ID R5Y8D9_9FIRM Unreviewed; 1155 AA.
AC R5Y8D9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=BN695_01143 {ECO:0000313|EMBL:CDA12892.1};
OS Anaerotruncus sp. CAG:528.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1262700 {ECO:0000313|EMBL:CDA12892.1, ECO:0000313|Proteomes:UP000018024};
RN [1] {ECO:0000313|EMBL:CDA12892.1, ECO:0000313|Proteomes:UP000018024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:528 {ECO:0000313|Proteomes:UP000018024};
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:CDA12892.1}.
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DR EMBL; CBBE010000040; CDA12892.1; -; Genomic_DNA.
DR AlphaFoldDB; R5Y8D9; -.
DR STRING; 1262700.BN695_01143; -.
DR Proteomes; UP000018024; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000018024}.
FT DOMAIN 625..786
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 804..961
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 459..486
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1155 AA; 128046 MW; 36E71AD1C889DC89 CRC64;
MSCFSKVFEK SDEFKSLAGS ININGAAVGA TGVSDAVKAH MIHSLIQEKG EKAVIIMPDE
ASAVRMSENL GAVQAGVLFY PAREFTFQHV AGVSRDFEHI RLGVLSKIIN EEYTAIVCSV
NAATQLTMPP QELKKRTIVI KSGAQIDFDS LVSRLVFAGY SRYEQVDGTS QFAVRGGIID
IFPPGASEPV RIELWGDMVD SISSFDISTQ RRTGNLSEIE LIPATEVLFE SNEKFIKKLR
ALAESLKGKA IKAREGIYAD IDSLEAGVSL PCCDKYMPLA YESSGIFDYL SGLLFVCESS
KVKERSQNSE RLILEQIKWY LEDGTLCKGL DKYQLGFEEL RQIYSSHGAV YLDSLPRGSF
DTPVAHLSSF AVQSFNAWNG KTEDLKEDIA PLLKNGYTVC VMAGTARSAK ALAYDLNDDG
INAVFSNGYP LEFQKGAVTV TTGTITAGFV LPAAKFALIT HMKAQMQKAK KHKANAKNAI
HSLDELSVGD YIVHNVHGIG IFEGIHALEL NKVKKDYIKI SYAKGDVLYV PVTQLDLVSK
YIGPGESNNV KINRLGGNEW KKAKAKVRAS VKDMAKELIA LYAKRMSTKG YAFSEDTDFQ
RDFELRFAYD ETDDQLRCSE EIKRDMERSV PMERLLCGDV GFGKTEVALR AAFKCITEGK
QCALLVPTTV LAMQHFNTAK SRMEAFPVKI EMLSRFVSAA KQKEVIKGLE NGSVDFLIGT
HRIIGKDIKF RDLGLLIIDE EQRFGVAQKE KLKQKFPRVD VLTLSATPIP RTLNMALSGI
RDMSVIEEAP GDRYPVQTYV TEYDFGMLVE AMEKELARGG QCYYLHNNIE TIEHTAVKIK
KAIPDANVGI AHGRMTQEQL SDVWAALLNG EIDILVCTTI IETGIDVSNV NTLIIENADR
MGLAQLHQIR GRVGRSARRA YAYLTFTRGR ELSDVAQKRL EAIREYTEFG SGFKIAMRDL
EIRGAGSILG NRQHGHMESV GYDMYLKLLG DAVAEEKGEL KEGEEQAECL IDLPIEAHIP
DDYIESTPQR LSMYKRIAAI RTGADANDVR DELCDRFGTP PESINGLIEI SLLRNSAASL
GVYEIAQRNG SVLLYMNEPD VRYAVELNKV MKGRVLLSAS KKAYIAVKLG TESSLETVRT
ALELMHQAKR NFDKN
//
