ID A0A411WYV8_9BURK Unreviewed; 1147 AA.
AC A0A411WYV8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-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 ECO:0000313|EMBL:QBI01878.1};
GN ORFNames=EYF70_14215 {ECO:0000313|EMBL:QBI01878.1}, GCM10007387_21180
GN {ECO:0000313|EMBL:GGY38929.1};
OS Pseudoduganella albidiflava.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=321983 {ECO:0000313|EMBL:QBI01878.1, ECO:0000313|Proteomes:UP000292307};
RN [1] {ECO:0000313|EMBL:GGY38929.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY38929.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:QBI01878.1, ECO:0000313|Proteomes:UP000292307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17472 {ECO:0000313|EMBL:QBI01878.1,
RC ECO:0000313|Proteomes:UP000292307};
RA Miess H., Frediansyhah A., Gross H.;
RT "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GGY38929.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY38929.1};
RA Sun Q., Kim S.;
RL Submitted (DEC-2022) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BMWV01000004; GGY38929.1; -; Genomic_DNA.
DR EMBL; CP036401; QBI01878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WYV8; -.
DR KEGG; mali:EYF70_14215; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000292307; Chromosome.
DR Proteomes; UP000628442; 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}.
FT DOMAIN 618..779
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..954
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1147 AA; 127305 MW; 31215087472FA18E CRC64;
MPFDFTRALP KPGNRFALPA LYGSADSYAL AQAALQLKIE GRMLAVIVAS ASDGQRLLDE
IPWFASALRC HLLPDWETLP YDAFSPHQDL VSERLATLHE IRSGQCDVLL VPATTALVRM
APPSFLAAYT FFFKKGESLD EGRLKAQLTL AGYTHVTQVM SPGEYSVRGG LIDLFPMGSA
LPYRLDLFGD TIETIRTFDA DTQRSLYPVQ EVRLLPGREF PMDEAARTTF RSRWRETFEG
DPSRSVVYKD IKSGIASAGI EYYLPLFFEE TATLFDYLPD GAALALVGDI DGAIRRFWAD
TESRYKFLKA DRERPILPPE AIFLRDEAFF TCAKRHARIT IGKSLDGEPS ELSAPVPNIA
VNRHQDDPLT NLRAYVMRPD LRVMICADSA GRRETLQQYF AEFDLHPALV DGFGGFLASH
DRIVLGVAPL QAGFELHAGA ETLVFITETE IYAGSGRRVG KKKQEAVTQV ESMVRDLSEL
KIGDPVVHIN HGIGRYMGLV SMDLGEGETE FLHLEYAKDT KLYVPVSQLH VISRYSGGAP
EDAPLHALGS GQWDKAKRKA AEQVRDTAAE LLNLYARRAA RQGHAFEYSS HDYERFAESF
GFDETPDQAA AILNVIRDMT SGKPMDRLVC GDVGFGKTEV ALRAAFIAVM GGKQVAILAP
TTLLAEQHAQ TFADRFADWP VKIAEMSRFR TGKEIATAIK GMADGTLDIV IGTHKLLSED
VKFTRLGLVI IDEEHRFGVR QKEALKSLRA EVDVLTLTAT PIPRTLGMAL EGLRDFSVIA
TAPQKRLAIK TFVRSEDGSI IREAILRELK RGGQVYFLHN EVETIQNRLA QLTELVPEAR
IAVAHGQMHE RDLEKVMRDF VAQRYNILLC TTIIETGIDV PTANTIIMHR ADKFGLAQLH
QLRGRVGRSH HQAYAYLLVN DVQSLSKQAQ RRLDAIQQME ELGSGFYLAM HDLEIRGAGE
VLGESQSGEM LEVGFQLYTD MLNEAVRALK AGKEPDLAAP LATTTEINLH VPALLPADFC
GDVHERLSIY KRLANCESQE ALDGLQEELI DRFGKLPEPA KALVETHRLR VAAKTVGIVK
IDAHGEAANL QFMPQPPIDP MRIITLIQKH KHIKLNGQDK LKITASMPDL AARVAQIKTA
IKQLTSP
//
