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Database: UniProt
Entry: A0A1G3CQ65_9BURK
LinkDB: A0A1G3CQ65_9BURK
Original site: A0A1G3CQ65_9BURK 
ID   A0A1G3CQ65_9BURK        Unreviewed;      1184 AA.
AC   A0A1G3CQ65;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=A2X74_08855 {ECO:0000313|EMBL:OHC09618.1};
OS   Polynucleobacter sp. GWA2_45_21.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=1801989 {ECO:0000313|EMBL:OHC09618.1, ECO:0000313|Proteomes:UP000176957};
RN   [1] {ECO:0000313|EMBL:OHC09618.1, ECO:0000313|Proteomes:UP000176957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHC09618.1}.
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DR   EMBL; MHZG01000008; OHC09618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3CQ65; -.
DR   STRING; 1801989.A2X74_08855; -.
DR   Proteomes; UP000176957; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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          642..803
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          824..978
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          1148..1175
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1184 AA;  132554 MW;  AAC72672CC477C84 CRC64;
     MSDALKLAPP IPAPRAGQRF TFSGLVGSSD AALIAQSALR YRSEFSVMVI FCAQAQEAQR
     LLEEIPAFAP QLKTRLLPDW EILPYDHFSP HQDLVSERLA TLYELLNGSC DIVLVPITTA
     LQRLGPPNFL SGHTFFFRQG DKLNEAALKL QLQQAGYDPV SSVMRPGEYS IRGGLIDLFP
     MGSSLPYRLD LFGDEIEQIR AFDPDTQRSL YPVKGVRLLP GHEFPFDDAS RTAFRGRWRE
     VFEGDPTRCS IYKDANLGIP SAGIESYLPL FFEESSTVFD YFPRSGDPVW LVSIGDVEES
     IKSFWKDTLS RYEFLKHDLD RPILPPADLF LDVDQFFTAL KPNARLALEK EVDKEAKESP
     QFLAVPDLAV HRRDADPINR LRALVAQEKV RVLICSDSNG RKESIRQLFE ESNSVAGQNG
     KPLYPLKPEG FEGIADFIKS DSLFGLVTAQ LFNGFTWPAE NLIVVTEAEL FTTTARQRRK
     GKESESADPD MLFKDLSELK IGDPVVHSDH GIGRYQGLVL LNLAPPKEEP IFEEFLHLVY
     AKDATLYVPV QQLQMVTRYA GSDPDSAPLH QLGSGQWDKA RRKAAQQIRD TAAELLSLYA
     ARAIRKGHAF EFSAHDYAAF AESFGFEETP DQANAIAAVI GDMTSGTPMD RLVCGDVGFG
     KTEVALRASF VAVMGGKQVA ILAPTTLLAE QHVATWKDRF ADWPVRIVEL SRFKTTKEIN
     AALEAIAKGE ADIIIGTHKL LSKETQFANL GLVIADEEHR FGVRQKDALK ALRAEVDILT
     LTATPIPRTL GMAMEGLREF SIIATAPQKR LAIKTFVRRE GDGVIREAVL REIKRGGQVY
     FLHNEVETIQ NRKHALQELI PEARISVAHG QMHERELESV MREFVTQRTN ILLCTTIIET
     GIDVPTANTI IMHRADKFGL AQLHQLRGRV GRSHHQAYAY LLVPDPEALS KQAQLRLNAI
     QAMEELGSGF YLAMHDLEIR GAGEVLGDKQ SGEIHEIGFQ LYTEMLNRAV KSLRSGKEPD
     LLSPLQATTD VNLGVPALFP NDYCPDVHER LSMYKRFAGT HDFSELMGLR EELVDRYGDL
     PDQAKSLYET HRLRLEMAGF GIKKIDASPS SIQIQFIPNP PIDPMKIIHL IQSSKYIQLN
     GQDKLKILPQ KEKDFEKLEQ RLDQIRKILR SLNESAVLNT AQVN
//
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