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Database: UniProt
Entry: A0A0M9YNF7_9ACTN
LinkDB: A0A0M9YNF7_9ACTN
Original site: A0A0M9YNF7_9ACTN 
ID   A0A0M9YNF7_9ACTN        Unreviewed;      1177 AA.
AC   A0A0M9YNF7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=ADK56_04190 {ECO:0000313|EMBL:KOU54108.1};
OS   Streptomyces sp. MMG1522.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU54108.1, ECO:0000313|Proteomes:UP000037713};
RN   [1] {ECO:0000313|EMBL:KOU54108.1, ECO:0000313|Proteomes:UP000037713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1522 {ECO:0000313|EMBL:KOU54108.1,
RC   ECO:0000313|Proteomes:UP000037713};
RA   Noorani M.;
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:KOU54108.1}.
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DR   EMBL; LGDF01000036; KOU54108.1; -; Genomic_DNA.
DR   RefSeq; WP_030115459.1; NZ_LGDF01000036.1.
DR   AlphaFoldDB; A0A0M9YNF7; -.
DR   GeneID; 63980426; -.
DR   PATRIC; fig|1415545.3.peg.921; -.
DR   Proteomes; UP000037713; 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;  128660 MW;  1F3C8AC44F8F2FBF CRC64;
     MSLHGLLDVV VTDPALAEAV KAAGDGHRAH VDLVGPPGAR PFAVAALARQ TGRTVLAVTA
     TGREAEDLAA ALRTLLPPDT VAEYPSWETL PHERLSPRSD TVGRRLAVLR RLAHPREDDP
     ETGPVSVVVA PIRSVLQPQV KGLGELEPVS LESGQSADLG EVVEALAAAA YARVELVEKR
     GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKIAD QRSLEVAAHG LWAPPCRELL
     LTDQVRERAA VLAEEHPELG ELLGKIAEGI AVEGMESLAP VLVDDMELLL DVLPKGAMAI
     VCDPERVRTR AADLVATSQE FLQASWAASA GGGEAPIDVG AASLWGIADV RDRARELGMM
     WWTVSPFAAD AADHDDDTLQ LSMHAPEAYR GDTARALADT KGWLADGWRT VYVTEGQGLA
     SRTVEVLGGE GIAARLDADL TEITPSLVHV SCGAIDQGFV DPALKLAVLT ETDLTGQRTA
     TKDLGRMPAR RRKTIDPLTL EVGDYIVHEQ HGVGRYVEMV QRTVQGATRE YLLVEYAPAK
     RGQPGDRLYI PTDQLEQVTK YVGGEAPTLH RLGGADWTKT KQRAKKAVKE IAADLIKLYS
     ARMAAPGHAF GADTPWQREL EDAFPYAETP DQLSTIAEVK EDMEKTVPMD RLICGDVGYG
     KTEIAVRAAF KAVQDGKQVA VLVPTTLLVQ QHYGTFTERY SQFPVNVRAL SRFQSEAESK
     ATLEGLKDGS VDLVIGTHRL FSSETKFKDL GLVIVDEEQR FGVEHKEQLK KLRANVDVLT
     MSATPIPRTL EMAVTGIREM STITTPPEER HPVLTFVGPY EEKQIGAAVR RELLREGQVF
     YIHNRVESID RAAARLREIV PEARIATAHG QMSEQALEQV VVDFWEKKFD VLVSTTIVES
     GIDISNANTL IVERGDNFGL SQLHQLRGRV GRGRDRGYAY FLYPPEKPLT ETAHERLATI
     AQHTEMGAGM YVAMKDLEIR GAGNLLGGEQ SGHIAGVGFD LYVRMVGEAV ADYRAQMEGG
     VEEEPPLEVK IELPVDAHVP HDYAPGERLR LQAYRAIASA TSEDDIRAVR EELTDRYGPL
     PEPVENLLLV AGLRMLARAC GVGEIVLQGS NIRFAPVELR ESQELRLKRL HPKALIKPAA
     HQILVPRPTT GRIGGKPVIG RELLSWTGEF LTTILGS
//
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