ID A0A0W7VDX9_9HYPO Unreviewed; 585 AA.
AC A0A0W7VDX9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TGAMA5MH_00578 {ECO:0000313|EMBL:PNP48295.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PNP48295.1, ECO:0000313|Proteomes:UP000236546};
RN [1] {ECO:0000313|EMBL:PNP48295.1, ECO:0000313|Proteomes:UP000236546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5MH {ECO:0000313|EMBL:PNP48295.1,
RC ECO:0000313|Proteomes:UP000236546};
RA Gardiner D., Kazan K., Vos C., Harvey P.;
RT "Genomes of Trichoderma spp. with biocontrol activity.";
RL Submitted (FEB-2017) 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:PNP48295.1}.
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DR EMBL; MTYH01000009; PNP48295.1; -; Genomic_DNA.
DR RefSeq; XP_018657735.1; XM_018809068.1.
DR AlphaFoldDB; A0A0W7VDX9; -.
DR Proteomes; UP000236546; 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:SF11; KINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G12870)-RELATED; 1.
DR PANTHER; PTHR20275; 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 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 66414 MW; 1EC64F981C5C0EF1 CRC64;
MGREHDEDGA KTKPKHITFD QTSLDGSDED DGAVEVTFDD GSPYRRKSSM VASEAPAPAT
KRMQPGRRAE CVVHQLIEEQ RKSKERSAGN SPSRNQYHAH PIYSQSHRHD DPVDISSEKN
LDKIVDLKCP VDKQKCRAVL DPSCLDAENE IGQVDQEAWT KEMTKSDSEA EPHQQNDPVH
SRMLTKKQLS DMAWGVRELS RRLSSMRIRF RVRTIFLLTK IHDSDLIVHT RALAQWLLGK
ERDVKYVVYV EKQLKTNKRF DAAKLIDEVA HEYAKDGSVT EDVAREGVQR RLRYWDETMC
RSRPHSFDFV ITLGGDGTVL YASWLFQRIV PPVLSFALGS LGFLTKFDFE DYKPILTSAF
SKGVTVSLRL RFECTIMRSV RKRLSESESD EDDDVLHYRR DLVEELIGEE IEDEHTHKPE
GTFEILNELV VDRGPNPTMS FTEIFGDDEH FTSVLADGIC VSTPTGSTAY NLAAGGSLCH
PENPVMLVTS ICAHTLSFRP IILPDTIVLR VGVPYNARTA SWASFDGRER VELQPGDYVT
VSASRYPFAS VQAEGRRSED WINSISAKLG WNTRQKQKGF KEWDK
//
