ID A0A2G4SVQ5_RHIZD Unreviewed; 488 AA.
AC A0A2G4SVQ5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=RHIMIDRAFT_283554 {ECO:0000313|EMBL:PHZ12825.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ12825.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ12825.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ12825.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303849; PHZ12825.1; -; Genomic_DNA.
DR RefSeq; XP_023466533.1; XM_023613131.1.
DR AlphaFoldDB; A0A2G4SVQ5; -.
DR STRING; 1340429.A0A2G4SVQ5; -.
DR GeneID; 35444120; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR055916; DUF7493.
DR InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF31; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF24321; DUF7493; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242254};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 126..268
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 488 AA; 54640 MW; 01C1266AE7C72ED8 CRC64;
MVTTLKVTKG VHPVELTCDE QGLRIEGDFN ASQKLKKKII CCCIPVIQGK GPDPTLLPID
HEYILYAEYI QRTKTIQIRF VLPEDRSNDD STADFYELYY TVSDDKAQEA EAFCETLMDH
AYEGAKVHKR LLVLINPFGG QGKAKEIFEY HVRPIFQAAK CEVTVKNTQR QGHAIDIAKE
LDVDAYDAVV TVSGDGVVHE VINGFLARSD AKDVMKKITL GIIPGGTGNS LIISILGEKR
GFDPVYTALQ VIKGKPMPLD LCSITYDDHR YFSFLSQNYG IAAYADLATE HMRWMGDTRT
IVGLLQEIFA RHTYGVEAAI QVVESDKKKI IQECRVFKGS ILEQEELNLE DTLPPLSEPV
PSDWMVIKDN ISMFLASKVP LLSRGMLSHP CALPNDGTLD LLLIRRSPGI KKQLDVFTKV
EKGHHIHNDI VEYYKIKAFR LTPVLKPGQT AYVAIDGEHA PCKPFQVQVH PRLCSVLAIK
PTFLNTNI
//
