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Database: UniProt
Entry: A0A1D8T9F8_9NOCA
LinkDB: A0A1D8T9F8_9NOCA
Original site: A0A1D8T9F8_9NOCA 
ID   A0A1D8T9F8_9NOCA        Unreviewed;      1215 AA.
AC   A0A1D8T9F8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=BFN03_01930 {ECO:0000313|EMBL:AOW94282.1};
OS   Rhodococcus sp. WMMA185.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW94282.1, ECO:0000313|Proteomes:UP000178767};
RN   [1] {ECO:0000313|EMBL:AOW94282.1, ECO:0000313|Proteomes:UP000178767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMA185 {ECO:0000313|EMBL:AOW94282.1,
RC   ECO:0000313|Proteomes:UP000178767};
RA   Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT   "Draft Genome of Rhodococcus sp. WMMA185.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP017014; AOW94282.1; -; Genomic_DNA.
DR   RefSeq; WP_070380530.1; NZ_CP017014.1.
DR   AlphaFoldDB; A0A1D8T9F8; -.
DR   STRING; 679318.BFN03_01930; -.
DR   KEGG; rhw:BFN03_01930; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000178767; 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   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:UP000178767}.
FT   DOMAIN          667..828
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          853..1003
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1215 AA;  131475 MW;  D03A372754D53207 CRC64;
     MSSPLIATEP SADTPLAGLA KIALGDGVIT QVVEALGRDH LDVVAPPSAR PFVAAALAER
     THLLMVTATG READDLTAEL QEMIGDGVAQ FPSWETLPHE RLSPSADTVG RRMEVLRRLA
     RPDDPAYGAP LRVIVTTVRS LVQPMAPGLG EIEPITLREG TEHDFDGLIQ RLVDMAYTRV
     DMVGKRGEFA VRGGILDFFS PTADHPVRVE FWGDEVTELR AFSVADQRSL PELEIGSVVA
     PPCRELLLTE DVRARAAQLA VDNQADAALV EMLDKVSGGI PVEGMEALLP VLRPGQLQLL
     TDVLPDGAHI LLCDPEKIRT RATDLVRTGQ EFLEASWTAA SIGGAAPLDT SVLAGGGIDL
     GASAYRSLRQ VRESAEAAGL AWWNLSPLAS GSGEELELAV TPAPQVRGSD DLLAELFVNL
     RAHVTTGGRA VVVVAGSGTA HRVLERLHEA EVPATELAPG SEPVRGQVGV LRGSLHDGLV
     LPGDDATPGL VIVTETDLTG NRVAAVGDGK RLPAKRRNQV DPLALTAGDM VVHDQHGIGR
     FVEMVERTIG GARREYLVIE YAASKRGHPG DRLFVPMESL DQLSRYVGGE LPALSKLGGS
     DWANTKRKAR KAVREIAGEL VQLYAARQAA PGHAFGPDTP WQKEMEDAFA FTETHDQLTV
     ISEVKADMEK AVPMDRVVIG DVGYGKTEIA VRAAFKAVQD GKQVAVLVPT TLLAQQHLQT
     FTERMAAFPI TVRGLSRFTH TAEAKEIIDG MADGEVDVVI GTHRLLQTAV RWKDLGLVIV
     DEEQRFGVEH KEHIKALRTH VDVLTMSATP IPRTLEMSMA GIREMSTILT PPEERHPILT
     YVGAYADKQV AAAIRRELLR DGQVFYVHNR VSSIDKAAQR IRDLVPEARV VVAHGQMNED
     TLERTVQGFW ERDYDVLVCT TIVETGLDIS NANTLIVERA DSLGLSQLHQ LRGRVGRSRE
     RGYAYFLYPP EIPLTETAYD RLATISQNSD LGAGMAVAMK DLEIRGAGNV LGAEQSGHVA
     GVGFDLYVRL VGEAVEAFRA AADGKPIDAT ETPREVRIDL PVDAHIPPNY VTSDRLRLEG
     YRKLAAAGVL DEIAAVVEEL VDRYGPLPEE LRRLVSIAKL RLLCREYGIE EVAVVGTQLK
     ISPMALPDSK QLRLKRIYPS ARYRATTGMV QLPLPRAGSG GVGADRVRDL ELVQYIADLL
     LALDGKAAGS VVMEA
//
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