ID   MTEF1_RAT               Reviewed;         374 AA.
AC   Q9EPI8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Transcription termination factor 1, mitochondrial;
DE   AltName: Full=Mitochondrial transcription termination factor 1;
DE            Short=mTERF;
DE   Flags: Precursor;
GN   Name=Mterf1; Synonyms=Mterf;
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 [MRNA], SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC   TISSUE=Liver;
RX   PubMed=15087485; DOI=10.1093/nar/gkh528;
RA   Prieto-Martin A., Montoya J., Martinez-Azorin F.;
RT   "Phosphorylation of rat mitochondrial transcription termination factor
RT   (mTERF) is required for transcription termination but not for binding to
RT   DNA.";
RL   Nucleic Acids Res. 32:2059-2068(2004).
CC   -!- FUNCTION: Transcription termination factor. Binds to a 28 bp region
CC       within the tRNA(Leu(uur)) gene at a position immediately adjacent to
CC       and downstream of the 16S rRNA gene; this region comprises a tridecamer
CC       sequence critical for directing accurate termination. Binds DNA along
CC       the major grove and promotes DNA bending and partial unwinding.
CC       Promotes base flipping. Transcription termination activity appears to
CC       be polarized with highest specificity for transcripts initiated on the
CC       light strand (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15087485}.
CC   -!- DOMAIN: Contains nine structural repeats of about 35 residues, where
CC       each repeat contains three helices. The repeats form a left-handed
CC       superhelical assembly with a solenoid structure that wraps itself
CC       around DNA (By similarity). {ECO:0000250}.
CC   -!- PTM: Is a phosphoprotein. While the DNA-binding activity is unaffected
CC       by the phosphorylation/dephosphorylation state, only the phosphorylated
CC       form of the protein is active for termination activity. Functioning
CC       seems to be regulated by phosphorylation.
CC       {ECO:0000269|PubMed:15087485}.
CC   -!- SIMILARITY: Belongs to the mTERF family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ292524; CAC20864.1; -; mRNA.
DR   RefSeq; NP_445951.1; NM_053499.1.
DR   AlphaFoldDB; Q9EPI8; -.
DR   SMR; Q9EPI8; -.
DR   STRING; 10116.ENSRNOP00000010425; -.
DR   PaxDb; Q9EPI8; -.
DR   PRIDE; Q9EPI8; -.
DR   GeneID; 85261; -.
DR   KEGG; rno:85261; -.
DR   UCSC; RGD:621318; rat.
DR   CTD; 7978; -.
DR   RGD; 621318; Mterf1.
DR   eggNOG; KOG1267; Eukaryota.
DR   InParanoid; Q9EPI8; -.
DR   PhylomeDB; Q9EPI8; -.
DR   Reactome; R-RNO-163316; Mitochondrial transcription termination.
DR   PRO; PR:Q9EPI8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IBA:GO_Central.
DR   GO; GO:0032392; P:DNA geometric change; ISS:UniProtKB.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006393; P:termination of mitochondrial transcription; ISS:UniProtKB.
DR   Gene3D; 1.25.70.10; -; 2.
DR   InterPro; IPR003690; MTERF.
DR   InterPro; IPR038538; MTERF_sf.
DR   PANTHER; PTHR15437; PTHR15437; 1.
DR   Pfam; PF02536; mTERF; 1.
DR   SMART; SM00733; Mterf; 6.
PE   1: Evidence at protein level;
KW   DNA-binding; Mitochondrion; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Transcription termination;
KW   Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..374
FT                   /note="Transcription termination factor 1, mitochondrial"
FT                   /id="PRO_0000021782"
FT   REGION          146..147
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          224..228
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          301..308
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          332..335
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          361..368
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            139
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            179
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            327
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  42937 MW;  43FD94B40069B3F0 CRC64;
     MASRNIWRVR RNFLFDLRGW VPQYSAEVFL KSIPFRPFSV ECNSKDGENG DLLNNLLTMG
     VDVDMARRRQ PGVFNKAVTN EQELKMFLLS KGASDKVIGS IISRYPRAIT RTPESLSKRW
     DLWREIMASD LEIVNILERS PESFFRSNNN LNLENNIKFL CSVGLTHKCL CRLLTSAPRT
     FSNSLNLNKQ MVEFLQETGI SLGHNNPTDF VRKIISKNPS ILIQSTKRVK TNIEFLQSTF
     NLDKEDLLLL ICGPGARILD LSNDCTKRNY TNIKKRLLSL GCTEEEVQKF VLSYLNMIFL
     SEKKFNDKID CLLEEKISTS QILENPRVLD SSIHTLKTRI RELAHAGYDV STSSIALLSW
     SQRRYEAKLK RLSG