ID A0A221M7X1_9BACI Unreviewed; 1174 AA.
AC A0A221M7X1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ECO:0000313|EMBL:ASN03737.1};
GN ORFNames=CFK40_01330 {ECO:0000313|EMBL:ASN03737.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN03737.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN03737.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN03737.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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}.
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DR EMBL; CP022437; ASN03737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221M7X1; -.
DR KEGG; vne:CFK40_01330; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000204391; Chromosome.
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; 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; 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:UP000204391}.
FT DOMAIN 637..798
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 819..973
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 240..277
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1174 AA; 134703 MW; 49104E45584CF65E CRC64;
MKGIDTFLES KDDIKSIISG IESGMQEQLV AGLSGSARSL LVSVIEDSID KPVLLITHQL
VQAQQLYDDL SEFMGDQNVH LYPVNELIAS EIAIASPELR SQRIEALTEW SKKKSGILIA
PVTALKRILP PTSYWEKYQL HFRLGEDIDI DTYLNSLVDM GYERQTMVTT PGEFSRRGGI
IDIYPITEAH PIRIELFDEE VDSIRYFDAE TQRSLDKKKE VTIGPATELL LTEEDLLSGA
NRIETELAET LKKLKSNEAK EALSEALNQD LERLKNLEHF QEMYKYIGFL YKDPASLLDY
LPKNGLIILD EMSRIQETAT NIDTEEAEWY SNLLEANKMV KNSKFSFDWH EVWQKMEQPR
LYMSVFMRHI PNTQPQNIIN LSSRSMQEFH GQMHLFKNEL KRWMKSESSV VILVPNKKRM
EKIHSIFADY DIEATMAKSL KLPVEKPTIA IGNISSGIEL PMHKLVLITE NELFKKKTKR
VRKRQKISNA ERIKSYQELK IGDYVVHANH GIGKYIGIET LEMSDMHKDY MLIRYASDDK
LFVPIDQIDL VQKFVGSEGK EPKLYKLGGS EWAKVKKKVQ SSVEDIADDL IKLYAEREAQ
KGYAFSEETE MQREFEAAFP YQETEDQIRC IVEIKQDMEK ERPMDRLLCG DVGYGKTEVA
IRAAFKAVAD GKQVAILVPT TILAQQHYET IRERFQDQAV TIGLLSRFRT KKQLKETTAG
LKSGIVDIVI GTHRLLSKDV VYRDLGLLVV DEEQRFGVKH KEKIKQMKTN VDVLTLTATP
IPRTLHMSML GVRDLSVIET PPENRFPIQT YVLEYNPILI REAIEREMSR GGQVFFLYNR
VENIDSIARE IGTLVDDAKI AVAHGRMNET ELENVMFGFL EGEFDVLVST TIIETGVDIP
NVNTLIVYDA DRMGLSQLYQ LRGRVGRSNR VAYAYFTYKK DKVLTEVAEK RLQAIKEFTE
LGSGFKIAMR DLSIRGAGNL LGSQQHGFID SVGFDMYSKM LTDAIEARKF GKDVIDMKQF
EPELALKTDA YIPDTYIKDE KQKIDMYKRF QTLTSDDDFE DLREELVDRF GDYPEEVANL
FDVSSMKMHA RNERVESITE KGKKMELLVD ENRSQQIDGS KLFTLANEFG RGVQLGTDNK
KLKITIQWPK DAEHKRYELA TQFMEQLASV NRND
//
