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Database: UniProt
Entry: L9ZQ62_9EURY
LinkDB: L9ZQ62_9EURY
Original site: L9ZQ62_9EURY 
ID   L9ZQ62_9EURY            Unreviewed;       405 AA.
AC   L9ZQ62;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=ATP-NAD/AcoX kinase {ECO:0000313|EMBL:ELY88221.1};
GN   ORFNames=C483_15951 {ECO:0000313|EMBL:ELY88221.1};
OS   Natrialba hulunbeirensis JCM 10989.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=1227493 {ECO:0000313|EMBL:ELY88221.1, ECO:0000313|Proteomes:UP000011519};
RN   [1] {ECO:0000313|EMBL:ELY88221.1, ECO:0000313|Proteomes:UP000011519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10989 {ECO:0000313|EMBL:ELY88221.1,
RC   ECO:0000313|Proteomes:UP000011519};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY88221.1}.
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DR   EMBL; AOIM01000039; ELY88221.1; -; Genomic_DNA.
DR   RefSeq; WP_006654335.1; NZ_AOIM01000039.1.
DR   AlphaFoldDB; L9ZQ62; -.
DR   STRING; 1227493.C483_15951; -.
DR   PATRIC; fig|1227493.4.peg.3204; -.
DR   OrthoDB; 56451at2157; -.
DR   Proteomes; UP000011519; Unassembled WGS sequence.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR039065; AcoX-like.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   InterPro; IPR011386; Put_ATP-NAD_kin.
DR   PANTHER; PTHR40697; ACETOIN CATABOLISM PROTEIN X; 1.
DR   PANTHER; PTHR40697:SF2; ATP-NAD KINASE-RELATED; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   PIRSF; PIRSF016907; Kin_ATP-NAD; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ELY88221.1};
KW   Transferase {ECO:0000313|EMBL:ELY88221.1}.
FT   REGION          20..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  42367 MW;  2E4A04AE98D06E62 CRC64;
     MDALGVVVNP IAGMGGRVGL KGTDGKLTEA RERGAEPRAP ERAREALTSF SRHASDVPVY
     TAAGIMGEFA ARDAGLEPRV VYDPRDESER AGESADTPPD PTVDPADAET TAADTRRAVR
     ALLESGVDLV LLVGGDGTAV DVAGVLENEP DGQTPMLGVP AGVKIYSSVF AVTPRDAGRI
     AAEFERVESR EVNDIDEEAY REGEVRSELK AVVPVPVAPD VQSSKQLSSG SVDALAAGFA
     REVEPGRTYV FGPGGTVGAI ESELGIEPSP LGVDVWRAGS ADSEGGGDRN TATDGEIDGD
     GNLDDGQLLA TDAAEADILD VLESPVTVVV SPIGGQGVIF GRGNHQISPA VLEQVDEIVV
     VADEEKLAEI PALRVDTDDE AINEELRGWQ RVRTGRFTTR LVKVV
//
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