ID A0A0Q6WQ80_9BURK Unreviewed; 1151 AA.
AC A0A0Q6WQ80;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=ASD15_27445 {ECO:0000313|EMBL:KQV87929.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV87929.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV87929.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV87929.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV87929.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV87929.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQV87929.1}.
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DR EMBL; LMDJ01000005; KQV87929.1; -; Genomic_DNA.
DR RefSeq; WP_057154767.1; NZ_LMDJ01000005.1.
DR AlphaFoldDB; A0A0Q6WQ80; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000051876; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051876}.
FT DOMAIN 623..784
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 805..959
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1151 AA; 127638 MW; 84B7C5CEAF5FC192 CRC64;
MSFDLKKALP KPGNRFALPT LHGSADACAL AQAALELKAR GQMLAVIVAN ASDGQRLLDE
IPWFAGDGAD SALRCHLLPD WETLPYDAFS PHQDLVSERL ATLHEIQTGQ CDVMIVPATT
ALVRMAPPSF LAAYTFFFKK GESLDEAKLK SQLTLAGYTH VTQVMSPGEY SVRGGLIDLF
PMGSALPYRL DLFGDTIETI RTFDADTQRS LYPVSEVRLL PGREFPMDET ARTTFRSRWR
EQFEGDPSRS VVYKDISSGI ASAGIEYYLP LFFDQTATLF DYLPEGSTLA MVGDIDAAIK
RFWLDTQSRY RFLKSDRERP ILAPEAIFLG DEQFFTLAKP HARISISRED LGQASEISAP
VPNIAVNRHL DDPLTNLRAY LLQSGRRVMV CAESNGRRET LQQYFGEFDL TLAPVEGFDG
FLQSDAKLML GVAPLHAGFE WSAGKGQLVF ITETELYAGS GRRAGKKKQE GVTQVESMVR
DLSELKIGDP VVHINHGIGR YMGLTSMDLG EGETEFLHLE YAKDTKLYVP VSQLHVISRY
SGASPDDAPL HSLGSGQWEK AKRKAAEQVR DTAAELLNLY ARRALRQGHA FAYSAHDYER
FADSFGFDET PDQAAAIGNV LKDMTSGKPM DRLVCGDVGF GKTEVALRAA FIAVMGGKQV
AILAPTTLLA EQHAQTFADR FADWPVRIAE MSRFRTGKEI AQAIKGMSDG TLDIVIGTHK
LLSDDVKFER LGLVIIDEEH RFGVRQKEAL KSLRAEVDVL TLTATPIPRT LGMALEGLRD
FSVIATAPQK RLAIKTFVRS ENEGIIREAC LRELKRGGQV YFLHNEVETI QNRMAALTEL
LPEARIAVAH GQMHERDLEK VMRDFVAQRY NILLCTTIIE TGIDVPTANT IIMHRADKFG
LAQLHQLRGR VGRSHHQAYA YLLVNDVQSL SKQAQRRLDA IQQMEELGSG FYLAMHDLEI
RGAGEVLGEN QSGEMLEVGF QLYTDMLNEA VRSLKAGKEP DLAAPLSTTT EINLHVPALL
PADFCGDVHE RLSIYKRLAN CSAQDKIDDL QEEMIDRFGK LPEAAKALVE THRLRIAAAT
VGIVKIDAHS EAATLQFMPK PPIDPMRIIT LIQKNKQIKL NGQDKLKITA NMPDLSARVT
QIKTAIKQLV A
//
