GenomeNet

Database: UniProt
Entry: J3IW69_9PSED
LinkDB: J3IW69_9PSED
Original site: J3IW69_9PSED 
ID   J3IW69_9PSED            Unreviewed;      1058 AA.
AC   J3IW69;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=PMI38_02441 {ECO:0000313|EMBL:EJN38103.1};
OS   Pseudomonas sp. GM84.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1144340 {ECO:0000313|EMBL:EJN38103.1, ECO:0000313|Proteomes:UP000007504};
RN   [1] {ECO:0000313|EMBL:EJN38103.1, ECO:0000313|Proteomes:UP000007504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM84 {ECO:0000313|EMBL:EJN38103.1,
RC   ECO:0000313|Proteomes:UP000007504};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJN38103.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AKJC01000133; EJN38103.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3IW69; -.
DR   PATRIC; fig|1144340.3.peg.2302; -.
DR   Proteomes; UP000007504; 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}.
FT   DOMAIN          526..687
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          708..862
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1058 AA;  118320 MW;  AEFE008687C95732 CRC64;
     MPSLYRLPEL SHGILVVPIT TALHRLAPTR FLLGSSLVLD VGQTIDVEQM RTRLEASGYR
     CVDTVYEHGE FAVRGALIDL FPMGSKLPYR IDLFDDEIET LRTFDPETQR SIDKVDSIRL
     LPAREFPMQK EEVTRFKARF RERFDVDFRR SAIFQDLASG IIPAGIEYYL PLFFEETSTL
     FDYLPSDTQV FSLPGVEQAA EHFWNDVRGR YEDRRGDLTR PLLPPAELFL PVEDCFAQLK
     QWPRVVVSAD EVEPGAGRER FPARALPNLA IEAKANQPLA ALSEFLDQFP GRVLFTAESA
     GRREVLLELL ERLKLRPQTV EGWTDFITGK ERLAITIAPL DEGLLLEDPG LALVAESPLF
     GQRVMQRRRR DKRGEAANDA VIKNLTELRE GAPVVHIDHG VGRYLGLATL EIEGQAAEFL
     TLEYAEGAKL YVPVANLHLI ARYTGSDDAL APLHRLGSEA WQKAKRKAAE QVRDVAAELL
     DIYARRAARK GYAFADPAAD YATFSAGFPF EETPDQQNAI EAVRADMLAA KPMDRLVCGD
     VGFGKTEVAM RAAFIAVHSG RQVAVLVPTT LLAQQHYNSF RDRFADWPVT VEVMSRFKSA
     KEVAAAAADL AEGKIDILIG THKLLQDDVR FKDLGLVVID EEHRFGVRQK EQLKALRSEV
     DILTLTATPI PRTLNMAVAG MRDLSIIATP PARRLSVRTF VMEHNNSTVK EALLRELLRG
     GQVYYLHNDV KTIEKCAADL AELVPEARIG IGHGQMRERE LEQVMSDFYH KRFNVLIAST
     IIETGIDVPS ANTIVIERAD KFGLAQLHQL RGRVGRSHHQ AYAYLLTPAR QKVSSDAEKR
     LEAIANTQDL GAGFVLATND LEIRGAGELL GEGQSGQIQA VGFTLYMEML ERAVKAIRKG
     AQPNLEQPLS GGPEINLRLP ALIPEDYLPD VHARLILYKR IASAADEEGL KDLQVEMIDR
     FGLLPEPTKN LMRLTQLKLQ AEKLGIKKVD AGPNGGKLEF EAETPVDPLT LIKLIQGQPK
     RYKFEGATQF RFLVPMERPD ERFNTLEALF ERLTPQTA
//
DBGET integrated database retrieval system