ID A0A1X7FUH1_9ACTN Unreviewed; 1176 AA.
AC A0A1X7FUH1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ORFNames=SAMN02745830_04646 {ECO:0000313|EMBL:SMF58957.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF58957.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF58957.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF58957.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWZW01000010; SMF58957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7FUH1; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000192930; 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; 3.40.50.11180; -; 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:UP000192930}.
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; 128790 MW; BBA6D4C55B12E514 CRC64;
MSLHGLLDAV VEDTALAEAI PAAADGNRMH VDLVGPPAAR PFAIAALARE TGRTVLAVTA
TGREAEDLAA ALRSLLPADG VVEYPSWETL PHERLSPRSD TVGRRLAVLR RLAHPRSDDP
ETGPVSVVVA PVRSVLQPQV QGLGDLEPVA LRTGQQADLN KTVEALAAAA YARVELVEKR
GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
LTEDVRTRAR ALAEDHPELG ELLGRIAEGI AVEGMESLAP VLVDDMELLI DVLPKGAMAV
VCDPERVRTR AADLVATSQE FLQASWAATA GGGEAPIDVD AASLWSLADV RDRARELDMM
WWSVSPFAAD LELEADTLQF GMHAPDTYRG DTAKALADTK GWLADGWRVV FVTEAHGPAA
RTVEVLGGEG VAARLHTDLT EITPAVVHVA CGSIDYGFVD PALRLVVLTE TDLSGQKAAG
KDGARMPARR RKTIDPLTLE TGDYIVHEQH GVGRYIEMVQ RTVQGATREY LVVEYAPAKR
GQPGDRLYIP TDQLEQITKY VGGEAPTLHR LGGADWTKTK ARAKKAVKEI AADLIKLYSA
RMAAPGHAFG TDTPWQRELE DAFPYAETPD QLTTIAEVKD DMEKTVPMDR LICGDVGYGK
TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFGTFSERYA QFPVNVRALS RFQTDAEAKA
TLEGLREGSV DIVIGTHRLF SSETKFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE QKQIGAAVRR ELLREGQVFY
IHNRVESIDR AAARLREIVP EARIATAHGQ MSETALEQVV VDFWEKKFDV LVSTTIVESG
IDISNANTLI VERGDTFGLS QLHQLRGRVG RGRERGYAYF LYPPEKPLTE TAHERLATIA
QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YVRMVGEAVA DYRRQLETGG
IEEEPPLEVK IELPVDAHVP HDYAPGERLR LQAYRSIASA NSEDDIKAVR EELVDRYGKL
PEPVENLLLV AGLRMLARAC GVGEIVLQGT NIRFAPVELR ESQELRLKRL YPGSVIKPAV
HQVLVPRPKT AKVGGKPLVG RELLGWVGEF LTSVVS
//
