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Database: UniProt
Entry: A0A103ERA2_9BURK
LinkDB: A0A103ERA2_9BURK
Original site: A0A103ERA2_9BURK 
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}.
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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
//
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