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Database: UniProt
Entry: A0A1R3W6F1_9GAMM
LinkDB: A0A1R3W6F1_9GAMM
Original site: A0A1R3W6F1_9GAMM 
ID   A0A1R3W6F1_9GAMM        Unreviewed;      1127 AA.
AC   A0A1R3W6F1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05216526_1840 {ECO:0000313|EMBL:SIT73253.1};
OS   Ectothiorhodosinus mongolicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodosinus.
OX   NCBI_TaxID=233100 {ECO:0000313|EMBL:SIT73253.1, ECO:0000313|Proteomes:UP000223759};
RN   [1] {ECO:0000313|EMBL:SIT73253.1, ECO:0000313|Proteomes:UP000223759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M9 {ECO:0000313|EMBL:SIT73253.1,
RC   ECO:0000313|Proteomes:UP000223759};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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}.
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DR   EMBL; FTPK01000003; SIT73253.1; -; Genomic_DNA.
DR   RefSeq; WP_076756212.1; NZ_FTPK01000003.1.
DR   AlphaFoldDB; A0A1R3W6F1; -.
DR   STRING; 233100.SAMN05216526_1840; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000223759; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000223759}.
FT   DOMAIN          591..752
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          765..927
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1127 AA;  125571 MW;  89AD1B59B4D15396 CRC64;
     MTSSPAPGSA GFLAAAQQLQ SAQGVCVFIT DGAQAAERLR DALRFFLNDP QLPVLSLPDW
     ETLPYDVFSP HEDIISQRLK TLYALPELKR GALVLPISTA LLRLPPRSWL ASECLNLSVG
     ERLDRDTLLA QFTAAGYQSV SQVQAHGEFA VRGALLDVWP MGSEQPLRID LLDDEIETIR
     LFDPQTQRSL SHIEAVRLLP AHEFPLNEAS IKRFRANYRD QLAGDPNVSV IYREVSQGQA
     PSGIEYYLPL FFEQVETLFD HLPANLEIYE IGDVGSAAKQ FYEQLEARYE QRRYDPERPL
     LPPEALYLNP GDYQNRAKAQ RGRLMGKKSK ALPEVQLQGR DAQSAAGLRD FLNTLKGRCL
     LLAETAGRRE VLLDTLREQE LRPQVFEHWA DFIASDASLG LCIGPLESGF HLPEKELAVI
     TEAELFGQKA RQERRQKKPT RDADAIVRNL TDLHPSAPVV HEEHGVGRYL GLNTLSTGGQ
     VTEYLMLEYA GGDKLYVPVS ALHLISRYTG SDPEHAPLHK LGSEQWSKAR RKAAEKAHDV
     AAELLEIHAR RAARQGHAHA LSEHDYQAFT EAFPFEETPD QAEAIRAVIA DMQSTQPMDR
     VVCGDVGFGK TEVAMRAAFV AVQGGSQVAV LVPTTLLAQQ HEQNFRDRFA DWPVRIESLS
     RFGSAKEQKV VMQGLAEGKV DIVIGTHKLI QGMLEFKNLG LVIIDEEQRF GVRHKEKLKA
     LRAEVDLLTL TATPIPRTLN MALAGLRDLS IIATPPGERL AIKTFVSQDS DALVQEACWR
     EMRRGGQVYF LHNEVQSIER RARQLAELMP EARIGIAHGQ MREKDLERVM LDFYHRRFNI
     LVCTTIIESG IDVPTANTII MDRADKLGLS QLHQLRGRVG RSHHRAYAYL LTPHPSAMTK
     DAVKRLEAIE SLGELGVGFT LASHDLEIRG AGELLGEEQS GQIQEVGFSL YNDLLERAVK
     ALQSGQLPDL SRMGSDSTEV ELGLPALLPE DYVPDVHVRL ILYKRISACV DEDGLRELEV
     ELIDRFGLLP PPAKHLMASA RLRQQLAPLG VRKLEMGAAG GRLIFQDQPP VDAQSVIQLL
     QTAPTRYALD GPTKLRFTQP LPDLDKRIQA VADMLSILRP EPERKAA
//
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