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Database: UniProt
Entry: A9A5N7_NITMS
LinkDB: A9A5N7_NITMS
Original site: A9A5N7_NITMS 
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).
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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
//
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