TRM6_BOVIN
ID TRM6_BOVIN Reviewed; 497 AA.
AC Q2T9V5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 {ECO:0000250|UniProtKB:Q9UJA5};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase non-catalytic subunit TRM6 {ECO:0000250|UniProtKB:Q9UJA5};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6;
DE Short=tRNA(m1A58)MTase subunit TRM6 {ECO:0000250|UniProtKB:Q9UJA5};
GN Name=TRMT6; Synonyms=TRM6;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC methyltransferase, which catalyzes the formation of N(1)-methyladenine
CC at position 58 (m1A58) in initiator methionyl-tRNA. Together with the
CC TRMT61A catalytic subunit, part of a mRNA N(1)-methyltransferase
CC complex that mediates methylation of adenosine residues at the N(1)
CC position of a small subset of mRNAs: N(1) methylation takes place in
CC tRNA T-loop-like structures of mRNAs and is only present at low
CC stoichiometries. {ECO:0000250|UniProtKB:Q9UJA5}.
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies
CC of TRMT61A. {ECO:0000250|UniProtKB:Q9UJA5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}.
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}.
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DR EMBL; BC111249; AAI11250.1; -; mRNA.
DR RefSeq; NP_001033129.1; NM_001038040.2.
DR AlphaFoldDB; Q2T9V5; -.
DR SMR; Q2T9V5; -.
DR STRING; 9913.ENSBTAP00000001734; -.
DR PaxDb; Q2T9V5; -.
DR PRIDE; Q2T9V5; -.
DR Ensembl; ENSBTAT00000001734; ENSBTAP00000001734; ENSBTAG00000001314.
DR GeneID; 505816; -.
DR KEGG; bta:505816; -.
DR CTD; 51605; -.
DR VEuPathDB; HostDB:ENSBTAG00000001314; -.
DR VGNC; VGNC:36374; TRMT6.
DR eggNOG; KOG1416; Eukaryota.
DR GeneTree; ENSGT00390000008327; -.
DR HOGENOM; CLU_010916_0_1_1; -.
DR InParanoid; Q2T9V5; -.
DR OMA; TFHNRTE; -.
DR OrthoDB; 543764at2759; -.
DR TreeFam; TF314835; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000001314; Expressed in oocyte and 107 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IEA:Ensembl.
DR InterPro; IPR017423; TRM6.
DR PANTHER; PTHR12945; PTHR12945; 1.
DR Pfam; PF04189; Gcd10p; 1.
DR PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..497
FT /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT catalytic subunit TRM6"
FT /id="PRO_0000233097"
FT REGION 69..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..104
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 145..154
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 175..182
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 276..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..423
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 434..441
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT REGION 468..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA5"
SQ SEQUENCE 497 AA; 55979 MW; A5E2CD6EBDC3D63F CRC64;
MESSEDQPGP QPQYPGNHCI RDGDFVVLKR EDVFKAVQVQ RRKKVTFEKQ WFYLDNIIGH
SYGTTFEVTN GGSLQPKKKK EEPTSETKEA GTDNRNIIDD GKSQKLTQDD IKALKDKGIK
GEEIVQQLIE NSTTFRDKTE FAQDKYIKKK KKKYEAMITV VKPSTRILSV MYYAREPGKI
NHMRYDTLAQ MLTLGNIRAG NKMIVMETCA GLVLGAMMER MGGFGSIIQL YPGGGPVRAA
TACFGFPKSF LSGLYEFPLN KVDSLLNGTF SAEMLSSEPK DIASVEESNG TLEEKQTSEQ
ENEDSIAEAP ESNHPEEQER MEIVSQDPDY KEPKESGSKK DYIQEKQRRQ EEQKKRHLEA
AALLSERNAD GLIVASRFHP TPLLLSLLDF VAPSRPFVVY CQYKEPLLEC YTKLRERGGV
INLRLSETWL RNYQVLPDRS HPKLLMSGGG GYLLSGFTVA MDNLKADPSL KSSTSTLESH
KTEEPAAKKR KCPESDS
