ID A0A369C9H2_9GAMM Unreviewed; 1167 AA.
AC A0A369C9H2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=DFQ59_104116 {ECO:0000313|EMBL:RCX30680.1};
OS Thioalbus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalbus.
OX NCBI_TaxID=547122 {ECO:0000313|EMBL:RCX30680.1, ECO:0000313|Proteomes:UP000252707};
RN [1] {ECO:0000313|EMBL:RCX30680.1, ECO:0000313|Proteomes:UP000252707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26407 {ECO:0000313|EMBL:RCX30680.1,
RC ECO:0000313|Proteomes:UP000252707};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RCX30680.1}.
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; QPJY01000004; RCX30680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369C9H2; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000252707; 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:UP000252707}.
FT DOMAIN 634..795
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 816..970
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 131114 MW; 702A1132FBA056AF CRC64;
MNSPKPRSET RTDLTLDPRH PPLPATGERL RWGNLHGSST ALAVSNAARD HAGPVLVICT
DTLAANRLEE ELRFYTGASE TCPVLVLPDW ETLPYDRFSP HQDITSRRLE TLYRLGDLRH
GLVIAPVSTL MHRFPPRSYL DAGTLMLEQG QRLDLERLRK RLEAGGYLCV PQVMEHGEFA
VRGSLIDIYP MGSALPYRVD LFDDEVDTLR TFDPETQRSV DVVERIRLLP AREFPLDEAA
VTRFRQAWRA AFAGDPSGCP TYQDVSQGIA PAGVEYYLPL FFESCATLFD YLPEATLVTY
TAGVLSSAET FWDEAGERHE QLRHDSSHPL LPPARLFLQA HELFASLAAY SRVEIHRDPL
DPGAAHRNFA TDPPPSLTVD RRAEQPLQRL AGFLDAFAGR VLLCAETAGR RESLLELLQQ
LPLQPRACDS WQSFVDSEAQ AAIAVAPLDQ GILLPAGGLA VITESQLFGE QIRQRRRRVR
TRERDSDAVV RDLTELRTGA AVVHEEHGVG RYLGLQVIQL GDQAGEFLTL EYAGGDKLYV
PVSSLHLVSR YTGVDPDQAP LHRLGSEQWQ KARRKAAEQV RDVAAELLDL YARRAARKGH
AFDYATDQYA AFAESFPFEE TPDQEQAIES VLADLRSPRP MDRLVCGDVG FGKTEVAMRA
AFVAVQDGRQ VAVLVPTTLL AQQHYDNFRD RFADWPVRIE VLSRFGGKRQ QGETLDAVAD
GRADIVIGTH KLLQENVRFK RLGLVIIDEE HRFGVRQKER LKTLRSEVDI LTLTATPIPR
TLNMAISGMR DLSIIATPPA RRLSIKTFVR ERNSAVIREA ILREVLRGGQ VYYLHNEVES
IERLAREVEA LVPEARVSIA HGQMRERELE RVMSDFYHRR FNVLVCTTII ETGIDIPTAN
TIIMDRADKF GLAQMHQLRG RVGRSHHQAY AYLFTPPRRQ LTPDAVKRLD AIEQLEDLGA
GFALATHDLE IRGAGELLGE GQSGNMQAVG FGLYMEMLER AVKALKEGRE PELDKPFGHD
AEVDLHLPAF IPGDYLPDVP ARLTLYKRIA SAADERALEE LQVEMIDRFG LLPPQVKNLF
RATGLKLKAR PLGVLRLEAG TDGGRIEFRD QPDIDPMRII ELLQSRPNVY RLDGQTKLRF
NMPLETVDRR FEAVEELLLR LGRRDAA
//
