METL6_HUMAN
ID METL6_HUMAN Reviewed; 284 AA.
AC Q8TCB7; Q96LU4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase METTL6 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:32923617, ECO:0000269|PubMed:34268557, ECO:0000269|PubMed:34862464, ECO:0000269|PubMed:34922197};
DE AltName: Full=Methyltransferase-like protein 6 {ECO:0000305};
DE Short=hMETTL6 {ECO:0000303|PubMed:34862464};
GN Name=METTL6 {ECO:0000303|PubMed:32923617, ECO:0000312|HGNC:HGNC:28343};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH SARS1.
RX PubMed=28655767; DOI=10.1074/jbc.m117.798298;
RA Xu L., Liu X., Sheng N., Oo K.S., Liang J., Chionh Y.H., Xu J., Ye F.,
RA Gao Y.G., Dedon P.C., Fu X.Y.;
RT "Three distinct 3-methylcytidine (m3C) methyltransferases modify tRNA and
RT mRNA in mice and humans.";
RL J. Biol. Chem. 292:14695-14703(2017).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32923617; DOI=10.1126/sciadv.aaz4551;
RA Ignatova V.V., Kaiser S., Ho J.S.Y., Bing X., Stolz P., Tan Y.X., Lee C.L.,
RA Gay F.P.H., Lastres P.R., Gerlini R., Rathkolb B., Aguilar-Pimentel A.,
RA Sanz-Moreno A., Klein-Rodewald T., Calzada-Wack J., Ibragimov E.,
RA Valenta M., Lukauskas S., Pavesi A., Marschall S., Leuchtenberger S.,
RA Fuchs H., Gailus-Durner V., de Angelis M.H., Bultmann S., Rando O.J.,
RA Guccione E., Kellner S.M., Schneider R.;
RT "METTL6 is a tRNA m3C methyltransferase that regulates pluripotency and
RT tumor cell growth.";
RL Sci. Adv. 6:eaaz4551-eaaz4551(2020).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SARS1.
RX PubMed=34268557; DOI=10.1093/nar/gkab603;
RA Mao X.L., Li Z.H., Huang M.H., Wang J.T., Zhou J.B., Li Q.R., Xu H.,
RA Wang X.J., Zhou X.L.;
RT "Mutually exclusive substrate selection strategy by human m3C RNA
RT transferases METTL2A and METTL6.";
RL Nucleic Acids Res. 49:8309-8323(2021).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=34922197; DOI=10.1016/j.bbrc.2021.12.013;
RA Li S., Zhou H., Liao S., Wang X., Zhu Z., Zhang J., Xu C.;
RT "Structural basis for METTL6-mediated m3C RNA methylation.";
RL Biochem. Biophys. Res. Commun. 589:159-164(2021).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF TYR-49; HIS-61; GLU-85; CYS-93; ASP-110; PHE-111; SER-161
RP AND THR-217.
RX PubMed=34862464; DOI=10.1038/s42003-021-02890-9;
RA Chen R., Zhou J., Liu L., Mao X.L., Zhou X., Xie W.;
RT "Crystal structure of human METTL6, the m3C methyltransferase.";
RL Commun. Biol. 4:1361-1361(2021).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates N(3)-methylcytidine modification of residue 32 of the tRNA
CC anticodon loop of tRNA(Ser), including tRNA(Ser)(UGA) and
CC tRNA(Ser)(GCU) (PubMed:32923617, PubMed:34922197, PubMed:34268557,
CC PubMed:34862464). Interaction with SARS1/SerRS is required for N(3)-
CC methylcytidine methylation (PubMed:34268557).
CC {ECO:0000269|PubMed:32923617, ECO:0000269|PubMed:34268557,
CC ECO:0000269|PubMed:34862464, ECO:0000269|PubMed:34922197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:32923617, ECO:0000269|PubMed:34268557,
CC ECO:0000269|PubMed:34862464, ECO:0000269|PubMed:34922197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50957;
CC Evidence={ECO:0000269|PubMed:32923617, ECO:0000269|PubMed:34268557,
CC ECO:0000269|PubMed:34862464, ECO:0000269|PubMed:34922197};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 uM for tRNA(Ser) {ECO:0000269|PubMed:34922197};
CC KM=0.68 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:34922197};
CC Note=kcat is 7200 min(-1) for tRNA(Ser) (PubMed:34922197). kcat is
CC 7100 min(-1) for S-adenosyl-L-methionine (PubMed:34922197).
CC {ECO:0000269|PubMed:34922197};
CC -!- SUBUNIT: Monomer (PubMed:34862464). Interacts with SARS1/SerRS;
CC interaction is mediated via tRNA(Ser) and is required for N(3)-
CC methylcytidine methylation (PubMed:28655767, PubMed:34268557).
CC {ECO:0000269|PubMed:28655767, ECO:0000269|PubMed:34268557,
CC ECO:0000269|PubMed:34862464}.
CC -!- INTERACTION:
CC Q8TCB7; O95872: GPANK1; NbExp=3; IntAct=EBI-17861723, EBI-751540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34268557}. Nucleus
CC {ECO:0000269|PubMed:34268557}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TCB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCB7-2; Sequence=VSP_008480;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22400.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK057791; BAB71574.1; -; mRNA.
DR EMBL; AC027125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022400; AAH22400.1; ALT_SEQ; mRNA.
DR CCDS; CCDS43056.1; -. [Q8TCB7-1]
DR CCDS; CCDS87051.1; -. [Q8TCB7-2]
DR RefSeq; NP_001288721.1; NM_001301792.1.
DR RefSeq; NP_001317591.1; NM_001330662.1. [Q8TCB7-2]
DR RefSeq; NP_689609.2; NM_152396.3. [Q8TCB7-1]
DR RefSeq; XP_005264924.1; XM_005264867.3. [Q8TCB7-1]
DR RefSeq; XP_005264927.1; XM_005264870.4.
DR RefSeq; XP_006713033.1; XM_006712970.3. [Q8TCB7-1]
DR RefSeq; XP_016861207.1; XM_017005718.1. [Q8TCB7-1]
DR PDB; 7EZG; X-ray; 1.90 A; A=1-284.
DR PDB; 7F1E; X-ray; 2.59 A; A/B=1-284.
DR PDBsum; 7EZG; -.
DR PDBsum; 7F1E; -.
DR AlphaFoldDB; Q8TCB7; -.
DR SMR; Q8TCB7; -.
DR BioGRID; 126301; 17.
DR IntAct; Q8TCB7; 9.
DR STRING; 9606.ENSP00000407613; -.
DR iPTMnet; Q8TCB7; -.
DR PhosphoSitePlus; Q8TCB7; -.
DR BioMuta; METTL6; -.
DR DMDM; 269849620; -.
DR EPD; Q8TCB7; -.
DR jPOST; Q8TCB7; -.
DR MassIVE; Q8TCB7; -.
DR MaxQB; Q8TCB7; -.
DR PaxDb; Q8TCB7; -.
DR PeptideAtlas; Q8TCB7; -.
DR PRIDE; Q8TCB7; -.
DR ProteomicsDB; 74111; -. [Q8TCB7-1]
DR ProteomicsDB; 74112; -. [Q8TCB7-2]
DR Antibodypedia; 26744; 126 antibodies from 22 providers.
DR DNASU; 131965; -.
DR Ensembl; ENST00000383789.9; ENSP00000373299.5; ENSG00000206562.12. [Q8TCB7-2]
DR Ensembl; ENST00000383790.8; ENSP00000373300.3; ENSG00000206562.12. [Q8TCB7-1]
DR Ensembl; ENST00000443029.5; ENSP00000407613.1; ENSG00000206562.12. [Q8TCB7-1]
DR GeneID; 131965; -.
DR KEGG; hsa:131965; -.
DR MANE-Select; ENST00000383790.8; ENSP00000373300.3; NM_152396.4; NP_689609.2.
DR UCSC; uc003bzs.2; human. [Q8TCB7-1]
DR CTD; 131965; -.
DR DisGeNET; 131965; -.
DR GeneCards; METTL6; -.
DR HGNC; HGNC:28343; METTL6.
DR HPA; ENSG00000206562; Low tissue specificity.
DR MIM; 618903; gene.
DR neXtProt; NX_Q8TCB7; -.
DR OpenTargets; ENSG00000206562; -.
DR PharmGKB; PA142671462; -.
DR VEuPathDB; HostDB:ENSG00000206562; -.
DR eggNOG; KOG2361; Eukaryota.
DR GeneTree; ENSGT00940000156679; -.
DR HOGENOM; CLU_029724_2_2_1; -.
DR InParanoid; Q8TCB7; -.
DR OMA; PEFKANK; -.
DR OrthoDB; 987359at2759; -.
DR PhylomeDB; Q8TCB7; -.
DR TreeFam; TF321001; -.
DR PathwayCommons; Q8TCB7; -.
DR SignaLink; Q8TCB7; -.
DR BioGRID-ORCS; 131965; 7 hits in 1076 CRISPR screens.
DR GenomeRNAi; 131965; -.
DR Pharos; Q8TCB7; Tdark.
DR PRO; PR:Q8TCB7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8TCB7; protein.
DR Bgee; ENSG00000206562; Expressed in body of pancreas and 152 other tissues.
DR ExpressionAtlas; Q8TCB7; baseline and differential.
DR Genevisible; Q8TCB7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR026113; MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809; PTHR22809; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR PIRSF; PIRSF037755; Mettl2_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..284
FT /note="tRNA N(3)-methylcytidine methyltransferase METTL6"
FT /id="PRO_0000204454"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT BINDING 49
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 49
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT BINDING 61
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 85
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 87
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT BINDING 110
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT BINDING 136
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT BINDING 137
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT BINDING 157
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:34862464,
FT ECO:0007744|PDB:7EZG"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:34922197,
FT ECO:0007744|PDB:7F1E"
FT VAR_SEQ 178..284
FT /note="VLKPGKSVLFRDYGLYDHAMLRFKASSKLGENFYVRQDGTRSYFFTDDFLAQ
FT LFMDTGYEEVVNEYVFRETVNKKEGLCVPRVFLQSKFLKPPKNPSPVVLGLDPKS ->
FT CHGCSSELRQPWDKDDFAVTWDPWSPAIRVLLCHSGWSAVAWTWLTAASTSWAQAVLPP
FT QPLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008480"
FT MUTAGEN 49
FT /note="Y->F: Decreased affinity for S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 61
FT /note="H->N: Decreased affinity for S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 85
FT /note="E->Q: Strongly decreased affinity for S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 93
FT /note="C->S: Does not affect affinity for S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 110
FT /note="D->A: Nearly abolished affinity for S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 111
FT /note="F->L: Decreased affinity for S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 161
FT /note="S->A: Strongly reduced RNA (cytosine-3-)-
FT methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:34862464"
FT MUTAGEN 217
FT /note="T->A: Strongly reduced RNA (cytosine-3-)-
FT methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:34862464"
FT CONFLICT 67
FT /note="F -> L (in Ref. 1; BAB71574)"
FT /evidence="ECO:0000305"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:7F1E"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:7EZG"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:7EZG"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 179..191
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:7F1E"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7EZG"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:7EZG"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:7EZG"
SQ SEQUENCE 284 AA; 33251 MW; 445CAAE4D669B07F CRC64;
MASLQRKGLQ ARILTSEEEE KLKRDQTLVS DFKQQKLEQE AQKNWDLFYK RNSTNFFKDR
HWTTREFEEL RSCREFEDQK LTMLEAGCGV GNCLFPLLEE DPNIFAYACD FSPRAIEYVK
QNPLYDTERC KVFQCDLTKD DLLDHVPPES VDVVMLIFVL SAVHPDKMHL VLQNIYKVLK
PGKSVLFRDY GLYDHAMLRF KASSKLGENF YVRQDGTRSY FFTDDFLAQL FMDTGYEEVV
NEYVFRETVN KKEGLCVPRV FLQSKFLKPP KNPSPVVLGL DPKS
