ID Q6FMP8_CANGA Unreviewed; 185 AA. AC Q6FMP8; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 119. DE RecName: Full=Guanylate kinase {ECO:0000256|ARBA:ARBA00016296}; DE EC=2.7.4.8 {ECO:0000256|ARBA:ARBA00012961}; DE AltName: Full=GMP kinase {ECO:0000256|ARBA:ARBA00030128}; GN OrderedLocusNames=CAGL0K06281g {ECO:0000313|CGD:CAL0134671, GN ECO:0000313|EMBL:CAG61457.1}; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG61457.1, ECO:0000313|Proteomes:UP000002428}; RN [1] {ECO:0000313|EMBL:CAG61457.1, ECO:0000313|Proteomes:UP000002428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138 {ECO:0000313|Proteomes:UP000002428}; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L., RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- SIMILARITY: Belongs to the guanylate kinase family. CC {ECO:0000256|ARBA:ARBA00005790}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR380957; CAG61457.1; -; Genomic_DNA. DR AlphaFoldDB; Q6FMP8; -. DR FunCoup; Q6FMP8; 602. DR STRING; 284593.Q6FMP8; -. DR KEGG; cgr:2890461; -. DR CGD; CAL0134671; CAGL0K06281g. DR VEuPathDB; FungiDB:CAGL0K06281g; -. DR eggNOG; KOG0707; Eukaryota. DR HOGENOM; CLU_001715_0_4_1; -. DR InParanoid; Q6FMP8; -. DR OMA; NFITHEV; -. DR Proteomes; UP000002428; Chromosome K. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004385; F:GMP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046711; P:GDP biosynthetic process; IEA:EnsemblFungi. DR CDD; cd00071; GMPK; 1. DR FunFam; 3.30.63.10:FF:000002; Guanylate kinase 1; 1. DR FunFam; 3.40.50.300:FF:000776; Guanylate kinase 2; 1. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00328; Guanylate_kinase; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR017665; Guanylate_kinase. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR03263; guanyl_kin; 1. DR PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1. DR PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00100}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00100}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00100}; Reference proteome {ECO:0000313|Proteomes:UP000002428}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00100}. FT DOMAIN 2..183 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000259|PROSITE:PS50052" FT BINDING 9..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00100" SQ SEQUENCE 185 AA; 20424 MW; 33EEB9A90789CA08 CRC64; MSRPIVISGP SGTGKSTLLK KLFAEFPDTF GFSVSSTTRS PRPGEVHGKD YNFVTVDEFK SMIDGEKFIE WAQFSGNYYG TTVDSVKAVI SSGKTCILDI DMQGVKAVKT KDLNARFLFV APPSMDDLKA RLQGRGTETD ESLQKRLAAA DAEMEYANSG AHDKIIVNDD LDKAYNELKQ FIFEN //