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Database: UniProt
Entry: A0A0L0H9H3_SPIPD
LinkDB: A0A0L0H9H3_SPIPD
Original site: A0A0L0H9H3_SPIPD 
ID   A0A0L0H9H3_SPIPD        Unreviewed;      1423 AA.
AC   A0A0L0H9H3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|ARBA:ARBA00017632};
GN   ORFNames=SPPG_06597 {ECO:0000313|EMBL:KNC98195.1};
OS   Spizellomyces punctatus (strain DAOM BR117).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC   Spizellomycetaceae; Spizellomyces.
OX   NCBI_TaxID=645134 {ECO:0000313|EMBL:KNC98195.1, ECO:0000313|Proteomes:UP000053201};
RN   [1] {ECO:0000313|EMBL:KNC98195.1, ECO:0000313|Proteomes:UP000053201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM BR117 {ECO:0000313|EMBL:KNC98195.1,
RC   ECO:0000313|Proteomes:UP000053201};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA   White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142,
CC       ECO:0000256|RuleBase:RU004011}.
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DR   EMBL; KQ257461; KNC98195.1; -; Genomic_DNA.
DR   RefSeq; XP_016606235.1; XM_016754798.1.
DR   STRING; 645134.A0A0L0H9H3; -.
DR   GeneID; 27689889; -.
DR   VEuPathDB; FungiDB:SPPG_06597; -.
DR   eggNOG; KOG0888; Eukaryota.
DR   eggNOG; KOG0907; Eukaryota.
DR   InParanoid; A0A0L0H9H3; -.
DR   OrthoDB; 5481442at2759; -.
DR   Proteomes; UP000053201; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
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   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 6.
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   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46161; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR   PANTHER; PTHR46161:SF3; NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED; 1.
DR   Pfam; PF00334; NDK; 6.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 6.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 6.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00469; NDP_KINASES; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053201};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..1423
FT                   /note="Nucleoside diphosphate kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012136058"
FT   DOMAIN          278..418
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   DOMAIN          434..573
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   DOMAIN          616..755
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   DOMAIN          773..912
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   DOMAIN          957..1095
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   DOMAIN          1103..1243
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   REGION          66..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1239..1423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1245..1325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1423 AA;  154651 MW;  BE2DBAADBEF19C3D CRC64;
     MVRLVLLVFL FPLLALQLYN HREAACRVID SYIESSPLLT FVAHSSFAHW IAPCLAPGFV
     KGPKQYLSSQ SSRHHSPDPD QAQLGGADQE DCIPCSQLQD PYSRGKPSQK DMSAHAKRVE
     LQGTISVTTD AEWEALLSKP GLTVVDVYAK WAGPCEPMQN IFKRLKLDFG DEVTFVMAQT
     DAIDVLSKFR DKSCPLFLFF FNGVLVKMVK GANAPMVEKV IKDQLELEEK RMPHIPLVLD
     DLPNALTISN METESPISVT SQDALSPTSV VSPTTGPSEQ TLAIIKPEAM APGIVSSILD
     IIRRNRFDIV KKKKCWLTPE QVEELYREHE KAPYFQGVLT HMSTAPVLAL VLAKDNAVQE
     WRKIMGPANS GRARDDAPSS IRALHGTDNR LNAVYGSETP EAAQNEIELL FGSASAVFEI
     PLTDRDITPT SGQPEKTLAI IKPDMIDGEK VDAIVERIVC RGYQVLKREN VHLSPDEAAE
     LYSHQKEMPY FNDAVAFMAS GPVVALVLKG DDVIRGWREM IGPTDPEIAR REMPMSIRAV
     FGTDPVRNAV HGAESADGAV REIGQLFPNV LMRTESAIFG TRPSTGAGAS RPDLAADAAA
     KTTEHSTSQN DITSRTERTC ALIKPDAYAA GKKDEIVEKI KLAGFAIVAE KEVEMAREMA
     EEFYKEHHGK PFYDELVAWM SSTPIYAMVL ENDTAITAWR ELAGPTNSIK AKEIAPESIR
     ALYGTDGSHN AVHGSDSPGS AEREIRIIFG DSVRPFPAVN LASKTHLATR PLVERTLALI
     KPDAFGSGKK DEIVNRIKEQ GFAIVRESEV QWTEDKAKEF YKEHEGKGFY DQLVGWMSSA
     PIYAIVLEKE GAIAGWRELA GPTNSERARE MAPNSIRALY GKDGSHNAVH GSDSPQSAER
     EIRIVFGDTV SPFPSVQGAK PAVAASGSVS VLAHTGPETQ DPIQPVNAQL NGDVRRLERT
     LALIKPDAHS LHKEAILTRV QEAGFIIVKE SEIQFSPDMA KEFYKEHAGK GFYESLVEWM
     SSAPVYAMVL EREDAIQAWR DLAGPTNAEK AREIAPNSIR ALFGTDGSKN AVHGSDSPSS
     AAREIHVIFG DAVSPYPSGR PTLERTLALL KPDVASTTHK DEIISRIRQQ GFTILHEKEV
     LLSRQRAMEF YKEHDGKPFY NELVEWMSSA PIYAMVLERE GAVLKWRELA GATDPAKAKE
     TAPNSIRALY GSSQTHNAVH GSDSLASSAR EISILFPELG ASPSEPEPSD SSATNQNAKQ
     TIVTPRPPAT TKPTASSPSR ASSTTNITRK STATLATRAA SQKSLAGTNS KPGSRVGSTT
     ALDASRKAAV SKPASRAASK PSSRVASKQD LAGDAKKTRA SGLRSSTVAM DAEQDKGGEK
     DALAAAFEPA GHVTTHPGEG MDKVPVEGDA GPGIMEDPTN VTV
//
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