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Database: UniProt
Entry: A0A0Q7ZFS6_9ACTN
LinkDB: A0A0Q7ZFS6_9ACTN
Original site: A0A0Q7ZFS6_9ACTN 
ID   A0A0Q7ZFS6_9ACTN        Unreviewed;       293 AA.
AC   A0A0Q7ZFS6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:KQZ70412.1};
GN   ORFNames=ASD66_12405 {ECO:0000313|EMBL:KQZ70412.1};
OS   Nocardioides sp. Root151.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ70412.1, ECO:0000313|Proteomes:UP000051274};
RN   [1] {ECO:0000313|EMBL:KQZ70412.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ70412.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ70412.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ70412.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KQZ70412.1}.
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DR   EMBL; LMGG01000004; KQZ70412.1; -; Genomic_DNA.
DR   RefSeq; WP_056891135.1; NZ_LMGG01000004.1.
DR   AlphaFoldDB; A0A0Q7ZFS6; -.
DR   Proteomes; UP000051274; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.200.40; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR   PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQZ70412.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051274};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..134
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   293 AA;  31448 MW;  C8C7BD5770049D0D CRC64;
     MSTPRREIAL LVNPTAGRGK GARYASLAAP RLRDAGFDVR LLQGTSAEEA EALARGAVSD
     GCHALVACGG DGLVHLAVQA LAGTDTPLGI IPAGTGNDVA RYLNISRTDP LAAADRVVAS
     RRRRMDLARC GDRWFVTVLA AGFDAIVNER ANDMTWPRGQ MRYNLATLAE LRTFRPLHYT
     LELDGETRTL DAMLVAVGNG PSFGGGLRIT EGALLDDGFL DVVIIKAMSR PELIRTYPKL
     FSGTHTTHPA YEHHRVRRVT VATPGIVGYA DGERFGALPL TIECPPLALE VLL
//
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