(data stored in SCRATCH zone)

SWISSPROT: A5FTV2_ACICJ

ID   A5FTV2_ACICJ            Unreviewed;       311 AA.
AC   A5FTV2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   SubName: Full=Transcriptional regulator, LysR family {ECO:0000313|EMBL:ABQ29034.1};
DE            EC=4.2.1.1 {ECO:0000313|EMBL:ABQ29034.1};
GN   OrderedLocusNames=Acry_3428 {ECO:0000313|EMBL:ABQ29034.1};
OS   Acidiphilium cryptum (strain JF-5).
OG   Plasmid pACRY02 {ECO:0000313|EMBL:ABQ29034.1,
OG   ECO:0000313|Proteomes:UP000000245}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ29034.1, ECO:0000313|Proteomes:UP000000245};
RN   [1] {ECO:0000313|EMBL:ABQ29034.1, ECO:0000313|Proteomes:UP000000245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5 {ECO:0000313|EMBL:ABQ29034.1,
RC   ECO:0000313|Proteomes:UP000000245};
RC   PLASMID=Plasmid pACRY02 {ECO:0000313|Proteomes:UP000000245};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of plasmid2 pACRY02 of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000690; ABQ29034.1; -; Genomic_DNA.
DR   RefSeq; WP_011930620.1; NC_009468.1.
DR   ProteinModelPortal; A5FTV2; -.
DR   EnsemblBacteria; ABQ29034; ABQ29034; Acry_3428.
DR   KEGG; acr:Acry_3428; -.
DR   HOGENOM; HOG000233519; -.
DR   OMA; GIAWLPC; -.
DR   OrthoDB; POG091H057E; -.
DR   Proteomes; UP000000245; Plasmid pACRY02.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   4: Predicted;
DR   PRODOM; A5FTV2.
DR   SWISS-2DPAGE; A5FTV2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000245};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00253,
KW   ECO:0000256|SAAS:SAAS00661574}; Lyase {ECO:0000313|EMBL:ABQ29034.1};
KW   Plasmid {ECO:0000313|EMBL:ABQ29034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW   Transcription {ECO:0000256|PROSITE-ProRule:PRU00253,
KW   ECO:0000256|SAAS:SAAS00661597};
KW   Transcription regulation {ECO:0000256|PROSITE-ProRule:PRU00253,
KW   ECO:0000256|SAAS:SAAS00661673}.
FT   DOMAIN       13     70       HTH lysR-type DNA-binding.
FT                                {ECO:0000259|PROSITE:PS50931}.
FT   DNA_BIND     30     49       H-T-H motif. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00253}.
SQ   SEQUENCE   311 AA;  33996 MW;  88BD5286AA00317A CRC64;
     MNDYPNYWNN RVPSLSDYET FVAIVEAGSL TAASRRMNRS LQSVSRALAN IERDTGANLV
     RRTTRSMQPT DAGLVFYGRI KEALSDIAAA HTEAAELTRE IAGTLRIGSS TLFGPTYVVP
     TIAAFMRRHP AVAIQLVLED SFQDLLKAEL DLAIRIGELS DSRAMATRVG ALRRVAFAAP
     EYLLKHGRPK VPGDLRAHCC VIRTLTKSPQ RWTFESAGKP ETIPVAACFS SDNAGACNEA
     VAEAVGIGIA PLWQIAGMLE TGRVELILTE YEPPPTPVHV VWPQASLLPT RTRAFIDFLA
     ARLRSGLRAL R
//

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