ID H8L1K6_FRAAD Unreviewed; 1154 AA.
AC H8L1K6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 OrderedLocusNames=Fraau_0897 {ECO:0000313|EMBL:AFC85366.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC85366.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) 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; CP003350; AFC85366.1; -; Genomic_DNA.
DR RefSeq; WP_014402372.1; NC_017033.1.
DR AlphaFoldDB; H8L1K6; -.
DR STRING; 767434.Fraau_0897; -.
DR KEGG; fau:Fraau_0897; -.
DR eggNOG; COG1197; Bacteria.
DR HOGENOM; CLU_005122_1_0_6; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000005234; 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 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:UP000005234}.
FT DOMAIN 621..782
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1154 AA; 128695 MW; D86591138493BA3A CRC64;
MTPRFPTVPL PTSPRHRQFL LRPAGSAEAL LLAQTAAGHK GLLVAVCADT QGAIALESEL
KLFAGDLPVL QFPDWETLPY DVFSPHPDVV SQRIATLYRL PALERGILVV PVATLMQRIA
PASHIRGSGL MLYRGGRLDL VEEQRRLQSV GYRNVPQVSE PGDYAVRGSV LDIYAMGAPE
PYRVELLDDE IESIRRFDPE SQRSQDQIES VELLPAREFP VTEQAARDFR QRLRERFPID
IRRCPVYQDM KEGSTPGGIE YYLPMFFEAT ATLFDYLPAG AIFVLGEEVL ASAERFWTQI
ESRYDQRAHD IERPVLPPAE LYLPVEALRE QLNLRLRIEE VPAGHAHAFD SGSQSAPEVP
LNAKGQESGT ALRQLLQNDP RPLLIAADSA GRREALIEQL AELDLRPHGI DSWAQYLPLW
LDGKAPPLAI TVAPLEQGFS LQQPGLILLT ERELLGERVR TERRRRRGTA RDPEAIIRDL
TELTIGAPIV HVDHGVGQYQ GLLSMDIGGM AGEFLTIEYA KGDKLYVPVA QLGLVSRYSG
TAPELAPLHS LGGDAWERAR KKAAEKVRDV AAELLGIYAQ REARGGQSLE IDRRMVESFG
ASFPFDETPD QEQAIKAVLG DLSAPRAMDR VICGDVGFGK TEVALRAAFA AATAGKQVAV
LVPTTLLAQQ HYRNFADRFA DWPIRVDVLS RFRAKKDVDA ALQRLAEGQI DVIIGTHKLL
QPEIRFKDLG LVVVDEEQRF GVRQKEQLKK LRAEVDLLTM TATPIPRTLN MAMSGLRDLS
LIATPPAHRM AVSTFISTWE PALIREAFQR ELARGGQVYL LHNEVESIER CARDLQELIP
EARIGIAHGQ LPERELEQVM ADFHRQRFNV LVCTTIIETG IDIPTANTII INRADRFGLA
QLHQLRGRVG RSHHRAYAYL IVPDRKTISA DAEKRLEALA SLEELGAGFT LATHDLEIRG
AGELLGDEQS GQIQEIGFGL YTELLERAVR ALKSGKVPDF DLSSEHETEV ELHLPALIPD
DYLPDVHTRL TLYKRIASVR TDAALRELQV EMIDRFGLLP EQARTLFAVA SLKLAATPLG
IRKLEFGPLG GRLQFREKPD VDPMRIIQLV QRQPRIYKLD GQDKLRISME LEDGPARIEA
ARHLLRELGA RIGT
//
