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Database: UniProt
Entry: A0A126ZGR9_9BURK
LinkDB: A0A126ZGR9_9BURK
Original site: A0A126ZGR9_9BURK 
ID   A0A126ZGR9_9BURK        Unreviewed;      1160 AA.
AC   A0A126ZGR9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=AX767_18725 {ECO:0000313|EMBL:AMM26156.1};
OS   Variovorax sp. PAMC 28711.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM26156.1, ECO:0000313|Proteomes:UP000070169};
RN   [1] {ECO:0000313|EMBL:AMM26156.1, ECO:0000313|Proteomes:UP000070169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM26156.1,
RC   ECO:0000313|Proteomes:UP000070169};
RA   Park H.;
RT   "Complete genome of Variovorax sp.";
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CP014517; AMM26156.1; -; Genomic_DNA.
DR   RefSeq; WP_068632695.1; NZ_CP014517.1.
DR   AlphaFoldDB; A0A126ZGR9; -.
DR   STRING; 1795631.AX767_18725; -.
DR   KEGG; vaa:AX767_18725; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000070169; Chromosome.
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:UP000070169}.
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   1160 AA;  129430 MW;  4153500B8EADE392 CRC64;
     MDLPPLTAGK RFTLPRPPLS ADALLLSQLA TREKAMGHAT AVFTADANDA QRLIDEIAFF
     APELRCALFP DWETLPYDSF SPHQDLISER LATLWRISQK EADVVLVPAT TALYRLAPPS
     FLAGYTFHFK TKQKLEESKL KAQLTLAGYS HVTQVVSPGE YAVRGGLIDL FPMGSLVPFR
     VDLFDDEIDS IRTFDPDTQR SLYPVPEVRL LPGREFPMDD DARARFRSRW REMLDGDPTK
     SRIYKDMGNG VATAGIEYYL PLFFEETATV FDYLGTETTV VLHGDLEPAF QHFWQDTGER
     YRLVRGDPER PALPPETLFL NAEQFYQRAK PLAQLAIRGD VATDTPYAEF DKLPPFAVVR
     GADDPLTGLK AHIRATPHRV LVIAESNGRR ESLLDFLRAS GVSPPAFDSL AEFEASPDEK
     IGIATAALAS GFAWREQGID FVTETELFAT APTTRRRNKK QEQVSDVEAL IKDLSELNVG
     DPVVHSAHGI GRYRGLIHMD LGQGKDAEGK PLLQEMLHLE YADKATLYVP VSQLHLISRY
     TGVSADEAPL HKLGSGQWEK AKRKAAEQVR DSAAELLNIY ARRALRQGHA FRYSAADYEV
     FANDFGFEET ADQKAAIHAV IQDMISPQPM DRLVCGDVGF GKTEVALRAA FIAITGGKQV
     ALLAPTTLLA EQHYQTLVDR FAKWPVKVAE VSRFRSGKEV STALKGLADG NVDIVVGTHK
     LLSESTKFAN LGLLIIDEEH RFGVRHKEQM KALRAEVDVL TLTATPIPRT LGMALEGLRD
     LSVIATAPQR RLAIKTFVRN EGTGVIREAV LRELKRGGQV YFLHNEVETI ENRRQKLEEI
     LPEARIAVAH GQMPERELER VMRDFVAQRY NLLLCSTIIE TGIDVPTANT IVMSRADKFG
     LAQLHQLRGR VGRSHHQAYA YLMVPDTEGL TKQAAQRLDA IQQMEELGSG FYLAMHDLEI
     RGAGEVLGEN QSGNMMEIGF QLYNEMLSEA VRSLKEGKEP DLLSPLHVTT EINLHAPALL
     PDNYCGDVHL RLSFYKKLAT AKTSDQIDTL LEEIVDRFGK LPPQAQTLID THRLRVLARP
     YGVVKVDAAP GVIHITFKKD PPVDSMAIIH LIQKNKHIKL AGNEKLRIER ELKEPKERAQ
     MVRDVLRSLG QPKVQEPVAA
//
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