ID R8HGD6_BACCE Unreviewed; 1176 AA.
AC R8HGD6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=IIC_04213 {ECO:0000313|EMBL:EOO71933.1};
OS Bacillus cereus VD021.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053224 {ECO:0000313|EMBL:EOO71933.1, ECO:0000313|Proteomes:UP000014040};
RN [1] {ECO:0000313|EMBL:EOO71933.1, ECO:0000313|Proteomes:UP000014040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD021 {ECO:0000313|EMBL:EOO71933.1,
RC ECO:0000313|Proteomes:UP000014040};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD021.";
RL Submitted (DEC-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:EOO71933.1}.
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; AHES01000039; EOO71933.1; -; Genomic_DNA.
DR RefSeq; WP_016102352.1; NZ_KB976281.1.
DR AlphaFoldDB; R8HGD6; -.
DR PATRIC; fig|1053224.3.peg.4256; -.
DR HOGENOM; CLU_005122_1_3_9; -.
DR Proteomes; UP000014040; 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; 3.40.50.11180; -; 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}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 824..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1176 AA; 134091 MW; BA100CAE6D12546D CRC64;
MIGLLEQFYK NEEIQSVING LEDGLKEQLV SGMATSSRSL LMAALYKKTK QSQLIVTHNL
YQAQKVHEDL VALLGEKDVW LYPVNELIAS EVGVASPELK AQRIEVLNRL AAGENGIIVA
PVAGLRRFLP IKELWKQRQI EINLGQEIDL DALLHTLHHI GYERKSMVEA PGEFSLRGGI
LDIYPLTEEL PFRIEFFDTE VDSIRLFDVD EQRSQDKKES VKFGPATEFL FSQEELKSGI
KHLEEGLTKT MQKLSDDKLK TTVLETVSHE IEMLKNGQSI EQMFKYLSIF YKEPASLIDY
LPENGVVILD EISRIQETAS HLETEEAEWY ISLLGEGTII QDLSFSHSFE EFLHNKKRSF
VYLTLFLRHI AHTHPQNIVN VTCKTMQDFH GQMHLLKTEI DRWNEGNFTT VVLGTDDERV
KKLQHILSDY DIDADIVEAT DILLPGRLQI AVGDLHAGFE MPMQKFVVIT EKELFHKKVK
KSQRKQKLSN AERIKSYSEL KVGDHVVHVN HGIGKFLGIE TLEINGVHKD YLNIKYQGND
KLYVPIEQID QVQKYVGSEG KEPKVYKLGG NDWKKVKTKV EKSVQDIADD LIKLYAEREA
SKGYAYTPDT AEQQEFESLF PYQETEDQLR SIEEIKKDME RGRPMDRLLC GDVGYGKTEV
AIRAAFKAIM DEKQVAILVP TTILAQQHYE TIRERFQDYP INIGLLSRFR TRKQQNETIK
GLKDGTVDIV IGTHRILSKD VTYKDLGLLI IDEEQRFGVT HKEKIKQLKA NVDVLTLTAT
PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVVEYNPAL MREAIERELA RGGQIYFLYN
RVEDIERKAD EISMLVPDAR VTYAHGKMNE GELESVMLSF LEGQHDVLVS TTIIETGVDI
PNVNTLIVFD ADRMGLSQLY QLRGRVGRSN RVAYAYFAYK RDKVLSEVAE RRLQAIKEFT
ELGSGFKIAM RDLSIRGAGN LLGAEQHGFI DSVGFDLYSQ MLKDAIEQRR GTDGVENTVN
VEIDLEVDAY LPDAYISDSK QKIMMYKQFR GISAIEDIEE LQEEMIDRFG DYPQEVGYLL
QIANIKVLAM KEQIELIKQN KFEVTFLFSE QASQNIDGGK LFMLGSSFGR MIGLGMEGSQ
LKIVMKTNGL ETSKWLTIAE NLLKGLPDVK KEVINA
//
