ID C1A324_RHOE4 Unreviewed; 1229 AA.
AC C1A324;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
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:BAH35009.1};
GN OrderedLocusNames=RER_43010 {ECO:0000313|EMBL:BAH35009.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH35009.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH35009.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(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: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; AP008957; BAH35009.1; -; Genomic_DNA.
DR AlphaFoldDB; C1A324; -.
DR KEGG; rer:RER_43010; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_11; -.
DR Proteomes; UP000002204; 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; 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}.
FT DOMAIN 683..844
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 869..1019
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1229 AA; 132529 MW; E78DFCAC3D83DB5E CRC64;
MEILRSGCAS ATRHHCSGAR SLTSLSSAQT ALAGLAEVAL ADAAFTPVID SIGAPALDIV
APKPARPFIA AALAARTPVL LVTATGREAD DLTSELTEML GGGVAQFPSW ETLPHERLSP
SADTVGRRVE VLRRLARPDD ASYGSPLRVI VTTVRSLVQP MAPGLGEIEP ITLRVGTEID
FDSVLVRLVE MAYSRVDMVG KRGEFAVRGG ILDLFSPTAD HPVRIEFWGD EVSELRYFSV
ADQRSLPDVD VDSVIAPPCR ELILTADVRD RAAALAAENQ ADASLVEMLD KISAGIPVEG
MEALLPVLKP GELQLLSDVL PVGAHILLCD PEKVRTRATD LVRTGQEFLE ASWTAASIGG
AAPLDTSILN GGGVDLGASA YRSLRHVRES AEAAGRPWWT VSPLASGNGE ELEIPVQAAP
QVRGSDDLLA ELFVSLRAHV STGGRAAIVV AGAGTASRVV ERLGEAEVPA KMLEGGATPA
RGQVAVLRGS LHDGLVLAGD DSTPGMVIVT ESDLTGNRVA AVGDGKRLPA KRRNQVDPLA
LSAGDMVVHD QHGIGRFVEM VERTIGGARR EYLVIEYAPS KRGHPGDRLF VPMESLDQLS
RYVGGELPAL SKLGGSDWAN TKRKARKAVR EIAGELVQLY AARQAAPGHA FGPDTPWQKE
LEDAFAFTET IDQLTVISEV KADMEKPVPM DRVVIGDVGY GKTEIAVRAA FKAVQDGKQV
AVLVPTTLLA QQHLQTFTER MASFPVKVRG LSRFTDAKDS KEIIAGMAEG EIDIVVGTHR
LLQTGIRWKD LGLVIVDEEQ RFGVEHKEHI KALRTHVDVL TMSATPIPRT LEMSMAGIRE
MSTILTPPEE RHPILTYVGA YADKQVAAAI RRELLRDGQV FYVHNRVSSI DKAAKKIREL
VPEARVVVAH GQMNEDTLEK TVQGFWERDF DVLVCTTIIE TGLDISNANT LIVERADSLG
LSQLHQLRGR VGRSRERGYA YFLYPAEKPL TETAYDRLAT ISQNSDLGAG MAVAMKDLEI
RGAGNVLGAE QSGHVAGVGF DLYVRLVGEA VEAFRAAADG KPITMDEGTK EVRIDLPVDA
HIPPDYVTSD RLRLEGYRKL AAATDSDGIA AVVEELVDRY GPLPEEVRRL ISVAKLRLLC
REYQLEEVAV TGTQLKISPM SLPDSKQIRL KRIYPSAQYR ATTGLVQLPL PRTGGVGSDR
LRDVELLQYI ADFILAIDGR AAGAVLVEA
//
