MCE1_YEAST
ID MCE1_YEAST Reviewed; 459 AA.
AC Q01159; D6VU18; Q9URD1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=mRNA-capping enzyme subunit alpha;
DE AltName: Full=GTP--RNA guanylyltransferase;
DE Short=GTase;
DE AltName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50 {ECO:0000269|PubMed:6094533};
GN Name=CEG1; OrderedLocusNames=YGL130W; ORFNames=G2853;
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=DBY939;
RX PubMed=1315757; DOI=10.1016/s0021-9258(19)50122-3;
RA Shibagaki Y., Itoh N., Yamada H., Nagata S., Mizumoto K.;
RT "mRNA capping enzyme. Isolation and characterization of the gene encoding
RT mRNA guanylytransferase subunit from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:9521-9528(1992).
RN [2]
RP SEQUENCE REVISION TO 29-30.
RA Mizumoto K.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7500935; DOI=10.1007/bf00290360;
RA Yamagishi M., Mizumoto K., Ishihama A.;
RT "Isolation of temperature-sensitive mutants for mRNA capping enzyme in
RT Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 249:147-154(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8686378;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<145::aid-yea888>3.0.co;2-e;
RA Rodriguez-Belmonte E., Rodriguez Torres A.M., Tizon B., Cadahia J.L.,
RA Gonzalez-Siso I., Ramil E., Becerra M., Gonzalez-Dominguez M., Cerdan E.;
RT "Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII
RT reveals a novel member of the DnaJ family.";
RL Yeast 12:145-148(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
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 [7]
RP MUTAGENESIS.
RX PubMed=7991582; DOI=10.1073/pnas.91.25.12046;
RA Shuman S., Liu Y., Schwer B.;
RT "Covalent catalysis in nucleotidyl transfer reactions: essential motifs in
RT Saccharomyces cerevisiae RNA capping enzyme are conserved in
RT Schizosaccharomyces pombe and viral capping enzymes and among
RT polynucleotide ligases.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12046-12050(1994).
RN [8]
RP ACTIVE SITE, AND MUTAGENESIS OF LYS-59 AND LYS-70.
RX PubMed=8022828; DOI=10.1073/pnas.91.14.6624;
RA Fresco L.D., Buratowski S.;
RT "Active site of the mRNA-capping enzyme guanylyltransferase from
RT Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of
RT DNA and RNA ligases.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6624-6628(1994).
RN [9]
RP SUBUNIT.
RX PubMed=6389537; DOI=10.1016/s0021-9258(18)89833-7;
RA Itoh N., Mizumoto K., Kaziro Y.;
RT "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. I.
RT Purification and subunit structure.";
RL J. Biol. Chem. 259:13923-13929(1984).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RX PubMed=6094533; DOI=10.1016/s0021-9258(18)89834-9;
RA Itoh N., Mizumoto K., Kaziro Y.;
RT "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II.
RT Catalytic properties.";
RL J. Biol. Chem. 259:13930-13936(1984).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=3029058; DOI=10.1016/s0021-9258(18)61609-6;
RA Itoh N., Yamada H., Kaziro Y., Mizumoto K.;
RT "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large
RT scale purification, subunit functions, and subcellular localization.";
RL J. Biol. Chem. 262:1989-1995(1987).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Second step of mRNA capping. Transfer of the GMP moiety of
CC GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP
CC reaction intermediate. {ECO:0000269|PubMed:3029058,
CC ECO:0000269|PubMed:6094533}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000269|PubMed:6094533};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000269|PubMed:6094533};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for GTP {ECO:0000269|PubMed:6094533};
CC KM=4 uM for ppG-terminated RNA {ECO:0000269|PubMed:6094533};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:6094533};
CC -!- SUBUNIT: Heterodimer (PubMed:6389537, PubMed:3029058). The mRNA-capping
CC enzyme is composed of two separate chains alpha and beta, respectively
CC a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase
CC (PubMed:6389537, PubMed:3029058). {ECO:0000269|PubMed:3029058,
CC ECO:0000269|PubMed:6389537}.
CC -!- INTERACTION:
CC Q01159; O13297: CET1; NbExp=9; IntAct=EBI-10503, EBI-4473;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic GTase family. {ECO:0000305}.
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DR EMBL; D10263; BAA01103.1; -; Genomic_DNA.
DR EMBL; X87252; CAA60705.1; -; Genomic_DNA.
DR EMBL; Z72652; CAA96839.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07979.1; -; Genomic_DNA.
DR PIR; S59731; S59731.
DR RefSeq; NP_011385.3; NM_001180995.3.
DR PDB; 3KYH; X-ray; 3.00 A; C/D=1-459.
DR PDBsum; 3KYH; -.
DR AlphaFoldDB; Q01159; -.
DR SMR; Q01159; -.
DR BioGRID; 33121; 597.
DR ComplexPortal; CPX-580; mRNA cap methyltransferase complex.
DR DIP; DIP-2298N; -.
DR IntAct; Q01159; 27.
DR MINT; Q01159; -.
DR STRING; 4932.YGL130W; -.
DR iPTMnet; Q01159; -.
DR MaxQB; Q01159; -.
DR PaxDb; Q01159; -.
DR PRIDE; Q01159; -.
DR EnsemblFungi; YGL130W_mRNA; YGL130W; YGL130W.
DR GeneID; 852747; -.
DR KEGG; sce:YGL130W; -.
DR SGD; S000003098; CEG1.
DR VEuPathDB; FungiDB:YGL130W; -.
DR eggNOG; KOG2386; Eukaryota.
DR GeneTree; ENSGT00940000156953; -.
DR HOGENOM; CLU_021710_0_2_1; -.
DR InParanoid; Q01159; -.
DR OMA; KDYYVCE; -.
DR BioCyc; MetaCyc:G3O-30626-MON; -.
DR BioCyc; YEAST:G3O-30626-MON; -.
DR BRENDA; 2.7.7.50; 984.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR SABIO-RK; Q01159; -.
DR EvolutionaryTrace; Q01159; -.
DR PRO; PR:Q01159; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q01159; protein.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IGI:SGD.
DR GO; GO:0005634; C:nucleus; IPI:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IMP:SGD.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR017075; mRNA_cap_enzyme_alpha.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR PIRSF; PIRSF036959; mRNA_cap_alpha; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; mRNA capping; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..459
FT /note="mRNA-capping enzyme subunit alpha"
FT /id="PRO_0000210106"
FT REGION 415..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000269|PubMed:8022828"
FT MUTAGEN 57
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 58
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 59
FT /note="K->A,T,S,R: No effect."
FT /evidence="ECO:0000269|PubMed:8022828"
FT MUTAGEN 66
FT /note="Y->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 70
FT /note="K->A,R,M,I,T: Lethal."
FT /evidence="ECO:0000269|PubMed:8022828"
FT MUTAGEN 71
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 72
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 73
FT /note="G->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 95
FT /note="D->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 96
FT /note="R->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 97
FT /note="E->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 107..109
FT /note="RFP->AAA: Reduced growth at 25 degrees and lethal at
FT 37 degrees."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 114
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 115
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 116
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 117
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 118
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 129
FT /note="L->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 130
FT /note="D->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 131
FT /note="G->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 132
FT /note="E->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 134
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 218
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 219
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 225
FT /note="D->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 226
FT /note="G->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 241
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 242
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 249
FT /note="K->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 253
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 254
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 255
FT /note="T->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 257
FT /note="D->A: Lethal."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 274
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 275
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 276
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 395
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT MUTAGEN 396
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:7991582"
FT CONFLICT 45
FT /note="G -> S (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="D -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 126..137
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 144..156
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 224..235
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:3KYH"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:3KYH"
SQ SEQUENCE 459 AA; 52764 MW; F7F5A3E59EEFA15F CRC64;
MVLAMESRVA PEIPGLIQPG NVTQDLKMMV CKLLNSPKPT KTFPGSQPVS FQHSDVEEKL
LAHDYYVCEK TDGLRVLMFI VINPVTGEQG CFMIDRENNY YLVNGFRFPR LPQKKKEELL
ETLQDGTLLD GELVIQTNPM TKLQELRYLM FDCLAINGRC LTQSPTSSRL AHLGKEFFKP
YFDLRAAYPN RCTTFPFKIS MKHMDFSYQL VKVAKSLDKL PHLSDGLIFT PVKAPYTAGG
KDSLLLKWKP EQENTVDFKL ILDIPMVEDP SLPKDDRNRW YYNYDVKPVF SLYVWQGGAD
VNSRLKHFDQ PFDRKEFEIL ERTYRKFAEL SVSDEEWQNL KNLEQPLNGR IVECAKNQET
GAWEMLRFRD DKLNGNHTSV VQKVLESIND SVSLEDLEEI VGDIKRCWDE RRANMAGGSG
RPLPSQSQNA TLSTSKPVHS QPPSNDKEPK YVDEDDWSD
