ID A0A0N8K988_9SPHN Unreviewed; 1166 AA.
AC A0A0N8K988;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:KPP96657.1};
GN ORFNames=HLUCCO15_00755 {ECO:0000313|EMBL:KPP96657.1};
OS Erythrobacteraceae bacterium HL-111.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae.
OX NCBI_TaxID=1666908 {ECO:0000313|EMBL:KPP96657.1, ECO:0000313|Proteomes:UP000050295};
RN [1] {ECO:0000313|EMBL:KPP96657.1, ECO:0000313|Proteomes:UP000050295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-111 {ECO:0000313|EMBL:KPP96657.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPP96657.1}.
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DR EMBL; LJSW01000001; KPP96657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8K988; -.
DR PATRIC; fig|1666908.3.peg.1555; -.
DR Proteomes; UP000050295; 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; 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}.
FT DOMAIN 621..782
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1166 AA; 128416 MW; F81F29CEC282E8FE CRC64;
MPDLSRILAS ETPLTLTSLP RGSLPLVMGD LARAAKRRAV FIAPDDAAMR SVAEAARLFA
PEVEVIELPA WDCLPYDRAS PALSISAARL SALHRLQNPQ SGSQLLVTTV NAALQRVLTP
FRVRESVREF APGTTIGHDS LARLLTRAGY SRTDTVIDHG EFAVRGSIVD IFPSSLDQGL
RLDFFGDELE SLRLFDPGTQ RSTGTLNSHL LLPASEALLD EASIKRFRST YRELFGASAT
QDPLYEAVSE GRRLAGMEHW LPLFEERLST LFDHLDAADV MVIDAQAISA SEERIADIAD
YHDQRTRTGS DRSGSYRPLA PDALYLTRDE FAAALAAAPA HRASVFAAPE GEASLDFGFR
AGRDFAPERA RGDNVYEAAA QHLKAIARAG KRPLLAAYST GSAKRIGSIL SEAGTPTRIA
DTWQEALGLS ARGDATIMVL PLEAGFANDD LEIVTEQDVL GDRLVRRKKK RRDSDAFLAE
LQALSRGDLV VHVEHGIGKY LGLEPIPVGK SQHDCVALEY HGGDKLFIPV ENIDVLSRYG
SSEEAVPLDR LGGEAWQKRR ARLKERITAI AGELMKVAAE RALKKAPVFE PEEASFNQFV
DRFPWDETED QDRAIEEVLR DLESGRPMDR LVCGDVGFGK TEVALRAAFV AAMSGRQVAV
VAPTTLLARQ HYQNFASRFE GFPLKVGRLS RLVSPREMAE TREGLEKGDI DIVVGTHAIL
SKSTSFRDLG LVIVDEEQRF GVTHKEKLKQ LRSDVHMLTL TATPIPRTLQ MAMSGLRELS
TIQTPPVDRL AVRTYVMEWD DMVMREALLR EHHRGGQSFI VVSRISDMAP LEEWLHENVP
EVKVVSAHGQ MSPSEIEERM SAFYEGKYEV LLSTTIVESG LDLPSANTII IHRADRFGLA
QLYQLRGRVG RAKLRAYAYL TYEKDVQLSE IAEKRLKVLS DLDSLGAGFQ LASHDLDIRG
AGNLLGDEQS GHIREVGFEL YQSMLEDAIL AAKAGEMGLE PARDKVSPQI TVDAPIMIPE
DYVPDLAVRM ALYRRLNQAE GKAEIESLAA EMIDRFGDLP APTQNLVRLI EIKHQAIAAN
IAKIDVGARG TLVTFHKDDF PDPAGLVAYV DRLQGTAKLR PDMKLVINRA WGDPQSRLNG
LFQLTKGLSG IVKKAAKAKE KKTEAA
//
