ID G2NEE8_STREK Unreviewed; 1176 AA.
AC G2NEE8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=SACTE_2569 {ECO:0000313|EMBL:AEN10457.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN10457.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN10457.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN10457.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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; CP002993; AEN10457.1; -; Genomic_DNA.
DR RefSeq; WP_014046441.1; NC_015953.1.
DR AlphaFoldDB; G2NEE8; -.
DR STRING; 862751.SACTE_2569; -.
DR KEGG; ssx:SACTE_2569; -.
DR PATRIC; fig|862751.12.peg.2677; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000001397; 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:UP000001397}.
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; 128099 MW; 9C6DD8D13B0404A2 CRC64;
MSLHGLLDVV VTDPALAEAV KAATDGHRSH VDLVGPPAAR PFAVAALARE AGRTVLAVTA
TGREAEDLAA ALRTLLPPDT IAEFPSWETL PHERLSPRSD TVGRRLAVLR RLAHPRADDP
ETGPVGVVVA PIRSVLQPQV KGLGDLEPVA LSSGQTADLG EVVDALAAAA YARVELVEKR
GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKVAD QRSLEVAAHG LWAPPCRELL
LTEDVRNRAA ALAEAHPELG ELLGKIAEGI AVEGMESLAP VLVDEMELLL DVLPKGSMAL
VCDPERVRTR AADLVATSQE FLQASWAATA GGGDAPIDVG AASLWGIADV RDRARELGMM
WWSTSPFTAD EEVAEDTLTL GMRAPEAYRG DTARALADTK GWLADGWRTV YVTEGHGTAS
RIAGVLGGEG IAARVETELA EIAPSLVHVA CGAVDQGFVD PGLKLAVLTE TDLTGQRTAS
KDLGRMPARR RKSIDPLTLQ AGDYIVHEQH GVGRYIEMVQ RTVQGATREY LLVEYAPAKR
GQPGDRLYIP TDQLEQVTKY VGGEAPTLHR LGGADWTKTK QRAKKAVKEI AADLIKLYSA
RMAAPGHTFA PDTPWQRELE DAFPYAETPD QLSTIAEVKE DMEKSVPMDR LICGDVGYGK
TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HYGTFTERYA QFPVNVRALS RFQSDTESKA
TLEGLRDGSV DLVIGTHRLF SSETKFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE EKQIGAAVRR ELLREGQVFY
IHNRVESIDR AAARLREIVP EARIATAHGQ MGEGALEQVV VDFWEKKFDV LVSTTIVESG
IDISNANTLI VERGDNFGLS QLHQLRGRVG RGRDRGYAYF LYPPEKPLTE TAHERLATIA
QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YIRMVGEAVA DYRAAVDGGE
EEEAPLEVKI ELPVDAHVPH DYAPGERLRL QAYRAIASAN TEDDIRAVRE ELTDRYGKLP
EPVENLLLVA GLRMLARACG VGEIVLQGPN IRFAPVQLRE SQELRLKRLH PKTVIKAPAH
QILVPRPTAG RIGGKPVVGR ELLAWTGEFL TTILGS
//
