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Database: UniProt
Entry: A0A1Q9UP93_9MICO
LinkDB: A0A1Q9UP93_9MICO
Original site: A0A1Q9UP93_9MICO 
ID   A0A1Q9UP93_9MICO        Unreviewed;       295 AA.
AC   A0A1Q9UP93;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=BJF86_08510 {ECO:0000313|EMBL:OLT39449.1};
OS   Serinicoccus sp. CNJ-927.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Serinicoccus.
OX   NCBI_TaxID=1904970 {ECO:0000313|EMBL:OLT39449.1, ECO:0000313|Proteomes:UP000186856};
RN   [1] {ECO:0000313|EMBL:OLT39449.1, ECO:0000313|Proteomes:UP000186856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNJ-927 {ECO:0000313|EMBL:OLT39449.1,
RC   ECO:0000313|Proteomes:UP000186856};
RX   PubMed=27902408; DOI=10.1099/mic.0.000386;
RA   Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA   Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT   "Sequencing rare marine actinomycete genomes reveals high density of unique
RT   natural product biosynthetic gene clusters.";
RL   Microbiology 162:2075-2086(2016).
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:OLT39449.1}.
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DR   EMBL; MKKF01000050; OLT39449.1; -; Genomic_DNA.
DR   RefSeq; WP_075820094.1; NZ_MKKF01000050.1.
DR   AlphaFoldDB; A0A1Q9UP93; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000186856; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.200.40; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   PANTHER; PTHR12358:SF54; SPHINGOID LONG-CHAIN BASES KINASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..128
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   295 AA;  30715 MW;  F377BD19879A7C3B CRC64;
     MRYALAHGRR SGRRGGAVLG EQAVRRLRAE GHDVVEVVGD SLEQVRAACA ALVADGVDVL
     AVAGGDGLVS LGADVCAGAG TTLGVLPAGT GNDNARSLRL PREPDAAIDV LLTGTPRTVD
     TLHLSDLDRR VLGSVCCALD ARINARANEW PRWLGASSYT LSALVEIALL RRQPPLHYRL
     EVDGRTRDLH ALIVVAATMP YLGGGLPLAP DADPADGLLD LVVVSPVSPP EAVGLLRAIR
     AGRHTSHPAV HLTRAREVLV EGPPDIVAHG DGEPLAALPL GVRVDPASLR VLTPA
//
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