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Database: UniProt
Entry: A0A0Q7R0D3_9CAUL
LinkDB: A0A0Q7R0D3_9CAUL
Original site: A0A0Q7R0D3_9CAUL 
ID   A0A0Q7R0D3_9CAUL        Unreviewed;      1155 AA.
AC   A0A0Q7R0D3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=ASD25_15065 {ECO:0000313|EMBL:KQY64938.1};
OS   Brevundimonas sp. Root1423.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY64938.1, ECO:0000313|Proteomes:UP000051815};
RN   [1] {ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY64938.1, ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|EMBL:KQY64938.1,
RC   ECO:0000313|Proteomes:UP000051815};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQY64938.1}.
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DR   EMBL; LMFL01000078; KQY64938.1; -; Genomic_DNA.
DR   RefSeq; WP_056621527.1; NZ_LMFL01000078.1.
DR   AlphaFoldDB; A0A0Q7R0D3; -.
DR   Proteomes; UP000051815; 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:UP000051815}.
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   1155 AA;  126485 MW;  8BE9DF1A18D95990 CRC64;
     MDAAVPKRGD QELGGAPEGL DALTVAERLR AEGGLGVFVA RDYARMGEFV QAFGFFAQDI
     EVIEFPAWDC LPYDRLSPSS SVSAERMAAL TKLAQRQPGD SRPTLVVTTV GAAIQRTPPR
     EVTCGAGFET TVGLDLDTAA LERYFAANGY MRASTVSERG EFAVRGGVID VYPPGFEEPV
     RLDMFGSELE SIRTFDPATQ RSTGQRREVS LAPVSEALLD AESISRFRTG YLSLFGAAGD
     DPLYGAISEG ARRQGMEHWL PLLYDRLETL FDYLPDDAKV FLDNQVEAAR AERWTLTRDA
     YEARRDAAMS RKAGSGGSAY RALPPERLYL DEAEWNTALA GRRVWRMSPF HGAGEDAGGR
     LGRSFAAERA QDSVNLFEAV ARHAEAVKAA GKRVLFASWT EGSSERLAGM LADHGLEHVV
     AVRDWTDVQK APKDIYLRGV LPVEHGFETG DVAVISETDI LGDRLARPRK KRRASNFLAE
     ASALTTGDLV VHLDHGIGRY EGLKTLEIQQ APHDCLELLY AGDSKLYLPV ENIDLLTRYG
     SDSDGAQLDR LGGAGWQARK AKAKARLRDM AEGLIALAAK RSLRSSDPIT PPHGLFDEFC
     ARFPYEETDD QLNAIGDVLE DLGKGTPMDR LICGDVGFGK TEVALRAAFV VAMTGQQVAI
     VCPTTLLARQ HFKTFSERFA GWPVTVRHLS RMVTAKDAAE TRAGLKDGSF EIVVGTHAVL
     SEQVGFKDLG LVIVDEEQHF GVKHKEKLKS LRADVHLLTL TATPIPRTLQ MALSGIREMS
     IIATPPVDRL AVRTYVTPWD PVLVREALLR EKYRGGQAYY VVPRLSDLPD IEKFLREQVP
     EIKFVVGHGQ MSPTQLEDVM SAFYDGSYDL LLSTTIVESG LDVPTANTLI VHKADMFGLA
     QLHQIRGRIG RAKARAFAYL TTPPNKPMSL SSERRLQVLQ SLDNLGAGFQ LASHDLDQRG
     GGNLLGDEQS GHIREVGVEL YQQMLEDAVA ELRQAGEGGG VVDRGWSPAI NVGAAVLIPE
     EYVPDLNVRL SLYRRLSDAE NSETREALAA ELIDRFGPLP DEAKQLLRIV GIKANCKTAC
     IERIDIGPKG AVLTLRNNAF PNPMGLVGLI QKNHAFWKLR PDQKIVVKGE WDTAADRLKV
     AERITADLAR VAGAA
//
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