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Database: UniProt
Entry: A0A0M9YKS5_9ACTN
LinkDB: A0A0M9YKS5_9ACTN
Original site: A0A0M9YKS5_9ACTN 
ID   A0A0M9YKS5_9ACTN        Unreviewed;      1177 AA.
AC   A0A0M9YKS5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=ADK54_09065 {ECO:0000313|EMBL:KOU51075.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU51075.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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:KOU51075.1}.
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DR   EMBL; LGDD01000070; KOU51075.1; -; Genomic_DNA.
DR   RefSeq; WP_053725035.1; NZ_LGDD01000070.1.
DR   AlphaFoldDB; A0A0M9YKS5; -.
DR   PATRIC; fig|1415557.3.peg.2018; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000037774; 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}.
FT   DOMAIN          642..803
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          828..978
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1177 AA;  129179 MW;  E0CA832EE961B5B3 CRC64;
     MSLHGLLDAV VRDPALAEAV KAATDGHRMH VDLVGPPAAR PFAIAGLARE AGRPVLAVTA
     TGREAEDLAA ALRSMLPAEE IVEYPSWETL PHERLSPRSD TVGRRLAVLR RLTHPSKDDP
     SAGPVSVVVA PIRSVLQPQV KGLGDLEPVA LRIGQSADLN TVVEGLAAAA YSRVELVEKR
     GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKVAD QRSLEIAEHG LWAPPCRELL
     LTDDVRTRAA ALAEEHPELG ELLGKIAEGI AVEGMESLAP VLVDDMELLI DVLPKGSMAV
     VCDPERVRTR AADLVATSQE FLQASWAASA GGGQAPIDVD AASLWGIADV RDRARELGMM
     WWSVSPFAAD EADFDEETLK LGMHAPETYR GDTQRALTDT KQWLADGWRT VYVTEGHGPA
     SRTVEVLGGE GIAARLAVDL GELTPSVVQV ACGAIDYGFI DPALKLAVLT ETDLTGQRTA
     TKDLGRMPAR RRKTIDPLTL EVGDYIVHEQ HGVGRYIEMV QRTVQNATRE YLLVEYAPAK
     RGQPGDRLYI PTDQLEQVTK YVGGEAPTLH RLGGADWTKT KARAKKAVKE IAADLIRLYS
     ARMAAPGHAF GADTPWQREL EDAFPYAETP DQLSTIAEVK EDMEKTVPMD RLICGDVGYG
     KTEIAVRAAF KAVQDGKQVA VLVPTTLLVQ QHFGTFTERY AQFPVNVRAL SRFQSDTEAK
     ATLEGLKDGS VDLVIGTHRL FSSETKFKDL GLVIVDEEQR FGVEHKEQLK KLRANVDVLT
     MSATPIPRTL EMAVTGIREM STITTPPEER HPVLTFVGPY EEKQIGAAIR RELLREGQVF
     YIHNRVESID RAAARLREIV PEARIQTAHG QMGESQLEQV VVDFWEKKFD VLVSTTIVES
     GIDISNANTL IVERGDNFGL SQLHQLRGRV GRGRERGYSY FLYPPEKPLT ETAHERLATI
     AQHTEMGAGM YVAMKDLEIR GAGNLLGGEQ SGHIAGVGFD LYVRMVGEAV ADYRAQMEGG
     EQEEAPLEVK IELPVDAHVP HDYAPGERLR LQAYRAIASA NSEEDIKAVR EELTDRYGKL
     PEPVENLLLV AGLRMLARAC GVGEIVLQGP NIRFAPVELR ESQELRLKRL YPRTVIKAPT
     RQILVPRPTA GKIGGKPVVG RELLAWTGEF LTTILGS
//
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