ID B7A7D1_THEAQ Unreviewed; 699 AA. AC B7A7D1; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-APR-2021, entry version 58. DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969}; DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969}; GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969}; GN ORFNames=TaqDRAFT_5334 {ECO:0000313|EMBL:EED10623.1}; OS Thermus aquaticus Y51MC23. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=498848 {ECO:0000313|EMBL:EED10623.1, ECO:0000313|Proteomes:UP000005403}; RN [1] {ECO:0000313|EMBL:EED10623.1, ECO:0000313|Proteomes:UP000005403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y51MC23 {ECO:0000313|EMBL:EED10623.1, RC ECO:0000313|Proteomes:UP000005403}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., Brettin T.S., RA Mead D.; RT "Sequencing of the draft genome and assembly of Thermus aquaticus RT Y51MC23."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent CC release of RNAP and its truncated transcript from the DNA, and CC recruitment of nucleotide excision repair machinery to the damaged CC site. {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family. CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EED10623.1}. 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; ABVK02000003; EED10623.1; -; Genomic_DNA. DR STRING; 498848.TaqDRAFT_5334; -. DR EnsemblBacteria; EED10623; EED10623; TaqDRAFT_5334. DR eggNOG; COG1197; Bacteria. DR Proteomes; UP000005403; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule. DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule. DR Gene3D; 2.30.30.840; -; 1. DR Gene3D; 3.90.1150.50; -; 1. DR HAMAP; MF_00969; TRCF; 1. DR InterPro; IPR036101; CarD-like/TRCF_dom_sf. DR InterPro; IPR003711; CarD-like/TRCF_domain. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR004576; Mfd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR037235; TRCF-like_C. DR InterPro; IPR005118; TRCF_C. DR Pfam; PF02559; CarD_CdnL_TRCF; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF03461; TRCF; 1. DR SMART; SM01058; CarD_TRCF; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00982; TRCF; 1. DR SUPFAM; SSF141259; SSF141259; 1. DR SUPFAM; SSF143517; SSF143517; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00580; mfd; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00969}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00969}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969}. FT DOMAIN 178..339 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 360..517 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT COILED 110..137 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 533..553 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 699 AA; 78341 MW; 339E3A5824DA31BF CRC64; MRAGWSGGEE VLLTEALVFA TGAVRARVRL GEGLSDPGAL SPGDFLIHPE HGIGQYLGLE TREVLGVRRD YLVLRYRGEG RLYLPVEGLP LLKRHPGTTD DPPELSSLGK GEWQRAKEKA RKDVEELAAR LLVLHAKRKA TPGRAFPALP EWDPLVEAGF PHELTPDQRQ ALEEVLRDLE SPHPMDRLVS GDVGFGKTEV ALRAAHRVVG HGAQVAFLVP TTLLAEQHGR TFRERFRGLP VRVEVLSRFT PPKEEGAILK DLKEGRVDIV IGTHRLLQPD VAFKDLGLLI VDEEHRFGVA QKERIRELKE NVDTLYLSAT PIPRTLYSAL VGLKDLSSIK TPPPGRKPIK TFLAPFDPLL VREAILNELE RGGKAFYVHH RVASIEARRR YLEDLVPEAR IGVVHGQMPE GLIEETMMLF AEGAYDVLLA TTIIEAGLDV PEAGTILIER ADLLGLATLY QLRGRVGRRD QEAYAYLFHP PRLTEAAEKR LHAIADLSDL GSGHLLAEKD MEIRGVGNLL GPEQHGHIRA LSLEVYTELL EEALRKLKGE RVEERPHVTL DLALSARLPA EYVGSLEARS RYYSRFAEAK TLAEVSRLVR ELKERYGPLP EEAENFVNLT RLRLVAERKG ALSITEDLTH LVVVFPRYPL DYDARALKAL PHRVEITQYP PGFRLPKKGL RPRDYPEALM EVLYLFADR //