GenomeNet

Database: UniProt
Entry: D3EMV7_ATETH
LinkDB: D3EMV7_ATETH
Original site: D3EMV7_ATETH 
ID   D3EMV7_ATETH            Unreviewed;      1151 AA.
AC   D3EMV7;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=UCYN_00510 {ECO:0000313|EMBL:ADB94807.1};
OS   Atelocyanobacterium thalassa (isolate ALOHA).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Atelocyanobacterium;
OC   Candidatus Atelocyanobacterium thalassa.
OX   NCBI_TaxID=1453429 {ECO:0000313|Proteomes:UP000001405};
RN   [1] {ECO:0000313|EMBL:ADB94807.1, ECO:0000313|Proteomes:UP000001405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALOHA {ECO:0000313|Proteomes:UP000001405};
RX   PubMed=20173737; DOI=10.1038/nature08786;
RA   Tripp H.J., Bench S.R., Turk K.A., Foster R.A., Desany B.A., Niazi F.,
RA   Affourtit J.P., Zehr J.P.;
RT   "Metabolic streamlining in an open-ocean nitrogen-fixing cyanobacterium.";
RL   Nature 464:90-94(2010).
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   ---------------------------------------------------------------------------
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; CP001842; ADB94807.1; -; Genomic_DNA.
DR   RefSeq; WP_012953472.1; NC_013771.1.
DR   AlphaFoldDB; D3EMV7; -.
DR   STRING; 1453429.UCYN_00510; -.
DR   KEGG; cyu:UCYN_00510; -.
DR   PATRIC; fig|713887.8.peg.42; -.
DR   HOGENOM; CLU_005122_1_0_3; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000001405; 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; 3.40.50.11180; -; 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; 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; 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; 3.
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:UP000001405}.
FT   DOMAIN          621..783
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          803..958
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1151 AA;  131192 MW;  0650FC09C083BA25 CRC64;
     MVFSSLIHTL QSSSLIKNLS QQLKVKNELR LQGINRLSKG LISSVISQTN YQNLLVICAT
     SEEAGRWTKQ LEIMGWKDIN FYFVPDTSPY EELNIENEII WTQMQVLSNL FRAKQSKDTN
     FAIVTTERSL QPHLPSPSIF YDYCLNFKVG VTVYSKDFAQ TLSELGYKKV NLVEKEGEWS
     RRGDILDIFP VSSEIPIRLE WLGDELEKIR EFDISTQRSL NEIEEALLTP INFNIIAKDI
     IQKNPFSSEQ YVVEEKPKTL KNSSPKDQLP LSKSSSLFDY LPSDTLCAFD EIDQCKSHNH
     KWLEYVEKSW HETQNKEPKV HRSFEESFSS IEEMPKLYLS ELSDVNETDS IDILSRSIPV
     NPHQFSKLAE ILRGKREIFN EINISKYSIW LISAQPSRTV TLLQEHDYSA QFIPNIRDYP
     AIKKSHAQGM AVALKHSGLV GLEGFILPIF RIAVITDKEF FGQSTLGSSE FFKKRRRSNA
     KKVNLQKLNS GDHVVHKSHG IGKFLRLENL SNREYLVVQY SDGVLRVPAD SLDNLLRYSC
     TDSTPPKLHK MTGKDWGKLK QKIRKNIKKL AFNLLHLYAE RAQKKGYSYP ADSLWQQELE
     DSFPYQATPD QVQAIREVKI DLESNRPMDR LICGDVGFGK TEVAIRAIFK VVTSGHKQVV
     FLAPTTILTQ QHYNTLRTRF APYPISIGLL NRFRTTSEKK DIIERLTTGE LDIVVGTQQL
     LGKNIKFKDL GLLVIDEEQR FGVNHKEKIR TIKANVDVLT LTATPIPRTL HMSLSGIREM
     SLISTPPPSR RSIKTHLSSY DPNLVKAAVR AELDRGGQVF YVVPRIEHID ELVLQLKRMI
     PDAKILVAHG QMDVNNLELT MLSFNNGDAD ILVCTTIIES GLDIPKVNTI IIEDAQKFGL
     SQLYQLRGRV GRSGIQAHAW LFYPSRSELT DNALKRLNAL QEFSELGSGY HLATRDLEIR
     GAGNLLGAEQ SGQMEAIGFE LYMDMLQEAI KEVQGEKIPE VEDTQIDLKL TAFIPNDYIA
     DIEQKIIAYR TVAVASSKKE LDLIVAEWSE RYGSIPDPVK QLLKTIELKQ LSKSLGFSHI
     KIEGKNSVVL KTPMEEPAWI ILQNKLPEHL QTRFVYNSKK IIIRGLGSLS PQKQLESLLV
     WFKIMQENEK V
//
DBGET integrated database retrieval system