ID   TFS_METTL               Reviewed;         105 AA.
AC   Q9P9I8;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Transcription factor S {ECO:0000303|PubMed:10777522};
DE   AltName: Full=Transcription elongation factor IIS/RNA polymerase subunit homolog {ECO:0000303|PubMed:10777522};
DE            Short=TFIIS/RPSU homolog {ECO:0000303|PubMed:10777522};
GN   Name=tfs {ECO:0000312|EMBL:CAB66386.1};
OS   Methanothermococcus thermolithotrophicus (Methanococcus
OS   thermolithotrophicus).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=2186 {ECO:0000312|EMBL:CAB66386.1};
RN   [1] {ECO:0000312|EMBL:CAB66386.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=10777522; DOI=10.1074/jbc.275.17.12393;
RA   Hausner W., Lange U., Musfeldt M.;
RT   "Transcription factor S, a cleavage induction factor of the archaeal RNA
RT   polymerase.";
RL   J. Biol. Chem. 275:12393-12399(2000).
RN   [2]
RP   FUNCTION.
RX   PubMed=15130130; DOI=10.1111/j.1365-2958.2004.04039.x;
RA   Lange U., Hausner W.;
RT   "Transcriptional fidelity and proofreading in Archaea and implications for
RT   the mechanism of TFS-induced RNA cleavage.";
RL   Mol. Microbiol. 52:1133-1143(2004).
CC   -!- FUNCTION: Induces RNA cleavage activity in the RNA polymerase. In its
CC       presence, the cleavage activity of the RNA polymerase truncates the RNA
CC       back to position +15 in a stepwise manner by releasing mainly
CC       dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs
CC       are able to continue elongation (PubMed:10777522). Involved in
CC       transcriptional proofreading and fidelity. Misincorporation of
CC       nucleotides during elongation of transcription leads to arrested
CC       elongation complexes which are rescued by TFS-promoted removal of a
CC       dinucleotide from the 3'-end. TFS is able to induce a cleavage
CC       resynthesis cycle in stalled elongation complexes (resulting from the
CC       next missing nucleotide or a reduced incorporation rate of a wrong
CC       nucleotide) preventing misincorporation and enabling proofreading in a
CC       post-incorporation manner. Pausing of elongation complexes is the main
CC       determinant of TFS-induced RNA cleavage (PubMed:15130130).
CC       {ECO:0000269|PubMed:10777522, ECO:0000269|PubMed:15130130}.
CC   -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC       RNA polymerase family. {ECO:0000255|PIRNR:PIRNR005586,
CC       ECO:0000255|RuleBase:RU003474, ECO:0000305}.
CC   -!- CAUTION: More similar by sequence similarity to the eukaryotic RNA
CC       polymerase subunits. {ECO:0000305}.
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DR   EMBL; AJ271332; CAB66386.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P9I8; -.
DR   SMR; Q9P9I8; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR   InterPro; IPR006288; TFS.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   PANTHER; PTHR11239; PTHR11239; 1.
DR   Pfam; PF02150; RNA_POL_M_15KD; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR   SMART; SM00661; RPOL9; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   TIGRFAMs; TIGR01384; TFS_arch; 1.
DR   PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..105
FT                   /note="Transcription factor S"
FT                   /id="PRO_0000435351"
FT   ZN_FING         5..24
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:Q56254"
FT   ZN_FING         62..102
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ   SEQUENCE   105 AA;  12362 MW;  108CE1BD3C2B5260 CRC64;
     MVEFCPKCNN IMLPKNGRLK CTVCGFEEEL GNRTEEYELK EKIEAKKQEV TVIEDVDTLP
     TTRIECPSCG NMEASWWLQQ TRCADEPETR FYKCKKCGHT WREYD