ID A0A1M5Z7B7_9ACTN Unreviewed; 1177 AA.
AC A0A1M5Z7B7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05444521_5285 {ECO:0000313|EMBL:SHI20125.1};
OS Streptomyces sp. 3214.6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHI20125.1, ECO:0000313|Proteomes:UP000190947};
RN [1] {ECO:0000313|Proteomes:UP000190947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; LT670819; SHI20125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5Z7B7; -.
DR STRING; 1882757.SAMN05444521_5285; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000190947; Chromosome i.
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:UP000190947}.
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 1177 AA; 128735 MW; F3E4D25DB01DA63B CRC64;
MSLHGLLDAV VKDTALAEAI PAAADGNRMH VDLVGPPAAR PFAIAALARE SARTVLAVTA
TGREAEDLAA ALRSLLPPDG VVEYPSWETL PHERLSPRSD TVGRRLAVLR RLAHPRPDDP
ETGPVSVVVA PVRSVLQPQV KGLGDLEPVA LRTGRSADLN EIVEALAAAA YARVELVEKR
GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
LTEDVRTRAR ALAEQHPELG ELLNKIAEGI AVEGMESLAP VLVDDMELLL DVLPKGAMAV
VCDPERVRTR AADLVATSQE FLQASWAATA GGGEAPIDVG AASLWSLADV RDHARELDMM
WWSVSPFVAD LELEADTLQF GMHAPDTYRG DTAKALADTK GWLADGWRVV FVTEAHGPAA
RTVEVLGGEG VAARLDADLT DLGPSLVHVS CGSIDYGFVD PALRLAVLTE TDLSGQKAAG
KDGARMPARR RKTIDPLTLE AGDYIVHEQH GVGRYIEMVQ RTVQGATREY LVVEYAPAKR
GQPGDRLYIP TDQLEQITKY VGGEAPTLHR LGGADWTKTK ARAKKAVKEI AADLIKLYSA
RMAAPGHAFG TDTPWQRELE DAFPYAETPD QLTTIAEVKD DMEKTVPMDR LICGDVGYGK
TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFGTFSERYA QFPVKVRALS RFQTDTEAKA
TLEGLREGGV DVVIGTHRLF SSETKFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE QKQIGAAIRR ELLREGQVFY
IHNRVESIDR AAARLREIVP EARIATAHGQ MSETALEQVV VDFWEKKFDV LVSTTIVESG
IDISNANTLI VERGDTFGLS QLHQLRGRVG RGRERGYAYF LYPPEKPLTE TAHERLATIA
QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YVRMVGEAVA DYRRQLETGA
IEEEPPLEVK IELPVDAHVP HDYAPGERLR LQAYRAIASA NSEDDVKAVR EELVDRYGKL
PEPVENLLLV AGLRMLARAC DVGEIVLQGA NIRFAPVELR ESQELRLKRL YPGSVIKPAA
HQVLVPRPKT AKVGGKPLVG RDLLGWVGEF LATVLGS
//
