ID C7DFJ5_9RHOB Unreviewed; 1151 AA.
AC C7DFJ5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
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 ECO:0000313|EMBL:EET47969.1};
GN ORFNames=TR2A62_0642 {ECO:0000313|EMBL:EET47969.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET47969.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET47969.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET47969.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) 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; GG697169; EET47969.1; -; Genomic_DNA.
DR RefSeq; WP_009159038.1; NZ_GG697169.2.
DR AlphaFoldDB; C7DFJ5; -.
DR STRING; 633131.TR2A62_0642; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_2_0_5; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000004701; 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; 3.40.50.11140; -; 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}; 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:UP000004701}.
FT DOMAIN 612..773
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 794..948
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1151 AA; 126940 MW; 61B6448FB2CCCFE1 CRC64;
MSQANEHRVL GGAPEGFDVQ LILAEVARSN APVCHVARDD KRLEAMRAAL AFFAPDMPVI
VFPGWDCLPY DRVSPNADVS AQRMATLAAL THDMPSHYVL LTTLNAGTQR VPGRDVLREA
SFKAQVGDRI DEKALRAFLV RMGFVQTPTV TEPGDYAVRG GIIDVYPPGD SGPVRLDLFG
DDLDGARRFD PATQRTTEKL DLIELAPVSE VILDEAAITR FRQTYRIEFG AAGTDDPLYE
AVSAGRKHQG VEHWMGFFYD RLETIFDFLP GVTITLDDQV TPSRIARWES IADQYHARRE
ALAMKKRMDT VYKPAAPELL YLDEAAWDQA TANHRVVQFH ALAQASGPGV ADASGRIGRN
FAPERQQESI SLFGALADHI TAKLAHGPVV IASYSEGARE RLTGLIEDEG IAEAIPIRSF
DGVGKRGVHL AVWALEHGFE TPDLTVISEQ DVLGDRLIRK GPRKRRAENF LTETQSLTPG
DLVVHVDHGV GRFRGLEVVT AAGAAHECLL LEYAEQSKLY LPVENIELLS KYGHDEGLLD
KLGGGAWQAK KAKLKERIRQ IAERLIRVAA ERELRTAPIM TPPDGMWDSF CARFPYVETE
DQLGAISDVI EDMGAGRPMD RLVCGDVGFG KTEVAMRAAF VAAMSGTQVA IIAPTTLLAR
QHYKSFAERF RGFPINVRPL SRFVGTKDAA ATRDGISDGT ADIVVGTHAL LAKSIKFKDL
GLLIIDEEQK FGVTHKERLK SLRTDVHVLT LTATPIPRTL QLSLSGVREL SIIGTPPVDR
LAIRTYVSEF DTITLREALL REHYRGGQSF FVVPRISDLP EIEDFLKSEV PEVSYIQANG
QLAAGELDDR MNAFYDGKYD VLLATTIVES GLDIPTANTM IVHRADMFGL SQLYQIRGRV
GRSKTRAYAY MTTKPRQKLT QTAEKRLRVL ASLDSLGAGF TLASQDLDIR GAGNLLGEEQ
SGQMREVGYE LYQQMLEEQI GKIKSGEAEG ITDDGEWSPN INLGVPVLIP DDYVPDLDVR
LGLYRRLSEL ATKVELEGFA AELIDRFGTL PREVNTLMLV VRIKAMCKKA GVSKLDAGPK
GATVMFHNNK FASPEGLVQF IQDQRGLAAV KDNRIVVKRD WKTDADKIRG AFAIVRDLAE
QAGAIKRKKK A
//
