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Database: UniProt
Entry: A0A170YUD1_9ACTN
LinkDB: A0A170YUD1_9ACTN
Original site: A0A170YUD1_9ACTN 
ID   A0A170YUD1_9ACTN        Unreviewed;      1183 AA.
AC   A0A170YUD1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=STXM2123_3421 {ECO:0000313|EMBL:GAT82720.1};
OS   Streptomyces sp. F-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT82720.1, ECO:0000313|Proteomes:UP000078145};
RN   [1] {ECO:0000313|EMBL:GAT82720.1, ECO:0000313|Proteomes:UP000078145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT   "Streptomyces sp. F-3 geneom sequencing.";
RL   Submitted (MAY-2016) 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:GAT82720.1}.
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DR   EMBL; BDDR01000020; GAT82720.1; -; Genomic_DNA.
DR   RefSeq; WP_067396476.1; NZ_BDDR01000020.1.
DR   AlphaFoldDB; A0A170YUD1; -.
DR   STRING; 1840095.STXM2123_3421; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000078145; 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:UP000078145}.
FT   DOMAIN          647..808
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          826..983
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1183 AA;  129482 MW;  C3C24D2BF0AD50BE CRC64;
     MTLHGLLDAV VKDPALAEAI TAAADGNRMH IDLVGPPAAR PLAVAALARE TARPVLAVTA
     TGREAEDLAD ALRSLLPPHG VVEYPAWETL PHERLSPRSD TMGRRLAVLR RLAHPDPDDP
     ETGPVSVVVA PVRSVLQPQV KGLGDLEPVS LRTGQSADLD DVVEALAAAA YSRVELVEKR
     GEFAVRGGIL DVFPPTEEHP LRIEFWGDDV EEIRYFKVAD QRSLEVAEHG LWAPPCRELL
     LTEDVRARAR ELAERHPELG ELLGRIAEGI AVEGMESLAP VLVDDMELLL DVLPEGAMTV
     VCDPERVRTR AADLVATSQE FLQASWAATA GGAEAPIDVG AASLRSIADI RDHARELGMM
     WWTVSPFAAD ETAYGGEDEG ADTLKLGMRA PETYRGDTAR ALADTKGWLA DGWRTVFVTE
     GHGPASRTVE VLGGEGIAAR LDVDLKELSP SVVHVACGSV THGFVDPGLK LAVLTETDLT
     GQKTAGRDGA RMPVRRRKSI DPLTLEPGDY IVHEQHGVGR YIEMVQRTVQ GATREYLVVE
     YAPAKRGQPG DRLYIPTDQL EQITKYVGGE APTLHRLGGA DWTKTKARAR KAVKEIAADL
     IKLYSARMAA PGHAFGPDTP WQRELEDAFP YTETPDQLTT IAEVKADMEK PVPMDRLICG
     DVGYGKTEIA VRAAFKAVQD GKQVAVLVPT TLLVQQHFAT FSERYAQFPV NVKALSRFQT
     DAEAKAVLDG LRDGSVDVVI GTHRLFSSET KFKDLGLVIV DEEQRFGVEH KEQLKKLRAN
     VDVLTMSATP IPRTLEMAVT GIREMSTITT PPEERHPVLT FVGPYDEKQI GAAIRRELLR
     EGQVFYIHNR VESIDRAAAR LREIVPEARI ATAHGQMSEA ALEQVVVDFW EKKYDVLVST
     TIVESGIDIS NANTLIVERS DTFGLSQLHQ LRGRVGRGRE RGYAYFLYPP EKPLTETAHE
     RLATIAQHTE MGAGMYVAMK DLEIRGAGNL LGGEQSGHIA GVGFDLYVRM VGEAVADYRR
     QLETGEIKEE PPLEVKIELP VDAHVPHDYA PGERLRLQAY RSIASANSEE DIKAVREELT
     DRYGKLPEPV ENLLLVAGLR MLARACGVSE IVLQGTNIRF APVELRESQE LRLKRLYPGS
     VIKPAVHQVL VPRPKTAKVG GKPLVGRELL GWVGEFLTSA LGS
//
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