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TRM11_BOVIN
ID   TRM11_BOVIN             Reviewed;         460 AA.
AC   Q05B63;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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; BC122733; AAI22734.1; -; mRNA.
DR   RefSeq; NP_001073742.1; NM_001080273.2.
DR   AlphaFoldDB; Q05B63; -.
DR   SMR; Q05B63; -.
DR   STRING; 9913.ENSBTAP00000002544; -.
DR   PaxDb; Q05B63; -.
DR   PRIDE; Q05B63; -.
DR   GeneID; 514867; -.
DR   KEGG; bta:514867; -.
DR   CTD; 60487; -.
DR   eggNOG; KOG2671; Eukaryota.
DR   HOGENOM; CLU_029646_0_0_1; -.
DR   InParanoid; Q05B63; -.
DR   OrthoDB; 924753at2759; -.
DR   TreeFam; TF106161; -.
DR   Proteomes; UP000009136; 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..460
FT                   /note="tRNA (guanine(10)-N2)-methyltransferase homolog"
FT                   /id="PRO_0000328118"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4G4"
SQ   SEQUENCE   460 AA;  53039 MW;  684EB838E3F4027F CRC64;
     MAPPGILNRY LLLMAQEHLE FRLPEIKSLL SLFGGQFISS QETYGKSPFW ILSIPSEDIA
     RNLMKRTVCA KSIFELWGHG KCPEELYSSL KNYPVEKMVP FLHSDSTYKI KIHTFNKTLT
     QEEKVKRIDA LEFLPFEGKV NLKKPQHVFS ILEDYGLDPN HIPENPHNIY FGRWIADGQR
     ELIESYSVKK RHFIGNTSMD AGLSFIMANH GKVKKNDIVF DPFVGTGGLL IASAHFGAYV
     YGTDIDYNTV HGLGKASRKN QKWRGPDENI RANLRQYGLE KYYLDVLVSD ASKPSWRKGT
     YFDAIITDPP YGIRESTRRT GSQKEIPKGI EKCPESHVPV SLSYHLSDMF FDLLNFSAET
     LVLGGRLVYW LPVYTPEYTE EMVPWHPCLK LISNCEQKLS SHTSRRLITM EKVKEFENRD
     QYSHLLSDHF LLYQGHNSFR EKYFSGVTKR IAKEEKSSQE
 
 
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