TRM11_PONAB
ID TRM11_PONAB Reviewed; 463 AA.
AC Q5R962;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859531; CAH91698.1; -; mRNA.
DR RefSeq; NP_001127452.1; NM_001133980.1.
DR AlphaFoldDB; Q5R962; -.
DR SMR; Q5R962; -.
DR STRING; 9601.ENSPPYP00000019024; -.
DR GeneID; 100174524; -.
DR KEGG; pon:100174524; -.
DR CTD; 60487; -.
DR eggNOG; KOG2671; Eukaryota.
DR InParanoid; Q5R962; -.
DR OrthoDB; 924753at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; 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_0000230290"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4G4"
SQ SEQUENCE 463 AA; 53379 MW; C7A6AC1270807C9E CRC64;
MALSCTLNRY LLLMAQEHLE FRLPEIKSLL SLFGGQFGSS QETFGKSPFW ILSIPSEDIA
RNLMKRTVCA KSIFELWGHG QSPEELYSSL KNYPVEKMVP FLHSDSTYKI KIHTFNKTLT
QEEKIKRIDA LEFLPFEGKV NLKKPQHVFS VLEDYGLDPN CIPENPHNIY FGRWIADGQR
ELIESYSVKK RHFIGNTSMD AGLSFIMANH GKVKENDIVF DPFVGTGGLL IACAHFGAYV
YGTDIDYNTV HGLGKATRKN QKWRGPDENI RANLRQYGLE KYYLDVLVSD ASKPSWRKGT
YFDAIITDPP YGIRESTRRT GSQKEIPKGI EKWEKCPESH VPVSLSYHLS DMFLDLLNFA
AETLVLGGRL VYWLPVYTPE YTEEMVPWHP CLELISNCEQ KLSSHTSRRL ITMEKVKKFE
NRDQYSHLLS DHFLPYQGHN SFREKYFSGV TKRIAKEEKS TQE