ID A0A0G4P7A1_PENC3 Unreviewed; 491 AA.
AC A0A0G4P7A1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Diacylglycerol kinase, catalytic domain {ECO:0000313|EMBL:CRL22175.1};
GN ORFNames=PCAMFM013_S007g000156 {ECO:0000313|EMBL:CRL22175.1};
OS Penicillium camemberti (strain FM 013).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL22175.1, ECO:0000313|Proteomes:UP000053732};
RN [1] {ECO:0000313|EMBL:CRL22175.1, ECO:0000313|Proteomes:UP000053732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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DR EMBL; HG793140; CRL22175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4P7A1; -.
DR STRING; 1429867.A0A0G4P7A1; -.
DR Proteomes; UP000053732; 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, ECO:0000313|EMBL:CRL22175.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 120..259
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 491 AA; 53261 MW; 770564D08790963D CRC64;
MSSPDNSLQD PHDTTLTVDE SVTLTIGADS LLILDDRPAK ADRRCCGLLQ SKPETNHAIS
LYNILGAEVT ASNLVIAYAQ PAAKDDVSVT TVQYPISEKE KKVAETWVQQ LLDGAYGKAL
RGKRLKVLVN PFGGKGTAAS LYQRYAAPVF AAAKCQVDVQ TTEYRGQAIN IAENLDIDAY
DALVCCSGDG LPYEVFNGLG KRPDARKALA QTAVALLPCG SGNGLTWNAF GTGSVSIAAL
AIVKGLRTPL DLVSISQKDS RTLSFLSQSF GIVAECDLGT ENLRWMGAQR FTYGFLVRLM
RQTIWPCDIA IKVEIGDKER IKEHYAAWST RPEDPDADSK RLEIAAESPG LPELKYGTVT
DELPQGWQVV SGETMGNFYA GNMAIMSKDT NMFPATLPDD GLMDVITIDG TVSRGTAITM
MNEIPSGRFF DMPELNVRKA SAFRLVPHQK EGYISIDGER IPFEAFQAEI HQGLGTILTK
SGRSYEAAGP R
//
