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Database: UniProt
Entry: A0A1D8G1H1_9ACTN
LinkDB: A0A1D8G1H1_9ACTN
Original site: A0A1D8G1H1_9ACTN 
ID   A0A1D8G1H1_9ACTN        Unreviewed;      1176 AA.
AC   A0A1D8G1H1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:AOT59300.1};
GN   ORFNames=A4G23_02137 {ECO:0000313|EMBL:AOT59300.1};
OS   Streptomyces rubrolavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT59300.1, ECO:0000313|Proteomes:UP000095349};
RN   [1] {ECO:0000313|EMBL:AOT59300.1, ECO:0000313|Proteomes:UP000095349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJM4426 {ECO:0000313|EMBL:AOT59300.1,
RC   ECO:0000313|Proteomes:UP000095349};
RA   Kim J.-G.;
RT   "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) 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; CP017316; AOT59300.1; -; Genomic_DNA.
DR   RefSeq; WP_031133197.1; NZ_CP017316.1.
DR   AlphaFoldDB; A0A1D8G1H1; -.
DR   STRING; 285473.A4G23_02137; -.
DR   KEGG; srn:A4G23_02137; -.
DR   PATRIC; fig|285473.5.peg.2228; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000095349; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000095349}.
FT   DOMAIN          641..802
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          827..977
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1176 AA;  128371 MW;  EC3B5A3AFE07F3D2 CRC64;
     MSLHGLLDAV VKDPALAEAV KAAADGRRAH VDLVGPPAAR PFAVAALARD AGRPVLAVTA
     TGREAEDLAA ALRSLLDPDR VVEYPSWETL PHERLSPRSD TVGRRLAVLR RLAHPSPDDP
     AAGPVQVVVA PVRSVLQPQV KGLGDLEPVS LRTGQSADLG AVVEGLAAAA YQRVELVEKR
     GEFAVRGGIL DVFPPTEEHP VRIEFWGDDV EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
     LTPQVRERAA ALAEAHPELG ELLGKIAEGI AVEGMESLAP VLVDDMELLL DVLPQGSMAV
     VCDPERVRTR SADLVATSQE FLQASWAATA GGGEAPIDVG AASLWSIADV RDRARELGMP
     WWTVSPFAPD AELEADTIQL GMHAPEAYRG DTARALADTK GWLADGWRTV YVTEAHGPAA
     RTVEVLGGEG IAARLEGELG DIAPSVVHVA CGSVEHGFVD EGLKLAVLTE TDLTGQKAAG
     KDGRRMPTRR RKTIDPLTLE AGDYIVHEQH GVGRYIEMVQ RTVQGATREY LLVEYAPAKR
     GQPGDRLYIP TDQLEQVTKY VGGEAPTLHR LGGADWTKTK QRAKKAVKEI AADLIKLYSA
     RMAAPGHTFG PDTPWQRELE DAFPYAETPD QLSTIAEVKE DMEKSVPMDR LICGDVGYGK
     TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFGTFSERYA QFPVVVKALS RFQSDAEAKA
     TLEGLREGSV DVVIGTHRLF SSETRFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
     SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE ERQIGAAIRR ELLREGQVFY
     IHNRVESIDR AAARLREIVP EARIATAHGQ MSEQALEQVV VDFWEKKFDV LVSTTIVESG
     IDISNANTLI VERGDNFGLS QLHQLRGRVG RGRERGYAYF LYPPEKPLTE TAHERLATIA
     QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YVRMVGEAVA DYRASLEGGR
     EEEPPLEVKI ELPVDAHVPH DYAPGERLRL QAYRAIASAN SEEDIRAVRE ELTDRYGKLP
     EPVENLLLVA GLRMLARACG VGEIVLQGAN IRFAPVELRE SQELRLKRLY PRTVIKAPAR
     QILVPRPTAG TIGGKPVVGR DLLAWTGEFL TTILGS
//
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