ID R9K5H1_9FIRM Unreviewed; 1184 AA.
AC R9K5H1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=C809_04130 {ECO:0000313|EMBL:EOS41695.1};
OS Lachnospiraceae bacterium MD335.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS41695.1, ECO:0000313|Proteomes:UP000014081};
RN [1] {ECO:0000313|EMBL:EOS41695.1, ECO:0000313|Proteomes:UP000014081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COE1 {ECO:0000313|EMBL:EOS41695.1,
RC ECO:0000313|Proteomes:UP000014081};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium COE1.";
RL Submitted (APR-2013) 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:EOS41695.1}.
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; ASSW01000068; EOS41695.1; -; Genomic_DNA.
DR AlphaFoldDB; R9K5H1; -.
DR STRING; 1235793.C809_04130; -.
DR PATRIC; fig|1235793.3.peg.4306; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000014081; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
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; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 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; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF143517; TRCF domain-like; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000014081}.
FT DOMAIN 649..810
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 819..985
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1184 AA; 135279 MW; 25C2E883FACBAD58 CRC64;
MNLLFAPLKE LGEYEEIVKG LAAADGKVSI SGCVDTQKLH MVFGLGAGEM CTDFDVRLIV
TYSDMKAREL LEDCRLYCRD SYFYPAKDLI FYQADIHGRQ LSKERLEVQR RILEGAPITI
VTTFAALMAH QVPLSVLQEN IIEISKDSVI EENALARKLV AMGYEKSYQV EAAGQFSIRG
GIVDIFDLTA DNPVRIELWG DTVESIRSFD VLSQRSIEEN MTHVSVYPAT ELILSQKSLD
KGFHQIERDC KERAAYFRKN TKPEEAHRLE LYIQDLKEQV TQFQSYINLE SFLGYFYDNT
MSFADFFADR KCCVYIDEPL RVEEHARAVE LEFRESMSSR AMGGYILPKQ QDVLFGVPQI
MARLEGMRVL ALSTMEFKNF GLRFANRFSV NARNISSYNN SFPELVKDLK IYKKKGFRVL
LLSTSATRAK RLASDLMDEG LGAFYTEDCE RAQQPGEIIT YHGSALKGFE YPYLKLAVIS
ETDIFGKQQK KKKRKKSFSG GVKIQDFSDL KVGDYVVHEN HGLGIYKGIE KVEVDKVVKD
YIKIAYRDGG NLYILATGLD VIQKYAAADA AKKPKLNKLG TQEWAKTKSR VKTAVNEIAR
DLVELYAVRQ KKQGFVFSKD TVWQQEFEEM FPFEETDDQL LAIEATKSDM ESPRIMDRLI
CGDVGYGKTE IAIRAAFKAV QDGKQVAYLV PTTILAQQHY NTFLQRMKDF PVTVEMMSRF
RTAGEMKKTI EGLKKGMVDI VIGTHRLLSE DVKYKELGLL IIDEEQRFGV RHKEKIKQIK
DDVDVLTLTA TPIPRTLHMS LLGIRDMSVL EEAPGERQPI QTYVMEYNEE LVREAVLREL
SRGGQVYYVY NRVNNIDDVT DRIAKLVPEA NVAFAHGQMK EHELEKIMFE FINGEIDVLV
STTIIETGLD ISNVNTMIIH DSDNMGLSQL YQLRGRVGRS NRTAYAFLMY KKDKMLKEVA
EKRLQAIKEF TDLGSGFKIA MRDLEIRGAG NLLGERQHGH MEAVGYDLYC KMLNEAVKTL
KGVKTADEDF NTYVDMDVDA FIPASYIVNE VQKLDIYKRI ASLENEAECD DMRKELKDRF
GNVPKSVENL IKISLIRVTA HKRYVTEIKG KVGQITFFME AYAPVHVEKL PEFMGRYQGT
MEFSAKGTPN FVFRYKKYGL VEKEAELMME HTNRVLEDMA VLYV
//
