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Database: UniProt
Entry: R6UFU5_9FIRM
LinkDB: R6UFU5_9FIRM
Original site: R6UFU5_9FIRM 
ID   R6UFU5_9FIRM            Unreviewed;      1055 AA.
AC   R6UFU5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=BN503_01728 {ECO:0000313|EMBL:CDC69662.1};
OS   Oscillibacter sp. CAG:155.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillibacter; environmental samples.
OX   NCBI_TaxID=1262910 {ECO:0000313|EMBL:CDC69662.1, ECO:0000313|Proteomes:UP000017942};
RN   [1] {ECO:0000313|EMBL:CDC69662.1, ECO:0000313|Proteomes:UP000017942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:155 {ECO:0000313|Proteomes:UP000017942};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDC69662.1}.
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DR   EMBL; CBFT010000127; CDC69662.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6UFU5; -.
DR   Proteomes; UP000017942; 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:UP000017942}.
FT   DOMAIN          523..684
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          697..860
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1055 AA;  116026 MW;  BC46E0B596066A14 CRC64;
     MATADALCAR TLPPKLLHSL ALTLEVGSRA DLNELTDRLV SAGYTRCQQV EGVGQFALRG
     GILDVFSPLM DQPVRCEFFD DEIDSMGTFD PGTQRRTKNV ASAQILPAAE VLPHCAPGGL
     AGLAEQLETL AVKLAKKPKT EAAAQQLRQD AERFRTGAVP GGLDRYLAAV YPEICTGVDY
     LPKDAVVFLC ESGRVDERVK GTLLQLKQDE ESLLTAGLLA GEYARLTLSG EELYAALEEF
     PVVMEDTLPT SRHPLRPRGL MAVNAKQLSS YGGSLETAVS DLEHYRATGS AVLLLCAGET
     RANNLRHLLE ERGIPAVLDL ANTAMPAPGE VRITLGALTA GSEWPQLHLA VLTEGQLTAT
     SAGKRQRVKK TSNRQKIQSY TDLTPGDLVV HEHHGVGRFV GIQRLPVDGV EKDYIKIDYA
     GGDCLYVPAT QLDLVSKYIG GGEDQERTRL NKLGGTEWAK QKTKAKKAAK DLAKGLIALY
     AQRQKQPGFA FSPDSTWQRE FEESFDFTET DDQLRCIAEI KADMEKPRPM DRLLCGDVGY
     GKTEVALRAV MKCILDGKQA AILVPTTVLA QQHYATAVSR FRNFPVKIEV LSRFTPAKEQ
     KRILEAAAGG RVDLLIGTHK LLQKNMVFKD LGLLVIDEEQ RFGVTHKERL KEMSRQVDVL
     TLSATPIPRT LNMALSGLRD MSTLEEPPRD RQPVQTYVLE HDWAILEDAM RRELARGGQI
     YYLHNRVESI DLTASRIQKM LGPEVRIVVG HGKMSEHELS SVMQAMVDGE ADILVCTTII
     ETGIDISNVN TLIIEDADKM GLAQLHQIRG RIGRSSRRAY AYLTYRRGKV LQETAAKRLA
     AIREYVEFGS GFKIAMRDLE IRGAGNLLGP EQSGYLMSVG YDMYLKLLEE AVLEEKGEEK
     KVETECSADL TINANIPERY VPAPEQRMDL YRRIAAIRTN DDASDLLDEM LDRYGEAPKS
     VLALLDVALL RAAAAKAGVC DITQKGSMLR FTLAVFRPEA LVAVCGLSKY KFRLTLSAGE
     TPMLTLKLKP GEDTLEAALA LVEDLKLASE PSGQA
//
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