METL5_HUMAN
ID METL5_HUMAN Reviewed; 209 AA.
AC Q9NRN9; D3DPC9; Q9NVX1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=rRNA N6-adenosine-methyltransferase METTL5 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:32217665, ECO:0000269|PubMed:33357433, ECO:0000269|PubMed:33428944, ECO:0000269|PubMed:35033535};
DE AltName: Full=Methyltransferase-like protein 5 {ECO:0000303|PubMed:31328227};
GN Name=METTL5 {ECO:0000303|PubMed:31328227, ECO:0000312|HGNC:HGNC:25006};
GN ORFNames=DC3 {ECO:0000303|Ref.1}, HSPC133;
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].
RC TISSUE=Dendritic cell;
RA Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene from human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [6]
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., Buerckstuemmer T.,
RA 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 [7]
RP INVOLVEMENT IN MRT72, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31564433; DOI=10.1016/j.ajhg.2019.09.007;
RA Richard E.M., Polla D.L., Assir M.Z., Contreras M., Shahzad M., Khan A.A.,
RA Razzaq A., Akram J., Tarar M.N., Blanpied T.A., Ahmed Z.M., Abou Jamra R.,
RA Wieczorek D., van Bokhoven H., Riazuddin S., Riazuddin S.;
RT "Bi-allelic variants in METTL5 cause autosomal-recessive intellectual
RT disability and microcephaly.";
RL Am. J. Hum. Genet. 105:869-878(2019).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33357433; DOI=10.1016/j.celrep.2020.108544;
RA Rong B., Zhang Q., Wan J., Xing S., Dai R., Li Y., Cai J., Xie J., Song Y.,
RA Chen J., Zhang L., Yan G., Zhang W., Gao H., Han J.J., Qu Q., Ma H.,
RA Tian Y., Lan F.;
RT "Ribosome 18S m6A methyltransferase METTL5 promotes translation initiation
RT and breast cancer cell growth.";
RL Cell Rep. 33:108544-108544(2020).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TRMT112.
RX PubMed=32217665; DOI=10.1101/gad.333369.119;
RA Ignatova V.V., Stolz P., Kaiser S., Gustafsson T.H., Lastres P.R.,
RA Sanz-Moreno A., Cho Y.L., Amarie O.V., Aguilar-Pimentel A.,
RA Klein-Rodewald T., Calzada-Wack J., Becker L., Marschall S., Kraiger M.,
RA Garrett L., Seisenberger C., Hoelter S.M., Borland K., Van De Logt E.,
RA Jansen P.W.T.C., Baltissen M.P., Valenta M., Vermeulen M., Wurst W.,
RA Gailus-Durner V., Fuchs H., de Angelis M.H., Rando O.J., Kellner S.M.,
RA Bultmann S., Schneider R.;
RT "The rRNA m6A methyltransferase METTL5 is involved in pluripotency and
RT developmental programs.";
RL Genes Dev. 34:715-729(2020).
RN [10]
RP INTERACTION WITH TRMT112.
RX PubMed=34948388; DOI=10.3390/ijms222413593;
RA Brumele B., Mutso M., Telanne L., Ounap K., Spunde K., Abroi A., Kurg R.;
RT "Human TRMT112-Methyltransferase Network Consists of Seven Partners
RT Interacting with a Common Co-Factor.";
RL Int. J. Mol. Sci. 22:13593-13593(2021).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND INTERACTION WITH TRMT112.
RX PubMed=33428944; DOI=10.1016/j.jbc.2021.100270;
RA Yu D., Kaur G., Blumenthal R.M., Zhang X., Cheng X.;
RT "Enzymatic characterization of three human RNA adenosine methyltransferases
RT reveals diverse substrate affinities and reaction optima.";
RL J. Biol. Chem. 296:100270-100270(2021).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TRMT112, MUTAGENESIS OF
RP 126-ASN--PRO-128, VARIANT ASP-61, AND CHARACTERIZATION OF VARIANT ASP-61.
RX PubMed=35033535; DOI=10.1016/j.jbc.2022.101590;
RA Sepich-Poore C., Zheng Z., Schmitt E., Wen K., Zhang Z.S., Cui X.L.,
RA Dai Q., Zhu A.C., Zhang L., Sanchez Castillo A., Tan H., Peng J.,
RA Zhuang X., He C., Nachtergaele S.;
RT "The METTL5-TRMT112 N6-methyladenosine methyltransferase complex regulates
RT mRNA translation via 18S rRNA methylation.";
RL J. Biol. Chem. 298:101590-101590(2022).
RN [13] {ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND TRMT112, FUNCTION, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH TRMT112.
RX PubMed=31328227; DOI=10.1093/nar/gkz619;
RA van Tran N., Ernst F.G.M., Hawley B.R., Zorbas C., Ulryck N., Hackert P.,
RA Bohnsack K.E., Bohnsack M.T., Jaffrey S.R., Graille M., Lafontaine D.L.J.;
RT "The human 18S rRNA m6A methyltransferase METTL5 is stabilized by
RT TRMT112.";
RL Nucleic Acids Res. 47:7719-7733(2019).
CC -!- FUNCTION: Catalytic subunit of a heterodimer with TRMT112, which
CC specifically methylates the 6th position of adenine in position 1832 of
CC 18S rRNA (PubMed:31328227, PubMed:32217665, PubMed:33357433,
CC PubMed:33428944, PubMed:35033535). N6-methylation of adenine(1832) in
CC 18S rRNA resides in the decoding center of 18S rRNA and is required for
CC translation and embryonic stem cells (ESCs) pluripotency and
CC differentiation (PubMed:33357433). {ECO:0000269|PubMed:31328227,
CC ECO:0000269|PubMed:32217665, ECO:0000269|PubMed:33357433,
CC ECO:0000269|PubMed:33428944, ECO:0000269|PubMed:35033535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(1832) in 18S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyladenosine(1832) in 18S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:62612, Rhea:RHEA-COMP:16144, Rhea:RHEA-COMP:16145,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:32217665,
CC ECO:0000269|PubMed:33357433, ECO:0000269|PubMed:33428944,
CC ECO:0000269|PubMed:35033535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62613;
CC Evidence={ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:32217665,
CC ECO:0000269|PubMed:33357433, ECO:0000269|PubMed:33428944,
CC ECO:0000269|PubMed:35033535};
CC -!- ACTIVITY REGULATION: rRNA N6-adenosine-methyltransferase activity is
CC inhibited by zinc. {ECO:0000269|PubMed:33428944}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for 18S rRNA {ECO:0000269|PubMed:33428944};
CC KM=1.0 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:33428944};
CC Note=kcat is 13.1 h(-1) for 18S rRNA (PubMed:33428944). kcat is 17.6
CC h(-1) for S-adenosyl-L-methionine (PubMed:33428944).
CC {ECO:0000269|PubMed:33428944};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with TRMT112.
CC {ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:32217665,
CC ECO:0000269|PubMed:33428944, ECO:0000269|PubMed:34948388,
CC ECO:0000269|PubMed:35033535}.
CC -!- INTERACTION:
CC Q9NRN9; Q9UI30: TRMT112; NbExp=3; IntAct=EBI-12360031, EBI-373326;
CC Q9NRN9; O15062: ZBTB5; NbExp=3; IntAct=EBI-12360031, EBI-722671;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31564433}. Presynapse
CC {ECO:0000269|PubMed:31564433}. Postsynapse
CC {ECO:0000269|PubMed:31564433}.
CC -!- TISSUE SPECIFICITY: Expressed from very early development (8 post-
CC conceptual weeks) and expression persists through adulthood in multiple
CC substructures of the brain, including the cerebellar cortex,
CC hippocampus, and striatum. {ECO:0000269|PubMed:31564433}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 72
CC (MRT72) [MIM:618665]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period. MRT72 patients manifest
CC moderate to severe intellectual disability, microcephaly, and
CC dysmorphic facial features. {ECO:0000269|PubMed:31564433}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000305}.
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DR EMBL; AF201938; AAF86874.1; -; mRNA.
DR EMBL; AK001321; BAA91622.1; -; mRNA.
DR EMBL; AC009967; AAY14869.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11254.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11255.1; -; Genomic_DNA.
DR EMBL; BC093014; AAH93014.1; -; mRNA.
DR EMBL; BC000921; AAH00921.1; -; mRNA.
DR CCDS; CCDS33320.1; -.
DR RefSeq; NP_001280115.1; NM_001293186.1.
DR RefSeq; NP_001280116.1; NM_001293187.1.
DR RefSeq; NP_054887.2; NM_014168.3.
DR PDB; 6H2U; X-ray; 1.60 A; A=1-209.
DR PDB; 6H2V; X-ray; 2.49 A; A/C=1-209.
DR PDBsum; 6H2U; -.
DR PDBsum; 6H2V; -.
DR AlphaFoldDB; Q9NRN9; -.
DR SMR; Q9NRN9; -.
DR BioGRID; 118851; 5.
DR IntAct; Q9NRN9; 2.
DR STRING; 9606.ENSP00000260953; -.
DR iPTMnet; Q9NRN9; -.
DR PhosphoSitePlus; Q9NRN9; -.
DR BioMuta; METTL5; -.
DR DMDM; 74761664; -.
DR EPD; Q9NRN9; -.
DR jPOST; Q9NRN9; -.
DR MassIVE; Q9NRN9; -.
DR MaxQB; Q9NRN9; -.
DR PaxDb; Q9NRN9; -.
DR PeptideAtlas; Q9NRN9; -.
DR PRIDE; Q9NRN9; -.
DR ProteomicsDB; 82397; -.
DR Antibodypedia; 35324; 85 antibodies from 20 providers.
DR DNASU; 29081; -.
DR Ensembl; ENST00000260953.10; ENSP00000260953.5; ENSG00000138382.15.
DR Ensembl; ENST00000392640.6; ENSP00000376415.2; ENSG00000138382.15.
DR Ensembl; ENST00000409965.5; ENSP00000386582.1; ENSG00000138382.15.
DR GeneID; 29081; -.
DR KEGG; hsa:29081; -.
DR MANE-Select; ENST00000260953.10; ENSP00000260953.5; NM_014168.4; NP_054887.2.
DR UCSC; uc002ufn.4; human.
DR CTD; 29081; -.
DR DisGeNET; 29081; -.
DR GeneCards; METTL5; -.
DR HGNC; HGNC:25006; METTL5.
DR HPA; ENSG00000138382; Low tissue specificity.
DR MalaCards; METTL5; -.
DR MIM; 618628; gene.
DR MIM; 618665; phenotype.
DR neXtProt; NX_Q9NRN9; -.
DR OpenTargets; ENSG00000138382; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA142671461; -.
DR VEuPathDB; HostDB:ENSG00000138382; -.
DR eggNOG; KOG3420; Eukaryota.
DR GeneTree; ENSGT00390000000227; -.
DR HOGENOM; CLU_074702_1_1_1; -.
DR InParanoid; Q9NRN9; -.
DR OMA; DVVYSIH; -.
DR OrthoDB; 1528520at2759; -.
DR PhylomeDB; Q9NRN9; -.
DR TreeFam; TF314953; -.
DR PathwayCommons; Q9NRN9; -.
DR SignaLink; Q9NRN9; -.
DR BioGRID-ORCS; 29081; 68 hits in 1055 CRISPR screens.
DR ChiTaRS; METTL5; human.
DR GenomeRNAi; 29081; -.
DR Pharos; Q9NRN9; Tbio.
DR PRO; PR:Q9NRN9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NRN9; protein.
DR Bgee; ENSG00000138382; Expressed in skeletal muscle tissue of biceps brachii and 203 other tissues.
DR ExpressionAtlas; Q9NRN9; baseline and differential.
DR Genevisible; Q9NRN9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008988; F:rRNA (adenine-N6-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Intellectual disability; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Synapse; Transferase.
FT CHAIN 1..209
FT /note="rRNA N6-adenosine-methyltransferase METTL5"
FT /id="PRO_0000251919"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2U"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2V"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V"
FT BINDING 108..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31328227,
FT ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V"
FT VARIANT 61
FT /note="G -> D (unknown pathological significance; found in
FT patients with intellectual disability and microcephaly;
FT impaired interaction with TRMT112)"
FT /evidence="ECO:0000269|PubMed:35033535"
FT /id="VAR_086154"
FT VARIANT 202
FT /note="V -> G (in dbSNP:rs1051387)"
FT /id="VAR_051507"
FT MUTAGEN 126..128
FT /note="NPP->AAA: In METTL5-3A; abolished methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:35033535"
FT CONFLICT 27
FT /note="E -> G (in Ref. 2; BAA91622)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:6H2V"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:6H2V"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6H2V"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:6H2V"
SQ SEQUENCE 209 AA; 23719 MW; 060B1C2C0D2BA169 CRC64;
MKKVRLKELE SRLQQVDGFE KPKLLLEQYP TRPHIAACML YTIHNTYDDI ENKVVADLGC
GCGVLSIGTA MLGAGLCVGF DIDEDALEIF NRNAEEFELT NIDMVQCDVC LLSNRMSKSF
DTVIMNPPFG TKNNKGTDMA FLKTALEMAR TAVYSLHKSS TREHVQKKAA EWKIKIDIIA
ELRYDLPASY KFHKKKSVDI EVDLIRFSF
