TFS_THECE
ID TFS_THECE Reviewed; 110 AA.
AC Q56254;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
OS Thermococcus celer.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8171001; DOI=10.1073/pnas.91.9.3854;
RA Kaine B.P., Mehr I.J., Woese C.R.;
RT "The sequence, and its evolutionary implications, of a Thermococcus celer
RT protein associated with transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3854-3856(1994).
RN [2]
RP STRUCTURE BY NMR OF 58-110 IN COMPLEX WITH ZINC.
RX PubMed=9634694; DOI=10.1016/s0969-2126(98)00058-6;
RA Wang B., Jones D.N.M., Kaine B.P., Weiss M.A.;
RT "High-resolution structure of an archaeal zinc ribbon defines a general
RT architectural motif in eukaryotic RNA polymerases.";
RL Structure 6:555-569(1998).
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; L27650; AAA72052.1; -; Unassigned_DNA.
DR PIR; A55263; A55263.
DR PDB; 1QYP; NMR; -; A=58-110.
DR PDBsum; 1QYP; -.
DR AlphaFoldDB; Q56254; -.
DR SMR; Q56254; -.
DR EvolutionaryTrace; Q56254; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA: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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..110
FT /note="Transcription factor S"
FT /id="PRO_0000121483"
FT ZN_FING 4..25
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 67..107
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:9634694"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:9634694"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:9634694"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:9634694"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1QYP"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1QYP"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1QYP"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1QYP"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1QYP"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:1QYP"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1QYP"
SQ SEQUENCE 110 AA; 12970 MW; 3AE99D6905FD4E4E CRC64;
MKFCPKCGNL MLPDRKRKVW VCRSCGYEEP FDEEKDREKT VIKQEVKHKP DEGIVVIEQD
LKTLPTTKIT CPKCGNDTAY WWEMQTRAGD EPSTIFYKCT KCGHTWRSYE
