ID A0A183QEP9_9TREM Unreviewed; 230 AA.
AC A0A183QEP9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=NAD(+) kinase {ECO:0000256|ARBA:ARBA00012120};
DE EC=2.7.1.23 {ECO:0000256|ARBA:ARBA00012120};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000210601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000210601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the NAD kinase family.
CC {ECO:0000256|ARBA:ARBA00010995}.
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DR AlphaFoldDB; A0A183QEP9; -.
DR STRING; 6188.A0A183QEP9; -.
DR WBParaSite; SROB_0000210601-mRNA-1; SROB_0000210601-mRNA-1; SROB_0000210601.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE 3: Inferred from homology;
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 230 AA; 25830 MW; 3CBFE67D9745BC2D CRC64;
MAEKAARKGK MKQLCGTTKK LAGRYSKPER PNKDKEDNHG DTRTEEKIDE LKNDDLFYPI
IQQYVNLGND EFKQATIEHD VSGLRENTAE SCSKINTRSS VKIFDHTVRN KIDLIVCLGG
DGTLLQIGSM FQNSILLTNS HILLLRLVSH SGSSYCVLRT RLCCQVIRSS VMNHNSNNNF
DIQNTSTTSS CSSENQPQAS NYSNDIGSRS STPDTEYHVS ILFYFSDNYA
//