ID A0A2K3Q8B9_9HYPO Unreviewed; 546 AA.
AC A0A2K3Q8B9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=NAD(+) kinase {ECO:0000313|EMBL:PNY23713.1};
GN ORFNames=TCAP_06323 {ECO:0000313|EMBL:PNY23713.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY23713.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY23713.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY23713.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) 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:PNY23713.1}.
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; NRSZ01001054; PNY23713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3Q8B9; -.
DR STRING; 45235.A0A2K3Q8B9; -.
DR OrthoDB; 455155at2759; -.
DR Proteomes; UP000236621; 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:PNY23713.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 59851 MW; EB42410D7CABF436 CRC64;
MASVPSVPPV IVGNNTSAAP DSTGSSSADD PRTPSSAGPA AGGTCSSIPR QTIMKALASV
ARKNKPETLS LDNMLAVQNG AGNSAPASAA SSQRLADALH DLARKQSTPS TALTAMQSPC
FYHQRFDDAV DIAKVLEEIK NDESMSHSRL VQTATGVREV SKQLQRRPIK RAVRNVMIVT
KARDNQLVHL TRELATWLLR TPRYGSHVGV NVYVDAKLRN SRRFNAGSIL ADDARFEHML
KYWTPDLCWS QPEMFDLVLT LGGDGTVLFT SWLFQRVVPP VLSFSLGSLG FLTTFEFEKY
KDHLSRVMGD DGMKINLRMR FTCTVWRHDS RGQRMDEGEQ FEVLNELVID RGPSPYVSNL
ELYGDDELLT VVQADGCIFS TPTGSTAYSL SAGGSLVHPD IPAILLTPIC PHTLSFRPMV
LSDTMALRVA VPRNSRATAY CAFDGKGRIE LRQGDHVTIT ASQYPFPTVT RTDTEWFDSV
SRTLRWNVRA AAQKPFDAGS VADGVSSQGE NDDNCWDIDT DSAYYPSEEG SVSTSPVRRQ
MSMLGL
//