ID R5C0S4_9FIRM Unreviewed; 1113 AA.
AC R5C0S4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=BN499_01772 {ECO:0000313|EMBL:CCX58462.1};
OS Blautia hydrogenotrophica CAG:147.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1263061 {ECO:0000313|EMBL:CCX58462.1, ECO:0000313|Proteomes:UP000018163};
RN [1] {ECO:0000313|EMBL:CCX58462.1, ECO:0000313|Proteomes:UP000018163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:147 {ECO:0000313|Proteomes:UP000018163};
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:CCX58462.1}.
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DR EMBL; CAWR010000108; CCX58462.1; -; Genomic_DNA.
DR RefSeq; WP_021845320.1; NZ_HF986397.1.
DR AlphaFoldDB; R5C0S4; -.
DR GeneID; 85237218; -.
DR Proteomes; UP000018163; 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; 3.40.50.300; 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; 3.
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:UP000018163}.
FT DOMAIN 578..739
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 748..914
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1113 AA; 128035 MW; F641517657B18A5B CRC64;
MEAFVQPLRG LAEYEEISSR IGRNPGLVQI AGCVESQKAH LICGLSGLFP CRLILAQDES
RAKELYEDYR FYDKKVFYYP AKDLLFFQAD IHGNLLIKQR MQVVRALLEE ESVTVVTSVD
GCMDYLMPLG QIKENLVCLN SESTVDLEEL SKKLVWLGYE RVPQVERSGQ FAVRGGILDI
YSLTEENPWR IEMWGDEVDS IRSFDAYSQR SIENLETITI YPAAERLGEE GMVSFADYFP
VEKTLLILDE PNRMLEKGQE VEDEFRQSQK NRLEKGNRPL ADNLLFEISK LCGKLNRYHG
AALCMMEPAK KFWKVQERFE LTVKSVSSYN NSFELLVKDL RQWKKSGYRV ALLSGSRTRA
KRLAQDLMNE GLSSFYSEDY SRPIQPGEIM VVYGHAHRGF EYPLIKFVLI TESDIFGKEQ
KKRKKKKQYS GQKIQDFAEL TVGDYVVHEN HGLGIYRGIE KVEVDKVVKD YIKIEYRDGS
NLYILATQLD ALQKYAGQEA KTPRLNKLGT QEWNRTKTRV KGAVKDIARD LVKLYATRQE
KEGFVYGTDT VWQKEFEEMF PYEETEDQIQ AIEDTKRDME STKIMDRLIC GDVGYGKTEI
ALRAAFKAIQ EGKQVVYLVP TTILAQQHYN TFVQRMKEFP VRVELLCRFR TPAEQRKTLE
GLKKGWVDVV IGTHRVLSKD VEYKDLGLLI IDEEQRFGVT HKEKIKKLKN NVDVLTLTAT
PIPRTLHMSL IGIRDMSVLE EPPMDRMPIQ TYVMEYDEET VREAVQRELK RGGQVYYVYN
RVNDIAEVAS RLSQLLPDVQ VGFAHGQMSE RELEKVMYEF INGELDVLVS TTIIETGLDI
SNVNTMIIHD SDRYGLSQLY QLRGRIGRSN RTAYAFLMYR KNSILKETAE KRLSAIREFT
DLGSGFKIAM RDLELRGAGN LLGAQQHGHM QAVGYDLYCK MLNEAVKEAK GITVMEDFET
TIDLSMDAFI PNSYIANEFQ KLDIYKRIAG IENQEEYEDM LEELLDRFGE PPKAVMNLLA
IATLKAAAHR AYLREIKQRG AQVKLTLHEE AKIDAAGIPI LLKEYGRRLQ FRAEEKPYFL
FDLNGEGILG VQNLVERLEQ LAKDFAAQER QKG
//
