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Database: UniProt
Entry: A0A0D1ZLJ8_9EURO
LinkDB: A0A0D1ZLJ8_9EURO
Original site: A0A0D1ZLJ8_9EURO 
ID   A0A0D1ZLJ8_9EURO        Unreviewed;       537 AA.
AC   A0A0D1ZLJ8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=NAD+ kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV11_03199 {ECO:0000313|EMBL:KIV87668.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV87668.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV87668.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV87668.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
CC       {ECO:0000256|ARBA:ARBA00010995}.
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DR   EMBL; KN846951; KIV87668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1ZLJ8; -.
DR   STRING; 1016849.A0A0D1ZLJ8; -.
DR   HOGENOM; CLU_008831_1_1_1; -.
DR   OrthoDB; 455155at2759; -.
DR   Proteomes; UP000053599; 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:UP000053599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..537
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  60348 MW;  AD2C78B1037DE838 CRC64;
     MSESQGAPHL SRRISECLPD HDGSSSEDEF NRKIEVVFDS DTARRRKSSF VLSDSPLIDQ
     PLKENAARLK SQCLVHKLVE KTSLGQQPKV ESKLEQIDEV DPGMPSEDGA ETASGKEEVR
     ATESRLLTKK QLSDMAVSVR ALAKKLGNLK VKLKIRAIFL LTKIYDKTLI VKTREVARWL
     LSKDRSVPYI VYVQDTLKDN PIFDAKGLTD EDPACGERLK YWDVDLARKR PHTFDFVITL
     GGDGTVLYAS WLFQRVVPPV LSFALGSLGF LTKFDFTNYE DTLSQAIKDG VTISLRLRFE
     GTVMRSHKRH DDAEHRDIVE ELIGEEADDR NTHKPDSTFE ILNDIVVDRG PNPTMSTIEL
     FGDEEHLTTV QADGICVATP TGSTAYNLAA GGSLCHPENP VILVTAICAH TLSFRPIILP
     DTIVLRLGVP YDARSNSWAS FDGRERIELF PGDYVTISAS RYPFANVLPP GRRSEDWVNS
     ISRTLQWNSR QRQKAYQEWD GDHTESADLK NKKNDSKSED YDRSDQRRGG EGHPGYH
//
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