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Database: UniProt
Entry: A0A0P6WP54_9BACI
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ID   A0A0P6WP54_9BACI        Unreviewed;      1176 AA.
AC   A0A0P6WP54;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=AM506_18690 {ECO:0000313|EMBL:KPL58069.1};
OS   Rossellomorea vietnamensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL58069.1, ECO:0000313|Proteomes:UP000050398};
RN   [1] {ECO:0000313|EMBL:KPL58069.1, ECO:0000313|Proteomes:UP000050398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL58069.1,
RC   ECO:0000313|Proteomes:UP000050398};
RA   Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT   "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL   Submitted (AUG-2015) 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:KPL58069.1}.
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DR   EMBL; LIXZ01000020; KPL58069.1; -; Genomic_DNA.
DR   RefSeq; WP_060674217.1; NZ_LIXZ01000020.1.
DR   AlphaFoldDB; A0A0P6WP54; -.
DR   PATRIC; fig|218284.4.peg.1960; -.
DR   eggNOG; COG1197; Bacteria.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000050398; 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; 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}; 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:UP000050398}.
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"
SQ   SEQUENCE   1176 AA;  133845 MW;  3CC0FC4810658C0E CRC64;
     MKGILKQVHQ SEELQSIIAG VEERLSEQLV AGLSGSSRTA YIADVYLQTN KSTVVVTHNL
     FQAQKVYDDL IQFLSEDEVY LYSANELIAA ELSVASPELR AQRIEVMNKL SNHQQGVYIV
     PVAGLRKILP PKSMWATNQI SFQMGEDIDL DEVLNQLVQM GYQRTGMVST PGEFSLRGGI
     VDIFPLTTQN PVRIELFDTE IDSIRLFSVE DQRSIDKLNE IEIGPATEVL LKYENMERLI
     HEINAGLSTS LKKVKSAAVK EKMTEYIGHE VGQLENGEVP EQIFKYLSLA YDKPSSLLDY
     LPEDGVLFFD EYSRVQEMSE SLEKEEAEWY TSLLQEGQII HDVHVSHTFS SLVSKTKLPK
     VYFSLFLRHI PNTSPQNIFN VSTKPMQNFH GQMNVLKAEL DRWKKGKYTV VLLGPDQERV
     KKLQRVLDDY KIEIAFVEDG DKLLSGTIQM INGSLTSGFE LPLQKLAVIT EEELFNKKTK
     KKPRRQKLSN AERIKSYSEL KVGDHVVHVN HGIGKFLGIE TLEINGVHKD YLHVKYQGND
     KLYVPVDQIE LVQKYVASEN KDPKLYKLGG SEWKKVKSKV QSSVQDIADD LIKLYAEREA
     AKGYAFSPDG DMQREFEMAF PYEETDDQLR SVSEIKLDME RERPMDRLLC GDVGYGKTEV
     AIRAAFKAIA DGKQVAILVP TTILAQQHFE TIKERFQDFP VEIGLLSRFR TRKQQQETTK
     GLKNGTVDIV VGTHRLLSKD IQYRDIGLLI IDEEQRFGVT HKEKIKQLKT NIDVLTLTAT
     PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVMEYNGAL IKEAIEREMA RNGQVYFLYN
     RVEDIERKAD EISMLVPDAR IAYAHGQMSE NELEAVILSF LAGEYDVLVT TTIIETGVDI
     PNVNTLIVFD ADRMGLSQLY QLRGRVGRSN RVAYAYFTYR KDKVLTEVAE KRLQAIKEFT
     ELGSGFKIAM RDLTIRGAGN LLGAQQHGFI DSVGFDLYSQ MLKEAIEERK GDLPKQPESS
     FEVDIEIDAY IPDDYIKDGH QKIEMYKRFR SLSSLPEIEE LEEEILDRFG EYPEEVGYLF
     LISEMKIYAK NTKLESIKQD KKTVNIFMSP EGTAQIDGSK VFNLCNKHGR AVGLGMEGSK
     LKISINTARL EASKWFNMAY DIIKHLDEAV KIEESV
//
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