ID Q884J1_PSESM Unreviewed; 1150 AA.
AC Q884J1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 151.
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:AAO55619.1};
GN OrderedLocusNames=PSPTO_2101 {ECO:0000313|EMBL:AAO55619.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO55619.1, ECO:0000313|Proteomes:UP000002515};
RN [1] {ECO:0000313|EMBL:AAO55619.1, ECO:0000313|Proteomes:UP000002515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO55619.1; -; Genomic_DNA.
DR RefSeq; NP_791924.1; NC_004578.1.
DR RefSeq; WP_011103850.1; NC_004578.1.
DR AlphaFoldDB; Q884J1; -.
DR STRING; 223283.PSPTO_2101; -.
DR GeneID; 1183748; -.
DR KEGG; pst:PSPTO_2101; -.
DR PATRIC; fig|223283.9.peg.2132; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_0_3_6; -.
DR OrthoDB; 9804325at2; -.
DR PhylomeDB; Q884J1; -.
DR Proteomes; UP000002515; 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; 3.40.50.11140; -; 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:UP000002515}.
FT DOMAIN 618..779
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 800..954
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1150 AA; 128854 MW; A9BE46F0E110FBF3 CRC64;
MPVLRLPLLS AAAGKQHWGN LPGAALSLAI AEAASAAKRF TLLLTADSQS AERLEQELKF
FAPTLPVLHF PDWETLPYDL FSPHQDIISQ RIASLYRLPE LEHGVLVVPI TTALHRLAPT
KFLLGSSLVL DVGQKLDVNA MRTRLEASGY RYVDTVYEHG EFTVRGALID LFPMGSKLPF
RIDLFDDEIE TLRTFDPDTQ RSIDKVESVR LLPAREFPLQ KEEVTRFKAR FRERFDVDFR
RSPIFQDLSS GITPAGIEYY IPLFFEETST LFDYLPQDTQ VFSLPGIEQA AENFWNDVRN
RYEERRVDPA RPLLPPAELF LPVEDCFARL KNWPRVVASQ QDVDAGAGRE RFPAQALPDL
SIEAKATQPL AALAKFLDDF PGRVLFTAES AGRREVLLEL LERLKLRPKT VDGWLDFVEG
EDRLAITIAP LDEGLLLDQP ALALVAESPL FGQRVMQRRR REKRTDGGNN DAVIKNLTEL
REGAPVVHID HGVGRYLGLA TLEVENQVAE FLMLAYAEDA KLYVPVANLH LIARYTGSDD
EMAPLHRLGS ETWQKAKRKA AEQVRDVAAE LLDIYARRAA REGYAFADPK ADYATFSAGF
PFEETPDQQT TIEAVRADML APRPMDRLVC GDVGFGKTEV AMRAAFIAVH GGRQVAILVP
TTLLAQQHYN SFRDRFADWP VTVEVMSRFK SAKEVSAAVA NLAEGKIDIV IGTHKLLQDD
VKIKNLGLVI IDEEHRFGVR QKEQLKALRS EVDILTLTAT PIPRTLNMAV SGMRDLSIIA
TPPARRLSVR TFVMEQNKPT IKEALLRELL RGGQVYYLHN DVKTIEKCAA DLAELVPEAR
IGIGHGQMRE RDLEQVMSDF YHKRFNVLIA STIIETGIDV PSANTIIIER ADKFGLAQLH
QLRGRVGRSH HQAYAYLLTP PRKQITSDAE KRLEAIANTQ DLGAGFVLAT NDLEIRGAGE
LLGDGQSGQI QAVGFTLYME MLERAVKSIR KGEQPNLDQP LGGGPEINLR VPALIPEAYL
PDVHTRLILY KRIANAADED ALKDLQVEMI DRFGLLPEPT KNLVRITLLK LQAEQLGIKK
VDGGPQGGRI EFATETPVDP LTLIKLIQSQ PNRYKFEGAT LFKFMVPMER PEERFNTIEA
LFERLTPKTA
//
