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mRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) (RG7MT1) (mRNA (guanine-N(7)-)-methyltransferase) (mRNA cap methyltransferase) (hCMT1) (hMet) (hcm1p)

 MCES_HUMAN              Reviewed;         476 AA.
O43148; B0YJ90; D3DUJ5; O94996; Q9UIJ9;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=mRNA cap guanine-N7 methyltransferase;
EC=2.1.1.56 {ECO:0000269|PubMed:10347220, ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270, ECO:0000269|PubMed:9790902};
AltName: Full=RG7MT1;
AltName: Full=mRNA (guanine-N(7)-)-methyltransferase;
AltName: Full=mRNA cap methyltransferase;
Short=hCMT1;
Short=hMet;
Short=hcm1p;
Name=RNMT; Synonyms=KIAA0398;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=9790902; DOI=10.1006/bbrc.1998.9402;
Tsukamoto T., Shibagaki Y., Niikura Y., Kiyohisa M.;
"Cloning and characterization of three human cDNAs encoding mRNA
(guanine-7-)methyltransferase, an mRNA cap methylase.";
Biochem. Biophys. Res. Commun. 251:27-34(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
TISSUE SPECIFICITY, AND INTERACTION WITH POLYMERASE II AND RNGTT.
PubMed=9705270; DOI=10.1074/jbc.273.34.21443;
Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J.;
"Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA
polymerase IIo complexes.";
J. Biol. Chem. 273:21443-21446(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10589710;
Yamada-Okabe T., Mio T., Kashima Y., Matsui M., Arisawa M.,
Yamada-Okabe H.;
"The Candida albicans gene for mRNA 5'-cap methyltransferase:
identification of the additional residues essential for catalysis.";
Microbiology 145:3023-3033(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-203; ARG-239;
TYR-289; PHE-291 AND PHE-354.
PubMed=10347220; DOI=10.1074/jbc.274.23.16553;
Saha N., Schwer B., Shuman S.;
"Characterization of human, Schizosaccharomyces pombe, and Candida
albicans mRNA cap methyltransferases and complete replacement of the
yeast capping apparatus by mammalian enzymes.";
J. Biol. Chem. 274:16553-16562(1999).
[9]
SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH IMPORTIN
ALPHA.
PubMed=11114884; DOI=10.1101/gad.848200;
Wen Y., Shatkin A.J.;
"Cap methyltransferase selective binding and methylation of GpppG-RNA
are stimulated by importin-alpha.";
Genes Dev. 14:2944-2949(2000).
[10]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 80-LYS--LYS-83;
103-LYS--ARG-107 AND ARG-127.
PubMed=15767670; DOI=10.1128/MCB.25.7.2644-2649.2005;
Shafer B., Chu C., Shatkin A.J.;
"Human mRNA cap methyltransferase: alternative nuclear localization
signal motifs ensure nuclear localization required for viability.";
Mol. Cell. Biol. 25:2644-2649(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
FUNCTION, SUBUNIT, AND INTERACTION WITH RAM/FAM103A1.
PubMed=22099306; DOI=10.1016/j.molcel.2011.08.041;
Gonatopoulos-Pournatzis T., Dunn S., Bounds R., Cowling V.H.;
"RAM/Fam103a1 is required for mRNA cap methylation.";
Mol. Cell 44:585-596(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 165-476 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE.
Wu H., Lunin V.V., Zeng H., Antoshenko T., MacKenzie F., Weigelt J.,
Arrowsmith C.H., Edwards A.M., Bochkarev A., Min J., Plotnikov A.N.;
"The crystal structure of human RNA (guanine-7-) methyltransferase in
complex with SAH.";
Submitted (NOV-2007) to the PDB data bank.
[14]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 165-476.
Zeng H., Amaya M.F., Loppnau P., Bountra C., Weigelt J.,
Arrowsmith C.H., Edwards A.M., Botchkarev A., Min J., Plotnikov A.N.,
Wu H.;
"Crystal structure of mRNA cap guanine-N7 methyltransferase (RNMT) in
complex with sinefungin.";
Submitted (SEP-2008) to the PDB data bank.
[15]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 167-476 IN COMPLEX WITH
RAM/FAM103A1 AND S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, ENZYME
REGULATION, INTERACTION WITH RAM/FAM103A1, AND MUTAGENESIS OF TRP-178;
LYS-393; PHE-398; LYS-409; LYS-413; ALA-417; ARG-450 AND PRO-452.
PubMed=27422871; DOI=10.1093/nar/gkw637;
Varshney D., Petit A.P., Bueren-Calabuig J.A., Jansen C.,
Fletcher D.A., Peggie M., Weidlich S., Scullion P., Pisliakov A.V.,
Cowling V.H.;
"Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation
by RAM.";
Nucleic Acids Res. 44:10423-10436(2016).
-!- FUNCTION: Catalytic subunit of the mRNA-capping methyltransferase
RNMT:RAM/FAM103A1 complex that methylates the N7 position of the
added guanosine to the 5'-cap structure of mRNAs (PubMed:9790902,
PubMed:9705270, PubMed:10347220, PubMed:11114884, PubMed:22099306,
PubMed:27422871). Binds RNA containing 5'-terminal GpppC
(PubMed:11114884). {ECO:0000269|PubMed:10347220,
ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:22099306,
ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270,
ECO:0000269|PubMed:9790902}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00895, ECO:0000269|PubMed:10347220,
ECO:0000269|PubMed:27422871, ECO:0000269|PubMed:9705270,
ECO:0000269|PubMed:9790902}.
-!- ENZYME REGULATION: Methyltransferase activity is activated by
RAM/FAM103A1 (PubMed:27422871). {ECO:0000269|PubMed:27422871}.
-!- SUBUNIT: Interacts with importin alpha, leading to stimulate both
RNA-binding and methyltransferase activity (PubMed:11114884).
Interaction with importin alpha and beta is required for its
nuclear localization, importin beta dissociating in response to
RanGTP, allowing RNMT-importin alpha to bind RNA substrates
(PubMed:11114884). Interacts with elongating form of polymerase II
and RNGTT (PubMed:9705270). Interacts with RAM/FAM103A1, this
interaction significantly enhances RNA-binding and cap
methyltransferase activity (PubMed:22099306, Ref.14).
{ECO:0000269|PubMed:11114884, ECO:0000269|PubMed:22099306,
ECO:0000269|PubMed:9705270, ECO:0000269|Ref.14}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11114884,
ECO:0000269|PubMed:15767670}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=hCMT1a;
IsoId=O43148-1; Sequence=Displayed;
Name=2; Synonyms=hCMT1b;
IsoId=O43148-2; Sequence=VSP_020241;
-!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9705270,
ECO:0000269|PubMed:9790902}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. mRNA cap 0 methyltransferase
family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
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EMBL; AB022604; BAA74464.1; -; mRNA.
EMBL; AB022605; BAA74463.1; -; mRNA.
EMBL; AF067791; AAC63269.1; -; mRNA.
EMBL; AB020966; BAA82447.1; -; mRNA.
EMBL; AB007858; BAA23694.1; -; mRNA.
EMBL; EF445026; ACA06068.1; -; Genomic_DNA.
EMBL; CH471113; EAX01505.1; -; Genomic_DNA.
EMBL; CH471113; EAX01506.1; -; Genomic_DNA.
EMBL; BC036798; AAH36798.1; -; mRNA.
CCDS; CCDS11867.1; -. [O43148-1]
CCDS; CCDS77156.1; -. [O43148-2]
RefSeq; NP_001295192.1; NM_001308263.1. [O43148-2]
RefSeq; NP_003790.1; NM_003799.2. [O43148-1]
RefSeq; XP_005258219.1; XM_005258162.1. [O43148-1]
RefSeq; XP_016881550.1; XM_017026061.1. [O43148-2]
UniGene; Hs.592347; -.
PDB; 3BGV; X-ray; 2.30 A; A/B/C/D=165-476.
PDB; 3EPP; X-ray; 2.41 A; A/B=165-476.
PDB; 5E8J; X-ray; 2.35 A; A/B=167-476.
PDB; 5E9J; X-ray; 3.47 A; A/B=167-416, A/B=457-476.
PDB; 5E9W; X-ray; 2.28 A; A/B/C/D=167-476.
PDBsum; 3BGV; -.
PDBsum; 3EPP; -.
PDBsum; 5E8J; -.
PDBsum; 5E9J; -.
PDBsum; 5E9W; -.
ProteinModelPortal; O43148; -.
SMR; O43148; -.
BioGrid; 114269; 19.
IntAct; O43148; 8.
STRING; 9606.ENSP00000262173; -.
iPTMnet; O43148; -.
PhosphoSitePlus; O43148; -.
BioMuta; RNMT; -.
EPD; O43148; -.
MaxQB; O43148; -.
PaxDb; O43148; -.
PeptideAtlas; O43148; -.
PRIDE; O43148; -.
Ensembl; ENST00000262173; ENSP00000262173; ENSG00000101654. [O43148-1]
Ensembl; ENST00000383314; ENSP00000372804; ENSG00000101654. [O43148-1]
Ensembl; ENST00000543302; ENSP00000446426; ENSG00000101654. [O43148-1]
Ensembl; ENST00000589866; ENSP00000466252; ENSG00000101654. [O43148-1]
Ensembl; ENST00000592764; ENSP00000466111; ENSG00000101654. [O43148-2]
GeneID; 8731; -.
KEGG; hsa:8731; -.
UCSC; uc002ksk.2; human. [O43148-1]
CTD; 8731; -.
DisGeNET; 8731; -.
EuPathDB; HostDB:ENSG00000101654.17; -.
GeneCards; RNMT; -.
HGNC; HGNC:10075; RNMT.
HPA; HPA039409; -.
MIM; 603514; gene.
neXtProt; NX_O43148; -.
OpenTargets; ENSG00000101654; -.
PharmGKB; PA34448; -.
eggNOG; KOG1975; Eukaryota.
eggNOG; ENOG410Y7HG; LUCA.
GeneTree; ENSGT00390000002368; -.
HOVERGEN; HBG081963; -.
InParanoid; O43148; -.
KO; K00565; -.
OMA; LNLVSCQ; -.
OrthoDB; EOG091G0C9Y; -.
PhylomeDB; O43148; -.
TreeFam; TF314347; -.
BioCyc; MetaCyc:HS02296-MONOMER; -.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
ChiTaRS; RNMT; human.
EvolutionaryTrace; O43148; -.
GeneWiki; MRNA_(guanine-N7-)-methyltransferase; -.
GeneWiki; RNMT; -.
GenomeRNAi; 8731; -.
PRO; PR:O43148; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000101654; -.
CleanEx; HS_RNMT; -.
ExpressionAtlas; O43148; baseline and differential.
Genevisible; O43148; HS.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0031533; C:mRNA cap methyltransferase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR016899; mRNA_G-N7_MeTrfase.
InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF03291; Pox_MCEL; 1.
PIRSF; PIRSF028762; ABD1; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51562; RNA_CAP0_MT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Methyltransferase; mRNA capping; mRNA processing; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 476 mRNA cap guanine-N7 methyltransferase.
/FTId=PRO_0000248321.
DOMAIN 128 476 mRNA cap 0 methyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
REGION 176 177 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
MOTIF 126 128 Nuclear localization signal.
BINDING 180 180 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3BGV,
ECO:0000244|PDB:5E9J,
ECO:0000244|PDB:5E9W,
ECO:0000255|PROSITE-ProRule:PRU00895,
ECO:0000269|PubMed:27422871}.
BINDING 205 205 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3BGV,
ECO:0000244|PDB:5E9J,
ECO:0000244|PDB:5E9W,
ECO:0000255|PROSITE-ProRule:PRU00895,
ECO:0000269|PubMed:27422871}.
BINDING 227 227 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3BGV,
ECO:0000244|PDB:5E9J,
ECO:0000244|PDB:5E9W,
ECO:0000255|PROSITE-ProRule:PRU00895,
ECO:0000269|PubMed:27422871}.
BINDING 261 261 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000244|PDB:3BGV,
ECO:0000244|PDB:5E9J,
ECO:0000244|PDB:5E9W,
ECO:0000269|PubMed:27422871}.
BINDING 284 284 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:3BGV,
ECO:0000244|PDB:5E9J,
ECO:0000244|PDB:5E9W,
ECO:0000269|PubMed:27422871}.
BINDING 288 288 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 289 289 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3BGV,
ECO:0000244|PDB:5E9J,
ECO:0000244|PDB:5E9W,
ECO:0000269|PubMed:27422871}.
BINDING 370 370 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 467 467 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 208 208 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 214 214 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 239 239 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D0L8}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D0L8}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2U7}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2U7}.
VAR_SEQ 465 476 SIYLVFAFEKQQ -> RLTVTIMREAWLSTVGPGRAPVAAS
SVKWGTPRPAMQFIL (in isoform 2).
{ECO:0000303|PubMed:9790902}.
/FTId=VSP_020241.
MUTAGEN 80 83 KKRK->AAAA: Does not abolish nuclear
localization. Abolishes nuclear
localization; when associated with 103-
AAAAA-107 and I-127.
{ECO:0000269|PubMed:15767670}.
MUTAGEN 103 107 KKRKR->AAAAA: Does not abolish nuclear
localization. Abolishes nuclear
localization; when associated with 80-
AAAA-83 and I-127.
{ECO:0000269|PubMed:15767670}.
MUTAGEN 127 127 R->I: Does not abolish nuclear
localization. Abolishes nuclear
localization; when associated with 80-
AAAA-83 and 103-AAAAA-107.
{ECO:0000269|PubMed:15767670}.
MUTAGEN 178 178 W->C: Loss of methyltransferase activity
in presence or absence of RAM/FAM103A1;
when associated with C-417. Complete
restored RAM/FAM103A1-mediated
methyltransferase activity under reducing
conditions; when associated with C-417.
Loss of methyltransferase activity in
presence or absence of RAM/FAM103A1; when
associated with C-417; C-393 and C-398.
Partially restored RAM/FAM103A1-mediated
methyltransferase activity under reducing
conditions; when associated with C-417;
C-393 and C-398.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 203 203 D->A: Loss of activity.
{ECO:0000269|PubMed:10347220}.
MUTAGEN 239 239 R->A: Loss of activity.
{ECO:0000269|PubMed:10347220}.
MUTAGEN 289 289 Y->A: Loss of activity.
{ECO:0000269|PubMed:10347220}.
MUTAGEN 291 291 F->A: Strongly impairs enzyme activity.
{ECO:0000269|PubMed:10347220}.
MUTAGEN 354 354 F->A: Loss of activity.
{ECO:0000269|PubMed:10347220}.
MUTAGEN 393 393 K->C: Loss of methyltransferase activity
in presence or absence of RAM/FAM103A1;
when associated with C-178; C-398 and C-
417. Partially restored RAM/FAM103A1-
mediated methyltransferase activity under
reducing conditions; when associated with
C-178; C-398 and C-417.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 398 398 F->C: Loss of methyltransferase activity
in presence or absence of RAM/FAM103A1;
when associated with C-178; C-393 and C-
417. Partially restored RAM/FAM103A1-
mediated methyltransferase activity under
reducing conditions; when associated with
C-178; C-393 and C-417.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 409 409 K->E: Decreased S-adenosyl-L-methionine
binding and methyltransferase activity in
absence of RAM/FAM103A1; when associated
with E-413. Decreased interaction with
RAM/FAM103A1; when associated with E-413.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 413 413 K->E: Decreased S-adenosyl-L-methionine
binding and methyltransferase activity in
absence of RAM/FAM103A1; when associated
with E-409. Decreased interaction with
RAM/FAM103A1; when associated with E-409.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 417 417 A->C: Loss of methyltransferase activity
in presence or absence of RAM/FAM103A1;
when associated with C-178. Complete
restored RAM/FAM103A1-mediated
methyltransferase activity under reducing
conditions; when associated with C-178.
Loss of methyltransferase activity in
presence or absence of RAM/FAM103A1; when
associated with C-178. Loss of
methyltransferase activity in presence or
absence of RAM/FAM103A1; when associated
with C-178; C-393 and C-398. Partially
restored RAM/FAM103A1-mediated
methyltransferase activity under reducing
conditions; when associated with C-178;
C-393 and C-398.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 450 450 R->E: Increased S-adenosyl-L-methionine
binding and methyltransferase activity in
absence of RAM/FAM103A1; when associated
with E-452. No change in interaction with
RAM/FAM103A1; when associated with E-452.
{ECO:0000269|PubMed:27422871}.
MUTAGEN 452 452 P->E: Increased S-adenosyl-L-methionine
binding and methyltransferase activity in
absence of RAM/FAM103A1; when associated
with E-450. No change in interaction with
RAM/FAM103A1; when associated with E-450.
{ECO:0000269|PubMed:27422871}.
CONFLICT 179 179 M -> I (in Ref. 3; BAA82447).
{ECO:0000305}.
HELIX 170 193 {ECO:0000244|PDB:5E9W}.
STRAND 200 204 {ECO:0000244|PDB:5E9W}.
TURN 207 211 {ECO:0000244|PDB:5E9W}.
HELIX 212 217 {ECO:0000244|PDB:5E9W}.
STRAND 221 228 {ECO:0000244|PDB:5E9W}.
HELIX 230 244 {ECO:0000244|PDB:5E9W}.
STRAND 245 248 {ECO:0000244|PDB:5E9W}.
STRAND 254 259 {ECO:0000244|PDB:5E9W}.
TURN 262 264 {ECO:0000244|PDB:5E9W}.
HELIX 267 269 {ECO:0000244|PDB:5E9W}.
STRAND 271 273 {ECO:0000244|PDB:5E8J}.
STRAND 278 285 {ECO:0000244|PDB:5E9W}.
HELIX 287 292 {ECO:0000244|PDB:5E9W}.
HELIX 294 305 {ECO:0000244|PDB:5E9W}.
STRAND 308 319 {ECO:0000244|PDB:5E9W}.
HELIX 321 330 {ECO:0000244|PDB:5E9W}.
STRAND 331 337 {ECO:0000244|PDB:5E9W}.
STRAND 339 346 {ECO:0000244|PDB:5E9W}.
STRAND 357 362 {ECO:0000244|PDB:5E9W}.
TURN 363 365 {ECO:0000244|PDB:5E8J}.
STRAND 368 371 {ECO:0000244|PDB:5E9W}.
HELIX 375 382 {ECO:0000244|PDB:5E9W}.
HELIX 383 385 {ECO:0000244|PDB:5E9W}.
STRAND 387 394 {ECO:0000244|PDB:5E9W}.
HELIX 395 402 {ECO:0000244|PDB:5E9W}.
HELIX 406 414 {ECO:0000244|PDB:5E9W}.
STRAND 418 422 {ECO:0000244|PDB:5E8J}.
TURN 434 437 {ECO:0000244|PDB:5E8J}.
HELIX 438 443 {ECO:0000244|PDB:5E8J}.
STRAND 453 456 {ECO:0000244|PDB:5E9W}.
HELIX 458 464 {ECO:0000244|PDB:5E9W}.
STRAND 467 474 {ECO:0000244|PDB:5E9W}.
SEQUENCE 476 AA; 54844 MW; EC919BC41BD5E2B3 CRC64;
MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK
EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG
DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK
SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY
EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM
LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF
NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP
YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ


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