ID A0A1K1MMK2_9FIRM Unreviewed; 1160 AA.
AC A0A1K1MMK2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN02910447_00990 {ECO:0000313|EMBL:SFW23158.1};
OS Ruminococcus sp. YE71.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=244362 {ECO:0000313|EMBL:SFW23158.1, ECO:0000313|Proteomes:UP000182164};
RN [1] {ECO:0000313|EMBL:SFW23158.1, ECO:0000313|Proteomes:UP000182164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE71 {ECO:0000313|EMBL:SFW23158.1,
RC ECO:0000313|Proteomes:UP000182164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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: 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}.
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DR EMBL; FPIR01000004; SFW23158.1; -; Genomic_DNA.
DR RefSeq; WP_072417118.1; NZ_FPIR01000004.1.
DR AlphaFoldDB; A0A1K1MMK2; -.
DR STRING; 244362.SAMN02910447_00990; -.
DR Proteomes; UP000182164; 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; 4.
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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SFW23158.1};
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:UP000182164}.
FT DOMAIN 627..788
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 809..963
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1160 AA; 129495 MW; 9646A481EC30AB94 CRC64;
MNIFDRILHK TEFYNDLYNT AAGGYTPISV TGVAGIHKAH IAAALAADTS VLLVCADEAA
AVRAAQDINT LADRRLACVF PEKEFVFVPM EGVSNEYVHR RIEALSLILT GECRVLCCSA
AAACQATVPP DVLEEYSFRL EVGGEINTDT LIRRLTAAGY SRCEMVEGQA QFSVRGSVVD
IFPVSDSEPV RIELWGDEID SAARFDTETQ RRTEPVDCVT VFPALEVIFG SQEEFCERID
KLSQSLRMKN ADAVRAYLMR DREMVETGLS LTNPDKYYSL AYETSAFVTD YFSKGVCLVS
EYTSACENLR GFSDQLSEDL KLMYESGIMF KRLEGYMADS GLLEAKMLAL PCIFLDTFMR
QNGSIRFKKL INTDCRQTAG WGGSMTALTE ELNEYIGQGY SVVLLAGSEK TLPIIVSDLC
EDGFRAEILT EDSEPEAGRV YVRTGSLSSG VDYPTAGCAV ITQMKSANIV KKKKKRKNDD
VIRALTELHP GDLVVHSIHG IGRFRGIESI AANGVKKDYI TIKYSGTDVL YVPVTQLDLV
SRYVGASDDT TVKLSRLGSI EWQKTRSRVK KAVRDMAEEL TKLYAQRQTV FGHAFSPDND
WQRDFEDRFD YQETDDQLRC INEIKEDMEK VQPMDRLLCG DVGFGKTEVA LRAAFKCVLD
SKQAAILVPT TVLAWQHYQT AIKRFEHFPI KVELLSRFRT PQQQAQIVRE LKRGTIDVII
GTHRLVSKDV GFKDLGLVII DEEQRFGVAA KEKLKELFTG VDVLTLSATP IPRTLNMALS
GIRDMSVIEE PPQDRRPIQT YVTEHSPAVI GQAISKELRR GGQVYYIHNR IDTIYRTADE
IAKLVPGARV GVAHGRLSEH ELSEIWRQLI EGEIDVLVCT TLIETGVDVP NVNTLIIEDA
DYLGLSQMHQ LRGRVGRSSR RAYAYLTFRR GKVLSEVATK RLEAIKEFTK FGSGFHIAMR
DLEIRGAGSI LSGRQHGHME AVGYDLYLQL LNEAIAEQKG EAPPPSPEDC LIDIMIDAFI
PETYIESDML RIDAYRRIAS IVSVEDSRDV IDEFIDRFGD PPKPVMGLIN VALVRNSAAA
LGIREISQKG AKAVFTMREF KPEYAPKLLE KYGKRLRFIQ GDAPGFSIDI SAKQPTAELI
TEVVAVMRGQ DGKPDNVKKK
//
