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Database: UniProt
Entry: J9SJ48_9ACTN
LinkDB: J9SJ48_9ACTN
Original site: J9SJ48_9ACTN 
ID   J9SJ48_9ACTN            Unreviewed;       499 AA.
AC   J9SJ48;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Eukaryotic diacylglycerol kinase-like sphingosine kinase {ECO:0000313|EMBL:AFR49684.1};
GN   ORFNames=KTR9_3049 {ECO:0000313|EMBL:AFR49684.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49684.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR49684.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR49684.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
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DR   EMBL; CP002907; AFR49684.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9SJ48; -.
DR   STRING; 337191.KTR9_3049; -.
DR   KEGG; gor:KTR9_3049; -.
DR   PATRIC; fig|337191.3.peg.3395; -.
DR   eggNOG; COG0671; Bacteria.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_5_0_11; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01610; PAP2_like; 1.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   PANTHER; PTHR14969:SF13; AT30094P; 1.
DR   PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AFR49684.1};
KW   Transferase {ECO:0000313|EMBL:AFR49684.1}.
FT   DOMAIN          208..331
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          89..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  52625 MW;  D6D2E47A7FCD46C6 CRC64;
     MHRLPPRSSG LSQITRGMGT LDAEIYDSIA RSPSPLLDVT MPALTRAADH SKLWMAVAAG
     LAVSGRPSLQ RGAARGMVSL AVTSLVTNQG AKRVRRRSRP AHGLIPVPRQ GSRRPTSNSL
     PSGHSASAAA FAVGVGVENP PAGLLLSALA GLVGLSRVAT GAHYPGDVVA GLGIGAAIAT
     IGARVIPPIT EPSLSLAAPS VVDVDRNPDG AGLVVVVNPG SADGRGRRVV ETIRGRLPAA
     EIVELDETDD MAAVFAEVAT RATILGVAGG DGTAACAAGP ALAADIPLAV FPAGTFNHFA
     RDIGCGTVDA TIEAIRAGSA SRVDAMWLND SRLILNTASI GAHPDFVRVR RRLQRRISRP
     LATAAAVLHV LRKDPHVRIE VEGRVLDASL FLVGNSIYQP TGFLPSRRVR LDDGLLDVRI
     LETSHRWATL RLLGSLAVGR LERSRLYHEM QVPEFRFTAV DGPVAVSHDG EVEDSYSHAD
     FRVDYRALKV FRPAARRRS
//
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