ID A0A1V2M8I1_9FIRM Unreviewed; 1174 AA.
AC A0A1V2M8I1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AN641_05990 {ECO:0000313|EMBL:ONI44766.1};
OS Epulopiscium sp. SCG-C07WGA-EpuloA2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1712378 {ECO:0000313|EMBL:ONI44766.1, ECO:0000313|Proteomes:UP000189533};
RN [1] {ECO:0000313|Proteomes:UP000189533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ngugi D.K., Miyake S., Stingl U.;
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: 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:ONI44766.1}.
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DR EMBL; LJHE01000054; ONI44766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2M8I1; -.
DR STRING; 1712378.AN641_05990; -.
DR Proteomes; UP000189533; 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:UP000189533}.
FT DOMAIN 644..805
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 814..980
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1174 AA; 134075 MW; EB766902AF99892A CRC64;
MINKKTALTS SLKKLDGIGE FINEFNKHKT GIVSGIIEAA KGHLIYTLSE FLNVCPFVIA
SSEEEGETLK EDLAFLFGEE NVMYYPSRDI LFYNADVHSN DIVKQRIEVL DAIIKNKNMI
IVTTIDALLN PLSSKEKFVK SQITIKNSDT LDLEILALQL IEIGYERTAR VETVGQFALR
GGIIDIFSPA NNAPVRIELW DTLVDSIRRF SPITQRSIDK TDKVTLYPNQ EIIISKEALI
KAVPKIQEEL KLTVQTLRNN DQEEVATKLE DKTTKDIEEI LEGRHAEVQI LYAPFCDLKT
TTIFSYLQDD KTIFITDVKK CKNKLYRVFT EYEESVKSRL EYGHILPNMI NFIFNKNDII
SQIFKNNYVA FMNFFIKDED IITKNILEIK INDTSTKYKN LKTFEDELKD YKKQNKITIF
LAGTKTKAVN IVKQLEEQQI YTALGDLNYD VQKGQILVTS GSLKHGFIYE DIGFVILSDR
ELFGKDKKTT SNKKKYKGAK IESFLELIEG DYVVHENHGI GVFVGIEKIV TDGVARDNLK
INYNGGVLYV NINQMDLVQK YVGSEGSVPK LNTLGNPEWK KAKTKAKCAT KNIAKELIAL
YSKREHSRGF VYEQDSIWQT EFEEMFPYQE TSDQLDAIKA VKEDMQSDKI MDRLVLGDVG
YGKTEVAIRA AFKAVLNQKQ VAYLVPTTVL SQQHYERFLK RMEAHAVSVG VLSRFRTPKQ
VKETLKGLEQ GTIDIVIGTH RLLSKDVKFK DLGLIIIDEE QRFGVTHKEK LKLLRTEVDA
LTLTATPIPR TLQMSLIGIR DMSVIEEAPS ERRAVQTYVL EESDEFIKDA INREINREGQ
VYFLSNRVQN IEEKAMKLSA MVPNAKVAFA HGQMSVRELE DIMERFENKE INVLVCTTII
ETGLDIANAN TIIINDADKM GLSQLYQLRG RVGRSDKQAY AYLLYQKDKT LSEIAEKRLN
AIKQFTQLGA GFKIAMRDLE IRGAGDLLGA SQSGHMEKIG YELYSKMLKE AIQIEQGAIL
KEKIETTVEI KINAFIPNNY IKDEIQKLDI YKKIASIQNE EDYHNVIEEI TDRYGDIPTT
VLNLLDIAII KALANEQEIS LISQNIHILM LKFSHKAKGK SLSLLAKKYS HNMKVNIDKE
VKILFDMKEI HQKDYLNFIK NVLFTIKEQE INNR
//
