TFB2M_BOVIN
ID TFB2M_BOVIN Reviewed; 394 AA.
AC Q32LD4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Dimethyladenosine transferase 2, mitochondrial {ECO:0000250|UniProtKB:Q9H5Q4};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H5Q4};
DE AltName: Full=Mitochondrial 12S rRNA dimethylase 2;
DE AltName: Full=Mitochondrial transcription factor B2;
DE Short=mtTFB2;
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2;
DE Flags: Precursor;
GN Name=TFB2M {ECO:0000250|UniProtKB:Q9H5Q4};
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 (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent rRNA methyltransferase
CC which may methylate two specific adjacent adenosines in the loop of a
CC conserved hairpin near the 3'-end of 12S mitochondrial rRNA. Component
CC of the mitochondrial transcription initiation complex, composed at
CC least of TFB2M, TFAM and POLRMT that is required for basal
CC transcription of mitochondrial DNA. In this complex TFAM recruits
CC POLRMT to a specific promoter whereas TFB2M induces structural changes
CC in POLRMT to enable promoter opening and trapping of the DNA non-
CC template strand. Stimulates transcription independently of the
CC methyltransferase activity. {ECO:0000250|UniProtKB:Q9H5Q4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in rRNA + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyladenosine in rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58728, Rhea:RHEA-COMP:15198, Rhea:RHEA-COMP:15199,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000250|UniProtKB:Q9H5Q4};
CC -!- SUBUNIT: Homodimer. Component of the mitochondrial transcription
CC initiation complex, composed at least of TFB2M, TFAM and POLRMT. In
CC this complex TFAM recruits POLRMT to the promoter whereas TFB2M induces
CC structural changes in POLRMT to enable promoter opening and trapping of
CC the DNA non-template strand. Interacts with mitochondrial RNA
CC polymerase POLRMT. Interacts with TFAM. {ECO:0000250|UniProtKB:Q9H5Q4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; BC109634; AAI09635.1; -; mRNA.
DR RefSeq; NP_001033216.1; NM_001038127.2.
DR AlphaFoldDB; Q32LD4; -.
DR SMR; Q32LD4; -.
DR STRING; 9913.ENSBTAP00000000080; -.
DR PaxDb; Q32LD4; -.
DR PRIDE; Q32LD4; -.
DR Ensembl; ENSBTAT00000000080; ENSBTAP00000000080; ENSBTAG00000000072.
DR GeneID; 516874; -.
DR KEGG; bta:516874; -.
DR CTD; 64216; -.
DR VEuPathDB; HostDB:ENSBTAG00000000072; -.
DR VGNC; VGNC:35783; TFB2M.
DR eggNOG; KOG0820; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_051778_1_0_1; -.
DR InParanoid; Q32LD4; -.
DR OMA; RAQACKK; -.
DR OrthoDB; 1169941at2759; -.
DR TreeFam; TF325100; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000000072; Expressed in tongue muscle and 105 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016861; TFB2M.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR PANTHER; PTHR11727:SF13; PTHR11727:SF13; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..394
FT /note="Dimethyladenosine transferase 2, mitochondrial"
FT /id="PRO_0000273178"
FT REGION 326..327
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H5Q4"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 394 AA; 44952 MW; 2887946E05A22731 CRC64;
MWVPGAGIPS RLTLSAFTRA ARFCVLNSGV ARWKDVPAEN CRGLYDFHTQ LKPDVEFGKL
SSRLYKSRSE TKRYVTSPRV AETVVRVLRG KRKAGQLILE CNPGPGVLTR ALLESGARVI
ALESDKNFIP ELKSLGNSVN GRLEVIYCDF FKLDPRNHGM VTPPVMTSDM LFQYLGVKAH
PWKKGFPLKV VGILPAKTER NTLWKILHDL YSCSSVYKYG RAELNLFISE KECRKLTANP
QTPALYQSLS VLGQTACGIK VLCTEPSSLF DTYAIKGELE KQRHRESLEQ NLCFVQLTPH
RNLFTGTLTP FNYDVFFHML RQCFMKRNAK LIDHLPSLSP IDAVHILKQI KKKKDVRVVD
MYPKDFLRLF ETIECSKDDT CKWLYDEFME DALS
