TFB2M_RAT
ID TFB2M_RAT Reviewed; 397 AA.
AC Q5U2T7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Dimethyladenosine transferase 2, mitochondrial {ECO:0000305};
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:0000312|RGD:1307091};
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 [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC085870; AAH85870.1; -; mRNA.
DR RefSeq; NP_001008294.1; NM_001008293.1.
DR AlphaFoldDB; Q5U2T7; -.
DR SMR; Q5U2T7; -.
DR STRING; 10116.ENSRNOP00000003618; -.
DR PaxDb; Q5U2T7; -.
DR Ensembl; ENSRNOT00000003618; ENSRNOP00000003618; ENSRNOG00000002695.
DR GeneID; 289307; -.
DR KEGG; rno:289307; -.
DR CTD; 64216; -.
DR RGD; 1307091; Tfb2m.
DR eggNOG; KOG0820; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_051778_1_0_1; -.
DR InParanoid; Q5U2T7; -.
DR OMA; RAQACKK; -.
DR OrthoDB; 1169941at2759; -.
DR PhylomeDB; Q5U2T7; -.
DR TreeFam; TF325100; -.
DR Reactome; R-RNO-163282; Mitochondrial transcription initiation.
DR PRO; PR:Q5U2T7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002695; Expressed in heart and 19 other tissues.
DR Genevisible; Q5U2T7; RN.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
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:0006390; P:mitochondrial transcription; ISO:RGD.
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..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..397
FT /note="Dimethyladenosine transferase 2, mitochondrial"
FT /id="PRO_0000273181"
FT REGION 329..330
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 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 397 AA; 46021 MW; 8F0E6B9940F3455E CRC64;
MRGLAMRLPP RLALSVLAGR GPSCILGSGA ATRKDWQERN RRSFSDLYTQ PLPDCDFEES
SSWTHKSRSE PTRHIACKKS ARNLVRDLLE HQNPSHQLIL ECNPGPGILT GALLKAGARV
VAFESEKMFI PHLESLRKNA DGELQVVHCD FFKIDPRYQE LVRPDVNSHT IFQNLGIKAV
PWSAGVPIKV FGILPNKHER RLLWKILFDL YSCESIYRYG RVELNMFISE KEFRKLIATP
KRPDLYQVLG VLWQVACEIK FLHMEPWSSF SVHAENGHLE KSKHSESLNL LKQNLYLVRM
TPRRTLFTEN LSPLNYDMFF HLVKHCFGKR NAPIIHHLRS LSTVDPINIL RQIRKRPGDT
AAKMYPHDFK RLFETIERSE DSVFKWIYDY CSDDSEL
