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Database: UniProt
Entry: A0A101UHB7_9ACTN
LinkDB: A0A101UHB7_9ACTN
Original site: A0A101UHB7_9ACTN 
ID   A0A101UHB7_9ACTN        Unreviewed;      1177 AA.
AC   A0A101UHB7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=AQJ58_17265 {ECO:0000313|EMBL:KUO10703.1};
OS   Streptomyces sp. DSM 15324.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO10703.1, ECO:0000313|Proteomes:UP000053431};
RN   [1] {ECO:0000313|EMBL:KUO10703.1, ECO:0000313|Proteomes:UP000053431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO10703.1,
RC   ECO:0000313|Proteomes:UP000053431};
RA   Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL   Submitted (OCT-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:KUO10703.1}.
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DR   EMBL; LMXA01000015; KUO10703.1; -; Genomic_DNA.
DR   RefSeq; WP_067251093.1; NZ_KQ949027.1.
DR   AlphaFoldDB; A0A101UHB7; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000053431; 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:UP000053431}.
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   1177 AA;  128724 MW;  46CB32599FD1B886 CRC64;
     MSLHGLLDAV VKDTALAEAI PAAADGNRMH IDLVGPPAAR PFAIAALARE TGRTVLAVTA
     TGREAEDLAA ALRSLLPPDT VVEYPSWETL PHERLSPRSD TVGRRLAVLR RLSHPRPDDP
     ETGPVSVVVA PVRSVLQPQV KGLGDLEPVA LRTGGQADLN QTVAALAAAA YARVELVEKR
     GEFAVRGGIL DVFPPTEEHP LRIEFWGDDI EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
     LTDDVRARAR ALAEQHPELG ELLHKIAEGI AVEGMESLAP VLVDDMELLI DVLPKGAMSV
     VCDPERVRTR AADLVATSQE FLQASWAATA GGGEAPIDVG AASLWSIADV REHARERDMM
     WWSVSPFAAD LELEADTLQL GMHAPETYRG DTAKALADTK GWLADGWRVV FVTEGQGPAA
     RTVEVLGGEG VAARLDTDLA SLSPSVVQVA CGSVEYGFVD PALKLVVLTE TDLSGQKAAG
     KDGARMPARR RKTIDPLTLE AGDYIVHEQH GVGRYIEMVQ RTVQGATREY LVVEYAPAKR
     GQPGDRLYIP TDQLEQITKY VGGEAPTLHR LGGADWTKTK ARAKKAVKEI AADLIKLYSA
     RMAAPGHAFG TDTPWQRELE DAFPYAETPD QLTTIAEVKD DMEKTVPMDR LICGDVGYGK
     TEIAVRAAFK AVQDGKQVAV LVPTTLLVQQ HFGTFSERYA QFPVNVRALS RFQTDTEAKA
     VLEGLREGAV DVVIGTHRLF SSETKFKDLG LVIVDEEQRF GVEHKEQLKK LRANVDVLTM
     SATPIPRTLE MAVTGIREMS TITTPPEERH PVLTFVGPYE EKQIGAAIRR ELLREGQVFY
     IHNRVESIDR AAARLREIVP EARIATAHGQ MSESALEQVV VDFWEKKFDV LVSTTIVESG
     IDISNANTLI VERGDTFGLS QLHQLRGRVG RGRERGYAYF LYPPEKPLTE TAHERLATIA
     QHTEMGAGMY VAMKDLEIRG AGNLLGGEQS GHIAGVGFDL YVRMVGEAVA DYRRQLETGE
     IEEEPPLEVK IELPVDAHVP HDYAPGERLR LQAYRAIASA TSEEDVRAVR EELVDRYGKV
     PEPVENLLLV AGLRMLARAC GVGEIVLQGT NIRFAPVELR ESQELRLKRL YPGSVIKPAV
     HQILVPRPKT AKVGGKPLVG RELLGWVGEF LASVLGS
//
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