ID A0A1G0X530_9BACT Unreviewed; 1126 AA.
AC A0A1G0X530;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=A2523_11425 {ECO:0000313|EMBL:OGV28771.1};
OS Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV28771.1, ECO:0000313|Proteomes:UP000177243};
RN [1] {ECO:0000313|EMBL:OGV28771.1, ECO:0000313|Proteomes:UP000177243}
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:OGV28771.1}.
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DR EMBL; MHBA01000102; OGV28771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0X530; -.
DR STRING; 1798454.A2523_11425; -.
DR Proteomes; UP000177243; 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; 3.
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 573..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 755..909
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 505..532
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1126 AA; 127884 MW; 11D1688A52726C5C CRC64;
MKSILDDLKK ISSLVNLAQL INNSPTDKFP LFVTNLFGFT KNLFVKLLCE SEHQVYLLCE
DSKSLDESNA ELSIMGLSDK TIIINELKPD ILQEMLTEIT NRNDFILLST YDLLTCALPD
KEQIRKNTTQ ISVGGDLSYN NLVEYFNLLN YQKENFVEAP GDYSQRGAII DFWSYSEKNP
VRLEFDGDFI ESIRHFDPES QRSIESIPTS TLAGELSPSL RENISNIFDY LINPVVMAGK
YALDNLTLIR TAASHEEIHF AAPDSKKEDV AEEDDFPDAD TQIAETKTQA SHVDLQSLID
KSTARWIIED ELGLSDRKHE LGFSEAPTIG SNYDVLFRTL TEFATSGFRI VLTAENDLQS
NRLRELLAEL HEETLALLDS GQVKIETLPL KKGFVHRDSK LVVLTDYQIF NKPYRTKVIS
KARAAKSKSK SFSSIKRGDF VVHEDYGIGK YVGLETIKIG DANQETMKIL YAEGGVVYVN
LNYLNLVKRY SSQEKLAPTL STLGTSEWQN TKQRTKKKIK EAARELINLY ARRKATKGFS
FGKDTVWQKE LEASFIYEDT EDQEKVTGEV KQDMEAENPM DRLVCGDVGF GKTEVAVRAA
FKATQEGKQT AVLVPTTILA EQHFNTFQDR LVQFPIKVAA ISRFQTKKEQ VEVVKDLECG
KIDVIVGTHR LLSKDIVFKD LGLLIIDEEH RFGVIAKEKL RSFKHNVDTL TLTATPIPRT
LNLSLLGARD LSIIATPPPN RQPIYTHVST FDILKIKEWI KTELSRNGQI YFVHDRVESI
DKLAGYLKKY IPEIQIGIAH GQMKPSQLEK VIHGFLNRQY DVLLSTKIIE SGIDIPNVNT
IIINRADRFG LAELHQLRGR VGRAARQAYA YFIVPSMSSI NKKALRRLQA IEEFTELGSG
FNISMRDLEI RGAGNLLGIE QTGFVNDVGF DLFVKLINEA VEELKYEEFK ELFQTLPKPK
EKTEPTIDTY FEIGIPQTYM PEQSDRLNFY TALYSVSSIE EVEDLVEEMK DRFGSLPQMV
SLLISAAMLK LFASQALFER IIIQRKNIFI ILPKGEKEDY YKHHFTVMMR HIMEKYSDRV
KFNQQKETLR LIIPNNFASP SALLESLIGF AKDVSLILNP KIPAVA
//
