ID A0A182X5Q8_ANOQN Unreviewed; 551 AA.
AC A0A182X5Q8;
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 quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA005144-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., 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 quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA005144-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA005144-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; A0A182X5Q8; -.
DR STRING; 34691.A0A182X5Q8; -.
DR EnsemblMetazoa; AQUA005144-RA; AQUA005144-PA; AQUA005144.
DR VEuPathDB; VectorBase:AQUA005144; -.
DR Proteomes; UP000076407; 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 68..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 61211 MW; B63FA9B6A3C99917 CRC64;
MAYLSDVDLA TLHQSRLEER VQYRLSALWT HGAESGRDYQ RSLPAVSSSA SSSSTSLTMF
GDREAAKLRA VKQSHHHASS SGGGKHVEWS DDDHLHDDGY FSSDTRRRRS GTWPSGHQQQ
QQNNHRHHQS NGAGGGYSPS AEDDIPADED 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
DIVRGIENLE N
//
