ID A0A165B5Q9_9APHY Unreviewed; 389 AA.
AC A0A165B5Q9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 22.
DE SubName: Full=ATP-NAD kinase {ECO:0000313|EMBL:KZT00299.1};
GN ORFNames=LAESUDRAFT_739675 {ECO:0000313|EMBL:KZT00299.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT00299.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT00299.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT00299.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the NAD kinase family.
CC {ECO:0000256|ARBA:ARBA00010995}.
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; KV427689; KZT00299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165B5Q9; -.
DR STRING; 1314785.A0A165B5Q9; -.
DR InParanoid; A0A165B5Q9; -.
DR OrthoDB; 455155at2759; -.
DR Proteomes; UP000076871; 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:KZT00299.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 389 AA; 42611 MW; 38A02973F48BB409 CRC64;
MASSNSVHAS VADVRNVRVL AARHARPYRY RLSNTTCWFH MVLYEASPEA SLPCELRWFC
DVNFTRPPKS VLIVNKHRTK VIVDAIETLL SYLREKYPDV RIFHEDRPDM PGGVEKWHPG
TDAEKIDLVI TLGGDGTILH ASSLFKVGAV PPVLSFSMGT LGFLLPFHID DYAKAIDSAF
EGRATVLHRM RLSCKFQNAD GEHVNAHCED WQVMNEVALH RGSSPHLITI DIFVDGQHLT
EAVSDGLIVS TPTGSTAYSL SAGGPIVHPS LSALVLTPIC PRSLSFRPLV FPSSSSLTLK
VSERSRASAG LSMDGQVSHV LGPGEAVTVH ASLHPIPCIN RSSIAEPLDM LEGEGAGPGK
EDDWVRDINN LLQYNATFRS KALLRHSRA
//
