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Database: UniProt
Entry: A0A1V6MT93_9ACTN
LinkDB: A0A1V6MT93_9ACTN
Original site: A0A1V6MT93_9ACTN 
ID   A0A1V6MT93_9ACTN        Unreviewed;      1176 AA.
AC   A0A1V6MT93;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=BM536_014380 {ECO:0000313|EMBL:OQD55691.1};
OS   Streptomyces phaeoluteigriseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=114686 {ECO:0000313|EMBL:OQD55691.1, ECO:0000313|Proteomes:UP000184286};
RN   [1] {ECO:0000313|Proteomes:UP000184286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41896 {ECO:0000313|Proteomes:UP000184286};
RA   Schniete J.K., Salih T., Algora Gallardo L., Martinez Fernandez S.,
RA   Herron P.R.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OQD55691.1, ECO:0000313|Proteomes:UP000184286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41896 {ECO:0000313|EMBL:OQD55691.1,
RC   ECO:0000313|Proteomes:UP000184286};
RA   Salih T.S., Algora Gallardo L., Melo Santos T., Filgueira Martinez S.,
RA   Herron P.R.;
RT   "Draft genome sequence of Streptomyces phaeoluteigriseus type strain
RT   DSM41896.";
RL   Submitted (FEB-2017) 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:OQD55691.1}.
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DR   EMBL; MPOH02000011; OQD55691.1; -; Genomic_DNA.
DR   RefSeq; WP_073496110.1; NZ_MPOH02000011.1.
DR   AlphaFoldDB; A0A1V6MT93; -.
DR   STRING; 114686.BM536_014380; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000184286; 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          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;  128913 MW;  C1AB9F60FE965DB3 CRC64;
     MSLHGLLDAV VKDPALAEAT SAAADGNRMH IDLVGPPAAR PFTIAALARE TTRTVLAVTA
     TGRETEDLAA ALRTLLPPDG VVEYPSWETL PHERLSPRSD TVGRRLAVLR RLAHPRTDDP
     ETGPVSVVVA PVRSVLQPQV KGLGDLEPVA LRGGQTADLN EIVEALAAAA YARVELVEKR
     GEFAVRGGIL DVFPPTEEHP LRVEFWGDDV EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
     LTDDVRARAR ALAEQHPELG DLLGRLAEGI AVEGMESLAP VLVDDMELLL DVLPKGSMAV
     VCDPERVRTR ASDLVATSQE FLQASWAATA GGGEAPIDVG AASLWSIADV RDRARELDMM
     WWSVSPFAAD LELEADTLKL GMRAPEAYRG DTAKALADTK GWLAEGRRVV FVTEGHGTAA
     RTAEVLGNEG VPARLDTDLT ELTRSLVHVS CGSIDHGFVD PALDLVVLTE TDLTGQKAAG
     KDGARMPARR RKTIDPLTLE AGDYIVHEQH GVGRYIEMVQ RTVQSATREY LVVEYAPAKR
     GQPGDRLYIP TDQLEQITKY VGGEAPTLHR LGGADWTKTK ARAKKAVKEI AADLIKLYSA
     RMAAPGHAFG ADTPWQRELE DAFPYVETPD QLTTIAEVKD DMEKSVPMDR LICGDVGYGK
     TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFGTFSERYA QFPVKVKALS RFQSETEAKA
     VLEGLREGSV DVVIGTHRLF SSETRFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
     SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE ERQIGAAVRR ELLREGQVFY
     IHNRVESIDR AAARLREIVP EARIATAHGQ MSEAALEQVV VDFWEKRFDV LVSTTIVESG
     IDISNANTLI VERGDNFGLS QLHQLRGRVG RGRERGYAYF LYPPEKPLTE TAHERLATIA
     QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YVRMVGEAVA DYRRQLETGE
     IEEEAPLEVK IELPVDAHVP HDYAPGERLR LQAYRAIASA NSEDDVKAVR EELVDRYGKL
     PEPVENLLLV AGLRMLARSC GVGEIVLQGN NIRFAPVELR ESQELRLKRV YPGSVIKPAA
     HQLLVPRPKP AKMGGKPVVG RELLGWVGEF LVTVLG
//
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