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Database: UniProt
Entry: A0A0A0ENC3_9GAMM
LinkDB: A0A0A0ENC3_9GAMM
Original site: A0A0A0ENC3_9GAMM 
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}.
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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
//
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