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Database: UniProt
Entry: A0A2N3HL27_9FLAO
LinkDB: A0A2N3HL27_9FLAO
Original site: A0A2N3HL27_9FLAO 
ID   A0A2N3HL27_9FLAO        Unreviewed;      1135 AA.
AC   A0A2N3HL27;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:PKQ45643.1};
GN   ORFNames=CSW08_06125 {ECO:0000313|EMBL:PKQ45643.1};
OS   Confluentibacter flavum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Confluentibacter.
OX   NCBI_TaxID=1909700 {ECO:0000313|EMBL:PKQ45643.1, ECO:0000313|Proteomes:UP000233435};
RN   [1] {ECO:0000313|EMBL:PKQ45643.1, ECO:0000313|Proteomes:UP000233435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B {ECO:0000313|EMBL:PKQ45643.1,
RC   ECO:0000313|Proteomes:UP000233435};
RA   Yu L.;
RT   "Confluentibacter flavum sp. nov., isolated from the saline lake.";
RL   Submitted (DEC-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}.
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:PKQ45643.1}.
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DR   EMBL; PJEO01000017; PKQ45643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3HL27; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000233435; 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:UP000233435}.
FT   DOMAIN          592..753
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          762..928
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1135 AA;  130149 MW;  56B2C4CEA673B441 CRC64;
     MSKTNLSQTY SQILQVQNLQ KAIAQNKSRT HLKGLVGSSF SFVLSSVFKD ADKPFLLVFN
     DKEEAAFYLN DLERLINTKD VLFYPGSYRR PYQIEETDNA NVLLRAEVLN RINSQKKPAI
     IVTYPDALFE KVVTRKELER NTLKISVGDN LSIDFVNEVL FEYQFKRVDF VTEPGEFSVR
     GGIVDVFSFS NDEPYRIEFF GDEVDSIRTF DVETQLSIEQ IKKINIIPNV ENKFLNEERA
     SFLKYIASKT VLCFKNMDLF FSRIDDFYGK AEDAFKTLST EIKHAKPEEL FCNSALLKRQ
     LLDFSIIEFG SSSVFNNVIA SATKQSASID EMASSQTPRH DEIIFNTSPQ PSFNKQFNLL
     IEDLNTNYDK GFTNYIACVS EQQAKRFHDI FDDSHLEVKP YKTITLSLHQ GFVDYDNNIV
     CYTDHQIFER YHKFHVKNGY AKKQSITLKE LTNLDIGDYV THIDHGIGRF GGLQKIDVEG
     KQQEAIKLVY GERDVLYLSI HSLHKITKFN GKDGKPPKIY KLGSNAWKTL KEKTKSRVKH
     IAFNLIQLYA KRKTEKGYQY HPDSYMQLEL ESSFLYEDTP DQITATADIK SDMESERPMD
     RLVCGDVGFG KTEVAIRAAF KAVDNGKQVA VLVPTTILAY QHSRTFSERL KDFPVTVDYL
     NRFRTTKERR DTLEKLENGK VDIIIGTHQL VNKDVKFKDL GLLIVDEEQK FGVAVKEKLK
     TLKENVDVLT LTATPIPRTL QFSLMAARDL SVITTPPPNR YPIESHVIRF NEETIRDAVS
     YEIQRGGQIF FIHNRIENIK EVAGMIQRLV PDAKIGIGHG QLDGKKLEQL MLAFMEGAFD
     VLVSTTIVES GLDVPNANTI FINNANNFGL SDLHQMRGRV GRSNKKAFCY FITPEYSAMT
     DDARKRITAL EQFTELGSGF NIAMKDLEIR GAGDLLGGEQ SGFINEIGFE TYQKILNEAI
     EELKENEFKD LYKEDIDNKI YVKEVTIDSD FELLFPDNYV NNIAERLNLY TQLNDLKTEE
     ELQKFETHLI DRFGELPTQV LDLMNSVRIK WIATKAGFEK IIMKQGKFIG YFINDQQSSF
     YQSNNFTKVL QYVQANPKIC QMKEKQTRNG LRLLLTFENI KTVKQALTVL EPIVA
//
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