ID H0F4Y2_9BURK Unreviewed; 1160 AA.
AC H0F4Y2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=KYC_09120 {ECO:0000313|EMBL:EHK66689.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK66689.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK66689.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK66689.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(2012).
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:EHK66689.1}.
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; AGUF01000038; EHK66689.1; -; Genomic_DNA.
DR AlphaFoldDB; H0F4Y2; -.
DR STRING; 477184.KYC_09120; -.
DR PATRIC; fig|477184.5.peg.1807; -.
DR eggNOG; COG1197; Bacteria.
DR Proteomes; UP000003113; 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 633..794
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 815..969
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 128155 MW; EFB07308EF4C4380 CRC64;
MSASSLMPSP SASAPAAPPV PATAPTLSAL KPGTRYAQPR PPGSGDAWLL ADLARQAGGP
LVILTAEPLE AQRLAEEIQL FAPNLRVRQL PDWETLPYDA FSPHQDLISE RLHTLHSLMM
KSVDVLTVPI TTALYRLAPP SFLAAYTFSF KQKDRLNEAA LRAQLTLANY NHVTQVTSPG
EFCLRGGLID LFPMGSVVPY RLDLFDDEIE TIRSFDVDTQ RSLYPVREVQ LLPGREFPMD
EDSRNRFRAR FREVFEGDPS RALPYKDIGN GIPFAGVEYY LPLFFEDTAT LFDYVAEGTV
MVTVGDIDDA IQRFNQDTAS RYGFLKSDRE RPVLPPSELF LDTESLYARL KDFRRLALAA
GQAHPDFRAA PDVSVARRSD DPIAKLRALV QTRQTRVLLC ADSAGRRETL VQMLNEFGVT
PDAQPDTIEA FLASDAHFGI VASALGTGFE LPGANLAFLT ENDLYPGVAG TGRRGKRDQE
RASNVEAMVR DLSELRAGDP VVHAQHGIGR YHGLVNMDMG EGEMEFLHLE YANGSTLYVP
VSQLHVIARY SGADPEAAPL HQLGSGQWDK ARRKAAKQVR DTAAELLALY AQRAAREGFA
FNLPLNDYEA FAEGFGFEET ADQAAAIEAV IGDMTSGRPM DRLVCGDVGF GKTEVALRAA
FLAVANGKQV ALLCPTTLLA EQHAQTFSDR FADWPVRVVE LSRFRSAKEV SAAIEGINDG
RVDIVIGTHK ILSKDVKFKR LGLVIIDEEH RFGVRQKEAL KALRAEVDVL TLTATPIPRT
LGMSLEGIRD FSVIATAPQK RLAIKTFVRR EDGSTLREAL LRELKRGGQC YFLHNEVETI
HNRRARLEEL VPEARIAVAH GQMPERELEQ VMKGFYQQRY NVLLCTTIIE TGIDVPSANT
IVIHRADRFG LAQLHQLRGR VGRSHHQAYA YLLTPGEDAI TSNAKKRLEA IQAMEELGSG
FYLAMHDLEI RGTGEVLGDS QSGNIQEVGF SMYNEMLNEA VRALRAGEEP DLDAPFNLAC
EVNLHAPALL PSDYCADVHA RLAIYKRLAH AADEDDLIHI QEELIDRFGK LPEAAQTLLA
THRLRLAAQP LGIVKIDASE TQALLQFGPK TTVDPAKIIE LVQRQRHIKL AGQDKLHVEI
KAAQVPARAD AVRAVLRALK
//
