ID A0A0A2G9L5_9PORP Unreviewed; 305 AA.
AC A0A0A2G9L5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Lipid kinase {ECO:0000313|EMBL:KGN99090.1};
GN ORFNames=HQ36_01075 {ECO:0000313|EMBL:KGN99090.1};
OS Porphyromonas gingivicanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=266762 {ECO:0000313|EMBL:KGN99090.1, ECO:0000313|Proteomes:UP000030134};
RN [1] {ECO:0000313|EMBL:KGN99090.1, ECO:0000313|Proteomes:UP000030134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-022 OH1391 {ECO:0000313|Proteomes:UP000030134};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas gingivicanis strain:COT-022_OH1391 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN99090.1}.
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DR EMBL; JQZW01000002; KGN99090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2G9L5; -.
DR STRING; 266762.HQ36_01075; -.
DR eggNOG; COG1597; Bacteria.
DR Proteomes; UP000030134; 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:KGN99090.1};
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:UP000030134};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..134
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 305 AA; 32775 MW; 286B0DC55FCB605A CRC64;
MKSVKKRVIA IINPISGIAS KHKVPALLAA AYQDREEELF LTYTKGEGHA AEVIKEAMVH
GLDSVIAVGG DGTINEIASA LSGSEVKLGI IPRGSGNGLA RALGIPMQND AEAVRIITEG
KLVSIDMGLA NGLPFFCTFG VGFDAQITKR YDDASTRGLL TYIKSAIDEY ISFKPQEYKI
SIDNHDIGGE AFLITCANIE QYGNNAYIAP NASPSDGLLD LVIIRPLEGI HAAQVALQLF
TKTIDKNARI ESYRGSHIVI ERSAFGPAQI DGESVQMGKK IEIGVRQQDL LVYAPLSFGE
AIQPF
//
