ID A0A068S7L5_9FUNG Unreviewed; 514 AA.
AC A0A068S7L5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 29.
DE SubName: Full=Atp-nad kinase {ECO:0000313|EMBL:CDH58279.1};
GN ORFNames=LCOR_09145.1 {ECO:0000313|EMBL:CDH58279.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH58279.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH58279.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH58279.1}.
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DR EMBL; CBTN010000055; CDH58279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S7L5; -.
DR STRING; 1263082.A0A068S7L5; -.
DR VEuPathDB; FungiDB:LCOR_09145.1; -.
DR OrthoDB; 455155at2759; -.
DR Proteomes; UP000027586; 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:CDH58279.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 58426 MW; 746875A38CF99BAF CRC64;
MPELNTDIPR PRRQSSVHSP PISSPIYPEH FESMLQKWDP NQNKLVIITK AGDKKLLRMT
RRLTEWLICT PRFGKQDPFT VYVDAHLEHV KCFRYHEMTQ VNLLIKKNLK FWTPKLLHEN
PRMFHLILTL GGDGTVLFTS WLFQSYVPPI LSFHLGSLNF LATYPYHDHR ETFKEVFEQG
YRTTARMRLS CTIYRHQQDN SACERRRQSE SILQACQLAH IETTWMKKQL KIESRNLSEP
ERDAVSKEIP CYTAAPCATY DVLNEIVVDR GPSAYMSVLE LFGDERHLTT VQADGIVIAT
PTGSTAYSLS AGGSLTHPEV RATLVTPICP HTLSFRPMLL PETMVIRVVV PFGSVRSAYC
SFDGRNRVEL KPGDHVKITV SQNPLTTVAR TGSTCDWFHS LQTSLQWNVR MRQKSFLVLE
EDDKKTPAVA SSPTKEDLPG HEEGLFGCLH NGKQQKQSNN GTDSSSTSTT ANNSETTTAY
NSEDEDEDDD LVVLPEWSIE ELQPPNPFAK CVKE
//
