ID A0A182N279_9DIPT Unreviewed; 491 AA.
AC A0A182N279;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=NAD(+) kinase {ECO:0000256|ARBA:ARBA00012120};
DE EC=2.7.1.23 {ECO:0000256|ARBA:ARBA00012120};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR001737-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR001737-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR001737-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the NAD kinase family.
CC {ECO:0000256|ARBA:ARBA00010995}.
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DR AlphaFoldDB; A0A182N279; -.
DR STRING; 7168.A0A182N279; -.
DR EnsemblMetazoa; ADIR001737-RA; ADIR001737-PA; ADIR001737.
DR VEuPathDB; VectorBase:ADIR001737; -.
DR OrthoDB; 455155at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-EC.
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};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 43..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54488 MW; DA2AAD6D4124FB53 CRC64;
MAEMHENDDF MADLVRFNHP SAAHHQHHHH QHQSHLNHLL YSTNQGNNHR QHNGSSSKDA
AAGASSSGIA NNGSTAYSPS AEDDIPAEED QLLLWRPKRR TRSLNAPSPF QQFGPCGRIM
KNSAMVMQIQ DPASQRLTWY KPPLAVLVIK KVRDSKVLQP FVQLVEWLIH EKHMVVWVEA
AILDDALLTG DKRFTKLQDK LITFKDGRDD LTDKIDFIIC LGGDGTLLYA SLLFQKSVPP
VMAFHLGSLG FLTPFQFDNF QEQVTNVLEG HAALTLRSRL RCIIVRKDKT EQEISTFKSS
QDPSTNILVL NEVVIDRGLS SYLSNIDLFL DGKHITSVQG DGLIVSTPTG STAYSAAAGA
SMIHPSVPAI LVTPICPHSL SFRPIVLPAG VELKIAISPD SRNSSWVSFD GRNRQELLHG
DSLHVTTSIY PVPSICAQDQ IADWFDSLAE CLHWNVRKRQ KCLDELSDLT GSGTEDSAID
DIVRGMENLE N
//
