MFD_RICPR
ID MFD_RICPR Reviewed; 1120 AA.
AC O05955;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
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=RP598;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-1120.
RC STRAIN=Madrid E;
RX PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA Andersson J.O., Andersson S.G.E.;
RT "Genomic rearrangements during evolution of the obligate intracellular
RT parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT nucleotide sequence.";
RL Microbiology 143:2783-2795(1997).
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}.
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DR EMBL; AJ235272; CAA15042.1; -; Genomic_DNA.
DR EMBL; Y11783; CAA72474.1; -; Genomic_DNA.
DR PIR; H71664; H71664.
DR RefSeq; NP_220966.1; NC_000963.1.
DR RefSeq; WP_004598992.1; NC_000963.1.
DR AlphaFoldDB; O05955; -.
DR SMR; O05955; -.
DR STRING; 272947.RP598; -.
DR PRIDE; O05955; -.
DR EnsemblBacteria; CAA15042; CAA15042; CAA15042.
DR GeneID; 57569723; -.
DR KEGG; rpr:RP598; -.
DR PATRIC; fig|272947.5.peg.616; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_3_2_5; -.
DR OMA; NKKAFCY; -.
DR Proteomes; UP000002480; 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; 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; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1120
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000102173"
FT DOMAIN 591..756
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 777..933
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; 127676 MW; 09C78EBE71D00482 CRC64;
MIQQKFPATA KCFYVIDNFT KNLNQDFILS VSNEEEALQL YKQALFFSSN DNIYYFPSYD
TIPYDHTSPN ANIVSRRAET LTKLITNSKG KLLITHAANL LNKLPPKDFF SKYFLKLYPK
IKFTMDELSM LLVENSFTRN TSSIDVGEFA VRGEIIDIIL PGPKGYRINF SWDYIESIKE
FDINTQISTK YCAELVISPA NEIVLNSETI GNFKNNYLRN FGVNHTDNPL YEAVISGRKF
AGYEQLLPLF YYSCSSLVDY LNNPICIFDN LSKQAILEFE NSYNDFYLAR SKANKLKVNN
FYPTLSPTSL YFTASAITEL LEQKNNILIS YENSEQASLI GNISSISFIE KKTIFDKLFE
IIKANFHKKI IICSSVLSSF ERIKSIIQNY EYTFNEINKL DEAKASVINI GIIPLNQSFY
TKEYLFITSS ELLEEKTLYT NTNKKLKNIL LELDNLKEGE FVVHKDHGIG QFLKLEAFKI
QGKLHDFLKI LYFGNDKLYV PVENIEVIKK YGSDNAELNK LGSVAWNKSK AKLKNRIKEI
SLHLIQIAAK RKLNISTPIE LDLEAYDKFC ANFPFSETED QLTAINDIRE DLTNGMLMDR
LICGDVGFGK TEVAMRAVFM VAKSLNEYLP QVAVVVPTTI LCSQHFSRFI ERFKGFGLNI
KQLSSVISSK EANIIRLELA SGKINIIIGT HALLHKNTKF FNLKLLIIDE EQHFGVSQKE
FLKSLKSSTH VLAMSATPIP RTLQMSMTGL KELSIIATPP LNRLEVRTSV MPFDPVIIRD
ALLREHFRGG RSFYVAPRIK DMEDIEKQLK QIVPELSYKI AHGKMTPSKI DEVMSEFYVG
KFDILISTTI IESGIDIAEA NTMIIHKADT LGLSQLYQLR GRIGRGKIRG YAYLTVASNK
KITSHSLRRL EIIQNSCSLG SGFTIASHDA DLRGFGNLIG EEQSGQIKEV GTELYQEMLE
EQIALLKDDP IVLEQAFIPN INLGLSVFIP DSYVSDSALK IGLYRRIGNL SNEMEVEKFK
DEMIDRFGLL PIEFNNLLDI VKIKLLCFKL NIENLDSGDD GFVIRFYKNA DMTDKILKFV
SRYSNQTKIK PNNKLVFIKK LVDKNIITEV NQLLWTLLEI
