(data stored in SCRATCH zone)

SWISSPROT: D6XV49_BACIE

ID   D6XV49_BACIE            Unreviewed;      1186 AA.
AC   D6XV49;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 71.
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=Bsel_0056 {ECO:0000313|EMBL:ADH97607.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97607.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97607.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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       ECO:0000256|SAAS:SAAS01144535}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase
CC       family. 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; CP001791; ADH97607.1; -; Genomic_DNA.
DR   RefSeq; WP_013171037.1; NC_014219.1.
DR   STRING; 439292.Bsel_0056; -.
DR   EnsemblBacteria; ADH97607; ADH97607; Bsel_0056.
DR   KEGG; bse:Bsel_0056; -.
DR   eggNOG; ENOG4108JA2; Bacteria.
DR   eggNOG; COG1197; LUCA.
DR   HOGENOM; HOG000216591; -.
DR   KO; K03723; -.
DR   OMA; LDIPRVN; -.
DR   OrthoDB; 234717at2; -.
DR   BioCyc; BSEL439292:G1GLR-63-MONOMER; -.
DR   Proteomes; UP000000271; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd00079; HELICc; 1.
DR   Gene3D; 2.30.30.840; -; 1.
DR   Gene3D; 3.90.1150.50; -; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR036101; CarD-like/TRCF_dom_sf.
DR   InterPro; IPR003711; CarD-like/TRCF_domain.
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; IPR037235; TRCF-like_C.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   Pfam; PF02559; CarD_CdnL_TRCF; 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; SSF141259; 1.
DR   SUPFAM; SSF143517; SSF143517; 1.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   TIGRFAMs; TIGR00580; mfd; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XV49.
DR   SWISS-2DPAGE; D6XV49.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144540}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144521};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144538};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144510};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00969};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969,
KW   ECO:0000256|SAAS:SAAS01144519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN      638    799       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      824    974       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   COILED      237    260       {ECO:0000256|SAM:Coils}.
FT   COILED      622    642       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1186 AA;  134284 MW;  DBB06E9BEFC67795 CRC64;
     MEGLLNSLSA AGELEKVIKG IEDGAGDQSL VGISGSARAM HLAALFRRTG KSQLIVTHNL
     FQAQKLYDDL ITVLNTDDVL LYPANELISS EIAVASPEMR GQRLEVMNEW STGAKRIVIA
     PVAGVRRLLS PPDLWQEQRL TFTVGEDVDF DRTLGQFVNM GYSRADMVSA PGEFSVRGGI
     IDVYPLTEEY PVRIELFDTE VDSIRLFDVE TQRSVDERST VVAGPAREII VQDVQYIRAA
     ERLDEQLAKS LKRLKDDQIK ETMINNVGEE IESLKNRQFF DAIYKYMTLL YERPATLFDY
     MPDDTLVVLD EWARVQETAA TLEREEAEWM TMMIAQGAMV HDLSVSATLE HLVSETERQK
     LYIMLFGRQI PKVGPDRTYN VQTKTMQQFH GQIHLLKTEV ERWKEAGYAI VFVSGDDERA
     EKLERVLADY EIEASPAKAG SEPVKGKALI VQGLLHNGFE LPLQRIVVIA EEDVFTRKSR
     KPKRRQKLSN AERIKNYSEL KTGDWVVHIN HGIGKYLGIE TLQVGDVHKD YLHISYAGND
     KLYVPVDQID QVQKYVANED KDPKLYSLGG SEWKKVKKKV QSSVQDIADD LIKLYAERQE
     TKGFAFSPDG LEQREFESTF PYQETDDQLQ AIEEIKKDME QDRPMDRLLC GDVGYGKTEV
     ALRAAFKAIM DGKQVAILVP TTILAQQHYE TIRERFQDFA INIGMLSRFR TRKQMKETTE
     ALRKGTCDIV VGTHRILSKD VAFKELGLLV VDEEQRFGVT HKEKIKQLKA NVDVLTLTAT
     PIPRTLHMSM LGVRDLSVIE TPPENRFPVQ TYVVEHNDAF VREAIERELA REGQVFYLYN
     RVEDIEMVAD RIGMMVPDAN IAFAHGRMTE AQLEAVMLDF LSGETDVLVT TTIIETGVDI
     PNVNTLIIQE ADRMGLSQLY QLRGRVGRSN RVAYAYFTHQ QDKVLTEVAE RRLQSIKEFT
     ELGSGFKIAM RDLSIRGAGN LLGAEQHGFI ASVGFDLYSQ MLKEAIDDRK AGMDGKEEAE
     AQPSQAPDID LDIQVDAYIP ESYIYDSKQK IDMYKRFKAI ESFDDVEDLQ VELIDRFGDF
     PDEVVRLFSV AKIRLYAKQE GVTSIAEKNK ECKVVLEEEA AAKIDGAKLF SLVNKLSSHI
     TLSSDGKGIT IHIKTKQIDD NLYLRLLEEV LARLDEVEKS RVTQGG
//

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