ID KCY_YEAST Reviewed; 204 AA. AC P15700; D6VXR0; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 207. DE RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UK {ECO:0000255|HAMAP-Rule:MF_03172}; DE EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=ATP:UMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Deoxycytidylate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=dCMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Suppressor of cdc8 protein; DE AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UMPK {ECO:0000255|HAMAP-Rule:MF_03172}; GN Name=URA6 {ECO:0000255|HAMAP-Rule:MF_03172}; Synonyms=SOC8; GN OrderedLocusNames=YKL024C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FL100A; RX PubMed=2556145; DOI=10.1016/0006-291x(89)91093-0; RA Liljelund P., Sanni A., Friesen J.D., Lacroute F.; RT "Primary structure of the S. cerevisiae gene encoding uridine RT monophosphokinase."; RL Biochem. Biophys. Res. Commun. 165:464-473(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND MUTAGENESIS OF RP LYS-29. RX PubMed=1655742; DOI=10.1016/s0021-9258(18)55267-4; RA Jiang Z., Abaigar L.T., Huang S.-H., Cai B., Jong A.Y.; RT "Molecular characterization of Saccharomyces cerevisiae URA6 gene. DNA RT sequence, mutagenesis analysis, and cell cycle regulation relevant to its RT suppression mechanism to cdc8 mutation."; RL J. Biol. Chem. 266:18287-18293(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP CATALYTIC ACTIVITY. RX PubMed=2549068; DOI=10.1016/s0021-9258(19)84872-x; RA Choi W.J., Campbell J.L., Kuo C.L., Jong A.Y.; RT "The Saccharomyces cerevisiae SOC8-1 gene and its relationship to a RT nucleotide kinase."; RL J. Biol. Chem. 264:15593-15599(1989). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBSTRATE SPECIFICITY. RX PubMed=2172245; DOI=10.1016/s0021-9258(17)30633-6; RA Ma J.J., Huang S.H., Jong A.Y.; RT "Purification and characterization of Saccharomyces cerevisiae uridine RT monophosphate kinase."; RL J. Biol. Chem. 265:19122-19127(1990). RN [8] RP FUNCTION, AND SUBSTRATE SPECIFICITY. RA Mueller-Dieckmann H.-J.; RT "Reinigung, charakterisierung und kristallisation der uridylatkinase aus RT Hefe."; RL Thesis (1990), Universitaet Freiburg im Breisgau, Germany. RN [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBSTRATE RP SPECIFICITY. RX PubMed=1333436; DOI=10.1016/0378-1119(92)90038-q; RA Schricker R., Magdolen V., Kaniak A., Wolf K., Bandlow W.; RT "The adenylate kinase family in yeast: identification of URA6 as a RT multicopy suppressor of deficiency in major AMP kinase."; RL Gene 122:111-118(1992). RN [10] RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, RP AND SUBSTRATE SPECIFICITY. RX PubMed=8391780; DOI=10.1006/abbi.1993.1339; RA Jong A., Yeh Y., Ma J.J.; RT "Characteristics, substrate analysis, and intracellular location of RT Saccharomyces cerevisiae UMP kinase."; RL Arch. Biochem. Biophys. 304:197-204(1993). RN [11] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [12] RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16240436; DOI=10.1002/bit.20747; RA Bao J., Ryu D.D.; RT "Cloning of deoxynucleoside monophosphate kinase genes and biosynthesis of RT deoxynucleoside diphosphates."; RL Biotechnol. Bioeng. 93:572-580(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-204 IN COMPLEX WITH ADP AND AMP. RX PubMed=8107116; DOI=10.1006/jmbi.1994.1140; RA Mueller-Dieckmann H.-J., Schulz G.E.; RT "The structure of uridylate kinase with its substrates, showing the RT transition state geometry."; RL J. Mol. Biol. 236:361-367(1994). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-204 IN COMPLEX WITH ADP AND RP AMP. RX PubMed=7877173; DOI=10.1006/jmbi.1994.0104; RA Mueller-Dieckmann H.-J., Schulz G.E.; RT "Substrate specificity and assembly of the catalytic center derived from RT two structures of ligated uridylate kinase."; RL J. Mol. Biol. 246:522-530(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in de CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CC dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP CC and dTMP. ATP and dATP are the best phosphate donors, but can also use CC GTP, dGTP, dCTP, and dTTP to some degree. {ECO:0000255|HAMAP- CC Rule:MF_03172, ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:2172245, CC ECO:0000269|PubMed:8391780, ECO:0000269|Ref.8}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172, ECO:0000269|PubMed:1333436, CC ECO:0000269|PubMed:16240436, ECO:0000269|PubMed:1655742, CC ECO:0000269|PubMed:2172245, ECO:0000269|PubMed:2549068}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172, ECO:0000269|PubMed:16240436, CC ECO:0000269|PubMed:8391780}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000269|PubMed:16240436, ECO:0000269|PubMed:8391780}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.15 mM for UMP {ECO:0000269|PubMed:2172245}; CC KM=1 mM for dUMP {ECO:0000269|PubMed:2172245}; CC KM=1.8 mM for dTMP {ECO:0000269|PubMed:2172245}; CC KM=0.11 mM for ATP {ECO:0000269|PubMed:16240436}; CC KM=0.53 mM for dCMP {ECO:0000269|PubMed:16240436}; CC Vmax=120 umol/min/mg enzyme (for dCDP synthesis) CC {ECO:0000269|PubMed:16240436}; CC pH dependence: CC Optimum pH is 6-9.5. {ECO:0000269|PubMed:8391780}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000269|PubMed:2172245, ECO:0000269|PubMed:7877173, CC ECO:0000269|PubMed:8107116}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:8391780}. Nucleus CC {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:1333436, CC ECO:0000269|PubMed:8391780}. Note=Predominantly cytoplasmic. CC {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:8391780}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000305|PubMed:7877173, ECO:0000305|PubMed:8107116}. CC -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- CAUTION: There is controversy about the substrate specificity of the CC enzyme. Next to the primary substrate UMP, PubMed:1333436 and Ref.8 CC report that the enzyme accepts also CMP and AMP as nucleoside CC monophosphates, but not GMP, whereas PubMed:2172245 and PubMed:8391780 CC report activity with GMP and dTMP, but not AMP or CMP. CC {ECO:0000305|PubMed:1333436, ECO:0000305|PubMed:2172245, CC ECO:0000305|PubMed:8391780, ECO:0000305|Ref.8}. 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; M31455; AAA35194.1; -; Genomic_DNA. DR EMBL; M69295; AAA35200.1; -; Genomic_DNA. DR EMBL; Z28024; CAA81859.1; -; Genomic_DNA. DR EMBL; AY558074; AAS56400.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09130.1; -; Genomic_DNA. DR PIR; A33572; A33572. DR RefSeq; NP_012901.3; NM_001179590.3. DR PDB; 1UKY; X-ray; 2.13 A; A=2-204. DR PDB; 1UKZ; X-ray; 1.90 A; A=2-204. DR PDBsum; 1UKY; -. DR PDBsum; 1UKZ; -. DR AlphaFoldDB; P15700; -. DR SMR; P15700; -. DR BioGRID; 34107; 284. DR DIP; DIP-4756N; -. DR MINT; P15700; -. DR STRING; 4932.YKL024C; -. DR iPTMnet; P15700; -. DR MaxQB; P15700; -. DR PaxDb; 4932-YKL024C; -. DR PeptideAtlas; P15700; -. DR EnsemblFungi; YKL024C_mRNA; YKL024C; YKL024C. DR GeneID; 853844; -. DR KEGG; sce:YKL024C; -. DR AGR; SGD:S000001507; -. DR SGD; S000001507; URA6. DR VEuPathDB; FungiDB:YKL024C; -. DR eggNOG; KOG3079; Eukaryota. DR GeneTree; ENSGT00940000160589; -. DR HOGENOM; CLU_032354_0_2_1; -. DR InParanoid; P15700; -. DR OMA; DVCVQRC; -. DR OrthoDB; 1330004at2759; -. DR BioCyc; MetaCyc:YKL024C-MONOMER; -. DR BioCyc; YEAST:YKL024C-MONOMER; -. DR BRENDA; 2.7.4.B1; 984. DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates. DR BioGRID-ORCS; 853844; 6 hits in 10 CRISPR screens. DR EvolutionaryTrace; P15700; -. DR PRO; PR:P15700; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P15700; Protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0004017; F:adenylate kinase activity; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central. DR GO; GO:0033862; F:UMP kinase activity; IBA:GO_Central. DR GO; GO:0009041; F:UMP/dUMP kinase activity; IDA:SGD. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:SGD. DR GO; GO:0046705; P:CDP biosynthetic process; IBA:GO_Central. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006266; UMP_CMP_kinase. DR NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1..204 FT /note="Uridylate kinase" FT /id="PRO_0000158947" FT REGION 46..76 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT REGION 141..151 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 26..31 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 52 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 74..76 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 104..107 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 111 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 142 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 148 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 159 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172, FT ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116" FT MUTAGEN 29 FT /note="K->E: Abolishes catalytic activity." FT /evidence="ECO:0000269|PubMed:1655742" FT TURN 13..15 FT /evidence="ECO:0007829|PDB:1UKZ" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:1UKZ" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 78..94 FT /evidence="ECO:0007829|PDB:1UKZ" FT STRAND 99..103 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 109..118 FT /evidence="ECO:0007829|PDB:1UKZ" FT STRAND 123..129 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 132..146 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 153..165 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 168..175 FT /evidence="ECO:0007829|PDB:1UKZ" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:1UKZ" FT STRAND 180..184 FT /evidence="ECO:0007829|PDB:1UKZ" FT HELIX 189..203 FT /evidence="ECO:0007829|PDB:1UKZ" SQ SEQUENCE 204 AA; 22933 MW; DDD7645EBCF4088D CRC64; MTAATTSQPA FSPDQVSVIF VLGGPGAGKG TQCEKLVKDY SFVHLSAGDL LRAEQGRAGS QYGELIKNCI KEGQIVPQEI TLALLRNAIS DNVKANKHKF LIDGFPRKMD QAISFERDIV ESKFILFFDC PEDIMLERLL ERGKTSGRSD DNIESIKKRF NTFKETSMPV IEYFETKSKV VRVRCDRSVE DVYKDVQDAI RDSL //