ID   A0A1Y2EH95_9PEZI        Unreviewed;       456 AA.
AC   A0A1Y2EH95;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   28-JUN-2023, entry version 16.
DE   SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:ORY70943.1};
GN   ORFNames=BCR38DRAFT_329378 {ECO:0000313|EMBL:ORY70943.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY70943.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY70943.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY70943.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
CC       {ECO:0000256|ARBA:ARBA00010995}.
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:ORY70943.1}.
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DR   EMBL; MCFJ01000001; ORY70943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2EH95; -.
DR   STRING; 1141098.A0A1Y2EH95; -.
DR   InParanoid; A0A1Y2EH95; -.
DR   OrthoDB; 455155at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00361; NAD_kinase; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   PANTHER; PTHR20275; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF26; NADH KINASE POS5, MITOCHONDRIAL; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ORY70943.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   456 AA;  49508 MW;  2095C8EEA42367D5 CRC64;
     MPSFRIASLA SSGLARSFTT TARRLEIRDV SELPNRIVPN YKNSPTSSLL SLEWPSPPRN
     VLIVPKLYAP LVISSAVEFA KHIHSEYPNL HLIFEQRIAS TIHDSLPFPI YSSDPTHFPT
     KIDLVATLGG DGTILRAASL FSLHASVPPI LSFSMGTLGF LGEWKFEEYK RAWREVYMSG
     SRVGVSDLQG PHTQAATNGW NDGGNDAVGT REGWATIRGK NMGTTRASKI LLRHRLKVGV
     YDENGANINA HLMPTSTAAL TQPLHPVPPE IKELSNTGEP VVPDLHAINE LVIHRGPNPH
     LAIVDVYVGN RFLTEAVADG ILISTPTGST AYSLSAGGTI IHPLTKTMLL TPICARTLSF
     RHLCLPLNKK VVLKVSKKNR GRELEVSIDG KRRAGVTIGM EIRVTGEVVG QVGDDDTWTG
     GVPCVIRSSG QGDEGDDDDG WVGGLNERLK FNYPVG
//