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Database: UniProt
Entry: A0A095V3S8_9BURK
LinkDB: A0A095V3S8_9BURK
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ID   A0A095V3S8_9BURK        Unreviewed;      1154 AA.
AC   A0A095V3S8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, 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=JL37_08880 {ECO:0000313|EMBL:KGD95904.1};
OS   Achromobacter sp. RTa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1532557 {ECO:0000313|EMBL:KGD95904.1, ECO:0000313|Proteomes:UP000035841};
RN   [1] {ECO:0000313|EMBL:KGD95904.1, ECO:0000313|Proteomes:UP000035841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RTa {ECO:0000313|EMBL:KGD95904.1,
RC   ECO:0000313|Proteomes:UP000035841};
RA   Prabhakaran M., Cougar B., Weirick T., Fathepure B.Z.;
RT   "Genome sequences of the lignin degrading proteobacteria.";
RL   Submitted (AUG-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:KGD95904.1}.
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DR   EMBL; JPYO01000027; KGD95904.1; -; Genomic_DNA.
DR   RefSeq; WP_043543838.1; NZ_JPYO01000027.1.
DR   AlphaFoldDB; A0A095V3S8; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000035841; 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}.
FT   DOMAIN          627..788
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          809..963
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1154 AA;  127719 MW;  2150B93579C968DB CRC64;
     MPAPTLPATA APSVPATAPT LSALKPGARY AQPRPPGSGD AWLLADLARQ ASAPLVILTA
     EPLEAQRLAE EIQLFAPHLR VRQLPDWETL PYDAFSPHQD LISERLHTLH SLMTKSVDVL
     TVPVTTALYR LAPPSFLAAY TFSFRQKDKL NEAALRAQLT LANYNHVTQV TAPGEFCLRG
     GLIDLFPMGS VVPYRLDLFD DEIETIRSFD VDTQRSLYPV REVQLLPGRE FPMDEDSRTR
     FRARFREVFE GDPSRALPYK DIGNGIPFAG VEYYLPLFFE ETATLFDYLT EGTVTVTVGD
     IDDAIQRFNQ DTASRYGFLK SDRERPVLPP SALFLDSEAL HSHLKAFRRL SLAAGQPHPD
     FRAAPDVSVA RRSDDPIAKL RALVQTSQTR VLLCADSAGR RETLVQMLNE FGITPDAQPD
     AIETFLASDA HFGIVAAPLS TGFQLPQAEL VFLTENDLYP GLATTGRRGK RDQERASNVE
     AMVRDLSELR AGDPVVHAQH GIGRYHGLVN MDMGEGEMEF LHLEYASGST LYVPVSQLHV
     IARYSGADPE AAPLHQLGSG QWDKARRKAA KQVRDTAAEL LALYAQRAAR EGYAFNLPLN
     DYQAFAEGFG FEETADQAAA IEAVIADMTS GRPMDRLVCG DVGFGKTEVA LRAAFLAVAN
     GKQVALLCPT TLLAEQHAQT FSDRFADWPV RVVELSRFRS AKEVSAAIEG INDGRVDIVI
     GTHKILSKDV KFKRLGLVII DEEHRFGVRQ KEALKALRAE VDVLTLTATP IPRTLGMSLE
     GIRDFSVIAT APQKRLAIKT FVRREDGSTL REALLRELKR GGQCYFLHNE VETIHNRRAR
     LEELVPEARI AVAHGQMPER ELEQVMKGFY QQRYNVLLCT TIIETGIDVP SANTIVIHRA
     DRFGLAQLHQ LRGRVGRSHH QAYAYLLTPG EDAITNNAKK RLEAIQAMEE LGSGFYLAMH
     DLEIRGTGEV LGDSQSGNIQ EVGFSMYNEM LNEAVRALRA GEEPDLDAPF NLACEVNLHA
     PALLPSDYCA DVHARLGIYK RLAHAADEDD LIRIQEELID RFGKLPEAAQ TLLATHRLRL
     AAQPLGIVKI DASETQALLQ FGAKTSVDPA RIIELVQRQR HIKLAGQDKL RVEIKAPQVP
     ARADAVRAVL RALK
//
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