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Database: UniProt
Entry: A0A100Y0S6_9ACTN
LinkDB: A0A100Y0S6_9ACTN
Original site: A0A100Y0S6_9ACTN 
ID   A0A100Y0S6_9ACTN        Unreviewed;      1176 AA.
AC   A0A100Y0S6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=ATE80_28485 {ECO:0000313|EMBL:KUH35559.1};
OS   Streptomyces kanasensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH35559.1, ECO:0000313|Proteomes:UP000054011};
RN   [1] {ECO:0000313|EMBL:KUH35559.1, ECO:0000313|Proteomes:UP000054011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZX01 {ECO:0000313|EMBL:KUH35559.1,
RC   ECO:0000313|Proteomes:UP000054011};
RA   Zhang G., Han L., Feng J., Zhang X.;
RT   "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT   kanasensis ZX01.";
RL   Submitted (NOV-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:KUH35559.1}.
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DR   EMBL; LNSV01000129; KUH35559.1; -; Genomic_DNA.
DR   RefSeq; WP_058945147.1; NZ_LNSV01000129.1.
DR   AlphaFoldDB; A0A100Y0S6; -.
DR   STRING; 936756.ATE80_28485; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000054011; 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:UP000054011}.
FT   DOMAIN          641..802
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          827..977
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1176 AA;  128167 MW;  17DFDD958BA89D9E CRC64;
     MSLHGLLDAV VKDPALAEAV KAAADGHRGH VDLVGPPAAR PFAVAALARD AGRPVLAVTA
     TGREAEDLAA ALRSLLDPDT VVEYPSWETL PHERLSPRSD TVGRRLAVLR RLTHPSADDP
     AVGPVSVVVA PVRSVLQPQV KGLGDLEPVA LRTGQQADLD EVVAGLAAAA YARVELVEKR
     GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
     LTDEVRRRAA ALAEEHPELG ELLGKIAEGI AVEGMESLAP VLVDDMELLL DVLPKGAMAV
     VCDPERVRTR AADLVATSQE FLHASWAATA TGGEAPIDVD AASLWGIADV RDRARDLGVM
     WWSVSPFAAD EELDADTIKL GMHAPESYRG DTARALADTK GWLADGWRAV YVTEAHGPAA
     RTVEVLGGEG IAARLDGDLT DISPAVVHVA CGSIDHGFVD PALRLAVLTE TDLSGQKAAG
     KDGQRMPTRR RKTIDPLTLE AGDYIVHEQH GVGRYIEMVQ RTVQGATREY LLVEYAPAKR
     GQPGDRLYIP TDQLEQVTKY VGGEAPTLHR LGGADWTKTK ARAKKAVKEI AADLIKLYSA
     RMAAPGHAFG PDTPWQRELE DAFPYVETPD QLSTIAEVKE DMEKTVPMDR LVCGDVGYGK
     TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFGTFSERYA QFPVVVRALS RFQSDAEAKA
     TLEGLREGSV DIVIGTHRLF SSETKFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
     SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE EKQIGAAVRR ELLREGQVFY
     IHNRVESIDR AAARLRDIVP EARIATAHGQ MSEQALEQVV VDFWEKKFDV LVSTTIVESG
     IDISNANTLI VERGDNFGLS QLHQLRGRVG RGRERGYAYF LYPPEKPLTE TAHERLATIA
     QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YVRMVGEAVA DYRASLEGGV
     EEEPPLEVKI ELPVDAHVPH DYAPGERLRL QAYRAIASAN SEEDVKAVRE ELTDRYGKLP
     EPVENLLLVA GLRMLARACG VGEIVLQGGN VRFAPVELRE SQELRLKRLH PRTVIKASAR
     QVLVPRPTSG TIGGKPVVGR ELLAWTGEFL TTILGS
//
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