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Database: UniProt
Entry: A0A3N0DZA1_9ACTN
LinkDB: A0A3N0DZA1_9ACTN
Original site: A0A3N0DZA1_9ACTN 
ID   A0A3N0DZA1_9ACTN        Unreviewed;      1172 AA.
AC   A0A3N0DZA1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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   ECO:0000313|EMBL:RNL80939.1};
GN   ORFNames=EFL95_00700 {ECO:0000313|EMBL:RNL80939.1};
OS   Nocardioides marmorisolisilvae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1542737 {ECO:0000313|EMBL:RNL80939.1, ECO:0000313|Proteomes:UP000277094};
RN   [1] {ECO:0000313|EMBL:RNL80939.1, ECO:0000313|Proteomes:UP000277094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIS18-7 {ECO:0000313|EMBL:RNL80939.1,
RC   ECO:0000313|Proteomes:UP000277094};
RA   Li F.;
RL   Submitted (NOV-2018) 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:RNL80939.1}.
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DR   EMBL; RJSG01000001; RNL80939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N0DZA1; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000277094; 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   CDD; cd18810; SF2_C_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:UP000277094}.
FT   DOMAIN          640..801
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          819..976
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1172 AA;  128266 MW;  93288F081EF57C88 CRC64;
     MRLAGLADAV LTDPVLAAAL ARAGDVDATV LDLTGPPALR PFAIAGLART GRTVLVVTAT
     VREAEDLVTE LADVVPAESL VHFPAWETLP HERLSPRSDT VGRRLAILRR LVHPGADAGN
     GPVRVVVAPV RSVLQPQVKG LADLEPVELV PGQEIELDQV VKNLVGAAYS RVDLVEKRGE
     FAVRGGIVDV FPPTEEHPVR VEFFGDEVDE IRTFAVADQR TIEKLPRLWA PPCRELLLTD
     EVRERAAELG RNHPELRELT DKLAEGIAVE GMESLTPALV DEMELLIDLL PKDTSVLVLD
     PERVRTRAHD LVATSEEFLG ASWAAAAAGG QAPIDLGAAS LRTLGDVRGA ALDQGKAWWG
     LSPFGLDEDD ESVVVQAAAV EPYRGDIDAA VKDIADHVAQ GRRVVVVQQG HGPAQRTVEV
     LGEHEVAARL VDGVPTGSTG TPDGVVLVTQ GCLTTGLVLE AAGLVVLTGE DLSGQKASTR
     DMRAMPTRRK KQIDPLELKP GDFVVHEQHG VGRFLEMKQR EVHGAMREYL VLEYGSSKRG
     QPADKLFVPA DALDQVTRYV GGEQPSLDRL GGADWAKRKG RAKKAVRQIA AELIKLYAAR
     QATKGHAFGP DTPWQRELED AFPFHETPDQ LTTVEEVKAD MRRTVPMDRL VCGDVGYGKT
     EIAVRAAFKA VQDGTQVAVL VPTTLLVTQH FSTFAERMSG FPVVLKQLSR FQTDKEAAEV
     IAGLADGTVD IVIGTHRLLN PDIRFKDLGL IVVDEEQRFG VEHKELMKRM RTSVDVLSMS
     ATPIPRTLEM AITGIREMST ITTPPEERHP VLTYVGAYED RQVIAAIRRE LLREGQVFFI
     HNRVTSIEKA AAKIKELVPE ARVATAHGQM GEHQLEQVML DFWERRFDVL VCTTIVESGL
     DVSNANTMII ERSDTLGLSQ LHQLRGRVGR SRERAYAYFL YPADKPLTET AHERLATLAQ
     HSDLGGGMAI AMKDLEIRGA GNLLGGEQSG HIADVGFDLY VRLVGEAVSE FRAGTGAGEA
     EEQLSEVRIE IPVDAHLPHD YVPSERLRLE MYKRLSEVRA DEDVDQLRAE MADRYGAPPA
     PVERLLAVAR FRGLCRRVGV GEITIQGKYV RFAPVELLDS RAVRLNRVYP GSLVKASVRT
     MLVPRPHGLR DEELLAWASR VIESILSQET AS
//
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