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Database: UniProt
Entry: A0A0D2FDW2_9EURO
LinkDB: A0A0D2FDW2_9EURO
Original site: A0A0D2FDW2_9EURO 
ID   A0A0D2FDW2_9EURO        Unreviewed;       653 AA.
AC   A0A0D2FDW2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=NAD+ kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV05_02793 {ECO:0000313|EMBL:KIW58254.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW58254.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW58254.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW58254.1,
RC   ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
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; KN847318; KIW58254.1; -; Genomic_DNA.
DR   RefSeq; XP_013318838.1; XM_013463384.1.
DR   AlphaFoldDB; A0A0D2FDW2; -.
DR   STRING; 348802.A0A0D2FDW2; -.
DR   GeneID; 25324701; -.
DR   HOGENOM; CLU_008831_7_1_1; -.
DR   OrthoDB; 455155at2759; -.
DR   Proteomes; UP000054342; 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; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF0; 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:UP000054342};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  71755 MW;  19C904C9F414F25B CRC64;
     MTNAVMHNAQ CSTLPSPTTS EATSISNFSP PTPALDNTHN VLPHGMASPN TKASVGDSIL
     RQYAHHLGAL HADDETHAVH DVSERDTAAV DETILNTVLN LADKPPNRTD RSSYLAHHPT
     VPVPKPLSLP KPFLTHRKNA KSTDIPRQTI MKALVSRRPS TGPITAPLAA NTLRTAAREA
     EAGEQNPPTS SPCLTATLGG LQPSVFSGCS PTSTSFMRSP CFFHQRFESI VDVQKVLDEI
     AEDDYSHSRL MQTAIGVREV SKQLQRKPLK RAVRNVMIVT KARDNSLVYL TRDLAEWLLS
     TPRYGSDVGV NVYVDAKLRH SKRFDAAGLV KKEPRFEQML KYWTPDLCWS SPETFDLVLT
     LGGDGTVLFT SWLFQRVVPP VLSFSLGSLG FLTNFEFDKY KEHLDRIMGD GGMRVNLRMR
     FTCTVWRADR SPGAEKGAVE EGEQFEVLNE LVIDRGPSAY VSNLELYGDD ELLTIVQADG
     CIFSTPTGST AYSLSAGGSL IHPSIPAILL TPICPHTLSF RPMVLSDTLL LRIAVPNKSR
     SSAYCSFDGK GRVELKRGDY VTLEASQYPF PTVMTGTNEW VESVQRALRW NVRGAVQKAW
     DDGDEADCDQ AEEKWDIDMD SSPAGGTDSG IGPSEDGDHV ASPMRRQLSL LNM
//
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