KCY_YEAST
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 03-AUG-2022, entry version 199.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03172,
CC ECO:0000269|PubMed:16240436, 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=1.0 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}.
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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; 232.
DR DIP; DIP-4756N; -.
DR MINT; P15700; -.
DR STRING; 4932.YKL024C; -.
DR iPTMnet; P15700; -.
DR MaxQB; P15700; -.
DR PaxDb; P15700; -.
DR PRIDE; P15700; -.
DR EnsemblFungi; YKL024C_mRNA; YKL024C; YKL024C.
DR GeneID; 853844; -.
DR KEGG; sce:YKL024C; -.
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; RFQFTHL; -.
DR BioCyc; MetaCyc:YKL024C-MON; -.
DR BioCyc; YEAST:YKL024C-MON; -.
DR BRENDA; 2.7.4.B1; 984.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
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:uridylate 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; -; 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 PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 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
