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REX_THEAQ
ID   REX_THEAQ               Reviewed;         211 AA.
AC   Q9X2V5;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Redox-sensing transcriptional repressor Rex {ECO:0000255|HAMAP-Rule:MF_01131};
GN   Name=rex {ECO:0000255|HAMAP-Rule:MF_01131};
OS   Thermus aquaticus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, AND SUBUNIT.
RC   STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX   PubMed=10076001; DOI=10.1093/nar/27.7.1690;
RA   Du X., Pene J.J.;
RT   "Identification, cloning and expression of p25, an AT-rich DNA-binding
RT   protein from the extreme thermophile, Thermus aquaticus YT-1.";
RL   Nucleic Acids Res. 27:1690-1697(1999).
CC   -!- FUNCTION: Modulates transcription in response to changes in cellular
CC       NADH/NAD(+) redox state. {ECO:0000255|HAMAP-Rule:MF_01131}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01131,
CC       ECO:0000269|PubMed:10076001}.
CC   -!- INTERACTION:
CC       Q9X2V5; Q9X2V5: rex; NbExp=3; IntAct=EBI-15532709, EBI-15532709;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01131}.
CC   -!- SIMILARITY: Belongs to the transcriptional regulatory Rex family.
CC       {ECO:0000255|HAMAP-Rule:MF_01131}.
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DR   EMBL; AF061257; AAD22519.1; -; Genomic_DNA.
DR   PDB; 1XCB; X-ray; 2.90 A; A/B/C/D/E/F/G=1-211.
DR   PDBsum; 1XCB; -.
DR   AlphaFoldDB; Q9X2V5; -.
DR   SMR; Q9X2V5; -.
DR   DIP; DIP-48428N; -.
DR   EvolutionaryTrace; Q9X2V5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0051775; P:response to redox state; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_01131; Rex; 1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009718; Rex_DNA-bd_C_dom.
DR   InterPro; IPR022876; Tscrpt_rep_Rex.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR35786; PTHR35786; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF06971; Put_DNA-bind_N; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding; NAD;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..211
FT                   /note="Redox-sensing transcriptional repressor Rex"
FT                   /id="PRO_0000097925"
FT   DNA_BIND        13..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01131"
FT   BINDING         87..92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01131"
FT   HELIX           5..21
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   TURN            22..25
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           31..38
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           42..50
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   TURN            75..78
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          103..111
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   TURN            115..119
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          143..146
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           150..162
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   TURN            189..192
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   HELIX           193..201
FT                   /evidence="ECO:0007829|PDB:1XCB"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:1XCB"
SQ   SEQUENCE   211 AA;  23222 MW;  A49C2755DDB1D7EC CRC64;
     MKVPEAAISR LITYLRILEE LEAQGVHRTS SEQLGELAQV TAFQVRKDLS YFGSYGTRGV
     GYTVPVLKRE LRHILGLNRK WGLCIVGMGR LGSALADYPG FGESFELRGF FDVDPEKVGR
     PVRGGVIEHV DLLPQRVPGR IEIALLTVPR EAAQKAADLL VAAGIKGILN FAPVVLEVPK
     EVAVENVDFL AGLTRLSFAI LNPKWREEMM G
 
 
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