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Database: UniProt
Entry: F9MPP5_9FIRM
LinkDB: F9MPP5_9FIRM
Original site: F9MPP5_9FIRM 
ID   F9MPP5_9FIRM            Unreviewed;      1095 AA.
AC   F9MPP5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
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:EGS33116.1};
GN   ORFNames=HMPREF1040_0699 {ECO:0000313|EMBL:EGS33116.1};
OS   Megasphaera sp. UPII 135-E.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS33116.1, ECO:0000313|Proteomes:UP000004137};
RN   [1] {ECO:0000313|EMBL:EGS33116.1, ECO:0000313|Proteomes:UP000004137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS33116.1,
RC   ECO:0000313|Proteomes:UP000004137};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUN-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:EGS33116.1}.
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DR   EMBL; AFUG01000032; EGS33116.1; -; Genomic_DNA.
DR   RefSeq; WP_007392799.1; NZ_AFUG01000032.1.
DR   AlphaFoldDB; F9MPP5; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000004137; 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:UP000004137}.
FT   DOMAIN          564..725
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          746..900
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1095 AA;  125793 MW;  878551F026A79B55 CRC64;
     MKQLFKWLDQ EENLRQIKNF FINGGCNHIH GVGGSAKHIL VAQGIDTALG VTLLITSSSE
     EMEKWKSDLQ FLVPTIPIFT FPFVVQELFS TAAKSMERVA RQMEVLAQLR EDKKCIILTT
     VEEASQYIIA PSQLDNRVIS FEVKQEYERA ALLEKLIQNG YERVELVERC GHFSIRGDIL
     DIYAVNQTKP IRLEFFGDTI EKIRLFDVLS QTSIQTVEQV QVLPFSLSWD EHQPYNATIL
     DYLHKGQIIW DEPNRLRDNL KKALTESDDY VSHLCPWRTW VTRTYPCSQV LISLLSPTFY
     DMKVESSIHL VTKRMSSFQK QFSLLKEELL HWHAEGKTVV LVIDNLNRKA SLQAWMQQEG
     FSIETHIPDT LQKGVCYLVT GNLQNGFEFP HAHLVILCER DIYGMQKRRL FLKHTQSQKI
     NTFTDLKKGD YVVHHSHGIG RYMGLKTMEI DDVHRDYLEI HYAGNDILYV PIEQMALVQR
     YIGNEGDIPK LHRMGGKDWQ KARAKAQKSV DNLAEKLLSL YAKREVVSGF AYPPDTPFQR
     EFEEAFPYEE TEDQLRAVAE IKKYMERPFP MDCLVCGDVG FGKTEVAMRA IFKAVMSHKQ
     VAVLVPTTVL AQQHFLTFTE RLASFGVQCE VLNRFRSVKE RKNILARTKL GQVDVLIGTH
     SILNKQVQFK QLGLLVVDEE QRFGVAQKEK WKSLAAHVDV LSLSATPIPR TLHMSLVKLR
     EMCIMETPPI DRFPVQTYVT EYDPTVIREA ITREKRRGGQ VFFIYNQVES MGYMKNELER
     LVPEFSIAMA HGQMSGAMLE AVMFDFYEGK YDILLCSSLV ENGLDVANAN TIIVYDADHF
     GLSQLYQMRG RVGRSHNLAY AYLCYRKNKV LSEIAEKRLS AIKEFTELGS GFKIAMRDLE
     IRGAGNLLGR EQHGNIAGVG FSMYCQMLEG AIKRLQNGIS DETERIETVL DIQVNAYIDN
     EYITNNGQKI DIYQRLAIAD TSDEINALEK ELTDRYGTMT DPVIALLQVA IIRVAARKLG
     ITLISQKKDY VEIKWQQVAQ MPHLSALDPA LQKRVRYIRG LPTVWRIDWM QEMDIISFIN
     YLIKVFCLQR KGTKK
//
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