ID L8IQQ7_9CETA Unreviewed; 384 AA.
AC L8IQQ7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=5-methylcytosine rRNA methyltransferase NSUN4 {ECO:0000256|ARBA:ARBA00040337};
DE AltName: Full=5-methylcytosine tRNA methyltransferase NSUN4 {ECO:0000256|ARBA:ARBA00041914};
DE AltName: Full=NOL1/NOP2/Sun domain family member 4 {ECO:0000256|ARBA:ARBA00042050};
GN ORFNames=E5288_WYG017204 {ECO:0000313|EMBL:MXQ88262.1}, M91_21635
GN {ECO:0000313|EMBL:ELR57472.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR57472.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR57472.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080}, and YakQH1
RC {ECO:0000313|EMBL:ELR57472.1};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
RN [2] {ECO:0000313|EMBL:MXQ88262.1, ECO:0000313|Proteomes:UP000322234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WY2019 {ECO:0000313|EMBL:MXQ88262.1};
RC TISSUE=Blood {ECO:0000313|EMBL:MXQ88262.1};
RA Liu Y.;
RT "The sequence and de novo assembly of the wild yak genome.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61484, Rhea:RHEA-COMP:15836, Rhea:RHEA-COMP:15837,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00036484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in tRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61468, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:15827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00036266};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; JH880979; ELR57472.1; -; Genomic_DNA.
DR EMBL; VBQZ03000044; MXQ88262.1; -; Genomic_DNA.
DR RefSeq; XP_005894286.1; XM_005894224.1.
DR AlphaFoldDB; L8IQQ7; -.
DR SMR; L8IQQ7; -.
DR STRING; 72004.ENSBMUP00000025024; -.
DR Ensembl; ENSBMUT00000028817; ENSBMUP00000025024; ENSBMUG00000018801.
DR GeneID; 102283196; -.
DR KEGG; bom:102283196; -.
DR CTD; 387338; -.
DR OrthoDB; 317522at2759; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR Proteomes; UP000322234; Unassembled WGS sequence.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:Ensembl.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 6.20.240.40; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR46955:SF6; 5-METHYLCYTOSINE RRNA METHYLTRANSFERASE NSUN-4; 1.
DR PANTHER; PTHR46955; PROTEIN CBG01349-RELATED; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000011080};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT DOMAIN 79..383
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 181..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 384 AA; 43199 MW; C457DAD9CDED2BD3 CRC64;
MAALVVRGVR DMLKRADFAT VPRRQRHKKK WASTEPKFPA TRLALQNFDM TYSVQFGDLW
PSIRVSLLSE QKYGALVNNF AAGDRVSAEL EQLKARDFVN EAVFHREPEP ENSQTAAPSP
ASWACSPNLR CFTFTRGDVS RFPPARLGSL GLMDYYLMDA ASLLPVLALG LQPGDTVLDL
CAAPGGKTLA LLQTGCCRNL AANDLSTSRT SRLQRVLHSY VPQDVRDKNR VRVTSWDGRK
WGELEGDTYD RVLVDVPCTT DRHSLHEEEN SIFQRSRKKE RQMLPVLQVQ LLAAGLLATK
PGGHIVYSTC SLSHLQNEYV VQGAIELLDN QYSIKVQVED LTHFRKLFMN TFSFFPSCQV
GELVIPNLMA NFGPMYFCKM CRMT
//
