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Database: UniProt
Entry: F9PNE3_9ACTO
LinkDB: F9PNE3_9ACTO
Original site: F9PNE3_9ACTO 
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
//
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