ID A0A3D8SQL5_9HELO Unreviewed; 578 AA.
AC A0A3D8SQL5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE SubName: Full=ATP-NAD kinase-like protein {ECO:0000313|EMBL:RDW88610.1};
GN ORFNames=BP6252_00642 {ECO:0000313|EMBL:RDW88610.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW88610.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW88610.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW88610.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW88610.1}.
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DR EMBL; PDLM01000001; RDW88610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8SQL5; -.
DR STRING; 1849047.A0A3D8SQL5; -.
DR Proteomes; UP000256645; 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, ECO:0000313|EMBL:RDW88610.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 64899 MW; 410667E1152EC11A CRC64;
MFPAPSPELN IPLIRKHSSD LGPMNPNEED HGHSSASDSE YQHALEVVFD AQNAHRRKSS
LIAADTPRHA FERRKNTECY VHALLESQRK QGRPSHSGLE DIAEGLKQRR LATETSETLD
TALEKDNALV EGKGSDGEAS GQEDEKAWKQ RHSAQADQKI EVQEGEDSTA VHSRLLTKKQ
LSDMAWGVRE LSKRLGKIRL KLKVKTVFLL TKAHDETLIG NTRDVAKWLL SPERDVKYTV
YVEENLKDNK KFDADGLMKE IEEATSSQEG ESNGVTKSAA RRLKYWSNTM CRTRPHNFDF
VVTLGGDGTV LYASWLFQRI VPPVLSFALG SLGFLTKFDY DEFEDTLTTA FRDGVTISLR
LRFEGTVMRS QKKKSKAITN GEEGTVEDED HQRRDLVEEL IGEEKEDERT HRPDGTYEIL
NDIVVDRGPN PTMSSTEIFG DDEHFTSVQA DGVCVATPTG STAYNLAAGG SLCHPENPVI
LVTAICAHTL SFRPIILPDT IVLRIGVPYD ARTSSWASFD GRERVELRPG DYVTISASRY
PFANVMPQGR RSEDWVNSIS GKLGWNTRQR QKSYKEWS
//
