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Database: UniProt
Entry: G8SIM6_ACTS5
LinkDB: G8SIM6_ACTS5
Original site: G8SIM6_ACTS5 
ID   G8SIM6_ACTS5            Unreviewed;      1203 AA.
AC   G8SIM6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=trcF {ECO:0000313|EMBL:AEV81824.1};
GN   Synonyms=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   OrderedLocusNames=ACPL_927 {ECO:0000313|EMBL:AEV81824.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV81824.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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}.
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DR   EMBL; CP003170; AEV81824.1; -; Genomic_DNA.
DR   RefSeq; WP_014687897.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8SIM6; -.
DR   STRING; 134676.ACPL_927; -.
DR   KEGG; ase:ACPL_927; -.
DR   PATRIC; fig|134676.3.peg.817; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_2_2_11; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000005440; Chromosome.
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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AEV81824.1};
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:UP000005440}.
FT   DOMAIN          666..827
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          845..1002
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1156..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1203 AA;  132065 MW;  7E1FDC1E9B2BD402 CRC64;
     MQLAGLIPAA LRDRGLARAR DLARKGFVDS DSMDLTAPVS LRPFVVATVA GPADAGGAQR
     PVLAVTATSR EADDLADALG CLIEPGRVAV YPSWETLPHE RLSPRSDTVG RRLAVLRRLA
     HPGDQPLQVV VAPVRSLLQP QLKGLGDLEP VELVTGREAE LEGVARRLSD MAYARVDLVT
     KRGEFAVRGG ILDVFPPTDE HPSRVEFWGD EVEEIRTFAV ADQRTIEQVE RLWAPPCREL
     LLTPAVREKA ALLATRHPEL AEILDRLAEG IPVEGMESLA PALLDGTDSM ELLIDCMPAG
     THVLLCDPER IRTRAHDLTR TSDEFLEASW AAAAVGGEAP IDVGAVAFKT LADVRAHAAV
     LHQPWWTLSP FGLATADEPA AALPWEDAGT VEVSPDTGDA VALAAQPVPL YHGDTERLAA
     DLAGWSAAGW AVALVFEGKG TAQRATELLR DAGLGVTPVD SIATPIADGQ LLVTCGGLNH
     GFVDEASRLA VITGNDISGG RGASTKDMRK MPARRRNTID PLELKMGDFV VHEQHGIGRY
     IELVQRTVNG ADREYLVIEY AASKRGQPGD RLYVPTDQLD QLSRYVGGEQ PTLHKMGGAD
     WQKSKARAKK AVKEIAAQLI QLYAARQASK GHSFGPDTPW QRELEDAFPY TETPDQMAAI
     IEVKHDMELQ TPMDRLICGD VGYGKTEIAV RAAFKAVQDG KQVAVLVPTT LLAQQHYNTF
     TERMSQFPVQ IRQLSRFQTP KEAALTLENA ADGTADIVIG THRLLSKSTR FKNLGLIIVD
     EEQRFGVEHK EQLKALRASV DVLTMSATPI PRTLEMAITG IREMSTIATP PEERHPVLTY
     VGAYDDKQVA AAIHRELLRD GQVFYLHNRV ESIDRAARRL RELVPEARVA VAHGQMSEEQ
     LEKVMVGFWE KEFDVLVCTT IVESGIDIPN ANTLILERAD LLGLAQLHQI RGRVGRGRER
     AYAYFLYPRE KPLTEHAHER LATIAQHTEL GAGMYVAMKD LEIRGAGNLL GGEQSGHIEG
     VGFDLYVRMV GEAVSAFKGE RPEEEPEVKI DLPIDAHLPT DYIAVERLRL EMYRKLAEAR
     DDARLDEVVA EMTDRYGEPP AAVVNLIAVA RFRQLARAYG LTDVSMQGRH LRFAPLALPD
     SKQMRLKRYH PDSVYKPAND QVSVPRPQTR RVGGEPLRDQ DLLQWCAQLL KDVLGDAPAP
     ARV
//
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