ID A0A0J8YUV3_9GAMM Unreviewed; 1151 AA.
AC A0A0J8YUV3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=AI29_02640 {ECO:0000313|EMBL:KMV73500.1};
OS bacteria symbiont BFo2 of Frankliniella occidentalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX NCBI_TaxID=1628856 {ECO:0000313|EMBL:KMV73500.1, ECO:0000313|Proteomes:UP000036794};
RN [1] {ECO:0000313|EMBL:KMV73500.1, ECO:0000313|Proteomes:UP000036794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFo2 {ECO:0000313|EMBL:KMV73500.1,
RC ECO:0000313|Proteomes:UP000036794};
RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT occidentalis [Pergande]).";
RL Submitted (MAY-2014) 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:KMV73500.1}.
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DR EMBL; JMSP01000154; KMV73500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8YUV3; -.
DR STRING; 1628856.WB67_03150; -.
DR PATRIC; fig|1628856.3.peg.517; -.
DR Proteomes; UP000036794; 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; 3.40.50.11140; -; 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:UP000036794}.
FT DOMAIN 616..777
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 798..952
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1151 AA; 130272 MW; 6CDBF2CA9832248C CRC64;
MMDIQQYSLP SKAGDVRQLG ELVGSAFAIE AARIAEQHDG LVVLIASDMQ NALQLTSEIG
QFTTLNVNTL PDWETLPYDS FSPHQDIISS RLSMLYQLPL MEKGLLILPV NTLMQRVCPH
SFLHSHALVM QRGDKLSRDT LIRQLDQAGY RHVEQVMVHG EYATRGALLD LFPMGSEAPY
RLDFLDDEID SLRSFDADTQ RTLNEVEAIS LLPAHEFPTD KASIERFRTQ WREQFDVLRE
SEHLYQQVSR GTLPAGIEYW QPLFFDEPLP PLFSYFPKQT LLVNTGDLAG SSERFWQDTG
NRYENRRVDP MRPLVEPAAL WLAPDVLFAE LKRWPRIQLF SQALPKKAAN TNLGYTVLPA
LHQPDNQQNP LDPLRALLEA HREDRVIFSV ESQGRRERLQ EMLARIKLRP TSITQFTDAQ
QAGAYLMVGA AEKGFIAAPQ QLIFICENDL LGERVVRRRQ DTRRAINPDV LIRNLAELHP
GQPVVHLDHG VGRYVGMTTL ETGGVTAEYL VLNYANEAKL YIPISSLHLI SRYAGGADEN
APLHKLGSDA WNRARQKAAE KVRDVAAELL DIYAQRAAKT GFAFTQNREH YQQFCESFPY
DTTPDQKQAI SAVISDMCQP LAMDRLVCGD VGFGKTEVAM RAAFLAVENN KQVAVLVPTT
LLAQQHYDNF RDRFADWPVR VEMLSRFRSA KEQSQVLQDA ADGKVDILIG THKLLMSDLQ
WSDLGLLIVD EEHRFGVRHK ERIKAMRADV DILTLTATPI PRTLNIAMSG MRDLSIIATP
PARRLAVKTF VREYDALTVR EAILREILRG GQVYYLYNDV ENINKAAEKL AELVPEARIG
IGHGQMRERE LEKVMNDFHH QRFNVLVCTT IIETGIDIPT ANTIIIERAD HFGLAQLHQL
RGRVGRSHHQ AYAWLLTPHP KAMTTDARKR LEAIASLEDL GAGFALATHD LEIRGAGELL
GDDQSGQMET LGFTLYMELL ENAVESLKAG KEPSLEDLSQ RHTDVELRMP ALIPDEFISD
INTRLSLYKR IASASESAEL NDIKVEMIDR FGLLPDPTRN LLMQTEIRLH AESLGIAKIE
AGEKGGYIEF AEHNNVDPGW LIGLLQQDPK QWKLEGPVKL RFTRDLTERQ SRIDWLMELL
AQMDKHRVKA Q
//