ID A0A1H3I6V7_9FIRM Unreviewed; 1184 AA.
AC A0A1H3I6V7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN02910264_01748 {ECO:0000313|EMBL:SDY23417.1};
OS Ruminococcaceae bacterium YAD3003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1520816 {ECO:0000313|EMBL:SDY23417.1, ECO:0000313|Proteomes:UP000199204};
RN [1] {ECO:0000313|EMBL:SDY23417.1, ECO:0000313|Proteomes:UP000199204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAD3003 {ECO:0000313|EMBL:SDY23417.1,
RC ECO:0000313|Proteomes:UP000199204};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNPA01000011; SDY23417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3I6V7; -.
DR STRING; 1520816.SAMN02910264_01748; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000199204; 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; 3.40.50.11180; -; 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; 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; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SDY23417.1};
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:UP000199204}.
FT DOMAIN 629..790
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 799..965
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1184 AA; 132080 MW; 4BA9383D03640E35 CRC64;
MDNKLIELLS RIESDKELVS EFSLSLKTGK HLNITGLCNE QKVFVAMALA RLNNRKAVFI
EPDSARARST ASYCAAFTDG PVSLLMPSEL SLVSAEASSR ELELNRSASL SELVTGDFGA
AVITAGALLN KLERADVFAK RIIKLKTGGE MERDDLVDLL VLNGYENVPQ VMEKGEFSVR
GDIVDIYSPS YSEPVRISFF DTEIDQIKTF DRETQRSTGQ LEETVVVPAS VYAFPEDKRD
EIAELILERV REDLSKMNTA TREARRASEL LSRTATGDAE KVRNGIEPTG IARWLGVILE
DFQTAIDYIN SDDVVFFADE MVDIDARLNA YAGEYAQRCR ESFEIGIAPT CSPMAMVNLS
KLMKSLDNLD NIVTLSMFQS SGNGLPGGKT HTVTGFPADN YSGRAEELAT LLKKNQNVYL
IAHHGRRSEQ LKERLSGYDC FTDIIDSPLP AGFNYPLLGI TILGEQELYG AEQKRPTKKK
GGNRINFFSE ISPGDYVVHD KHGVGRYEGL INMKVGEIRK DYLKLTYAKG ETLYILPENL
DSLQKYVGPG EKDPKLSRLG GDEWKKSVSR AREAIKKVAY DLLKIYAARS VNKGFACAPD
EEQQKLFEDK FPFVETDDQL RAVHEIKADM ESERPMDRLL CGDVGFGKTE VAFRAMFKAV
MNGRQVIMLA PTTLLAQQHY ENFMSRVKDF PVNVCLLSRF VPQATIRQNL TDIKNGKIDV
IIGTHRVLSN DVKPPHLGLL VIDEEQRFGV NHKEKIKSLK TDVDVLSLSA TPIPRTLHMS
LSGIRDISTL EEAPFNRRAV QTYVMGYDEQ IITQACMREI ARGGQIFYLY NKTSDIDKVA
DLLSKAMPGV RVTYAHGQMP ENGLETVVTD FIEGKYDILV CTTIIENGVD MPNVNTLIVE
NADRFGLSQL YQIKGRVGRS DRQAYAYITY NADSVLNEEA TKRLNALREF TELGSGVRIA
MRDLEVRGAG SLLGAEQHGQ MDVIGYELYC RLLDEEVRRL KTGKDEVLDS DVLAGHSETA
EKGFSVEVDY DAYIPASYIQ DEAARMSCYR RIGDISGFES YSDFIDEVTD RYGDAPSEVF
ILSGISLMRS LAGSLGFTKA SIRNAGVRLY LNPNLQIDMQ ALGALMRDNF YGARVTINAT
GAVPYMLFKP SSVKQDKTVQ EIVGLMRILD DNRTVNDKPE EVKV
//
