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Database: UniProt
Entry: A0A1Y1HIV6_KLENI
LinkDB: A0A1Y1HIV6_KLENI
Original site: A0A1Y1HIV6_KLENI 
ID   A0A1Y1HIV6_KLENI        Unreviewed;       378 AA.
AC   A0A1Y1HIV6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|RuleBase:RU004013};
DE            EC=2.7.4.6 {ECO:0000256|RuleBase:RU004013};
GN   ORFNames=KFL_000040250 {ECO:0000313|EMBL:GAQ77823.1};
OS   Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ77823.1, ECO:0000313|Proteomes:UP000054558};
RN   [1] {ECO:0000313|EMBL:GAQ77823.1, ECO:0000313|Proteomes:UP000054558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ77823.1,
RC   ECO:0000313|Proteomes:UP000054558};
RX   PubMed=24865297; DOI=10.1038/ncomms4978;
RA   Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA   Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA   Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA   Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA   Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA   Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA   Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA   Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA   Tabata S., Ida S., Kurokawa K., Ohta H.;
RT   "Klebsormidium flaccidum genome reveals primary factors for plant
RT   terrestrial adaptation.";
RL   Nat. Commun. 5:3978-3978(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC         deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000082,
CC         ECO:0000256|RuleBase:RU004013};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC         triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000937};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000256|ARBA:ARBA00004430}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|RuleBase:RU004011}.
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DR   EMBL; DF236953; GAQ77823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1HIV6; -.
DR   STRING; 105231.A0A1Y1HIV6; -.
DR   OrthoDB; 5471350at2759; -.
DR   Proteomes; UP000054558; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   CDD; cd04412; NDPk7B; 1.
DR   Gene3D; 2.30.29.170; -; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 2.
DR   InterPro; IPR006602; DM10_dom.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR011410; NDPK7.
DR   InterPro; IPR037993; NDPk7B.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   PANTHER; PTHR43109; NUCLEOSIDE DIPHOSPHATE KINASE 7; 1.
DR   PANTHER; PTHR43109:SF2; NUCLEOSIDE DIPHOSPHATE KINASE 7; 1.
DR   Pfam; PF00334; NDK; 2.
DR   PIRSF; PIRSF036503; NDK7; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00676; DM10; 1.
DR   SMART; SM00562; NDK; 2.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 2.
DR   PROSITE; PS51336; DM10; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR036503-51,
KW   ECO:0000256|RuleBase:RU004013}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:GAQ77823.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR036503-51,
KW   ECO:0000256|RuleBase:RU004013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054558};
KW   Transferase {ECO:0000256|RuleBase:RU004013}.
FT   DOMAIN          5..93
FT                   /note="DM10"
FT                   /evidence="ECO:0000259|PROSITE:PS51336"
FT   ACT_SITE        208
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036503-50"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036503-51"
FT   BINDING         147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036503-51"
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036503-51"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036503-51"
SQ   SEQUENCE   378 AA;  42561 MW;  9A94E0653F090D5B CRC64;
     MVDSNMDHLA FIVHWLDVQA GVTWKYQLTY HASDKSLEMY DIKNRRTFLK RTEYPSVKPE
     HLYIGSIITV YSRQLHLMDY ADEHTRKKLD QKRETTLAMI KPDAIEHIGK ILNAIYGSGF
     LIKRMKMCHL SLTEAQQFYA VHQARPFFRT LTEFMSSGRV FAMELVTENA IAKWRKLIGP
     TNSDTARAED PDSLRANFGT DNTMNACHGS DAPETAKQEV SFFFDRADVG RCAQLRDCSL
     AIVKPHAVTA GHAGAIIDQI AAHFEITALQ QHILDQANAV EFLEVYKGVV PEYNGLVDEL
     KSGPLIALEV TSRDGSPDVV QELREFCGPA DPEIGKVLRP QSLRAQFGID KVKNAVHCTD
     LPEDGPLESN FFFDILLS
//
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