ID F9PNE3_9ACTO Unreviewed; 1251 AA.
AC F9PNE3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:EGV11522.1};
GN ORFNames=HMPREF9058_0430 {ECO:0000313|EMBL:EGV11522.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV11522.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV11522.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV11522.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGV11522.1}.
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DR EMBL; AFUR01000007; EGV11522.1; -; Genomic_DNA.
DR RefSeq; WP_009407572.1; NZ_AFUR01000007.1.
DR AlphaFoldDB; F9PNE3; -.
DR eggNOG; COG1197; Bacteria.
DR Proteomes; UP000004281; 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}.
FT DOMAIN 690..851
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 876..1026
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1251 AA; 133940 MW; 76C91786D3A4D729 CRC64;
MLLTALLPPL LADADIARTV RASSSRSRTD RSLVVAPGAR PAVLAAMALG EEGVQRVAGG
DAPTAGSAEA SGTPLLVVTA TGREAEETAL ALRSYLPAEN VAVMPAWETL PHERLSPRAD
TVAQRLSVLR RLAHPEEGGA IRVLIVPVRA LLAPVIAGLG ELEPVQLAPG LTVGLEETAR
RLEAAAYTRV DMVESRGEYA VRGGILDVFP PSEPRPVRVD FFGDEIDEVS SFAVADQRTI
ETLGAVTATA CRELVLTDAV RERAAALADA VPGAADMLEK ISQGIAVEGM ESLAPVLVEK
MVPLLDLVGD RLTVLLEPER VRKRAEDLTA TTTEFLAAAW TSAASGGTVP VDLSAAAFAH
LAEARALALS SNRGWWSFTA LAAGPETTRL DLSDPHTYRG ELERAVADLG RLARQGWTVV
VATDGPGPGR RMAQLLGDGD VPARIVDQLS EVGELGRDSD WVPAPAAVAD ETDADGSAGA
PTAGPGDGVV RVTQASAGHG FLAEGLRLAL IAESDLTGRA SAGPRERRSL PARRARRSVD
PLSLHAGDLV VHAQHGVGRF IELSRRTVGG ARSSATREYL VIEYAPSKRG QPGDRLLVPT
DALDQVTKYV GGDSPALSKM GGADWAKTKS KARKAVREIA GELVRLYAAR AATTGHAFSP
DTPWQTELEE AFPYTETPDQ LSTIDEVKAD MEKAQPMDRL VCGDVGYGKT EIAVRAAFKA
VQDGKQVAVL VPTTLLVSQH AETFTERYAG FPVTVAALSR FQDATESAKV LEGLEKGSVD
VVVGTHRLIT GQVKFKDLGL VIIDEEQRFG VEHKETLKAL RTNVDVLSMS ATPIPRTLEM
AVTGLREMST LATPPEDRHP ILTYVGAYET KQVSAAIRRE LLREGQVFFV HNRVEDIDAT
AARLAELVPE ARVATAHGQM NEHQLEAVID SFWRKETDVL VCTTIVETGL DVSNANTLIV
DRADRMGLSQ LHQLRGRVGR GRERAYAYFL YPSDKPLTET ALERLRTIAT NTDLGAGMQV
AMKDLEIRGS GNLLGGEQSG HIAGVGFDLY VRMVSEAVAA YKKALARSGK AGADAIGFEE
GDEEDVELRI ELPVDATVPE DYIPHERLRL EAYTKFAAAR SGEQVDDVLE ELTDRYGPVP
EATALLAALA RLRALAAELG VREIVAQGKS VRFAPVDLPE SARMKVTRLY PGTVLKPATR
TIVVPAPGTN RMGGAALSGE EVVRWAEVLL RAVVQGDTTY ETEATTYRKR R
//