ID MFD_RICCN Reviewed; 1122 AA.
AC Q92H58;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 132.
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=RC0913;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03451.1; -; Genomic_DNA.
DR PIR; A97814; A97814.
DR RefSeq; WP_010977513.1; NC_003103.1.
DR AlphaFoldDB; Q92H58; -.
DR SMR; Q92H58; -.
DR GeneID; 928843; -.
DR KEGG; rco:RC0913; -.
DR PATRIC; fig|272944.4.peg.1038; -.
DR HOGENOM; CLU_005122_3_2_5; -.
DR Proteomes; UP000000816; 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 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 CDD; cd18810; SF2_C_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; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding.
FT CHAIN 1..1122
FT /note="Transcription-repair-coupling factor"
FT /id="PRO_0000281072"
FT DOMAIN 593..758
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT DOMAIN 779..933
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
FT MOTIF 711..714
FT /note="DEEQ box"
FT BINDING 606..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00969"
SQ SEQUENCE 1122 AA; 127560 MW; AA303708D4815E79 CRC64;
MLQQKFPAAA KSFFAIDNFT KNLKQDFILS ASNEEEALQL YKQALFFSSN ENIYYFPSYN
TIPYDHTSPN ANILSRRAET LIKLTTNNSN SNKLLITHTA NLLNKLPPKD FFSKYFLKLS
PKMKFTTDEL AMFLVENSFT RNASSIDVGE FAVRGEIIDI ILSGPKAYRI HFSWGYIESI
KEFDIDTQIS TKSCRELIIS PANEIVLNSE TIGNFKNNYL RNFGVNHTDN ALYEAVISGR
KFTGYEQLLP LFYDSCSNLI DYLNDPIFIF DNLSKKAILE FEHSYNDFYS ARSEANKLKF
NSFYPTLSPT SLYFTASEIT ELLEQKNNIL LTFENSEQAS LIKNIAATSF IEKKTVFDKL
FEVIKANSHK KIIIGSSVLS SFERIKSIIQ NYEYKYNEIN KLDEAKASII NVAIIPLNQS
FYTKEYLFIT ASELLEEKPS STNTNKKLKN ILLELDNLAE GEFVVHKDHG IGQFLKLEAL
EIKGKPHDFL KILYAGNDKL YIPVESIEVI KKYGNDNAEL DKLGSVSWQR SKAKLKKRIK
EIALHLIQIA AKRKLNSSAS VEFDLEEYDK FCANFPFSET EDQLIAINDI KEDLRNGMLM
DRLICGDVGF GKTEVAMRAV FMVAKSLNEH LPQVAVVVPT TILCSQHFSR FIERFKGFGL
NIKQLSSVIS SKEAKIIRSE LESGKINIII GTHSLLHKNI KFFNLKLLII DEEQHFGVGQ
KEFLKSLKSS SHVLAMSATP IPRTLQMSMT GLKELSIIAT PPLNRLEVHT SVMPYDPVII
RDALLREHFR GGRSFYVVPR IKDIEDIAKQ LKQIVPELSY KIAYGKMTPS KIDEVMSEFY
AGKFDILVST TIIESGIDIA EANTMIIHNA DMLGLSQLYQ LRGRIGRGKM RGYAYLTVAS
HKKMTSHSLR RLEIIQNSCA LGSGFTIASR DMDLRGFGNL IGEEQSGQIK EVGTELYQEM
LEEQIAIFKD ESIVSEQPFI PTINLGLSVF IPDNYVADAA LKLGLYRRIG NLSNEIEVET
FKDEMIDRFG LLPIEFNNLL DIVKIKLLCF KLNIENLDSG DNGFVIKFYK NADMTDKILK
FVTTYSNQAK IKPDNKLVYI KKLVDKNIIV EANQLLWNLS EV
//
