TFS_METJA
ID TFS_METJA Reviewed; 108 AA.
AC Q58548;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transcription factor S {ECO:0000250|UniProtKB:Q9P9I8};
DE AltName: Full=Transcription elongation factor IIS/RNA polymerase subunit homolog {ECO:0000250|UniProtKB:Q9P9I8};
DE Short=TFIIS/RPSU homolog {ECO:0000250|UniProtKB:Q9P9I8};
GN Name=tfs {ECO:0000250|UniProtKB:Q9P9I8}; OrderedLocusNames=MJ1148;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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. Involved in transcriptional
CC proofreading and fidelity. Misincorporation of nucleotides during
CC elongation of transcription leads to arrested elongation complexes
CC which are rescued by TFS-promoted removal of a dinucleotide from the
CC 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled
CC elongation complexes (resulting from the next missing nucleotide or a
CC reduced incorporation rate of a wrong nucleotide) preventing
CC misincorporation and enabling proofreading in a post-incorporation
CC manner. Pausing of elongation complexes is the main determinant of TFS-
CC induced RNA cleavage. {ECO:0000250|UniProtKB:Q9P9I8}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
CC -!- CAUTION: More similar by sequence similarity to the eukaryotic RNA
CC polymerase subunits. {ECO:0000305}.
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DR EMBL; L77117; AAB99148.1; -; Genomic_DNA.
DR PIR; C64443; C64443.
DR RefSeq; WP_010870659.1; NC_000909.1.
DR AlphaFoldDB; Q58548; -.
DR SMR; Q58548; -.
DR STRING; 243232.MJ_1148; -.
DR PRIDE; Q58548; -.
DR EnsemblBacteria; AAB99148; AAB99148; MJ_1148.
DR GeneID; 1452044; -.
DR KEGG; mja:MJ_1148; -.
DR eggNOG; arCOG00579; Archaea.
DR HOGENOM; CLU_093932_3_2_2; -.
DR InParanoid; Q58548; -.
DR OMA; MVKFCPK; -.
DR OrthoDB; 121393at2157; -.
DR PhylomeDB; Q58548; -.
DR Proteomes; UP000000805; Chromosome.
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; ISS: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; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..108
FT /note="Transcription factor S"
FT /id="PRO_0000121481"
FT ZN_FING 5..24
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 65..105
FT /note="TFIIS-type"
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 72
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"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 108 AA; 12750 MW; 33AE963C576AD1BC CRC64;
MVKFCPKCNN LMLPKDGKLK CAVCGYEEET TAEGSKEYEY KEHLENKKEK ITVIESEGLE
TLPTTRIECP KCGHNEAYWW LQQTRCADEP ETRFYKCKKC GHTWREYD
