NSUN6_MOUSE
ID NSUN6_MOUSE Reviewed; 476 AA.
AC Q7TS68; Q8R3C4; Q9D445;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=tRNA (cytosine(72)-C(5))-methyltransferase NSUN6 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8TEA1};
DE AltName: Full=NOL1/NOP2/Sun domain family member 6;
GN Name=Nsun6 {ECO:0000312|MGI:MGI:1921705};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryo, and Mammary tumor;
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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C5 position of cytosine 72 in
CC tRNA(Thr)(TGT) and tRNA(Cys)(GCA). In vitro also methylates
CC tRNA(Thr)(AGT). Methylation requires, in the acceptor stem region, the
CC presence of the 3'-CCA terminus, the target site C72, the discriminator
CC base U73, and the second and third base pairs (2:71 and 3:70) in the
CC tRNA substrates. {ECO:0000250|UniProtKB:Q8TEA1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(72) in tRNA(Thr) + S-adenosyl-L-methionine = 5-
CC methylcytidine(72) in tRNA(Thr) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21124, Rhea:RHEA-COMP:15877, Rhea:RHEA-COMP:15878,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q8TEA1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21125;
CC Evidence={ECO:0000250|UniProtKB:Q8TEA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(72) in tRNA(Cys) + S-adenosyl-L-methionine = 5-
CC methylcytidine(72) in tRNA(Cys) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61584, Rhea:RHEA-COMP:15875, Rhea:RHEA-COMP:15876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q8TEA1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61585;
CC Evidence={ECO:0000250|UniProtKB:Q8TEA1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TEA1}.
CC -!- DOMAIN: The PUA domain plays a role in tRNA recognition through
CC precisely recognizing the CCA end and the D-stem region of tRNA.
CC {ECO:0000250|UniProtKB:Q8TEA1}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK016811; BAB30442.1; -; mRNA.
DR EMBL; AK077778; BAC37002.1; -; mRNA.
DR EMBL; AK132428; BAE21163.1; -; mRNA.
DR EMBL; BC025622; AAH25622.1; ALT_INIT; mRNA.
DR EMBL; BC053751; AAH53751.1; -; mRNA.
DR CCDS; CCDS15703.1; -.
DR RefSeq; NP_001159413.1; NM_001165941.1.
DR RefSeq; NP_083226.3; NM_028950.4.
DR AlphaFoldDB; Q7TS68; -.
DR SMR; Q7TS68; -.
DR STRING; 10090.ENSMUSP00000075766; -.
DR iPTMnet; Q7TS68; -.
DR PhosphoSitePlus; Q7TS68; -.
DR EPD; Q7TS68; -.
DR jPOST; Q7TS68; -.
DR MaxQB; Q7TS68; -.
DR PaxDb; Q7TS68; -.
DR PRIDE; Q7TS68; -.
DR ProteomicsDB; 252861; -.
DR Antibodypedia; 25416; 135 antibodies from 25 providers.
DR DNASU; 74455; -.
DR Ensembl; ENSMUST00000028034; ENSMUSP00000028034; ENSMUSG00000026707.
DR Ensembl; ENSMUST00000076435; ENSMUSP00000075766; ENSMUSG00000026707.
DR Ensembl; ENSMUST00000195749; ENSMUSP00000141924; ENSMUSG00000026707.
DR GeneID; 74455; -.
DR KEGG; mmu:74455; -.
DR UCSC; uc008ikt.2; mouse.
DR CTD; 221078; -.
DR MGI; MGI:1921705; Nsun6.
DR VEuPathDB; HostDB:ENSMUSG00000026707; -.
DR eggNOG; KOG1122; Eukaryota.
DR GeneTree; ENSGT00940000155370; -.
DR InParanoid; Q7TS68; -.
DR OMA; YQGAMLY; -.
DR OrthoDB; 1040075at2759; -.
DR PhylomeDB; Q7TS68; -.
DR TreeFam; TF324225; -.
DR BioGRID-ORCS; 74455; 4 hits in 68 CRISPR screens.
DR ChiTaRS; Nsun6; mouse.
DR PRO; PR:Q7TS68; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q7TS68; protein.
DR Bgee; ENSMUSG00000026707; Expressed in lens placode and 189 other tissues.
DR ExpressionAtlas; Q7TS68; baseline and differential.
DR Genevisible; Q7TS68; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0002946; P:tRNA C5-cytosine methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..476
FT /note="tRNA (cytosine(72)-C(5))-methyltransferase NSUN6"
FT /id="PRO_0000263115"
FT DOMAIN 111..203
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 242..248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEA1"
FT CONFLICT 240
FT /note="D -> E (in Ref. 2; AAH53751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52279 MW; DA05123422CBFD30 CRC64;
MYVFPKISLR PEVENYLKES FLNEEAVSAS SRQEAERKFE TLLLRLSHPP SMTTVRVNTH
LGSVQHVRGL LLEELQKQFG ESSIPVVQHP ALPDVLLIPM TGPRKNIERQ QGEVIVGAQC
GNAVLRGAHV YVPGIVSASK FMKAGDVISV YSDINGKCKK GAKEFDGTKV FLGNGISELS
RKDIFNGLPD LKGIGIRMTE PIYLSPSFDN VLPSYIFLQN LPSTVVAHVL DPQPGEKILD
MCAAPGGKTT HTAALMQDKG EVIALDKILT KVNKLKQNAS LLGLHSIRAF CFDATKALKL
DTTDGIEGGP PFLPESFDRI ILDAPCSGMG QRPNMACTWT LKEVTSYQPL QRKLLHVAVQ
LLKPGGVLVY STCTITLAEN EEQVAWALRT FPCLQLQPQE PQIGGEGMVG AGLTLEQLKQ
LQRFDPSVVP LQNMDTDSLG EARREDMIWL ANKDCIGFFI AKFLKCQSTK AKVSQK
