ID R5GPE2_9FIRM Unreviewed; 1151 AA.
AC R5GPE2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=BN782_01344 {ECO:0000313|EMBL:CCY17569.1};
OS Eubacterium sp. CAG:786.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262893 {ECO:0000313|EMBL:CCY17569.1, ECO:0000313|Proteomes:UP000018127};
RN [1] {ECO:0000313|EMBL:CCY17569.1, ECO:0000313|Proteomes:UP000018127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:786 {ECO:0000313|Proteomes:UP000018127};
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:CCY17569.1}.
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DR EMBL; CAXS010000129; CCY17569.1; -; Genomic_DNA.
DR AlphaFoldDB; R5GPE2; -.
DR STRING; 1262893.BN782_01344; -.
DR Proteomes; UP000018127; 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 629..790
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 811..965
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1151 AA; 129197 MW; C006EB636AD9FE77 CRC64;
MDLFYNAAGL IPEFQRLSKY LDEKQKLPAL VTGVSHIHKA HFIGALLRKE ALRPVLTIAE
NEAEAQRLCT DINSMYGAGT ALLYPAKELL LGDYEAASRE YEHKRIFALS AMLNGECSTV
ICSPEAAAQL TIPPDVLKAR TLTLSQDMDI PLDDLTAGLI AAGYSRCDLI EGPGQFSVRG
GIVDIFPPSS AAPCRLELWG DTIDSLTYFD LETQRRTEPI ESIRISPAAE VLFTSSEELC
GRIEALAKKL RGRNAAEMRE RLEQDCQKLR GGISLSTVDR FFPLCYDKEA TIFDYANALF
VCENTSVREN YRAIAAQHAE DLRIQTEEKR ICRGLDRFML TKNELYSEID ERVCAYFDTF
IRGRDMQLGL LLDLQGAIQT SPWSGELAVL QTELQNYLDM GFSCVIFSGT EKGAHTLASD
LQDEGFKADL AADPEKPVKG RVIVIPGTLG AGIEYSTIKF AVFTHTAVHA NRKRPPKKKP
GEEIRSLSDI SIGDLVVHYS HGIGIFDGVH KIETDGVAKD YIKIRYAGAD VLHIPVTQLD
LVSRYIGAGD VNTVKLNKLN SDQWQKSKAK AKAAAKEMAS ELIELYSRRM KSKGYEFPPD
DSLQEDFEAH FNYIETNSQL RCIDEIKADM MKPVPMERLL CGDVGFGKTE VALRAAFKCA
EAGKQCAVLV PTTVLAWQHF QTFCNRMEGF PINIALLSRH KTPAEQREIL RRLKAGSIDI
IIGTHRIIQE DIKFKDLGLV IIDEEQRFGV AHKEKFKEMF SGVDVLTLSA TPIPRTLNMA
MSGIRDMSVI DEPPQDRQPI TTYVMEHDWG VIMQAIEKEL RRSGQVYYIH NRIDSIYSCA
EKIRSLIPEA RVGVAHGKMS EEQMLEIWRH LLDGSLDVLV CTTIIETGVD VPNVNTLIIE
NSDYMGLAQL HQLRGRVGRT NKRAYAYFTF QRGKVLSEIS QKRLDAIREF TQFGSGFRIA
MRDLEIRGAG SILGSSQSGH LANVGYDMYL QLLDEAVREE RGEKDVHKEE CLVDIKIDAF
IPEDYISNQA QRVDCYRKIA RIQTEEDSVD VTDELIDRYG DPPKSVRGLI EVARLRNMAS
AADIVEITQM NNDLLFYLGK FDMKKIAAVS KLYGKRMLLE TADRGHIRVT LDKNEKPLDA
MRSVINTMNE A
//
