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REX_THET2
ID   REX_THET2               Reviewed;         211 AA.
AC   Q72I39;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Redox-sensing transcriptional repressor Rex {ECO:0000255|HAMAP-Rule:MF_01131};
GN   Name=rex {ECO:0000255|HAMAP-Rule:MF_01131}; OrderedLocusNames=TT_C1293;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
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   -!- 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; AE017221; AAS81635.1; -; Genomic_DNA.
DR   RefSeq; WP_011173693.1; NC_005835.1.
DR   PDB; 3IKT; X-ray; 2.26 A; A/B=1-206.
DR   PDB; 3IKV; X-ray; 2.40 A; A/B=1-206.
DR   PDB; 3IL2; X-ray; 2.49 A; A/B=1-206.
DR   PDBsum; 3IKT; -.
DR   PDBsum; 3IKV; -.
DR   PDBsum; 3IL2; -.
DR   AlphaFoldDB; Q72I39; -.
DR   SMR; Q72I39; -.
DR   STRING; 262724.TT_C1293; -.
DR   EnsemblBacteria; AAS81635; AAS81635; TT_C1293.
DR   GeneID; 3168513; -.
DR   KEGG; tth:TT_C1293; -.
DR   eggNOG; COG2344; Bacteria.
DR   HOGENOM; CLU_061534_1_0_0; -.
DR   OMA; HEQRKAG; -.
DR   OrthoDB; 1872374at2; -.
DR   EvolutionaryTrace; Q72I39; -.
DR   Proteomes; UP000000592; Chromosome.
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: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; DNA-binding; NAD; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..211
FT                   /note="Redox-sensing transcriptional repressor Rex"
FT                   /id="PRO_1000065428"
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..24
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           31..38
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           42..50
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:3IKV"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:3IKV"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   TURN            115..119
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   STRAND          125..129
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           130..135
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   STRAND          143..146
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           153..162
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   HELIX           189..201
FT                   /evidence="ECO:0007829|PDB:3IKT"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:3IKT"
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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