ID A0A229WXZ6_9EURO Unreviewed; 498 AA.
AC A0A229WXZ6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=NAD(+) kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV55_104504 {ECO:0000313|EMBL:RHZ55091.1}, CFD26_102230
GN {ECO:0000313|EMBL:RLL93639.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL93639.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL93639.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ55091.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RLL93639.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NKHV02000165; RHZ55091.1; -; Genomic_DNA.
DR EMBL; NIDN02000283; RLL93639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229WXZ6; -.
DR STRING; 1245748.A0A229WXZ6; -.
DR OrthoDB; 455155at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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 Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 56054 MW; 600DE589A618A52A CRC64;
MEKGLSRDDF GDHGGAISDP ETHNQLEVVL YPDCSHRRKS SLVSVDDTRS RPHLDNTDER
TACFVHSLIM GEWIAPTSKS DLRPDVRQSK AHETSVDDDA ITPSEAKDQK ALKATPTVVQ
SRHLTKKQLS DMAWNVRKLS KKLGSIKLKL TVKSVLLVTK VRDESLVVLT RKVTQWLLSK
DHSTKYVVYV EKRLETHPDF GAVQLIQEEP TAEGRLKYWD DNMASEEAHL FDFVVTLGGD
GTVLYTSWLF QHVVPPVLSF SLGSLGFLTR FDFNQYQSIL ETAFKDGVVV SLRLRFECTI
MRSNRRPEDD PSNITKRDLV EELIGEEKEG TLTHRPDKVF QILNDVVLDR GPNPTMSQIE
LFGDNEHFTT LLADGVCIAT PTGSTAYNLA AGGSLCHPEN PVILVTAICA HTLSFRPIIL
PDTIVLRMGV PYDARTSSWA SFDGRERIEL HPGDYVTVSA SRYPFANVLP HNRRGEDWVQ
SISKTLNWNS RQKPKSFK
//
