INGK_ECOLI
ID INGK_ECOLI Reviewed; 434 AA.
AC P0AEW6; P22937; Q2MBV0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Guanosine-inosine kinase {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000303|PubMed:10879466, ECO:0000303|PubMed:7665468};
DE EC=2.7.1.73 {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468};
GN Name=gsk {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000303|PubMed:7665468,
GN ECO:0000303|PubMed:7721718}; OrderedLocusNames=b0477, JW0466;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=7721718; DOI=10.1128/jb.177.8.2236-2240.1995;
RA Harlow K.W., Nygaard P., Hove-Jensen B.;
RT "Cloning and characterization of the gsk gene encoding guanosine kinase of
RT Escherichia coli.";
RL J. Bacteriol. 177:2236-2240(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10 AND 400-434,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=7665468; DOI=10.1128/jb.177.17.4921-4926.1995;
RA Mori H., Iida A., Teshiba S., Fujio T.;
RT "Cloning of a guanosine-inosine kinase gene of Escherichia coli and
RT characterization of the purified gene product.";
RL J. Bacteriol. 177:4921-4926(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-316.
RC STRAIN=K12;
RX PubMed=2051480; DOI=10.1016/0022-2836(91)90180-e;
RA Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.;
RT "Isolation and characterization of visible light-sensitive mutants of
RT Escherichia coli K12.";
RL J. Mol. Biol. 219:393-398(1991).
RN [7]
RP PROTEIN SEQUENCE OF 1-5, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10879466; DOI=10.1271/bbb.64.972;
RA Kawasaki H., Shimaoka M., Usuda Y., Utagawa T.;
RT "End-product regulation and kinetic mechanism of guanosine-inosine kinase
RT from Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 64:972-979(2000).
RN [8]
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=11440147; DOI=10.1271/bbb.65.1230;
RA Matsui H., Shimaoka M., Takenaka Y., Kawasaki H., Kurahashi O.;
RT "gsk disruption leads to guanosine accumulation in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 65:1230-1235(2001).
RN [9] {ECO:0007744|PDB:6VWO, ECO:0007744|PDB:6VWP}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEXES WITH GUANOSINE; ADP AND
RP PPGPP, ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-7; PHE-321; LYS-383;
RP SER-393 AND GLN-396.
RX PubMed=32857952; DOI=10.1016/j.molcel.2020.08.005;
RA Wang B., Grant R.A., Laub M.T.;
RT "ppGpp coordinates nucleotide and amino-acid synthesis in E. coli during
RT starvation.";
RL Mol. Cell 80:29-42.e10(2020).
CC -!- FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP
CC and IMP, respectively (PubMed:7721718, PubMed:7665468,
CC PubMed:10879466). Can also use deoxyguanosine and xanthosine, but not
CC adenosine, uridine, cytidine or deoxythymidine (PubMed:7665468,
CC PubMed:10879466). Shows a strong preference for guanosine
CC (PubMed:7665468, PubMed:10879466). dATP can serve as a phosphate donor
CC as well as ATP. Shows weaker activity with UTP and CTP (PubMed:7665468,
CC PubMed:10879466). {ECO:0000269|PubMed:10879466,
CC ECO:0000269|PubMed:7665468, ECO:0000269|PubMed:7721718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + guanosine = ADP + GMP + H(+); Xref=Rhea:RHEA:27710,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16750, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02246,
CC ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27711;
CC Evidence={ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + inosine = ADP + H(+) + IMP; Xref=Rhea:RHEA:21140,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17596, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456216; EC=2.7.1.73;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02246,
CC ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21141;
CC Evidence={ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02246,
CC ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:7665468};
CC Note=Mg(2+) is probably required for activity in addition to its role
CC in forming the Mg-ATP complex. {ECO:0000269|PubMed:10879466};
CC -!- ACTIVITY REGULATION: Guanosine and inosine kinase activities are both
CC inhibited by ppGpp, a nucleotide messenger universally produced in
CC bacteria following nutrient starvation. ppGpp binds to Gsk, and
CC inhibits its activity by blocking conformational dynamics and inducing
CC tetramerization. Inhibiting purine nucleotide synthesis is required
CC during starvation to maintain levels of the metabolite 5'-
CC phosphoribosyl-1'-diphosphate (pRpp), which is required for the
CC synthesis of histidine and tryptophan (PubMed:32857952). Activity is
CC slightly increased in the presence of pyrimidine nucleotides, while it
CC is markedly inhibited by GDP and GTP (PubMed:10879466). Activity is
CC stimulated by K(+) ions (PubMed:7665468). Guanosine and inosine kinase
CC activities are inhibited by Cu(2+) or Zn(2+) (PubMed:7665468).
CC {ECO:0000269|PubMed:10879466, ECO:0000269|PubMed:32857952,
CC ECO:0000269|PubMed:7665468}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.1 uM for guanosine {ECO:0000269|PubMed:7665468};
CC KM=7.8 uM for guanosine {ECO:0000269|PubMed:10879466};
CC KM=2.1 mM for inosine {ECO:0000269|PubMed:7665468};
CC KM=1.5 mM for inosine {ECO:0000269|PubMed:10879466};
CC KM=4.3 mM for deoxyguanosine {ECO:0000269|PubMed:10879466};
CC KM=0.49 mM for ATP {ECO:0000269|PubMed:10879466};
CC KM=0.51 mM for ATP (for guanosine kinase activity)
CC {ECO:0000269|PubMed:7665468};
CC KM=0.71 mM for ATP (for inosine kinase activity)
CC {ECO:0000269|PubMed:7665468};
CC KM=2.4 mM for dATP (for guanosine kinase activity)
CC {ECO:0000269|PubMed:7665468};
CC KM=0.66 mM for dATP (for inosine kinase activity)
CC {ECO:0000269|PubMed:7665468};
CC Vmax=2.9 umol/min/mg enzyme with guanosine as substrate
CC {ECO:0000269|PubMed:7665468};
CC Vmax=4.9 umol/min/mg enzyme with inosine as substrate
CC {ECO:0000269|PubMed:7665468};
CC pH dependence:
CC Optimum pH is 8.2 for guanosine kinase activity. Optimum pH is 6.9
CC for inosine kinase activity. {ECO:0000269|PubMed:7665468};
CC Temperature dependence:
CC Optimum temperature is 38 degrees Celsius for guanosine kinase
CC activity and between 26 and 39 degrees Celsius for inosine kinase
CC activity. {ECO:0000269|PubMed:7665468};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from inosine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_02246,
CC ECO:0000305|PubMed:11440147}.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000305|PubMed:11440147}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10879466}.
CC -!- INTERACTION:
CC P0AEW6; P75767: ybhK; NbExp=5; IntAct=EBI-548746, EBI-550390;
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene causes a considerable
CC amount of guanosine accumulation together with a slight increase in the
CC inosine productivity. {ECO:0000269|PubMed:11440147}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000255|HAMAP-Rule:MF_02246, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA14306.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L35149; AAC36932.1; -; Genomic_DNA.
DR EMBL; D00798; BAA00690.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40231.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73579.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76256.1; -; Genomic_DNA.
DR EMBL; D90259; BAA14306.1; ALT_FRAME; Genomic_DNA.
DR PIR; JQ0812; JQ0812.
DR RefSeq; NP_415010.1; NC_000913.3.
DR RefSeq; WP_000671574.1; NZ_STEB01000007.1.
DR PDB; 6VWO; X-ray; 1.78 A; A=1-434.
DR PDB; 6VWP; X-ray; 3.45 A; A/B/C/D/E/F/G/H=1-434.
DR PDBsum; 6VWO; -.
DR PDBsum; 6VWP; -.
DR AlphaFoldDB; P0AEW6; -.
DR SMR; P0AEW6; -.
DR BioGRID; 4259850; 4.
DR BioGRID; 850931; 3.
DR DIP; DIP-48148N; -.
DR IntAct; P0AEW6; 9.
DR STRING; 511145.b0477; -.
DR jPOST; P0AEW6; -.
DR PaxDb; P0AEW6; -.
DR PRIDE; P0AEW6; -.
DR EnsemblBacteria; AAC73579; AAC73579; b0477.
DR EnsemblBacteria; BAE76256; BAE76256; BAE76256.
DR GeneID; 60903753; -.
DR GeneID; 946584; -.
DR KEGG; ecj:JW0466; -.
DR KEGG; eco:b0477; -.
DR PATRIC; fig|1411691.4.peg.1799; -.
DR EchoBASE; EB1094; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_060237_0_0_6; -.
DR InParanoid; P0AEW6; -.
DR OMA; LLGVMCN; -.
DR PhylomeDB; P0AEW6; -.
DR BioCyc; EcoCyc:GSK-MON; -.
DR BioCyc; MetaCyc:GSK-MON; -.
DR BRENDA; 2.7.1.73; 2026.
DR UniPathway; UPA00591; UER00647.
DR UniPathway; UPA00909; -.
DR PRO; PR:P0AEW6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106366; F:guanosine kinase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0008906; F:inosine kinase activity; IDA:EcoCyc.
DR GO; GO:0032263; P:GMP salvage; IMP:EcoCyc.
DR GO; GO:0032264; P:IMP salvage; IMP:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_02246; Gua_Ino_kinase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR046405; IngK.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase; Magnesium;
KW Nucleotide-binding; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..434
FT /note="Guanosine-inosine kinase"
FT /id="PRO_0000080070"
FT BINDING 40..45
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02246,
FT ECO:0000305|PubMed:32857952"
FT BINDING 93..97
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02246,
FT ECO:0000305|PubMed:32857952"
FT BINDING 198
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02246,
FT ECO:0000305|PubMed:32857952"
FT BINDING 284..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02246,
FT ECO:0000305|PubMed:32857952"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02246,
FT ECO:0000305|PubMed:32857952"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02246,
FT ECO:0000305|PubMed:32857952"
FT MUTAGEN 7
FT /note="R->A: Mutant is less sensitive to ppGpp inhibition."
FT /evidence="ECO:0000269|PubMed:32857952"
FT MUTAGEN 321
FT /note="F->A: Mutant is less sensitive to ppGpp inhibition."
FT /evidence="ECO:0000269|PubMed:32857952"
FT MUTAGEN 383
FT /note="K->A: Mutant is insensitive to ppGpp and GDP
FT inhibition. Mutant accumulates abnormally high levels of
FT purine nucleotides following amino-acid starvation,
FT compromising cellular fitness and cell growth."
FT /evidence="ECO:0000269|PubMed:32857952"
FT MUTAGEN 393
FT /note="S->A: Mutant is less sensitive to ppGpp inhibition."
FT /evidence="ECO:0000269|PubMed:32857952"
FT MUTAGEN 396
FT /note="Q->A: Mutant is less sensitive to ppGpp inhibition."
FT /evidence="ECO:0000269|PubMed:32857952"
FT CONFLICT 314
FT /note="A -> V (in Ref. 6; BAA14306)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="R -> P (in Ref. 1; AAC36932)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="LH -> PD (in Ref. 1; AAC36932)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="L -> S (in Ref. 1; AAC36932)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..423
FT /note="PER -> AV (in Ref. 1; AAC36932)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6VWP"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:6VWP"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6VWP"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6VWO"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:6VWO"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6VWO"
FT TURN 314..321
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6VWP"
FT HELIX 356..376
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 394..409
FT /evidence="ECO:0007829|PDB:6VWO"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6VWO"
FT HELIX 426..433
FT /evidence="ECO:0007829|PDB:6VWP"
SQ SEQUENCE 434 AA; 48449 MW; 04693F70D1540236 CRC64;
MKFPGKRKSK HYFPVNARDP LLQQFQPENE TSAAWVVGID QTLVDIEAKV DDEFIERYGL
SAGHSLVIED DVAEALYQEL KQKNLITHQF AGGTIGNTMH NYSVLADDRS VLLGVMCSNI
EIGSYAYRYL CNTSSRTDLN YLQGVDGPIG RCFTLIGESG ERTFAISPGH MNQLRAESIP
EDVIAGASAL VLTSYLVRCK PGEPMPEATM KAIEYAKKYN VPVVLTLGTK FVIAENPQWW
QQFLKDHVSI LAMNEDEAEA LTGESDPLLA SDKALDWVDL VLCTAGPIGL YMAGFTEDEA
KRKTQHPLLP GAIAEFNQYE FSRAMRHKDC QNPLRVYSHI APYMGGPEKI MNTNGAGDGA
LAALLHDITA NSYHRSNVPN SSKHKFTWLT YSSLAQVCKY ANRVSYQVLN QHSPRLTRGL
PEREDSLEES YWDR
