ID A0A0C2BRC0_9BURK Unreviewed; 1146 AA.
AC A0A0C2BRC0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, 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=TSA66_20160 {ECO:0000313|EMBL:KIF82614.1};
OS Noviherbaspirillum autotrophicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF82614.1, ECO:0000313|Proteomes:UP000031572};
RN [1] {ECO:0000313|EMBL:KIF82614.1, ECO:0000313|Proteomes:UP000031572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA66 {ECO:0000313|EMBL:KIF82614.1,
RC ECO:0000313|Proteomes:UP000031572};
RA Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL Submitted (DEC-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:KIF82614.1}.
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; JWJG01000028; KIF82614.1; -; Genomic_DNA.
DR RefSeq; WP_040041291.1; NZ_JWJG01000028.1.
DR AlphaFoldDB; A0A0C2BRC0; -.
DR STRING; 709839.TSA66_20160; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000031572; 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:UP000031572}.
FT DOMAIN 618..779
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..954
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1146 AA; 127684 MW; 721B859C25B77630 CRC64;
MSFDLKKSLP KPGNRFALPA VHGSADAFVL AQGAIELKAQ KRMLAVVVAN ATDAQRLLDE
IPWFGGEAEL RCHLLPDWET LPYDAFSPHQ DLVSERLATL YEVQNGQCDV LIVPATTALL
RMAQPSFLAA HTFYFKQGET LDEARLKSQL TLAGYTHVSQ VMSPGEYSVR GGLIDLFPMG
SALPYRLDLF GDTIETIRTF DADTQRSLYP VREVRLLPGR EFPMDEASRT AFRGRWREEF
EGDPSKSPIY KDIGNGIASA GIEYYLPLFF DETATLFQYL PDDATFALVG DIDGAIKRFW
SDTQSRYKFL KADRERPLLS PERLFLKDED FFTLAKPHGR WVIQAGDTAS EISAPIPNIA
VNRRVDDPLT NLRSYLLQTG KRVMICAESN GRRETLQQYF NEYNLALAPC EGFAGFASAS
DKLMLGVAPL HAGFELGFDH GNLAFITETE LYAGSGRRAG KRKQEGATQV ESMVRDLSEL
KIGDPVVHVN HGIGRYMGLL SMDLGEGETE FLHLEYAKDT KLYVPVSQLH VISRYSGASP
EDAPLHVLGS GQWEKAKRKA AQQIRDTAAE LLNLYARRAA RQGHAFQYSA HDYEAFAESF
GFEETPDQSA AINAVIKDMT GGKPMDRLIC GDVGFGKTEV ALRAAFVAVM GGKQVAILAP
TTLLAEQHAQ TFADRFADWP VKIAELSRFR TGKEVTAAIK GMAEGTIDIV IGTHKLLSNE
VKFSRLGLVI IDEEHRFGVR QKEALKALRA EVDVLTLTAT PIPRTLGMAL EGLRDFSVIA
TAPQKRLAIK TFVRSENDSV IREACLRELK RGGQVYFLHN EVETIQNRMA MLEELLPEAR
IAVAHGQMHE RDLEKVMRDF VAQRFNILLC TTIIETGIDV PTANTIIMHR ADKFGLAQLH
QLRGRVGRSH HQAYAYLLVH DVHGLTKQAQ RRLDAIQQME ELGSGFYLAM HDLEIRGAGE
VLGENQSGEM MEIGFQLYSD MLNEAVRSLK NGKEPDLAAP LSTTTEINLH VPALLPQDYC
GDVHERLSLY KRLANCDRQE AIDDLQEELI DRFGKMPDPA KALIETHRLR LAATPVGIVK
IDAHAELAVL HFQPNPPIDA MRIIELIQKN RHIKLHGQDK LRITANMPDL AARVSQVKAT
IRSLVG
//