ID R7B0I2_9CLOT Unreviewed; 1176 AA.
AC R7B0I2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=BN653_01487 {ECO:0000313|EMBL:CDD56732.1};
OS Clostridium sp. CAG:43.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262805 {ECO:0000313|EMBL:CDD56732.1, ECO:0000313|Proteomes:UP000018284};
RN [1] {ECO:0000313|EMBL:CDD56732.1, ECO:0000313|Proteomes:UP000018284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:43 {ECO:0000313|Proteomes:UP000018284};
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:CDD56732.1}.
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; CBHG010000251; CDD56732.1; -; Genomic_DNA.
DR AlphaFoldDB; R7B0I2; -.
DR STRING; 1262805.BN653_01487; -.
DR Proteomes; UP000018284; 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:UP000018284}.
FT DOMAIN 643..804
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 813..979
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1176 AA; 134067 MW; 8A9ED4346F61FB85 CRC64;
MSDLFANPLE EMIEFQDLKT DLQRGQGPLL VTGCLDSQKV HLLSELSDLT PWKLIVTYDD
SRAREICEDY RCFDTDISLY PARDLLFYTS DIHGNLLTKQ RIQVMRRVLE SSGGVVVTTI
DGLMEHLLPL AWMKERSLTI GAEDVVEVGK LTHALAEMGY EKVAQVEGSG QFSVRGGIID
IFPLTEEVPY RIELWGDEVD SIRTFDPESQ RSIEQVDEAV IYPATEMALT PEQIQDGTEA
IEKDRRKYVK KLRDAMKTEE AYRMDSAVSE VLEGLREGFR VHGLGSYIRY FCKETVSFLN
YFPVDELTIF LDEPLRLKEK AETTETEFRE SMSHRLEGGY LLPGQTSFLY SAKETLAMAM
RPRTLLLLGL DQKLSGMTVK KKYSLSVKNV NSYQNGFELL ISDLARWKKE KYRVVLLAGS
RTRASRLAGD LREYDLSAFC PDEGENTVKP GEILVTYGKL HRGFEYPLIK FVVITEGDMF
GGGRGRKKKK KTSYQGKKIQ SFSELSIGDY VVHESHGLGI YRGIEKIEQD KVVKDYIKIE
YRDGGNLYLP ATRLEGIQKY AGSDARTPKL NKLGGMEWNK TKSKVRGAVR DIAKDLVELY
AARQRSEGYQ YGPDTVWQRE FEEMFPFEET EDQLEAIEAT KKDMESRRIM DRLICGDVGY
GKTEIALRAA FKAIQEGKQV VYLVPTTILA QQHYNTFVQR MKDFPVRVDM LSRFRTAGEQ
KKTLEDLKKG QVDVVIGTHR VLSKDVVFKN LGLLIIDEEQ RFGVAHKEKI KKLKENVDVL
TLTATPIPRT LHMSLIGIRD MSVLEEPPVD RLPIQTYVME YNDEMVREAI HRELARGGQV
YYVYNRVNNI DEVANHVAAL VPEANVVFAH GQMHEHELEK IMLDFVEGNI DVLVSTTIIE
TGLDIPNANT IIIHDADRLG LSQLYQIRGR VGRSGRTSYA FLMYRRDKLL REEAEKRLQA
IREFTELGSG IKIAMRDLEL RGAGNLLGAE QHGHMQAVGY DLYCKLLNEA VLALRGENEA
EDFETVVDCD IDAYIPPSYI RNEYQKLDVY KRISGIENQE EYMDMQDELI DRFGEIPRSV
ENLLKIADLK ALAHQAGVVE VDVKKQDITI QMYQKADLDV SGIPALMEKY KGTLTFRTGD
VPSFYYRDVR QKHTDCETML VKAREILSGL AALAKK
//
