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Database: UniProt
Entry: G9WQI7_9FIRM
LinkDB: G9WQI7_9FIRM
Original site: G9WQI7_9FIRM 
ID   G9WQI7_9FIRM            Unreviewed;      1122 AA.
AC   G9WQI7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=HMPREF9625_01620 {ECO:0000313|EMBL:EHL09647.1};
OS   Oribacterium parvum ACB1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=796943 {ECO:0000313|EMBL:EHL09647.1, ECO:0000313|Proteomes:UP000018461};
RN   [1] {ECO:0000313|Proteomes:UP000018461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACB1 {ECO:0000313|Proteomes:UP000018461};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACB1 {ECO:0000313|Proteomes:UP000018461};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA   Epstein S., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Oribacterium sp. ACB1.";
RL   Submitted (MAR-2013) 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:EHL09647.1}.
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DR   EMBL; AFZC01000019; EHL09647.1; -; Genomic_DNA.
DR   RefSeq; WP_009535460.1; NZ_KE148312.1.
DR   AlphaFoldDB; G9WQI7; -.
DR   STRING; 796943.HMPREF9625_01620; -.
DR   GeneID; 84784463; -.
DR   PATRIC; fig|796943.3.peg.2084; -.
DR   HOGENOM; CLU_005122_1_3_9; -.
DR   Proteomes; UP000018461; 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; 3.40.50.300; 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:UP000018461}.
FT   DOMAIN          591..752
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          773..927
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1122 AA;  127694 MW;  B0171532B30E8661 CRC64;
     MLNNNEVNKG ESVYTNPVEE TLLFQSMRER LDLGGQVFYA GIVDSLKPLL ALPFAKNWAL
     YLCKNEERAK EVLQDCKAFS ENAYYYPPKD YLFYKADTRG HYILRERGEC LRHLLEEESG
     IVVTTFSSLM EKMEGKNAFQ VSLFTVKIGM HIELSDLQEK LSQMGYKRVE QIEMRGEYSI
     RGGIVDIFSN QMEDPVRIEF FGEEVDSIRH FSLESQRSLW QIEEAKLYPA GERGFSSSLK
     AFSLLDYFPK DAVVFLDEPA RLLEEAERVE AEFLNFFEAN TEEEEKVELF SPQTLLTEIG
     ERAFAAFSTL GTGLDSLVDV ADARKFTEKS VSSKEIPSYG KQPGLFQEDV KRLFKEKYRI
     LLYSPSVLRA SRLAEQLREE GISAYCPDEF SLPKEGEKSI QVCTGFLRHG FSLEEERLFV
     LTEAELFGQS LSLKKKKKKK KVEGVRIGSL TEIEKGDYVV HESHGIGIYQ GIERITTDGV
     SKDFIKILYG DGGNLYLPVT KLDGIEKYAG KEAKVPKLNR LNGTEWQKTK AKVQGAVKEI
     ARELLRLYAK RQNEEGYAFS EDTVWQKEFE EAFPYEETGD QILAIEATKE DMESRKIMDR
     LVCGDVGYGK TEIALRAAFK AVQDSKQVAY LCPTTILAQQ IYNNFTERMK GFPVETRLLS
     RFQSGKELKK SLEELSHGRA DIAIGTHRLL SKDVHFKNLG LLIVDEEQRF GVSDKERIKS
     LKENVDVLTL SATPIPRTLH MSLVGIRDLS VLEEPPLDRL PIQTYVMEEN EASVREAIER
     ELRRDGQVYY VHNRVKSIAD TAMRVQHLVP YARVAYAHGQ MGERELEKIM LSFISGEIDV
     LVSTTIIETG LDIPNANTLI IQDADKMGLS QLYQIRGRVG RSSRISYAFL LYKKGKSLTE
     ESEKRLKAIR EFTELGSGIR IALRDLEIRG AGNVLGAEQH GHMEAVGYEL YTKLLRHAVL
     LEKGEKTEEE SIECQIDVDL DAYIPESYIP NEEQKLEAYQ KISTIGSDEE EIDLKDELID
     RYGDLPDMVE NLFRVAMLKL SLSKIGVLEC KIKRGEILLQ FSPKAKLDTA KIPALVQDSN
     GELRFQNGEK PALLYKKKNQ RELPNIRETM DKAGEIATLL SL
//
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