ID A0A063B454_9BURK Unreviewed; 1158 AA.
AC A0A063B454;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=LIG30_0326 {ECO:0000313|EMBL:KDB06705.1};
OS Burkholderia sp. lig30.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB06705.1, ECO:0000313|Proteomes:UP000027020};
RN [1] {ECO:0000313|EMBL:KDB06705.1, ECO:0000313|Proteomes:UP000027020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA Brown S.D., Hazen T.C.;
RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT Isolated from Wet Tropical Forest Soil.";
RL Submitted (MAR-2014) 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:KDB06705.1}.
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DR EMBL; JGVW01000096; KDB06705.1; -; Genomic_DNA.
DR RefSeq; WP_038714615.1; NZ_JGVW01000096.1.
DR AlphaFoldDB; A0A063B454; -.
DR STRING; 1192124.LIG30_0326; -.
DR PATRIC; fig|1192124.4.peg.4018; -.
DR eggNOG; COG1197; Bacteria.
DR Proteomes; UP000027020; 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:UP000027020}.
FT DOMAIN 619..780
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 789..955
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1158 AA; 128082 MW; 0945356FD9DB7A5B CRC64;
MPDNASTPSA SPVALVKPGQ RFAFDGAHGS ADALAIARYL AAYRQDVPLL AVICANAVDA
QRLAQEIGYF SPDARVRLLP DWETLPYDTF SPHQDLVSER LATLHDLGEG RCDILLVPAT
TALYRMPPAS FMAAYTFAFA QGERLDEAKL KAQLTLAGYE HVSQVVRPGE YCVRGSLIDL
FPMGSPLPYR IDLFDDQVDS IRAFDPDTQR SLYPVRDVRL LPGREFPFDE AARTAFRSRW
RETFEGDPSR ATIYKDIGNG VPSAGIEYYL PLFFDDTATL FHYLPAGAHL VFSGDLDTAI
RRFTADTRQR HAFLSHDRER PILEPQRLFL SDDDFYTFAK PFARVVLPAQ PEGGWASALP
ELSIDRHADD PLAALRAFVG SSGKRVLLTV ESAGRRETIS QLLAEHRLKP ASSDHFAGWL
ASDETFALGV APLAGGFAVP GEGYAIVTET ELYGALGRRA GRRRQEQASN VDAMVRDLSE
LKEGDPVVHA QHGIGRYMGL VSMDLGEGET EFLHLEYAGD SKLYVPVAQL HVISRYSGAD
PDSAPLHALG SGQWERAKRK AAQQIRDTAA ELLNLYARRA AREGHAFGLE PRDYVKFAES
FGFEETPDQA AAIAAVIGDM TSGKPMDRLV CGDVGFGKTE VALRAAFIAV MGGKQVALLS
PTTLLAEQHT QTFIDRFADW PVRVAELSRF KSAKEVNAAI GQINEGSVDI VIGTHKLLSS
DVQFKRLGLV IIDEEHRFGV RQKEALKALR AEVDVLTLTA TPIPRTLGMA LEGLRDFSVI
ATAPQKRLAI KTFVRREEES VIREAMLREL KRGGQVYFLH NEVETIDNRR AMLEALVPEA
RIAIAHGQMH ERELERVMRD FVAQRANVLL CTTIIETGID VPSANTIIMH RSDKFGLAQL
HQLRGRVGRS HHQAYAYLLV HDPQALTKQA QRRLEAIQQM EELGSGFYLA MHDLEIRGTG
EVLGDKQSGE IHEIGFQLYT EMLNDAVKAL KNGKEPDLTA PLAATTEINL HAPAILPADY
CVDVQERLSL YKRLANCEHG DAIDGIQEEL IDRFGKMPPQ AHALVETHRL RLAAKPLGIV
KIDASEVAIG LQFVPNPPID PMRIIEMVQK HRHIKLAGQD KLRIETRTPD LAVRVSTVKE
TLRALGHPIR EGTAAAPR
//
