ID K6DCQ3_9BACI Unreviewed; 1178 AA.
AC K6DCQ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=BABA_05811 {ECO:0000313|EMBL:EKN70317.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70317.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN70317.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:EKN70317.1}.
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; AJLS01000040; EKN70317.1; -; Genomic_DNA.
DR AlphaFoldDB; K6DCQ3; -.
DR STRING; 1117379.BABA_05811; -.
DR PATRIC; fig|1117379.3.peg.1215; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000006316; 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 CDD; cd18810; SF2_C_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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}; 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:UP000006316}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 820..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 413..440
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1178 AA; 134392 MW; 037D480E9B41D8F3 CRC64;
MNSLKTLFLQ QEDVHSMIAG IEGGLKEQLA AGLSGSSRTV LTACIYEQMK RPIILVTHNL
LQAQKLYDDI VNLLSEREVF LFPANEVIAA ELSIASPELK AQRIEALNHW SRSNQGILIV
PIAGLKKIIP PKSLWNHYQL KLAVGEDIQI DKLFNTFVKM GYVRVEMVTT PGEFSVRGGI
IDIYPLTEAD PLRLELFDTE IDSIRYFSLE DQRSKGKIKE VLIGPATEIL LEEEDFNRIT
IKLEQGLAHS LKKLKDDKAK MQLSQNISHD LEQLKNGQKP DQVYKYLSLA YDRPASLLDY
LPRNGLVFID EISRVQEMND SLVKEEAEWY TGLLGEGQMI HDLHISHDLQ LLLQKKEFPI
LYMSLFLRHV ANTNPQNIIN ISCKQMQNFH GQMHLLKAEI DRWKKGNYSV VFLGQDEERV
KKLERVLEDY EIDAVIVKAD QQLLPGRVQI MKGNLQAGFE LSIQKIAIIT EEELFNKRVK
KSKSRQKLSN AERIKSYSEL KIGDYVVHVN HGIGKYLGIE TLVINGVHKD YLHIRYQGTD
KLYVPVEQID LVQKYVGSEG KEPKVYKLGG TDWKKVKKKV ESSVQDIADD LIKLYAEREA
AVGYGFSPDG DMQREFETSF AYQETEDQLR SIVEIKKDME RLRPMDRLLC GDVGYGKTEV
AIRAAFKAIA DGKQVAFLVP TTILAQQHFE TLRERFQDYP INIGLLSRFR SKKQQTETMK
GLKAGTVDIV VGTHRLLSKD IVYRDLGLLI IDEEQRFGVT HKEKIKKLKT NVDVLTLTAT
PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVMEYNGSL VREAIERELA RDGQVYFLYN
RVEDIERKAE EISMLVPDAR VTCAHGQMTE NELESVMISF LAGEFDVLVS TTIIETGVDI
PNVNTLIVFD ADRMGLSQLY QLRGRVGRSN RVAYAYFTYR KDKVLTEVAE KRLQAIKEFT
ELGSGFKIAM RDLSIRGAGN LLGAQQHGFI DSVGFDLYSQ MLKEAIEARR GELGAEVKKS
VEIDLEIDAY IPDTYIKDGH QKIEMYKRFR AIESLEDMEE LQEEMHDRFG EYPAEVDYLF
QIAEIKVHSL INGVEQIKQA KQEVTVLVNE QVTNTIDGAK IFHIGGKFDR NVNPGMEGSK
LKIVIRIKDY DTIQWLHIVN EMVKGIPLAK RGQENPVK
//
