ID METH_HUMAN Reviewed; 1265 AA.
AC Q99707; A1L4N8; A9Z1W4; B9EGF7; Q99713; Q99723;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 01-MAY-2013, entry version 135.
DE RecName: Full=Methionine synthase;
DE EC=2.1.1.13;
DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE AltName: Full=Vitamin-B12 dependent methionine synthase;
DE Short=MS;
GN Name=MTR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CBLG ILE-881 DEL AND ASP-920.
RC TISSUE=Fibroblast;
RX PubMed=8968737; DOI=10.1093/hmg/5.12.1867;
RA Leclerc D., Campeau E., Goyette P., Adjalla C.E., Christensen B.,
RA Ross M., Eydoux P., Rosenblatt D.S., Rozen R., Gravel R.A.;
RT "Human methionine synthase: cDNA cloning and identification of
RT mutations in patients of the cblG complementation group of
RT folate/cobalamin disorders.";
RL Hum. Mol. Genet. 5:1867-1874(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8968735; DOI=10.1093/hmg/5.12.1851;
RA Li Y.N., Gulati S., Baker P.J., Brody L.C., Banerjee R., Kruger W.D.;
RT "Cloning, mapping and RNA analysis of the human methionine synthase
RT gene.";
RL Hum. Mol. Genet. 5:1851-1858(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS TYR-255 AND GLY-919.
RC TISSUE=Fetal liver;
RX PubMed=9013615; DOI=10.1074/jbc.272.6.3444;
RA Chen L.H., Liu M.-L., Hwang H.-Y., Chen L.-S., Korenberg J., Shane B.;
RT "Human methionine synthase. cDNA cloning, gene localization, and
RT expression.";
RL J. Biol. Chem. 272:3628-3634(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-919.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP VARIANTS CBLG ILE-881 DEL AND LEU-1173, AND VARIANT LYS-61.
RX PubMed=8968736; DOI=10.1093/hmg/5.12.1859;
RA Gulati S., Baker P.J., Li Y.N., Fowler B., Kruger W.D., Brody L.C.,
RA Banerjee R.;
RT "Defects in human methionine synthase in cblG patients.";
RL Hum. Mol. Genet. 5:1859-1865(1996).
RN [9]
RP ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
RX PubMed=12375236; DOI=10.1086/344209;
RA Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S.,
RA Mitchell L.E.;
RT "Maternal genetic effects, exerted by genes involved in homocysteine
RT remethylation, influence the risk of spina bifida.";
RL Am. J. Hum. Genet. 71:1222-1226(2002).
RN [10]
RP NO ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
RX PubMed=15979034; DOI=10.1016/j.ymgme.2005.02.003;
RA O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C.,
RA Conley M., Weiler A., Peng K., Shane B., Scott J.M.,
RA Parle-McDermott A., Molloy A.M., Brody L.C.;
RT "Analysis of methionine synthase reductase polymorphisms for neural
RT tube defects risk association.";
RL Mol. Genet. Metab. 85:220-227(2005).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC methionine. Subsequently, remethylates the cofactor using
CC methyltetrahydrofolate (By similarity).
CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine =
CC tetrahydrofolate + L-methionine.
CC -!- COFACTOR: Methylcobalamin (MeCBL).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC novo pathway; L-methionine from L-homocysteine (MetH route): step
CC 1/1.
CC -!- INTERACTION:
CC Q15714:TSC22D1; NbExp=1; IntAct=EBI-1045782, EBI-712609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at the highest
CC levels in pancreas, heart, brain, skeletal muscle and placenta.
CC Expressed at lower levels in lung, liver and kidney.
CC -!- DOMAIN: Modular enzyme with four functionally distinct domains.
CC The isolated Hcy-binding domain catalyzes methyl transfer from
CC free methylcobalamin to homocysteine. The Hcy-binding domain in
CC association with the pterin-binding domain catalyzes the
CC methylation of cob(I)alamin by methyltetrahydrofolate and the
CC methylation of homocysteine. The B12-binding domain binds the
CC cofactor. The AdoMet activation domain binds S-adenosyl-L-
CC methionine. Under aerobic conditions cob(I)alamin can be converted
CC to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-
CC methionine and flavodoxin regenerates methylcobalamin (By
CC similarity).
CC -!- DISEASE: Methylcobalamin deficiency type G (cblG) [MIM:250940]:
CC Autosomal recessive inherited disease that causes mental
CC retardation, macrocytic anemia, and homocystinuria. Mild
CC deficiency in MS activity could be associated with mild
CC hyperhomocysteinemia, a risk factor for cardiovascular disease and
CC possibly neural tube defects. MS mutations could also be involved
CC in tumorigenesis. Note=The disease is caused by mutations
CC affecting the gene represented in this entry.
CC -!- DISEASE: Folate-sensitive neural tube defects (FS-NTD)
CC [MIM:601634]: The most common NTDs are open spina bifida
CC (myelomeningocele) and anencephaly. Note=Disease susceptibility is
CC associated with variations affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom (By
CC similarity).
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine
CC synthase family.
CC -!- SIMILARITY: Contains 1 AdoMet activation domain.
CC -!- SIMILARITY: Contains 1 B12-binding domain.
CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain.
CC -!- SIMILARITY: Contains 1 Hcy-binding domain.
CC -!- SIMILARITY: Contains 1 pterin-binding domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=5-methyltetrahydrofolate-
CC homocysteine methyltransferase entry;
CC URL="http://en.wikipedia.org/wiki/5-Methyltetrahydrofolate-homocysteine_methyltransferase";
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DR EMBL; U71285; AAC51188.1; -; mRNA.
DR EMBL; U75743; AAB58906.1; -; mRNA.
DR EMBL; U73338; AAB39704.1; -; mRNA.
DR EMBL; AL359185; CAH73198.1; -; Genomic_DNA.
DR EMBL; AL359259; CAH73198.1; JOINED; Genomic_DNA.
DR EMBL; AL359259; CAH70983.1; -; Genomic_DNA.
DR EMBL; AL359185; CAH70983.1; JOINED; Genomic_DNA.
DR EMBL; CH471098; EAW70066.1; -; Genomic_DNA.
DR EMBL; BC130616; AAI30617.1; -; mRNA.
DR EMBL; BC136440; AAI36441.1; -; mRNA.
DR IPI; IPI00743284; -.
DR RefSeq; NP_000245.2; NM_000254.2.
DR UniGene; Hs.498187; -.
DR PDB; 2O2K; X-ray; 1.60 A; A/B=925-1265.
DR PDBsum; 2O2K; -.
DR ProteinModelPortal; Q99707; -.
DR IntAct; Q99707; 1.
DR STRING; 9606.ENSP00000355536; -.
DR PhosphoSite; Q99707; -.
DR DMDM; 2842762; -.
DR PaxDb; Q99707; -.
DR PRIDE; Q99707; -.
DR Ensembl; ENST00000366577; ENSP00000355536; ENSG00000116984.
DR GeneID; 4548; -.
DR KEGG; hsa:4548; -.
DR UCSC; uc001hyi.4; human.
DR CTD; 4548; -.
DR GeneCards; GC01P236958; -.
DR HGNC; HGNC:7468; MTR.
DR HPA; HPA044474; -.
DR MIM; 156570; gene.
DR MIM; 250940; phenotype.
DR MIM; 601634; phenotype.
DR MIM; 603174; phenotype.
DR neXtProt; NX_Q99707; -.
DR Orphanet; 2170; Methylcobalamin deficiency type cblG.
DR Orphanet; 3388; Neural tube defect.
DR PharmGKB; PA31272; -.
DR eggNOG; COG1410; -.
DR HOGENOM; HOG000251409; -.
DR HOVERGEN; HBG006347; -.
DR InParanoid; Q99707; -.
DR KO; K00548; -.
DR OMA; VRKEFWG; -.
DR OrthoDB; EOG41JZBC; -.
DR PhylomeDB; Q99707; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00051; UER00081.
DR ChiTaRS; MTR; human.
DR DrugBank; DB00200; Hydroxocobalamin.
DR DrugBank; DB00134; L-Methionine.
DR DrugBank; DB00116; Tetrahydrofolic acid.
DR EvolutionaryTrace; Q99707; -.
DR GenomeRNAi; 4548; -.
DR NextBio; 17533; -.
DR ArrayExpress; Q99707; -.
DR Bgee; Q99707; -.
DR CleanEx; HS_MTR; -.
DR Genevestigator; Q99707; -.
DR GermOnline; ENSG00000116984; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008898; F:homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008705; F:methionine synthase activity; IEA:EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0032259; P:methylation; TAS:Reactome.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 1.10.1240.10; -; 1.
DR Gene3D; 3.10.196.10; -; 1.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.20.20.330; -; 1.
DR Gene3D; 3.40.50.280; -; 1.
DR InterPro; IPR003759; Cbl-bd_cap.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR011822; MetH.
DR InterPro; IPR000489; Pterin-binding.
DR InterPro; IPR003726; S_MeTrfase.
DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR PANTHER; PTHR21091:SF9; PTHR21091:SF9; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF02607; B12-binding_2; 1.
DR Pfam; PF02965; Met_synt_B12; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF000381; MetH; 1.
DR SMART; SM01018; B12-binding_2; 1.
DR SUPFAM; SSF52242; Cbl-bd; 1.
DR SUPFAM; SSF51717; DHP_synth_like; 1.
DR SUPFAM; SSF56507; Met_synth_B12; 1.
DR SUPFAM; SSF47644; Met_synth_Cbl-bd; 1.
DR SUPFAM; SSF82282; S_methyl_trans; 1.
DR TIGRFAMs; TIGR02082; metH; 1.
DR PROSITE; PS50974; ADOMET_ACTIVATION; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51337; B12_BINDING_NTER; 1.
DR PROSITE; PS50970; HCY; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cobalamin; Cobalt;
KW Complete proteome; Cytoplasm; Disease mutation; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Polymorphism;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
KW Zinc.
FT CHAIN 1 1265 Methionine synthase.
FT /FTId=PRO_0000204530.
FT DOMAIN 19 338 Hcy-binding.
FT DOMAIN 371 632 Pterin-binding.
FT DOMAIN 662 759 B12-binding N-terminal.
FT DOMAIN 772 907 B12-binding.
FT DOMAIN 923 1265 AdoMet activation.
FT REGION 860 861 Cobalamin-binding (By similarity).
FT REGION 1227 1228 S-adenosyl-L-methionine binding (By
FT similarity).
FT METAL 260 260 Zinc (By similarity).
FT METAL 323 323 Zinc (By similarity).
FT METAL 324 324 Zinc (By similarity).
FT METAL 785 785 Cobalt (cobalamin axial ligand) (By
FT similarity).
FT BINDING 830 830 Cobalamin (By similarity).
FT BINDING 974 974 S-adenosyl-L-methionine (By similarity).
FT BINDING 1172 1172 S-adenosyl-L-methionine; via carbonyl
FT oxygen (By similarity).
FT BINDING 1176 1176 Cobalamin; via carbonyl oxygen (By
FT similarity).
FT VARIANT 52 52 R -> Q (in dbSNP:rs12749581).
FT /FTId=VAR_050033.
FT VARIANT 61 61 R -> K.
FT /FTId=VAR_004326.
FT VARIANT 255 255 C -> Y.
FT /FTId=VAR_004327.
FT VARIANT 314 314 D -> N (in dbSNP:rs2229274).
FT /FTId=VAR_061338.
FT VARIANT 881 881 Missing (in cblG).
FT /FTId=VAR_004328.
FT VARIANT 919 919 D -> G (may be associated with
FT susceptibility to FS-NTD;
FT dbSNP:rs1805087).
FT /FTId=VAR_004329.
FT VARIANT 920 920 H -> D (in cblG; dbSNP:rs28933097).
FT /FTId=VAR_004330.
FT VARIANT 1173 1173 P -> L (in cblG).
FT /FTId=VAR_004331.
FT HELIX 932 937
FT HELIX 944 946
FT STRAND 956 962
FT HELIX 966 970
FT HELIX 976 987
FT HELIX 995 998
FT HELIX 1005 1022
FT STRAND 1026 1040
FT STRAND 1043 1046
FT HELIX 1053 1055
FT STRAND 1059 1063
FT HELIX 1082 1085
FT HELIX 1089 1091
FT STRAND 1095 1106
FT HELIX 1107 1116
FT HELIX 1120 1147
FT TURN 1152 1155
FT HELIX 1160 1164
FT STRAND 1168 1171
FT HELIX 1185 1192
FT HELIX 1195 1199
FT STRAND 1209 1220
FT HELIX 1235 1245
FT HELIX 1249 1255
FT HELIX 1257 1259
SQ SEQUENCE 1265 AA; 140527 MW; B04C26BCBE9A57C2 CRC64;
MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA
RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC
SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA
KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT
GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET
PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL
EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG
MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD
FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI
LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY
HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV
IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG
DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV
KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM
IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV
FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL
ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY
CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE
LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL
GYDTD
//
