ID A0A1I1UQS7_9BACI Unreviewed; 1175 AA.
AC A0A1I1UQS7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05216238_103330 {ECO:0000313|EMBL:SFD73137.1};
OS Lentibacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=640948 {ECO:0000313|EMBL:SFD73137.1, ECO:0000313|Proteomes:UP000199474};
RN [1] {ECO:0000313|EMBL:SFD73137.1, ECO:0000313|Proteomes:UP000199474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22530 {ECO:0000313|EMBL:SFD73137.1,
RC ECO:0000313|Proteomes:UP000199474};
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; FOMR01000003; SFD73137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1UQS7; -.
DR STRING; 640948.SAMN05216238_103330; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000199474; 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}.
FT DOMAIN 637..798
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 819..973
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1175 AA; 134443 MW; 47B592686CC43BB0 CRC64;
MNGVHDFLRS NEDVASIIDG ISNGMNEQLV AGLSGSARSL FVSALNDSLE RPVLLVTHQL
VQAQQLYDDL TAFLGEDHIY LYPVNELIAS EIAVASPELK GQRIEALTEW SQKESGILIA
PIAALKRMLP PTDYWKKYQL DFQTEREIDV EAYLSRLVDM GYEHASMVSK PGEFSRRGGI
IDIYPVTETY PVRIELFDDE IDSIRFFDAG SQRSLDKQEA ITVGPATEML LTEEDRLRAA
QRLENALAES LRKLNNAEAK ETLAETIEYD IDRLKNLEHF QELYKYIGFL YDKPASLLDY
LPENGMVVLD EMSRIQETAT SLDAEESEWY STLLETNKMV RDSRFSFDWN TVWNSITPQR
VYMSVFLRHI PNTQPQNIIN LSTRTMQEFH GQMNLFKNEL KRWEKGDFSV VVLAPDEDRA
EKIQSIFMDY AIEADVVNEL ELPVRRPTIT VGEVSNGIEF PMHKLVLVTE NELFKKKTKR
PRKKQKISNA ERIKNYQELK VGDYVVHAHH GIGKYLGIET LEMNGLHKDF MLIKYSGDDK
LYVPIDQIDL VQKFVASEGK EPKLYKLGGS EWAKVKRKVQ SNVEDIADDL IELYAERQAR
KGYAFSEESE IQQEFEAAFP YEETEDQLRC IAEIKADMEK ERPMDRLLCG DVGYGKTEVA
IRAAFKAIAD GKQVALLVPT TILAQQHYET IQERFQDQAV TIRMLSRFRT RSQQKETIEG
IQKGKVDIVI GTHRLLSKDV TYRDLGLLIV DEEQRFGVKH KEKIKQLKSN VDVLTLTATP
IPRTLHMSML GVRDLSVIET PPENRFPIQT YVMEYNPIFV REAIEREMAR GGQVFFLHNR
VDNIDKVARD LGMLVDDVRI AVAHGQMNET ELESIIFGFL EGEYDVLVST TIIETGVDIP
NVNTLIVNQA DRMGLSQLYQ LRGRVGRSNR VAYAYFTYQK DKVLSEVAEK RLEAIKEFTE
LGSGFKIAMR DLSIRGAGNL LGAQQHGFID SVGFDMYSQM LKDAIEARKS GKKLDEVETF
EPELSLTTDA YIPDSYIDDE KQKIDIYKQF QAIASEEDIL ELKDELIDRF GDYPEEVENL
FAVSSLKRHA KQQRVESISE KSGKIELLVS TQRSQEVDGS KLFELANQFG REIQLGTEGN
KLKVLFKWSR NTKHKRYELL EDFISQLSHV DRAAG
//
