ID A0A103ERA2_9BURK Unreviewed; 1157 AA.
AC A0A103ERA2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=WS68_20070 {ECO:0000313|EMBL:KVE39617.1};
OS Burkholderia sp. TSV86.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1385594 {ECO:0000313|EMBL:KVE39617.1, ECO:0000313|Proteomes:UP000066043};
RN [1] {ECO:0000313|EMBL:KVE39617.1, ECO:0000313|Proteomes:UP000066043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV86 {ECO:0000313|EMBL:KVE39617.1,
RC ECO:0000313|Proteomes:UP000066043};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
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:KVE39617.1}.
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; LOWB01000017; KVE39617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103ERA2; -.
DR Proteomes; UP000066043; 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 788..954
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1157 AA; 128597 MW; A71179736EA92D8E CRC64;
MSDNASSSPS PVALVKAGQR YTFDGAHGSA DALAIARYFT AHRMQVPLVA VICANAVDAQ
RLSQELGYFA PGARVRVLPD WETLPYDTFS PHQDLVSERL ATLHDLGEGR CDILLVPATT
ALYRMPPASF LAAYTFAFAQ GERLDEAKLK AQLTLAGYEH VSQVVRPGEY CVRGSLIDLF
PMGSPLPYRI DLFDDQVDSI RSFDPDTQRS LYPVRDVRLL PGREFPFDEH ARTAFRNRWR
ETFEGDPSRA PIYKDIGNGV PSAGIEYYLP LFFEETATLF HYLPERAHLV FAGDLDASIK
RFTADTKQRY AFLSHDRERP ILEPKKLFLS DDDFYALAKP FARVALPAQP EGGWATPLPP
LALDRHADDP VAALRRYLDT TANRVLFTVE SAGRRETIAQ LLADNRLRPA ANDSFASWLA
SDERFALGVA PLASGFAVPG EGWAVVTETE LYGALGRRSS RRRQEQASNV DAMVRDLSEL
KLGDPVVHAQ HGIGRYMGLV SMDLGEGETE FLHLEYAGDS KLYVPVAQLH VISRYSGADP
DSAPLHSLGS GQWERAKRRA ALQIRDTAAE LLNLYARRAA RQGHAFALEP RDYVKFADSF
GFDETPDQAA AIAAVIGDMT SGKPMDRLVC GDVGFGKTEV ALRAAFIAVM GGKQVALLSP
TTLLAEQHTQ TFIDRFADWP VKIAELSRFK SAKEVSAAIR QINEGSVDIV IGTHKLLSSD
VQFKRLGLVI IDEEHRFGVR QKEALKALRA EVDVLTLTAT PIPRTLGMAL EGLRDFSVIA
TAPQKRLAIK TFVRREEESV IREAMLRELK RGGQVYFLHN EVETIEERKT MLEALVPEAR
IVIAHGQMHE RELERVMRDF VAQRANVLLC TTIIETGIDV PSANTIIMHR ADKFGLAQLH
QLRGRVGRSH HQAYAYLLVH DPQALTKQAQ RRLEAIQQME ELGSGFYLAM HDLEIRGTGE
VLGDKQSGEI HEIGFQLYTE MLNDAVKALK NGKEPDLTAP LAATTEINLH TPAILPADYC
VDVQERLSLY KRLANCEHGD AIDGIHEELI DRFGKLPPQA HALVETHRLR LAAKPLGIVK
IDASEAAIGL QFVPNPPIDP MRIIDMVQKH RHVKLAGQDR LRIETRTPDL AVRVSTIKET
LRALGQPQKP REQAAAR
//