ID A9A5N7_NITMS Unreviewed; 374 AA.
AC A9A5N7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:ABX13042.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ABX13042.1};
GN OrderedLocusNames=Nmar_1146 {ECO:0000313|EMBL:ABX13042.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX13042.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX13042.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX13042.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX13042.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A5N7; -.
DR STRING; 436308.Nmar_1146; -.
DR EnsemblBacteria; ABX13042; ABX13042; Nmar_1146.
DR KEGG; nmr:Nmar_1146; -.
DR eggNOG; arCOG02833; Archaea.
DR HOGENOM; CLU_020120_2_0_2; -.
DR InParanoid; A9A5N7; -.
DR PhylomeDB; A9A5N7; -.
DR Proteomes; UP000000792; 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:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABX13042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000792}.
FT DOMAIN 261..359
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 374 AA; 39470 MW; 07E4C9BBB762B2DF CRC64;
MFRNNSKILL GGVVFSVVLM LGLSVAFLSP VLAQDNSYSS ENLQSNVESS SDLSLVEIFE
RSEFGVVSIA VTKTSPHGDA SGVGSGFIFD KEGHIITNNH VVRDSKKIDV TFTDGTSYRA
KVVGTDPYAD IAVLKIDVNS EKLYPLPIGD SSNLKVGEQI TAIGNPFGLS GSMTSGIVSQ
LGRLLPTGVG FSIPDVIQTD TAINPGNSGG PLLNMKGEVV GVNTAIYSSD GSFSGVGFSI
PSNVILKIVP VLITDGEFHH PWVGISSANI TPDLAELLNL EDAKGVLVMT VVKDSPANKA
GLRGSSETAV YDEIEYTIGG DIILSIDGKE VRKIDDLLTH LQREKNVGDT LDLGIIRDGK
AINVVLTLEP RPGS
//