ID A0A1E7DLX6_9BACI Unreviewed; 1173 AA.
AC A0A1E7DLX6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=BA724_10380 {ECO:0000313|EMBL:OES44063.1};
OS Domibacillus iocasae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714016 {ECO:0000313|EMBL:OES44063.1, ECO:0000313|Proteomes:UP000095658};
RN [1] {ECO:0000313|EMBL:OES44063.1, ECO:0000313|Proteomes:UP000095658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29979 {ECO:0000313|EMBL:OES44063.1,
RC ECO:0000313|Proteomes:UP000095658};
RA Verma A., Pal Y., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus iocasae genome sequencing.";
RL Submitted (JUN-2016) 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:OES44063.1}.
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; MAMP01000023; OES44063.1; -; Genomic_DNA.
DR RefSeq; WP_069939296.1; NZ_MAMP01000023.1.
DR AlphaFoldDB; A0A1E7DLX6; -.
DR STRING; 1714016.BA724_10380; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000095658; 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:UP000095658}.
FT DOMAIN 638..799
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 813..974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1173 AA; 132214 MW; D26B15DD8DB0C57A CRC64;
MNHLLDLFLK NDEAVSVING MELGMKEQLA AGLSGSLRAV FAAAAHRKLQ KPVMIITYNM
LQAQKLYDDI VQFIPDEHVY VYAANELIAA EISIASPELR AQRIEMLNHL ALQGTGIYIV
PVAGLKKLLP SKDRWKRLQK IFTAGEEVEL ENLKHELVEM GYERADMVYA PGEFSIRGGI
IDLYPLTSEH PVRIELFDTE IDSIRTFAPD TQRSIENMNS ILIGPAAEMP ASAEELAALA
GRLQDALDDT LKKIGSPEVK KQLSSYVSAD IEKLKQGIRI DELGKYTSLL YAQTTLVTSY
LPENGVVFFD EMSRIKEISE SLEKEEAEWY TALIEDGKAV HGLTLAHTLQ EAIQATVQPS
VYLSLFMRQT AGGKPENIVN FSARPMQNFH GQMNVLEGEV ERWKKSGTTV LFLGETMERV
EKIKATLNDY GMEITMLKDQ NEVIEGVVQT GPGALTSGFE FPLLKVAVVT EQELFNKRAP
KSKRRQKLSN AERIKSYSEL KTGDYVVHVN HGIGKYLGIE TLQINNVHKD YLKIKYQGTD
ELFVPVEQIE LVQKYVGSEG KEPKIYKLGG SEWKRVKKKV ESSVQDIADD LIKLYAEREA
ARGYAFSPDG DMQREFEAAF PYEETEDQLR SIQEIKRDME REQPMDRLLC GDVGYGKTEV
AIRAAFKATA DGKQVAILVP TTILAQQHYE TLKERLQDFP VNVGLLSRFR TRKQQTETLK
GLKAGTVDIV IGTHRLLSKD VQYQDLGLLV VDEEQRFGVT HKEKIKQLKT NVDVLTLTAT
PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVVEHNLGL IREAAEREIA RGGQVFYLYN
RVEDIERRAD EISMLVPDAR VAYAHGQMTE TELEAVILGF LEGESDVLVT TTIIETGVDI
PNVNTLIVHD ADRMGLSQLY QIRGRVGRSN RVAYSYFMYR KDKVLSEPAE KRLQAIKEFT
ELGSGFKIAM RDLSIRGAGN LLGSQQHGFI DSVGFDLYSQ MLKEAIEQKQ GGDKEEKVPS
FEVDVTIDAY IPDAYITDSA QKIDMYKRFR SADSFDEINE LKEEMTDRFG DYPQEVADLF
TVAEMKIHAA KTKLESIKQS RDTVTILMSD EGTKEIDGSK VFAICNKFGR MCGLGMEDQR
LKITIDVKKA PEQGWFNASF ELIKELETAK KQV
//
