ID   TRM11_RAT               Reviewed;         463 AA.
AC   Q7TNK6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=tRNA (guanine(10)-N2)-methyltransferase homolog;
DE            EC=2.1.1.-;
DE   AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11 homolog;
GN   Name=Trmt11;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen Y., Huang C.-H.;
RT   "Molecular identification and conserved evolution of a novel RNA methylase
RT   protein gene in higher eukaryotic organisms.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TRMT112. {ECO:0000250|UniProtKB:Q7Z4G4}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM11 methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00959}.
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DR   EMBL; AF532978; AAQ10285.1; -; mRNA.
DR   RefSeq; NP_932168.1; NM_198051.1.
DR   AlphaFoldDB; Q7TNK6; -.
DR   SMR; Q7TNK6; -.
DR   STRING; 10116.ENSRNOP00000019436; -.
DR   iPTMnet; Q7TNK6; -.
DR   PhosphoSitePlus; Q7TNK6; -.
DR   PaxDb; Q7TNK6; -.
DR   GeneID; 378794; -.
DR   KEGG; rno:378794; -.
DR   UCSC; RGD:727798; rat.
DR   CTD; 60487; -.
DR   RGD; 727798; Trmt11.
DR   eggNOG; KOG2671; Eukaryota.
DR   InParanoid; Q7TNK6; -.
DR   OrthoDB; 924753at2759; -.
DR   PhylomeDB; Q7TNK6; -.
DR   PRO; PR:Q7TNK6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RNA_methylase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR   Pfam; PF01170; UPF0020; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
DR   PROSITE; PS51627; SAM_MT_TRM11; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Methyltransferase; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4G4"
FT   CHAIN           2..463
FT                   /note="tRNA (guanine(10)-N2)-methyltransferase homolog"
FT                   /id="PRO_0000230291"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4G4"
SQ   SEQUENCE   463 AA;  53103 MW;  A3AB4D43B7630177 CRC64;
     MALPGSLNRY LLLMAQEHLE FRLPEIKSLL SVIGGQFTNS QETYGKSPFW ILNIPSEDIA
     RNLMKRTVCA KSLFELWGHG KSPEELYSSL KSYPVEKMVP FLHSDSTYKI KIHTFNKTLT
     QEEKVKRIDA LEFLPFEGKV NLKKPQHVFS ILEDYGLDPN CIPENPHNIY FGRWIADGQR
     ELIESYSVKK RHFIGNTSMD AGLSFIMANH AKVKENDLVF DPFVGTGGLL IASAHFGAYV
     CGTDIDYNTV HGLGKASRKN QKWRGPDENI RANLRQYGLE KFYLDVLVSD ASKPSWRKGT
     YFDAIITDPP YGIRESTRRT GSQKEILKGI EKCPESHVPV SLTYHLSDMF LDLINFAAET
     LVLGGRLVYW LPVYTPEYTE KMVPWHPCLR LVSNCEQKLS SHTARRLITM EKVKEFENPD
     EYSRLLSDHF LPYQGHNSFR EKYFSGVTKR IATEEQCSHE GKL