ID A0A1C3YRD5_9NEIS Unreviewed; 1136 AA. AC A0A1C3YRD5; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 11-DEC-2019, entry version 17. 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=GA0061082_10186 {ECO:0000313|EMBL:SCB72643.1}; OS Snodgrassella sp. R-53583. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Snodgrassella; unclassified Snodgrassella. OX NCBI_TaxID=1798181 {ECO:0000313|EMBL:SCB72643.1, ECO:0000313|Proteomes:UP000198676}; RN [1] {ECO:0000313|EMBL:SCB72643.1, ECO:0000313|Proteomes:UP000198676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-53583 {ECO:0000313|EMBL:SCB72643.1, RC ECO:0000313|Proteomes:UP000198676}; RA Seilhamer J.J.; RL Submitted (AUG-2016) 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 -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. A damage recognition complex composed of 2 CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB CC and probably causes local melting of the DNA helix, facilitating CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB CC probes one DNA strand for the presence of a lesion. If a lesion is CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex CC is formed. This complex is subsequently bound by UvrC and the second CC UvrB is released. If no lesion is found, the DNA wraps around the other CC UvrB subunit that will check the other stand for damage. CC {ECO:0000256|SAAS:SAAS00384282}. CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for CC lesions. Interacts with UvrC in an incision complex. CC {ECO:0000256|SAAS:SAAS00088351}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969, CC ECO:0000256|SAAS:SAAS01200955}. CC -!- SIMILARITY: Belongs to the UvrB family. CC {ECO:0000256|SAAS:SAAS00571129}. 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 --------------------------------------------------------------------------- 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; FMAP01000001; SCB72643.1; -; Genomic_DNA. DR Proteomes; UP000198676; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. 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:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW. 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 InterPro; IPR004807; UvrB. DR InterPro; IPR041471; UvrB_inter. DR PANTHER; PTHR24029; PTHR24029; 2. DR Pfam; PF02559; CarD_CdnL_TRCF; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF03461; TRCF; 1. DR Pfam; PF17757; UvrB_inter; 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; 4. 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 ECO:0000256|SAAS:SAAS01200956}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969, ECO:0000256|SAAS:SAAS01200952}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|SAAS:SAAS01200947}; KW DNA excision {ECO:0000256|SAAS:SAAS00460563}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|SAAS:SAAS01200950}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00969}; KW Excision nuclease {ECO:0000256|SAAS:SAAS00460694}; KW Helicase {ECO:0000313|EMBL:SCB72643.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|SAAS:SAAS01200961}; KW SOS response {ECO:0000256|SAAS:SAAS00088434}. FT DOMAIN 607..768 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 789..941 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT COILED 550..570 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 591..611 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 1136 AA; 126983 MW; F2EB0F69CCC9A664 CRC64; MPSVAPFVLP QANQTAFWPD LNAGSLPLLL SKHLPEKKLK IILTADAEQA IRIQSAWQFF DPSARIVFFP DWETLPYEHF SPHQELVSER LSTLWQLKNG LVDVLLLPLA TAMQKIAPPS FLLGRTFWLK TGQQLDIEAL KHSLIEAGYN HVTHVVATGE FATRGGILDI FPMGSEIPFR LDLFDNEIDT IKTFDADSQR TLSSVDEIRL LPAHEFPTDS DAQKIFRSRF REEISSDARK ATVYAAVSEG HFGAGVEYYL PLFFEEECVS IFDYIHEDAI LVCLGDIYNE AARIWQDVKQ RYTLAQGDPA YPPLAPNYLY LSEDQFGAHI KTYARLIPQL SAENIYTLPG VAVDRQADDP LHALKNFLKQ YTGRVLICAE SLGRRETMLN FMREHNLQPN VVNGWQDFLN GSTKLCLTVA PLSYGCLLPE QQLAIITEAD LYQYVVRGRR TRRKHSAISD GMLRDLAEIK IGDPVVHEQH GIGRYLGLVT LDLGEGASEM MLLEYAEGSQ LYVPVNQLQL ISRYAGSAHE NVSLHKLGHG AWDKARHKAA EKARDTAAEL LNLYAQREAQ QGHRFSLNEM DYQAFAQGFG YEETEDQAAA IAATIKDLCA EKPMDRLICG DVGFGKTEVA LRAAFVAAMA GKQVVVLAPT TLLVEQHAQN FADRFADFPI KVAQLSRFNT SKQTQATLSG LADGTVDIVI GTHKLVQPDV HFKNLGLVII DEEHRFGVRQ KEQLKRLRAN VDVLTLTATP IPRTLSMALE GLRDFSLITT APSRRLAVKT FVRQFSDGLI REAVMRELKR GGQVFFLHNE VDTIANTHEK LSTLLPEARI GIAHGQLRER ELEQVMRDFL QQRYNILLCS TIIETGIDIP NANTIIIERA DKFGLAQLHQ LRGRVGRSHH QAYAYLLVPE AMTKDAQKRL EAIEIADDLG AGFTLAMQDL EIRGAGEILG EGQSGEMIQV GFTLYTEMLK QAVRNLKKGR EPDLDAPLGI TSDIKLHSPA LLPENYCPDI HARLVLYKRL ASCETIAEID QIHEELIDRF GLPEPAVSTL IASHHLRIEA ASLGIDTIDA SSEAITFTFG KHHRINPATI VAIMQSDKNY RLVGADKLRV NIAIEDVMQR VQIIKNIMKQ LAVDAG //