ID I3VTB9_THESW Unreviewed; 1166 AA.
AC I3VTB9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Tsac_0742 {ECO:0000313|EMBL:AFK85764.1};
OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK85764.1, ECO:0000313|Proteomes:UP000006178};
RN [1] {ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA Brown S.D., Land M.L., Herring C.D.;
RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFK85764.1, ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT Thermoanaerobacterium saccharolyticum during the Degradation of
RT Hemicellulose.";
RL Appl. Environ. Microbiol. 80:5001-5011(2014).
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; CP003184; AFK85764.1; -; Genomic_DNA.
DR AlphaFoldDB; I3VTB9; -.
DR STRING; 1094508.Tsac_0742; -.
DR KEGG; tsh:Tsac_0742; -.
DR PATRIC; fig|1094508.3.peg.749; -.
DR eggNOG; COG1197; Bacteria.
DR Proteomes; UP000006178; 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 CDD; cd18810; SF2_C_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}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 808..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1166 AA; 133394 MW; 3F0D9DE62415270F CRC64;
MFIKPIENLR EVGEINEALT DERLPLLIYG LTDSQKAHIA HYIVKKLGKK VLFITYNDVE
AKLMHEDLSS LLNGDAYLIP SRDALFYKVD ASSLDITGKK LAAIRKILDD KPYAFVASID
GVLNKVAPKD VFLKYKRKYK IGDTIDLNEL SSFFVTMGYE RVPMVEGKGQ FSIRGGIIDF
FSPMEEEGFR IELFDDEIDS IRSFDTFTQR SLDNVDEVEL FPAREFVLED ENIKKGLSNL
SKRVNSYISK IKETQSGRAE KIKKKFDEIM ENISETRNIT NIGELIGFFY DNLYSIVDYF
DGAFIIVDEN LRVKERASNI VKEFNENFKS LLLSGEVIPD QSNLLFGYDD ILKKLSDKSL
ILMNTIVKSD ENIQVKKIVN FVSRTMHSFH GKLDLLADDL KFYKSSGYKV VMLSSNLERG
KLLRNSLIGY GLEIPIIEDE EYDIPEGGVL IYPGTISKGF EYVDAKFALI SDVEIFGQSR
RSKKSLKVKN SGRIKNFTEL TVGSYVVHVN YGIGKYEGIE KITVDGVTKD YLKIKYAGDD
KLFVPVEQLD LVQKYIGPED KPPKLNKLGS SDWSKLKKRA KKAVEDIAKD LIKLYAKRQT
MKGYAFSKDT PWQKDFEERF PYEETEDQLR CIEEIKKDME SDKPMDRLLC GDVGYGKTEV
ALRAAFKAVA DGKQVAFLCP TTILAEQHYN NFVQRFKDFP VKIEMLSRFR SNKEQSQIIK
MVADGTVDIL VGTHKILQND VKFKDLGLLI IDEEQRFGVK HKEKIKKLKE NIDVLSLSAT
PIPRTLHMSL VGIRDMSVLE NPPEDRYPVQ TYVVEFNEDL IRDAILRELG RGGQVYFVYN
RIDGIERMAS ILKELVPEAR IAVAHGQMDE GRLEDIMIGF LNREYDILVC TTIIETGLDI
PNVNTIIVYD SDKMGLSQLY QLRGRVGRSN RLAYAYFTYR KDKVITEVAE KRLEAIKEFT
EFGSGFKIAM RDLEIRGAGN LLGAEQHGHI DAVGYDMYLR LLDEAIKNLK GISEEDKPNT
AIDIKVSAYI DKEYIEDENQ RLEMYKKISS IENEKDVEDI KDELIDRFKE YPKAVEALID
VAYLKALARD ANILEITERG NSIILKFKDN KSINSRIVDA LVNEFKGKIM FSGQIPPYIT
YKYGKKEDLL KELINLVSKI KCLQIN
//
