ID A0A1R4I7P8_9ACTN Unreviewed; 1200 AA.
AC A0A1R4I7P8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=FM114_00005 {ECO:0000313|EMBL:SJN15323.1};
OS Luteococcus japonicus LSP_Lj1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Luteococcus.
OX NCBI_TaxID=1255658 {ECO:0000313|EMBL:SJN15323.1, ECO:0000313|Proteomes:UP000188342};
RN [1] {ECO:0000313|EMBL:SJN15323.1, ECO:0000313|Proteomes:UP000188342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSP_Lj1 {ECO:0000313|EMBL:SJN15323.1,
RC ECO:0000313|Proteomes:UP000188342};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUKQ01000001; SJN15323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4I7P8; -.
DR STRING; 1255658.FM114_00005; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000188342; 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}; 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:UP000188342}.
FT DOMAIN 656..817
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 835..992
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 489..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 130703 MW; 03FBD961C3ED3C56 CRC64;
MTLTGLTDLL ASDPVVARAI EQSTATTTLD LTAPTAARAA LTATLSRGLG RPVLLVTSTY
REAEQLVAEL GSWTGADEVA YYPAWETLPH ERLSPRSDTV GRRLAVLRRL AGNDPAGVPR
IVVAPVRSVL QPQVKGLAEL TPVRIAVGEE VDIAELSAAL VGAAYHRVDL VERRGEFAVR
GGIVDIFPPT EEHPVRVDFF GDQVEEIRHF TVADQRSMPS TRDGVIASPC RELLLDETVR
SRARALVPDH PELVEMLDKI AEGHAVEGME ALTPALVDGL ELLLDVLPTD TVVLVSDPEL
VRTRAHDLVQ TSQEFLHASW AAAAAGGKAP IDLGATAYWS LADVRAHALE RGQSWWSLSS
FSAAPVDQGP VFADDGQRVD LAGLTGTGVD SRNLSWKAAE NWKGDTEGAV AEIGQAVASG
EAVVLSVEGK GLASRMAEVL TDHEIGSHVA DALVEAPEKG TVTIIPTSQR HGFRVPGLGL
SLFTTGDLAG NKPADKSERR MPSRRKNQIS PLELKAGDPV VHEQHGVGRY VEMMQRTVAG
STREYLVIEY AASKKGQPGD RLFVPMDQLD QVTRYVGGES PTLDKMGGAD WNKRKSRARK
AVKQIAAELI KLYAARQATR GHAFGPDTAW QRELEDAFNY VETPDQLVCI QEVKHDMEQV
VPMDRLICGD VGYGKTEIAV RAAFKAVQDG KQVAVLVPTT LLVTQHHATF SERYAGFPVN
VAQLSRFQTD TEAKAVIEGV ASGKVDVVVG THRLFGGEVQ FKDLGLVIID EEQRFGVEHK
ESLKKLRLNV DVLAMSATPI PRTLEMAITG IREMSVIATP PEERHPVLTF AGPYDEAQVV
AAVRRELARE GQVFYVHNRV QSIEKTAARL RELVPEARVV TAHGQMNEHQ LEDVMQQFLD
RQADVLVSTT IVEAGIDIST ANTLLIERAD LMGLSQLHQL RGRVGRGRER GYAYFLYPPD
KPLTETAHDR LATMAAHTDL GAGMQIAMKD LEIRGAGNLL GGEQSGHIAD VGFDLYIRLV
GEAVADFRGG PEAEPEPEMR IELPVDANLP NDYVESERLR LEMYKRLAEV RSEEDIAEVR
AELEDRYGPL PGPTRVLLEV ARFRLLCRSV GVTEVVGQGN NIRFSPANLP DSRQLRLGRL
HPGSVIKHQA GFVLIPRPTT APVLGQPLTG HDLLEWATRV LVDIFDAKPP AAGEPVTAAR
//
