ID R8VU71_9CLOT Unreviewed; 1154 AA.
AC R8VU71;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=HMPREF1526_02579 {ECO:0000313|EMBL:EOQ35999.1};
OS Butyricicoccus pullicaecorum 1.2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Butyricicoccus.
OX NCBI_TaxID=1203606 {ECO:0000313|EMBL:EOQ35999.1, ECO:0000313|Proteomes:UP000013981};
RN [1] {ECO:0000313|EMBL:EOQ35999.1, ECO:0000313|Proteomes:UP000013981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1.2 {ECO:0000313|EMBL:EOQ35999.1,
RC ECO:0000313|Proteomes:UP000013981};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Van Immerseel F., Eeckhaut V.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Butyricicoccus pullicaecorum 1.2.";
RL Submitted (JAN-2013) 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:EOQ35999.1}.
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DR EMBL; AQOB01000010; EOQ35999.1; -; Genomic_DNA.
DR RefSeq; WP_016148695.1; NZ_KB976104.1.
DR AlphaFoldDB; R8VU71; -.
DR PATRIC; fig|1203606.4.peg.2550; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_3_9; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000013981; 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:UP000013981}.
FT DOMAIN 629..790
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..965
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1154 AA; 127209 MW; 8B37C7D3ABDA3EF2 CRC64;
MQNITLSITD SKEYKELFNA IRSGQTPALA VGLPPAAKAQ LAAALRLETS RPVCILTDED
NAALRLASDL ESFSELPVLH VPARELTMAG MEGMSRQYEQ ARIAALAQLS DAPLVTISAA
ALVQKTLPPA VLHNASLTIR VGDLTPLADL TAKLVTAGYQ RCAQVEGPGQ FSVRGGILDV
FPPRADAPVR IEFWGDEIDS ISAFDVGSQR RGASLNALTC LPCMEALPAC APGGIRGLCK
ALDQATRAKR KKHPDLVRNL ERDIERLTET QSLPAADKYL PLIYPEAATP LDYLPEDTIF
LIDDAPRLRE AVGGYILRLA GDLEALAERG ELPQQPEAFA LDFVALCRSL LGRPLVRLDT
FLSSVNELTP KTLVSFSVNQ MNAFGGSFDM AAADIAGFLQ LKRAVCVLCS SDLRCKNMRE
ALEAHGIDAP ISNRLPAPGR VHILEGTLSA GLEYPGLGLT ILTEGHAPAR KKASRTKKSN
RDRVKSYTDL TPGDLVVHEH HGIGRYIGME RMVVDGAARD FIKIAFAGTD FLYVPATSLD
LISKYIGGGE PEKVRLNKLG GADWQRARSR AKAAAKELAA GLIQLYAERA RLKGFAFPHD
DIWQREFEQA FPYDETDDQL RCIEEIKRDM ESSRPMDRLL CGDVGFGKTE VALRAVMKCV
LAGKQAAILV PTTVLARQHY LTAVQRFAGY PVKIELISRY KTASEQKKIF DQLQSGMIDL
IIGTHKLFNK KIKFHDLGLL IIDEEQRFGV SHKETLKEMS KQVDVLTLSA TPIPRTLNMA
LSGIRDMSAI EEPPHDRWPV QTYVMEYNDA IVNDAIRREL ARGGQIYYLH NYVESIERTA
LRLQKDFPDA RIGVAHGKMH MRELANVMNE MSDGALDILV CTTIIETGID IPNANTLIIE
DADHMGLAQL HQIRGRVGRS SRRAFAYLTF RRGKVLSEIS QKRLSAIREF AEFGSGFKIA
MRDLEIRGAG NVLGPEQSGH MMSVGYDLYL KLLEEAVLEE KGETPPQRVE CAAELTLSAN
LPADYVPDPG QRVDLYRRIA LIRSDEGRSD LLDELIDRYG EPPAEAVALL DIALLRAQAG
DQGVTEIKQD AGRLYITFAQ TDFRRLSQLC GDPDFSGRLL LNAGSQPYLS LRLKPGETPM
QMAQTLVKKY AETK
//
