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Database: UniProt
Entry: A0A2S8Y2H6_9PSED
LinkDB: A0A2S8Y2H6_9PSED
Original site: A0A2S8Y2H6_9PSED 
ID   A0A2S8Y2H6_9PSED        Unreviewed;       303 AA.
AC   A0A2S8Y2H6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:PRA51754.1};
GN   ORFNames=CQZ98_18440 {ECO:0000313|EMBL:PRA51754.1};
OS   Pseudomonas sp. MYb115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA51754.1, ECO:0000313|Proteomes:UP000239970};
RN   [1] {ECO:0000313|EMBL:PRA51754.1, ECO:0000313|Proteomes:UP000239970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb115 {ECO:0000313|EMBL:PRA51754.1,
RC   ECO:0000313|Proteomes:UP000239970};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRA51754.1}.
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DR   EMBL; PCQM01000014; PRA51754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8Y2H6; -.
DR   Proteomes; UP000239970; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 1.
DR   Gene3D; 1.10.287.4290; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:PRA51754.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:PRA51754.1};
KW   Transferase {ECO:0000313|EMBL:PRA51754.1}.
SQ   SEQUENCE   303 AA;  32779 MW;  EB9B7AE771B84D85 CRC64;
     MNESVRFEDK VVIVTGAGGG LGRAHALLFA KQGARVLVND LGGSTQGEGA NASAADRVVA
     EIREAGGTAV ANHDSVTDGE KIVQHALDAF GRIDVVVNNA GILRDKTFHK MDDSDWDLVY
     RVHVEGAYKV TRAAWPHMRE QNYGRVIFTA STSGIYGNFG QSNYGMAKLG LYGLTRTLAL
     EGRKNNILVN AIAPTGGTRM TEGLIPPQVF EQLKPELVSP LVVYLASENC QETSGLFEVG
     GGWMGKVRWE RSLGAGFDPR EGFSPEDVAA HWQQICDFEG AAHPKDNIEA LKEMMGNLQK
     YAL
//
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