GenomeNet

Database: UniProt
Entry: A0A0G2JWR1_RAT
LinkDB: A0A0G2JWR1_RAT
Original site: A0A0G2JWR1_RAT 
ID   A0A0G2JWR1_RAT          Unreviewed;       438 AA.
AC   A0A0G2JWR1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=tRNA (guanine(10)-N2)-methyltransferase homolog {ECO:0000256|ARBA:ARBA00013960};
DE   AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11 homolog {ECO:0000256|ARBA:ARBA00032604};
GN   Name=Trmt11 {ECO:0000313|Ensembl:ENSRNOP00000069979.2,
GN   ECO:0000313|RGD:727798};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069979.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000069979.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069979.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000069979.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069979.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC       tRNA methyltransferase complex that mediates the methylation of the
CC       guanosine nucleotide at position 10 (m2G10) in tRNAs.
CC       {ECO:0000256|ARBA:ARBA00002425}.
CC   -!- SUBUNIT: Interacts with TRMT112. {ECO:0000256|ARBA:ARBA00033754}.
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DR   RefSeq; XP_006227814.1; XM_006227752.3.
DR   AlphaFoldDB; A0A0G2JWR1; -.
DR   Ensembl; ENSRNOT00000083276.2; ENSRNOP00000069979.2; ENSRNOG00000014240.7.
DR   RGD; 727798; Trmt11.
DR   VEuPathDB; HostDB:ENSRNOG00000014240; -.
DR   GeneTree; ENSGT00390000018131; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000014240; Expressed in thymus and 19 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JWR1; baseline and differential.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RlmKL-like_Mtase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF3; TRNA (GUANINE(10)-N2)-METHYLTRANSFERASE HOMOLOG; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF017259; tRNA_mtfrase_TRM11; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
DR   PROSITE; PS51627; SAM_MT_TRM11; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022555};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          188..319
FT                   /note="UPF0020"
FT                   /evidence="ECO:0000259|Pfam:PF01170"
SQ   SEQUENCE   438 AA;  49918 MW;  2076473A2476957F CRC64;
     MALPGSLNRY LLLMAQEHLE FRLPEITSLL SLFGGQFTSS QETKSPFWIL NIPSEDIARN
     LMKRTVCAKS LFELWGHGKS PEELYSSLKS YPVEKMVPFL HSDSTYKIKI HTFNKTLTQE
     EKVERIDALE FLPFEGKVNL KKPQHVFSIL EDYGLDPNCI PENPHNIYFG RWIADGQREL
     IESYSVKKRH FIGNTSMDAG LSFIMANHAK VKENDLVFDP FVGTGGLLIA SAHFGAYVCG
     TDIDYNTVHG LGKASRKNQK WRGPDENIRA NLRQYGLEKF YLDVLVSDAS KPSWRKGTYF
     DAIITDPPYG IRESTRRTGS QKEILKGIEK CPESHVPVSL TYHLSDMFLD LINFAAETLV
     LGGRLVYWLP VYTPEYTEKM VPWHPCLRLV SNCEQKLSSH TARRLITMEK VKEFEMRTPV
     GTEVLQFAQG HTAGNLQT
//
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