ID Q9CD43_MYCLE Unreviewed; 1224 AA.
AC Q9CD43;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 138.
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:CAC29760.1};
GN OrderedLocusNames=ML0252 {ECO:0000313|EMBL:CAC29760.1};
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC29760.1, ECO:0000313|Proteomes:UP000000806};
RN [1] {ECO:0000313|EMBL:CAC29760.1, ECO:0000313|Proteomes:UP000000806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN {ECO:0000313|EMBL:CAC29760.1,
RC ECO:0000313|Proteomes:UP000000806};
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583917; CAC29760.1; -; Genomic_DNA.
DR PIR; D86940; D86940.
DR RefSeq; NP_301309.1; NC_002677.1.
DR RefSeq; WP_010907633.1; NC_002677.1.
DR AlphaFoldDB; Q9CD43; -.
DR STRING; 272631.gene:17574070; -.
DR KEGG; mle:ML0252; -.
DR PATRIC; fig|272631.5.peg.390; -.
DR Leproma; ML0252; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_11; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000000806; 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:UP000000806}.
FT DOMAIN 667..828
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 846..1003
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1224 AA; 131157 MW; 85A8271412FBD57D CRC64;
MTAPGPACLD TPIAGLVELA LTAPTFGQLM ERAGTRPAEL ILAGPACARL FVASALARLG
PLLVVTATGR EASNLTAELR GVFGAAVAMF PSWETLPHER LSPGVDTVGA RLMVLRRLAH
PDDARLGPPL QVVVTAVRSL LQPMTAQLGL VEPVTLSVGD EIGFERVIAR LVELAYTRVD
MVGRRGEFAV RGGILDIFGP TAEHPVRVEF WGDEITEMRM FSVVDQRSIP EIGVDTLVAI
ACRELLLSDD VRARAVELAA QAAARRPTEE PAISGSVTDV LAKLAEGIPV DGMEALLPVL
CPDDYALLTD QFAADTPVLL CDPEKVRIQA ADLIKTDRAF LEASWSVAAI GADNAAPVDV
EQLYGSGFVE LGDVQAAAIR SGHPWWTLSQ LSDESALELD IRAAPSTRGH QHAIDGIFAM
LRAHVATGGY AAIVTPGTGT AHRVVERLAE SDIPGAMLEP AAAPGLGLRP GLVGVLKGPL
LDGVVIPGAN LVIITEADLT GSRATPVEGK RLAAKRRSAA DPLALTAGDL VVHDQHGIGR
FVEMVERTVG GARREYLVLE YASNKKSKQA DKLYVPMDSL DQLSRYVGGQ APALSRLGGS
DWANTKTKAR CAVREIAGEL VSLYAKRQAS PGHAFGPDTP WQAEMEDAFG FTETVDQLTA
ITEVKGDMEK SVPMDRVICG DVGYGKAEIA VRAAFKAVQD GKQVAVLVPT TLLADQHLRT
FTERMAGFPV TVKGLSRFTD AAESRAVIDG LAEGSVDIVI GTHRLLQTGV CWKDLGLVVV
DEEQWFGVEH KEHIKSLRTH VDVLTMSATP IPRTLEMSLA GIREMSTILT PPEERYPVLT
YVGPHDDKQV AAALRRELLR DGQAFYVHNR VSSIYQAAAR VCGLVPEARV VVAHGQMPED
LLETTMRGFW NREYDILVCT TIVETGLDIP NANTLVVERA DTFGLSQLHQ LRGRVGRSHE
RGYAYFLYPP QAPLTEIAYD RLVTIAQNNE LGAGMAVALK DLEIRGAGNV LGVEQSGHVA
GVGFDLYVRL VGEAVEAYRA VADGKTAITP EEPKDVRIDL PVDAHLPPDY IASDRLRLEG
YRRLAAASSD TEVAAVVDEL IDRYGALPEP AQRLVAVAQL RLLCRGSGII EVTAPSASTM
RLSPIRLIDS AQVRLKRMYP GAQYRATAAT VQVPIPRAGS SGGTLGVPCI RDVELVQAVA
DLITALQGLP RKVIGITGPE PTSK
//
