ID A0A0B4IJ75_METMF Unreviewed; 606 AA.
AC A0A0B4IJ75;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=NAD kinase associated with ferric reductase {ECO:0000313|EMBL:KIE01995.1};
DE Flags: Fragment;
GN ORFNames=MAJ_02217 {ECO:0000313|EMBL:KIE01995.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE01995.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KIE01995.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE01995.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KIE01995.1}.
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DR EMBL; AZNE01000006; KIE01995.1; -; Genomic_DNA.
DR RefSeq; XP_014580988.1; XM_014725502.1.
DR AlphaFoldDB; A0A0B4IJ75; -.
DR HOGENOM; CLU_008831_7_2_1; -.
DR OrthoDB; 455155at2759; -.
DR Proteomes; UP000031176; 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:KIE01995.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000031176};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIE01995.1"
SQ SEQUENCE 606 AA; 66476 MW; 7937B3AE6715F5C8 CRC64;
MTSERVSSPT ALHPAIGAHQ DGESQVSVNK GASASLDRPK TSSAAHGLSL NTVKATRSAD
DPCTPSTAVP ALGGESSNSL TSDVADTWPW AASTRAGYLG HRRNAPSHDS IPRQTIIKAL
ASVARNNKPE ALSLDNMLAT QNTETPGSAA SSQRLADALQ DLARKQSTPI TALAAMKSPC
FYHQRFDDAV DIAKVLEEIK NDEWMSHSRL VQTATGVREV SKQLQRRPIK RAVRNVMIVT
KARDHQLVYL TRELATWLLR TPRYGSDLGV NVYVDAKLRS SRRFDAPGIL AENTRFEHML
KYWTPDLCWS QPEKFDLVLT LGGDGTVLFT SWLFQRIVPP VLSFSLGSLG FMTTFEFEKY
KSHLSRVMGD EGMKINLRMR FTCTVWRHDA EGAQVGEGEQ FEVLNELVID RGPSPYVSNL
ELYGDDELLT VVQADGCIFS TPTGSTAYSL SAGGSLVHPD IPAILLTPIC PHTLSFRPMV
LSDTMALRVA VPRNSRATAY CAFDGKGRIE LRQGDHVTIT ASQYPFPTVT RTDTEWFDSV
SRTLRWNVRA TLQKPFDADA ASAGIASQGE DDSACWDIDT DSAYFPSEEG SVSASPIRRQ
MSMLGL
//
