ID A0A1C3YRD5_9NEIS Unreviewed; 1136 AA. AC A0A1C3YRD5; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-NOV-2016, entry version 2. 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; OC Neisseriaceae; Snodgrassella. OX NCBI_TaxID=1798181 {ECO:0000313|EMBL:SCB72643.1}; RN [1] {ECO:0000313|EMBL:SCB72643.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R-53583 {ECO:0000313|EMBL:SCB72643.1}; 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase CC family. 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 GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00969; TRCF; 1. 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; 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; 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 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 Helicase {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000313|EMBL:SCB72643.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969}. FT NP_BIND 620 627 ATP. {ECO:0000256|HAMAP-Rule:MF_00969}. FT MOTIF 721 724 DEAH box. {ECO:0000256|HAMAP-Rule: FT MF_00969}. 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 //