ID   MTEF1_PONAB             Reviewed;         398 AA.
AC   Q5R9U8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
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   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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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: Phosphoprotein with mostly four phosphate groups. While the DNA-
CC       binding activity is unaffected by the phosphorylation state, only the
CC       phosphorylated form of the protein is active for termination activity.
CC       Functioning seems to be regulated by phosphorylation (By similarity).
CC       {ECO:0000250}.
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; CR859284; CAH91462.1; -; mRNA.
DR   AlphaFoldDB; Q5R9U8; -.
DR   SMR; Q5R9U8; -.
DR   STRING; 9601.ENSPPYP00000019979; -.
DR   eggNOG; KOG1267; Eukaryota.
DR   InParanoid; Q5R9U8; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   DNA-binding; Mitochondrion; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Transcription termination;
KW   Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..398
FT                   /note="Transcription termination factor 1, mitochondrial"
FT                   /id="PRO_0000021781"
FT   REGION          169..170
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          246..250
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          323..330
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          354..357
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          383..390
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            162
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            202
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            287
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            349
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  45650 MW;  979D3AA784574E25 CRC64;
     MQSLSLGQTS ISKGLNYLTI MAPGNLWHMR NNFLFGSRCW MTRFSAENIF KSVSFRLFGV
     KCHNTDSEPL KNEDLLKNLL TMGVDIDMAR KRQPGVFHRM ITNEQDLKMF LLSKGASKEV
     IASIISRYPR AITRTPENLS KRWDLWRKIV TSDLEIVNIL ERSPESFFRS NNNLNLENNI
     KFLYSVGLTR KCLCRLLTNA PRTFSNSLDL NKQMVEFLQA AGLSLGHNDP ADFVRKIILK
     TLYLIQSTKR VKANIEFLRS TFNLNSEELL VLICGPGAEI LDLSNDYARR SYANIKEKLF
     SLGCTEEEVQ KFVLSYPDVI FLAEKKFNDK IDCLMEENIS ISQIIENPRV LDSSISTLKS
     RIKELVNAGC NLSTLNITLL SWSKKRYEAK LKKLSRFA