE
//
