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Database: UniProt
Entry: A0A0A2L0V1_PENIT
LinkDB: A0A0A2L0V1_PENIT
Original site: A0A0A2L0V1_PENIT 
ID   A0A0A2L0V1_PENIT        Unreviewed;       491 AA.
AC   A0A0A2L0V1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   28-JAN-2026, entry version 36.
DE   SubName: Full=ATP-NAD kinase, PpnK-type {ECO:0000313|EMBL:KGO72786.1};
GN   ORFNames=PITC_057620 {ECO:0000313|EMBL:KGO72786.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO72786.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO72786.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO72786.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO72786.1}.
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DR   EMBL; JQGA01000866; KGO72786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L0V1; -.
DR   STRING; 40296.A0A0A2L0V1; -.
DR   HOGENOM; CLU_013399_0_1_1; -.
DR   OMA; TMGNFYA; -.
DR   OrthoDB; 3853857at2759; -.
DR   PhylomeDB; A0A0A2L0V1; -.
DR   Proteomes; UP000030104; 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:KGO72786.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          120..259
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   491 AA;  53391 MW;  56F7750B594FCAC2 CRC64;
     MSSPDDSSQE PLDTTLVVNE SVSLTIGGDL LLILDDRPAK TDRRCCGLLQ SKPETNHAVS
     LYNILSAEIT ASNLVIAYAQ PAAKDEISVT TAQYPISEKE KKAVETWVQQ LLDRAYAKAL
     RGKRLKVLVN PFGGKGTAAS LYRRYAAPVF AAAKCQVDVQ TTEHRGHAIE IAENLDIDAY
     DAVVCCSGDG LPYEVFNGLG KRSDARKALA QTAVALLPCG SGNGLTWNAF GTGSVSIAAL
     AIVKALRTPL DLISISQKDS RTLSFLSQSF GIIAECDLGT ENIRWMGAQR FTYGFLVRLI
     RQTIWPCDIA IKVEIGDKER IKEHYAAWST RPQEIDADSK RLEIAAESPG LPELKYGTVT
     DELPQGWEVV SGETMGNFYA GNMAIMSKDT NMFPATLPDD GLMDVITIDG TLSRGTAITL
     MTEVPSGRFF DMPDLNIRKA SAFRLVPHQK EGYISIDGER VPFEAFQAEV HQGLGTILTK
     SGRSYEAAGP R
//
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