ID I2F4V8_9BACT Unreviewed; 1012 AA.
AC I2F4V8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=Theba_1273 {ECO:0000313|EMBL:AFK06961.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06961.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK06961.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(2012).
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 ---------------------------------------------------------------------------
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; CP003532; AFK06961.1; -; Genomic_DNA.
DR RefSeq; WP_014730939.1; NC_017934.1.
DR AlphaFoldDB; I2F4V8; -.
DR STRING; 660470.Theba_1273; -.
DR KEGG; mpg:Theba_1273; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_4_0; -.
DR Proteomes; UP000002881; 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; 3.40.50.11180; -; 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; 3.
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:UP000002881}.
FT DOMAIN 486..647
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 663..821
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1012 AA; 115403 MW; 933515213448BC17 CRC64;
MERVLYRVNE PISWVEKGNY NASRNLIIFP SERMLESFIE IHEKREGDGF FFSHDVFPFE
EIGTSSRIRS ERLALLRKLL LGELRTVYTS FHGILRKTVP IEVFEELSFK VEVGGPMTIT
ESQLQSLGYS RSFSVTIPGE FAIRGGIVDV FIPGSEMPVR IDTFDREIES IRSFDPVSQK
SLQRLNEVLI TPAAEGITAS PFRETALKRI RAAEQATGVS DEILLDRLDT MDTTAGIFYE
RQSILLDFLE GYNVIFVKPD DAIVEYGRRE RETLELLSEK AVRKFLYIRY GGVSSEVLMK
LKEYSIVSDG DVSSLDYDEE LTEELQIIKR PRREEEYLPR IPVVDWTELE EGDYVVHKEY
GIGRYLGVRT VENILGTREY LLLEYRDGNK IYVPVDRVDR VHKYIGSTEG IQLNSLRGTA
WTRQKSKVNK EVKALISDLS NLYGSREVTS GVPLTGDSEM EKGFRDSFPY VETEDQQKAV
EEVMEDLQST KPMDRLISGD AGYGKTEVAL RAAFRTVVSG KQVAVLVPTT VLARQHYENF
ERRLNPFGIR VEILDRYRTD VQRNKLLKKL KKGEVDVVVG THSLLSKEVG FADLGLVVVD
EEQLFGVLQK EHFKKLRLQV NVLSMSATPI PRTLYMSLSG LRDLSIISTP PAGRTSPEIY
VGQINDRLIR TAVLRETNRG GQTIFVHNRV TELQELLSRL RDLLPEVKID VAHGQMNKSA
FERTIRDFYL GELDMLLCTT IIESGVDVPN ANTLIVDDSH RYGLAQLYQL RGRVGRSNRR
AFSYFLYDPK RLSDPSRERL KALKEFSGAG SGMKIAMRDL EIRGFGTLLG AEQHGNINSV
GLYLYREMVE KAMRELHGEE EIGVEERTVD TELKNIPFDM VIPEEYVSDS IERLKIYRRI
AACKAQDEID EIESELLDRF GRLPSQVNSL LEASRVRLGA FNIGIKIVEY DPHSESIVML
HGENHIRDSL GIKGRRLVVN EREGKSILYG VPERHLMRTL KSLFLGAERN VQ
//
