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}.
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; 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
//