ID A0A0A0ENC3_9GAMM Unreviewed; 1183 AA.
AC A0A0A0ENC3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=N792_05200 {ECO:0000313|EMBL:KGM52471.1};
OS Lysobacter concretionis Ko07 = DSM 16239.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1122185 {ECO:0000313|EMBL:KGM52471.1, ECO:0000313|Proteomes:UP000030017};
RN [1] {ECO:0000313|EMBL:KGM52471.1, ECO:0000313|Proteomes:UP000030017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ko07 {ECO:0000313|EMBL:KGM52471.1,
RC ECO:0000313|Proteomes:UP000030017};
RA Zhang S., Wang G.;
RT "Genome sequencing of Lysobacter.";
RL Submitted (AUG-2013) 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:KGM52471.1}.
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; AVPS01000003; KGM52471.1; -; Genomic_DNA.
DR RefSeq; WP_036192711.1; NZ_AVPS01000003.1.
DR AlphaFoldDB; A0A0A0ENC3; -.
DR STRING; 1122185.N792_05200; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000030017; 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 CDD; cd18810; SF2_C_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:UP000030017}.
FT DOMAIN 654..815
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 836..990
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1183 AA; 130576 MW; 808C46E4D3EAE205 CRC64;
MSNPTFPTPP LPRAGQQRAW WRAPASPSAL AFHIAGAAAA HDGPLLVIAR DNQTAQQLES
DLRTLLGPAG TATGTAGVLP VLPGSPWLPV LHFPDWETLP YDHFSPHPEI VSQRLATLNR
LPTLQRGIVV VPVQTLLQRL APLRHVVGGS FDVQVGQRLD LGAEQSRLES AGYRHVPQVL
DPGDFAVRGG LLDVYPMGAG QPFRIELLDD EIDTIRGFDP ETQRSFDKID AVHLLPGREL
PLDEASLKHA LDALRERFDL DTRRSALYQD LKAGIAPAGI EYYLPLFFEG GDFEQTSTLF
DYLADNTLPL LGEGAAEAAD TFWRHTGERY EQRRHDLERP LLPPDALYLS PEALRERLNQ
GVRIEVCGEG HPQRERAQAL ASQPAPALPI AARDQIPAGE LKSFLGSYPG RVLVAADSPG
RREALLEILQ AAGLQPDVLP DWPSFAHPNL LPQAEEGSLS RFAIAVAPFD DGFALTEPAL
AILTERQLFP ERASQPRRRR RAGREPEAIV RDLGELSEGA PIVHEDHGVG RYRGLVTLEA
GGEKNEYLEI EYAKGDRLYV PVGQLHLINR YSGASVETAP LHSLGGEQWS KAKKKAQEKV
RDVAAELLEI QARRQARAGL AIDLDRAMYE PFAAAFPFEE TPDQHAAIEA VLRDLQSSQP
MDRVVCGDVG FGKTEVAVRA AFAMAAAGKQ VAVLVPTTLL AEQHYRNFSD RFADWPLKVE
VLSRFKTAKE IKAELEKAAE GTIDVIVGTH RLLQKDVRFK DLGLVIVDEE QRFGVRQKEA
LKALRANVHL LTLTATPIPR TLNMAMAGLR DLSIIATAPA HRMAVQTFVV PWDDSQLREA
FQREIARGGQ VYFLHNDVES IGRMQRELEA LVPEARIGIA HGQMPERELE RVMLDFQKQR
FNVLLCSTII ESGIDIPNAN TIIINRADKF GLAQLHQLRG RVGRSHHRAY AYLVVPDQRS
ISADAKKRLD AITAMDELGA GFTLATHDLE IRGAGELLGE DQSGQMAEVG FSLYTELLER
AVRSIRQGKL PDVDGTHDRG AEVELHVPAL IPDDYLPDVH TRLTLYKRIS GARNAEELRE
LQVEMTDRFG LLPDPAKHLF AIADLKLQAT ELGISKLDIG ATGGRLQFIE KPHVDPMAVI
KMIQGQPQLY RMDGPDKLRL SLDLPDAAAR IAAARALLIA LRP
//