ID A0A0S9NJN3_9BURK Unreviewed; 1158 AA.
AC A0A0S9NJN3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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=ASF44_25510 {ECO:0000313|EMBL:KQP45518.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP45518.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP45518.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP45518.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP45518.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP45518.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KQP45518.1}.
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DR EMBL; LMNA01000005; KQP45518.1; -; Genomic_DNA.
DR RefSeq; WP_056898998.1; NZ_LMNA01000005.1.
DR AlphaFoldDB; A0A0S9NJN3; -.
DR STRING; 1736318.ASF44_25510; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000051759; 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:UP000051759}.
FT DOMAIN 624..785
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 806..960
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1158 AA; 128470 MW; FF36DDE7DDC72AEE CRC64;
MDLPKLIPGK RFTLPRPPGS ADALLLARLA EREKAGRKVV AIVTSDANDA QRLLEELPFF
APTLRCALFP DWETLPYDTF SPHQDLISER LATLWRLYAG AAQGDPEAGV DVVLVPATTA
LYRVAPPSFL AGTTFQFKAK QRLDEARLKS QLTLAGYSHV TQVVSPGEYA VRGGLIDLFP
MGSPVPYRVD LFDDEIDSIR TFDPDSQRSL YPVPEVRLLP GREFPMDDAG RARFRSRWRE
LLEGDPTRSR IYKDMGNGVA TAGIEYYLPL FFEETATVFD YLGAGATVVL HGDLEAAFQR
FWQDTRERHR VLVGDPDRPV LPPEALFLSS EQFYGQANAH SQLALRPAQA EAADAVPYAE
FAPLPSLSVV RGADEPLARL SSHLRNTQQR LLLLAESDGR RESLLDFVRA SELQPPVFDS
LAEFEASTER LGMATGALGA GFAWLEGGID FVTETELFAA GPTARRRRKQ EQVSDVEALI
KDLAELNVGD PVVHAAHGIG RYLGLVSLDL GQGNTEFLHL EYADKAVLYV PVSQLHLISR
YTGVSAAEAP LHKLGSGQWD KARRKAAEQV RDAAAELLNI YARRAAREGH AFRYAPQDYE
AFANDFGFEE TADQKAAIHA VIQDMISPQP MDRLVCGDVG FGKTEVALRA AFVAVTGGKQ
VAFLAPTTLL AEQHYQTLVD RFSKWPVKIA EMSRFRSAKE ITAAGKGLED GSVDIVVGTH
KLLSASVKFK NLGLLIIDEE HRFGVRHKEA MKAMRAEVDV LTLTATPIPR TLGMALEGLR
DLSVIATAPQ RRLAIKTFVR SENNGVIREA VLRELKRGGQ VYFLHNEVET IENRRAKLEE
LLPEARIAVA HGQMPERELE RVMRDFTAQR SNVLLCSTII ETGIDVPTAN TIVMSRADKF
GLAQLHQLRG RVGRSHHQAY AYLMVPDIEG LTKQAAQRLE AIQQMEELGS GFYLAMHDLE
IRGAGEVLGE NQSGNMLEVG FQLYNEMLSE AVRSLKEGKE PDLLSPLSVT TEINLHAPAL
LPDDYCGDVH LRLSFYKKLA TAKNSDQVDR LLEEIVDRFG KLPAQAQTLI DVHRLRVLAR
PYGVVKVDAA PGVIHITFKP DAPIEPMRII ELIQKNRHIK LVGNEKLRIE RELPEPKDRA
QMVRDVLRHL GQPVAQTA
//
