ID A0A2Z6EUG6_9BURK Unreviewed; 1151 AA.
AC A0A2Z6EUG6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:GLR00273.1};
GN ORFNames=GCM10007934_00840 {ECO:0000313|EMBL:GLR00273.1}, MCB1EB_0900
GN {ECO:0000313|EMBL:BBE09061.1};
OS Mycoavidus cysteinexigens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Mycoavidus.
OX NCBI_TaxID=1553431 {ECO:0000313|EMBL:BBE09061.1, ECO:0000313|Proteomes:UP000282597};
RN [1] {ECO:0000313|EMBL:BBE09061.1, ECO:0000313|Proteomes:UP000282597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1-EB {ECO:0000313|EMBL:BBE09061.1,
RC ECO:0000313|Proteomes:UP000282597};
RX PubMed=29540638; DOI=10.1264/jsme2.ME17138;
RA Sharmin D., Guo Y., Nishizawa T., Ohshima S., Sato Y., Takashima Y.,
RA Narisawa K., Ohta H.;
RT "Comparative Genomic Insights into Endofungal Lifestyles of Two Bacterial
RT Endosymbionts, Mycoavidus cysteinexigens and Burkholderia rhizoxinica.";
RL Microbes Environ. 33:66-76(2018).
RN [2] {ECO:0000313|EMBL:GLR00273.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR00273.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLR00273.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR00273.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Mycoavidus cysteinexigens strain NBRC 110909.";
RL Submitted (JAN-2023) 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; AP018150; BBE09061.1; -; Genomic_DNA.
DR EMBL; BSOD01000001; GLR00273.1; -; Genomic_DNA.
DR RefSeq; WP_045362605.1; NZ_BSOD01000001.1.
DR AlphaFoldDB; A0A2Z6EUG6; -.
DR GeneID; 84623527; -.
DR KEGG; mcys:MCB1EB_0900; -.
DR Proteomes; UP000282597; Chromosome.
DR Proteomes; UP001156688; 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; 3.40.50.11140; -; 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; IPR048635; MFD_D3.
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; PF21132; MFD_D3; 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:UP000282597}.
FT DOMAIN 625..786
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 807..961
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1151 AA; 127996 MW; 81D2BBDFB8756FDC CRC64;
MPENITLASS YTPSLVKTGQ RFVFDGASGS SDALALARYF TAHRAQLPLL VVFCAQATDA
QRLQHEIAYF APEARVRLLP DWETLPYDAF SPHQDLVSAR LATLHDISAG HCDIVLVPAT
TALYRMAPPS FMAAYTFKFT QGEPLDIAQL KAQFLLAGYE HVSQVMRPGE YCVRGGLIDL
FPMGSALPYR LDLFDNQIDS IRAFDPDTQR SLYPVPEVKL LPGREFPFDE PARTAFRSRW
RELFDGDPSR VPLYKDIGVG IPSAGIEYYL PLFFDATATL FDYLPPTAHL AFIGDLDTAI
KQFANDTKQR YAFLSHHRER PILEPTRLFI SDEDFFILAK PFARLVLTPS PASQPQRNRW
AEPLPSLSIN RQAGDPVAAL RSWLANPSPR VLIVAESAGR RETILQMLNE HALKPTLLDS
FDAFTQAEAV RFALTTAPLA VGFALPAENL AIVTETELYG GQARRIGRRR QERASDVDAM
VRDLSELKIG EPVVHSQHGI GRYHGLASMD LGEGETEFLH LEYAANSTLY VPVSQLHVIS
RYSGAQPEQA PLHALGSGQW DKAKRKAAQQ IRDTAAELLN LYARRAAREG HVFSLSPNDY
ERFAQSFGFE ETPDQAAAIA AVMADMTSGK PMDRLVCGDV GFGKTEVALR AAFIAVLDGK
QVAILAPTTL LAEQHFQTFS DRFADWPVRI AELSRFKSAQ EITQAINALN DGTVDIVIGT
HKLLSPQINF KQLGLVIIDE EHRFGVRQKE ALKTLRAQVD ILTLTATPIP RTLGMALEGL
RDFSVIATAP QKRLAIKTFV RREDHSTIRE AMLRELKRGG QIYFLHNEVE TIHQRRLMLE
ELMPEARIAV AHGQMHEREL ERVMRDFVAQ RANVLLCTTI IETGIDVPSA NTILMHRADK
FGLAQLHQLR GRVGRSHHQA YAYLLVHDPE ALTKQAARRL EAIQQMEELG SGFYLAMHDL
EIRGTGEVLG DKQSGEIHEI GFQLYTEMLQ DAVNSLKAGK EPDLSAPLAA ATDINLHVPA
LLPADYCGDV QQRLSLYKRL ASCATDDQID AIHEELIDRF GALPAPAQAL IETHRLRLVA
KALGIVKIDV SESAITLLFG PNPSVNPAAI IALVQKHRHI KLVGQDKLRI ETQAQDLSAR
LTTLRVTLRM L
//
