ZCHC4_HUMAN
ID ZCHC4_HUMAN Reviewed; 513 AA.
AC Q9H5U6; B2RXF6; B4DRD8; B7ZW20; Q5IW78; Q96AN7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=rRNA N6-adenosine-methyltransferase ZCCHC4 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:30531910, ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:31799605};
DE AltName: Full=Zinc finger CCHC domain-containing protein 4 {ECO:0000305};
GN Name=ZCCHC4 {ECO:0000303|PubMed:30531910, ECO:0000312|HGNC:HGNC:22917};
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 [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Yue L., Zou X., Ci H., Li Y.;
RT "Homo sapiens zinc finger, DHHC domain containing, similar to Mus musculus
RT 4930449I23Rik.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-396.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-396.
RC TISSUE=Lung, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP HIS-396.
RC TISSUE=Brain cortex, and Kidney;
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 [5]
RP PRELIMINARY CHARACTERIZATION.
RX PubMed=15225602; DOI=10.1016/j.febslet.2004.03.126;
RA Albrecht M., Lengauer T.;
RT "Novel Sm-like proteins with long C-terminal tails and associated
RT methyltransferases.";
RL FEBS Lett. 569:18-26(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 276-ASP--PHE-279.
RX PubMed=30531910; DOI=10.1038/s41589-018-0184-3;
RA Ma H., Wang X., Cai J., Dai Q., Natchiar S.K., Lv R., Chen K., Lu Z.,
RA Chen H., Shi Y.G., Lan F., Fan J., Klaholz B.P., Pan T., Shi Y., He C.;
RT "N6-methyladenosine methyltransferase ZCCHC4 mediates ribosomal RNA
RT methylation.";
RL Nat. Chem. Biol. 15:88-94(2019).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TRIP4;
RP ASCC1; ASCC2; ASCC3; AHCYL1; AHCYL2 AND YTHDC2, AND MUTAGENESIS OF ASP-276.
RX PubMed=31799605; DOI=10.1093/nar/gkz1147;
RA Pinto R., Vaagboe C.B., Jakobsson M.E., Kim Y., Baltissen M.P.,
RA O'Donohue M.F., Guzman U.H., Malecki J.M., Wu J., Kirpekar F., Olsen J.V.,
RA Gleizes P.E., Vermeulen M., Leidel S.A., Slupphaug G., Falnes P.O.;
RT "The human methyltransferase ZCCHC4 catalyses N6-methyladenosine
RT modification of 28S ribosomal RNA.";
RL Nucleic Acids Res. 48:830-846(2020).
RN [9] {ECO:0007744|PDB:6UCA}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 24-464 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND
RP MUTAGENESIS OF TYR-173; TYR-340; ASP-341; ASN-342; HIS-343 AND LEU-345.
RX PubMed=31695039; DOI=10.1038/s41467-019-12923-x;
RA Ren W., Lu J., Huang M., Gao L., Li D., Wang G.G., Song J.;
RT "Structure and regulation of ZCCHC4 in m6A-methylation of 28S rRNA.";
RL Nat. Commun. 10:5042-5042(2019).
CC -!- FUNCTION: rRNA N6-methyltransferase that specifically methylates the
CC adenine in position 4220 of 28S rRNA (PubMed:30531910, PubMed:31328227,
CC PubMed:31799605, PubMed:31695039). N6-methylation of adenine(4220) in
CC 28S rRNA is required for translation (PubMed:30531910,
CC PubMed:31799605). {ECO:0000269|PubMed:30531910,
CC ECO:0000269|PubMed:31328227, ECO:0000269|PubMed:31695039,
CC ECO:0000269|PubMed:31799605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(4220) in 28S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyladenosine(4220) in 28S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58724, Rhea:RHEA-COMP:16142, Rhea:RHEA-COMP:16143,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000269|PubMed:30531910, ECO:0000269|PubMed:31328227,
CC ECO:0000269|PubMed:31695039, ECO:0000269|PubMed:31799605};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58725;
CC Evidence={ECO:0000269|PubMed:30531910, ECO:0000269|PubMed:31328227,
CC ECO:0000269|PubMed:31695039, ECO:0000269|PubMed:31799605};
CC -!- SUBUNIT: Interacts with components of the ASC-1 complex TRIP4, ASCC1,
CC ASCC2 and ASCC3 (PubMed:31799605). Interact with AHCYL1 and AHCYL2
CC (PubMed:31799605). Interact with YTHDC2 (PubMed:31799605).
CC {ECO:0000269|PubMed:31799605}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:30531910,
CC ECO:0000269|PubMed:31799605}. Cytoplasm {ECO:0000269|PubMed:30531910}.
CC Note=Accumulates in the nucleolus, where ribosome biogenesis takes
CC place. {ECO:0000269|PubMed:30531910}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H5U6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H5U6-2; Sequence=VSP_043359;
CC Name=3;
CC IsoId=Q9H5U6-3; Sequence=VSP_043360;
CC -!- DOMAIN: The regulatory loop blocks the catalytic center by bridging the
CC methyltransferase domain and the C-terminal CCHC-type zinc finger,
CC resulting in an autoinhibitory conformation.
CC {ECO:0000269|PubMed:31695039}.
CC -!- SIMILARITY: Belongs to the ZCCHC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16914.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15524.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY629351; AAV41218.1; -; mRNA.
DR EMBL; CH471069; EAW92837.1; -; Genomic_DNA.
DR EMBL; AK299211; BAG61250.1; -; mRNA.
DR EMBL; AK026677; BAB15524.1; ALT_INIT; mRNA.
DR EMBL; BC016914; AAH16914.1; ALT_INIT; mRNA.
DR EMBL; BC157834; AAI57835.1; -; mRNA.
DR EMBL; BC171821; AAI71821.1; -; mRNA.
DR CCDS; CCDS43218.1; -. [Q9H5U6-1]
DR RefSeq; NP_079212.2; NM_024936.2. [Q9H5U6-1]
DR PDB; 6UCA; X-ray; 3.10 A; A/B/C/D/E/F=24-464.
DR PDBsum; 6UCA; -.
DR AlphaFoldDB; Q9H5U6; -.
DR SMR; Q9H5U6; -.
DR BioGRID; 118838; 2.
DR IntAct; Q9H5U6; 1.
DR STRING; 9606.ENSP00000303468; -.
DR iPTMnet; Q9H5U6; -.
DR PhosphoSitePlus; Q9H5U6; -.
DR BioMuta; ZCCHC4; -.
DR DMDM; 85700439; -.
DR EPD; Q9H5U6; -.
DR jPOST; Q9H5U6; -.
DR MassIVE; Q9H5U6; -.
DR MaxQB; Q9H5U6; -.
DR PaxDb; Q9H5U6; -.
DR PeptideAtlas; Q9H5U6; -.
DR PRIDE; Q9H5U6; -.
DR ProteomicsDB; 80928; -. [Q9H5U6-1]
DR ProteomicsDB; 80929; -. [Q9H5U6-2]
DR ProteomicsDB; 80930; -. [Q9H5U6-3]
DR Antibodypedia; 23199; 83 antibodies from 14 providers.
DR DNASU; 29063; -.
DR Ensembl; ENST00000302874.9; ENSP00000303468.4; ENSG00000168228.16. [Q9H5U6-1]
DR Ensembl; ENST00000507760.5; ENSP00000422115.1; ENSG00000168228.16. [Q9H5U6-2]
DR GeneID; 29063; -.
DR KEGG; hsa:29063; -.
DR MANE-Select; ENST00000302874.9; ENSP00000303468.4; NM_024936.3; NP_079212.2.
DR UCSC; uc003grl.5; human. [Q9H5U6-1]
DR CTD; 29063; -.
DR DisGeNET; 29063; -.
DR GeneCards; ZCCHC4; -.
DR HGNC; HGNC:22917; ZCCHC4.
DR HPA; ENSG00000168228; Low tissue specificity.
DR MIM; 611792; gene.
DR neXtProt; NX_Q9H5U6; -.
DR OpenTargets; ENSG00000168228; -.
DR PharmGKB; PA134950003; -.
DR VEuPathDB; HostDB:ENSG00000168228; -.
DR eggNOG; KOG4399; Eukaryota.
DR GeneTree; ENSGT00390000012556; -.
DR HOGENOM; CLU_034589_0_0_1; -.
DR InParanoid; Q9H5U6; -.
DR OMA; EFCLYNM; -.
DR OrthoDB; 709190at2759; -.
DR PhylomeDB; Q9H5U6; -.
DR TreeFam; TF313872; -.
DR PathwayCommons; Q9H5U6; -.
DR SignaLink; Q9H5U6; -.
DR BioGRID-ORCS; 29063; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; ZCCHC4; human.
DR GenomeRNAi; 29063; -.
DR Pharos; Q9H5U6; Tdark.
DR PRO; PR:Q9H5U6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H5U6; protein.
DR Bgee; ENSG00000168228; Expressed in hindlimb stylopod muscle and 107 other tissues.
DR ExpressionAtlas; Q9H5U6; baseline and differential.
DR Genevisible; Q9H5U6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; 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:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR041370; Mlase_EEF1AKMT1/ZCCHC4.
DR InterPro; IPR039846; ZCCHC4.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR13493; PTHR13493; 1.
DR Pfam; PF10237; N6-adenineMlase; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..513
FT /note="rRNA N6-adenosine-methyltransferase ZCCHC4"
FT /id="PRO_0000150952"
FT DOMAIN 395..447
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ZN_FING 38..82
FT /note="GRF-type"
FT /evidence="ECO:0000255"
FT ZN_FING 443..460
FT /note="CCHC-type"
FT REGION 337..357
FT /note="Regulatory loop"
FT /evidence="ECO:0000269|PubMed:31695039"
FT REGION 466..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 172..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 243..244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:31695039,
FT ECO:0007744|PDB:6UCA"
FT VAR_SEQ 230..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043359"
FT VAR_SEQ 470..472
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043360"
FT VARIANT 382
FT /note="P -> L (in dbSNP:rs3752873)"
FT /id="VAR_053751"
FT VARIANT 396
FT /note="L -> H (in dbSNP:rs315675)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_024925"
FT MUTAGEN 173
FT /note="Y->A: Abolished rRNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31695039"
FT MUTAGEN 276..279
FT /note="DPPF->AAAA: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30531910"
FT MUTAGEN 276
FT /note="D->A: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31799605"
FT MUTAGEN 340
FT /note="Y->A: Strongly impaired rRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31695039"
FT MUTAGEN 341
FT /note="D->A: Increased rRNA methylation."
FT /evidence="ECO:0000269|PubMed:31695039"
FT MUTAGEN 342
FT /note="N->A: Strongly impaired rRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31695039"
FT MUTAGEN 343
FT /note="H->A: Decreased S-adenosyl-L-methionine-binding."
FT /evidence="ECO:0000269|PubMed:31695039"
FT MUTAGEN 343
FT /note="H->A: Strongly impaired rRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31695039"
FT MUTAGEN 345
FT /note="L->A: Increased rRNA methylation."
FT /evidence="ECO:0000269|PubMed:31695039"
FT CONFLICT 348
FT /note="H -> R (in Ref. 3; BAG61250)"
FT /evidence="ECO:0000305"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 284..298
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6UCA"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 412..415
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6UCA"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:6UCA"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6UCA"
SQ SEQUENCE 513 AA; 59010 MW; D74690827DC935F4 CRC64;
MAASRNGFEA VEAEGSAGCR GSSGMEVVLP LDPAVPAPLC PHGPTLLFVK VTQGKEETRR
FYACSACRDR KDCNFFQWED EKLSGARLAA REAHNRRCQP PLSRTQCVER YLKFIELPLT
QRKFCQTCQQ LLLPDDWGQH SEHQVLGNVS ITQLRRPSQL LYPLENKKTN AQYLFADRSC
QFLVDLLSAL GFRRVLCVGT PRLHELIKLT ASGDKKSNIK SLLLDIDFRY SQFYMEDSFC
HYNMFNHHFF DGKTALEVCR AFLQEDKGEG IIMVTDPPFG GLVEPLAITF KKLIAMWKEG
QSQDDSHKEL PIFWIFPYFF ESRICQFFPS FQMLDYQVDY DNHALYKHGK TGRKQSPVRI
FTNIPPNKII LPTEEGYRFC SPCQRYVSLE NQHCELCNSC TSKDGRKWNH CFLCKKCVKP
SWIHCSICNH CAVPDHSCEG PKHGCFICGE LDHKRSTCPN IATSKRANKA VRKQKQRKSN
KMKMETTKGQ SMNHTSATRR KKRRERAHQY LGS
