ID B9M729_GEODF Unreviewed; 1169 AA.
AC B9M729;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 ECO:0000313|EMBL:ACM22050.1};
GN OrderedLocusNames=Geob_3711 {ECO:0000313|EMBL:ACM22050.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM22050.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM22050.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM22050.1; -; Genomic_DNA.
DR AlphaFoldDB; B9M729; -.
DR STRING; 316067.Geob_3711; -.
DR KEGG; geo:Geob_3711; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_7; -.
DR Proteomes; UP000007721; Chromosome.
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; 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:UP000007721}.
FT DOMAIN 646..807
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 828..982
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1169 AA; 130908 MW; 05AD0375041F6271 CRC64;
MPFIPIAATV AMTAFISSPK KIVAAIAPDD ANVTLAGLKG SAPAYILSRL WDEHSRLLFI
ITPDADTAEE LYREMRFYSG SDERVLYFPP WDTAPFDTAS PHADIVGQRL NVLFRMMDGR
AGAVIVPLPA LMQKVLPRKT LGQISQYIVA GEEVERDLLL EKLVKLGYSH VPLVEDRGGF
SIRGGILDIF PPDLPTPVRI EFFGDFVDTI RTFDPVTQRS LQPLQELILL PSREVVISEE
VLTAFAPRLK RRCDALEIPA TRRRELLEQL QSAIYPPGVE YLQPLFHPDL ESLFDYCGED
FLKVIYDPAA MAAAENGFAE ELAAGERKSL EKDNIVCEIN DLFLDAVQLG SYLDQGRRLS
IPFLEIAGGR DAGQTIRLQV QDNSCFKLDV TAEGEGVLKP LVEKLLARQA EQKHVLMICH
QRNQAQRLYE MLSHYNLPLA LSERDFPGEL GRSDSQLRIM VGDISRGFQL AEDQLVIIAE
EEIFGVRIKR RGVSEARRKQ LLTSLAELKP GDYMVHIDFG VGIYRGLQHL TFSGMEGDFL
LLEYAGADKL YLPVDRINLV QRYVGAEGVE PHVDKLGGAG WEKTKAKARA AIQEMAGELL
KIYAARQVEE GHAFSPPDEL YQEFEAAFAY EETPDQQAAI EDVLLDMESK KPMDRLICGD
VGYGKTEVAL RGAFKAVMDG KQVAVLVPTT VLAQQHLETF SARLKSYPVK VEMLSRFRTP
KEQKEIIEGV KNGTVDVVIG THRLLQKDIV FKDLGLLIID EEQRFGVTHK ERLKKYRAVV
DIMTLTATPI PRTLYMSLMG IRDLSIIDTP PVDRLAIKTF VARTSDDLIR EAVLRELRRG
GQIFFVHNRV QTIGAMAEHL QRIVPEAKIA VGHGQMEEKE LERVMLSFMH GESNLLLCTT
IIESGLDIPT ANTLIVNRAD TFGLSQLYQL RGRVGRSKQR AYAYLLIPGE GAISADARER
LKIIQELTEL GAGFRIATHD LEIRGAGDLL GARQSGDIAA VGFELYTELL EEAIRQLKGE
ELAERVEPEI KLRIPAFIPE DYVREPNQRL IIYKRLTQAT SEEDVAEIMG ELVDRFGKLP
LAALYLVEVM KLRVALKAML VKEIEFDGKK LVLSFHQKTP VSPDTIIGLI RQQPKKYQFT
PDFRLCAELA DTSFDGVLKE AGNLLKTLG
//
