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Database: UniProt
Entry: N4UFC8_FUSC1
LinkDB: N4UFC8_FUSC1
Original site: N4UFC8_FUSC1 
ID   N4UFC8_FUSC1            Unreviewed;       238 AA.
AC   N4UFC8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|ARBA:ARBA00017632, ECO:0000256|RuleBase:RU004013};
DE            EC=2.7.4.6 {ECO:0000256|ARBA:ARBA00012966, ECO:0000256|RuleBase:RU004013};
GN   ORFNames=FOC1_g10014528 {ECO:0000313|EMBL:ENH68740.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH68740.1, ECO:0000313|Proteomes:UP000016928};
RN   [1] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142,
CC       ECO:0000256|RuleBase:RU004011}.
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DR   EMBL; KB730248; ENH68740.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4UFC8; -.
DR   STRING; 1229664.N4UFC8; -.
DR   VEuPathDB; FungiDB:FOC1_g10014528; -.
DR   HOGENOM; CLU_060216_0_0_1; -.
DR   OMA; HVFQSGW; -.
DR   Proteomes; UP000016928; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd04413; NDPk_I; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR   HAMAP; MF_00451; NDP_kinase; 1.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR11349:SF91; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004013};
KW   Kinase {ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:ENH68740.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004013};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..225
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  26017 MW;  130E02DB29CB47E8 CRC64;
     MAAEEPRQRE DPAASGKNWK QQQVRRSAEN LAPRFFALLF ALLALYILFS PPSSSLSPPV
     DLSSTSTSYS VPTSQVIPDK NIAKMSSSEQ TFIAIKPDGV QRGLVGPIIS RFENRGFKLA
     AIKLVSPGKE HLEKHYADLA GKPFFPGLIE YMSSGPICAM VWEGRDAVKT GRAILGATNP
     LASSPGTIRG DYAIDVGRNV CHGSDSVENA QKEIALWFKE GEVLSWKSAQ FNWVYEKA
//
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