MFD_RICBR
ID MFD_RICBR Reviewed; 1120 AA.
AC Q1RI82;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969}; OrderedLocusNames=RBE_0851;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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:0000255|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000255|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000255|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; CP000087; ABE04932.1; -; Genomic_DNA.
DR RefSeq; WP_011477517.1; NC_007940.1.
DR AlphaFoldDB; Q1RI82; -.
DR SMR; Q1RI82; -.
DR STRING; 336407.RBE_0851; -.
DR PRIDE; Q1RI82; -.
DR EnsemblBacteria; ABE04932; ABE04932; RBE_0851.
DR KEGG; rbe:RBE_0851; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_3_2_5; -.
DR OMA; NKKAFCY; -.
DR OrthoDB; 234717at2; -.
DR Proteomes; UP000001951; Chromosome.
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 transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
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_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
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; 2.
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; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding.
FT CHAIN 1..1120
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000281071"
FT DOMAIN 591..756
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 777..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 709..712
FT /note="DEEQ box"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1120 AA; 127304 MW; F36F46EEB2A403E5 CRC64;
MLQQKFPQAA KSFFTIDSFI KNSKQDFVLV TSNEEEALQL YKQALFFLPS ENIYYFPSYD
TIPYDHTSPN CNILSKRAET LSKLTTNKGN KLVITHATNL LNKLPPKDFF AKYYLKLFPK
MKLSANELSK FLVENSFTRN ASTVDVGEFA VRGEIVDLIL PESKGYRINF SWDYVESIKQ
FDIDTQISTR SCNELIISPA NEIVLNPETI SNFKDNYLRN FGVNHTDNPL YEAITGGRKF
SGYEQLLPLF YDSYSGLTDY LNNPVIIFDN LTKQAILEFE HSYNDFYKAR LDANKLKFNS
FYPTLSPSQL YFTSLEAIEL LEQENNILIS YENSEQASIV ENIAAASFVE KKTIFDKLFE
VIKANSRKKI IIGSSVLSSF ERVKSIIENY EYSYNEIEYL EEAKTNTINI AILPLNQSFS
TPEYLFIAAS ELLEEKVTPT NTNKKLKNIL LELDHLAEGE LIVHKDHGIG QFLKLEALEI
KGKLHDFLKI LYAGNDKLYI PVENIEVIKK YGSDVAQLDK LGSVSWQKNK AKLKNRIKEI
ALHLMQIAAK RKLNTTAAIE FDLEEYDKFC AKFPFTETED QLNAINDIRE DLSNGMLMDR
LICGDVGFGK TEVAMRAAFM VAKSLNENSP QVAVVVPTTI LCSQHFARFT ERFKDSDLNI
KQLSSVVSSK EAKIVRSELE SGKINIIIGT HSLLHKVTKF CNLKLLIIDE EQHFGVGQKE
FLKSLKSSTH VLAMSATPIP RTLQMSMTGL KELSIIATPP LNRLEVRTSV MPFDPVIIRD
ALLHEHFRGG KSFFVVPRIN DIEDIEKQLK QIVPELSYKV AHGKMSPNKI DEIMSEFYAG
KFDILISTTI IESGIDIQDA NTMIIHKADM LGLSQLYQLR GRIGRGKMRG YAYLTLPSHK
KMTPHSLRRL EIIQNSCALG SGFTIASHDM DLRGFGNLIG EEQSGQIREV GTELYQEMLE
EQIAIFKDEP ISGEQPFIPT INLGLSVFIP DNYVSDSVLK LGLYRRIGNL NDDLEVEKFK
DEMIDRFGSL PTEFNNLLDI VKIKLLCFKL NIENLDSGDN GFVIKFYKNA DMADKILKFV
STYTANAKIK PDNKLVFIKK LVGKTIITEA NQLLWNLSEI
