ID A0A0G2GQC8_9PEZI Unreviewed; 511 AA.
AC A0A0G2GQC8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Putative nad kinase atp nad kinase {ECO:0000313|EMBL:KKY25573.1};
GN ORFNames=UCDDS831_g02044 {ECO:0000313|EMBL:KKY25573.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY25573.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY25573.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY25573.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY25573.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY25573.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) 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:KKY25573.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAQI01000037; KKY25573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2GQC8; -.
DR Proteomes; UP000034182; 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:SF0; NAD KINASE; 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:KKY25573.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 56644 MW; 8B62D19D4C239B0E CRC64;
MKALASRPPP TSNMSIASSI NGLLQNNRDR DREQQQQQDP PQTRPGLSRK RLSNGIADLT
LNPESLAASR ISALASPCFF HKKFDAAVNI DRVLEEIHED DGMSHSRLLQ TATGVREVSK
QLQRRPVKIA VKNVMIVTKA RDNQLVDLTH ELADWLLTTP RHGRDVGVNV YVDHKLRNSR
RFDAAGLLRK DERFSSMLRY WTPELCLATP EKFDLVLTLG GDGTVLYTSW LFQRIVPPIL
SFSLGSLGFL TNFEFNSYKE QLSRVMGDAG MRVNLRMRFT CTVYRANPNH DASDPESPAH
LEAEQYEVLN ELVIDRGPSP YVSNLELYGE NELLTIVQAD GCIFSTPTGS TAYSLSAGGS
LVHPDIPAIL LTPICPHTLS FRPMLLNDSM LLRVAVPRNS RATAYCAFDG KGRVELRQGD
HVTIAASQYP FPTVLSRPTE WFDSLGRTLR WNTRGAQQKA WDGADEKGGA GEEKFDIDID
DDDPGKDSGY SAATSSAGNS SPVRRGSGLW A
//
