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Conserved domains on  [gi|499245618|ref|WP_010943158|]
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sulfurtransferase-like selenium metabolism protein YedF [Geobacter sulfurreducens]

Protein Classification

sulfurtransferase-like selenium metabolism protein YedF( domain architecture ID 11497016)

sulfurtransferase-like selenium metabolism protein YedF may function in detoxification or have a role in labile selenoprotein biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
selenium_YedF TIGR03527
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ...
 4-195 3.05e-97

selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis.


:

Pssm-ID: 274630 [Multi-domain]  Cd Length: 194  Bit Score: 279.89  E-value: 3.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499245618    4 IDCRNMACPAPVVTTKRALEEAGGETV-RVLVDAGAPRENVARFAANRGFRVAVEEADGGFA-ITIGSGEGAPSAPAENP 81
Cdd:TIGR03527   1 IDARGLACPQPVILTKKALDELGEEGVlTVIVDNEAAKENVSKFATSLGYEVEVEEKEEGYWiLIIKKGEGAAEASPDEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499245618   82 ARQGRTVMLITSDRLGDGPEDLGRLLMKSFIITLLDQESLPDRMMFLNSGVLLTTEGSEVLQALEQLGNRGVEVLSCGVC 161
Cdd:TIGR03527  81 AKEGKLVVVITSDKLGEGDEELGRILMKGFIYTLSELDPLPKRIIFVNGGVKLTTEGSEVLEDLKELEKKGVEILSCGTC 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 499245618  162 LDFFHCKEKLAAGTVTNMFTTAEALLTAGSVIRL 195
Cdd:TIGR03527 161 LDFYGLKDKLKVGTITNMYDIVEALTTADKVIRL 194
 
Name Accession Description Interval E-value
selenium_YedF TIGR03527
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ...
 4-195 3.05e-97

selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis.


Pssm-ID: 274630 [Multi-domain]  Cd Length: 194  Bit Score: 279.89  E-value: 3.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499245618    4 IDCRNMACPAPVVTTKRALEEAGGETV-RVLVDAGAPRENVARFAANRGFRVAVEEADGGFA-ITIGSGEGAPSAPAENP 81
Cdd:TIGR03527   1 IDARGLACPQPVILTKKALDELGEEGVlTVIVDNEAAKENVSKFATSLGYEVEVEEKEEGYWiLIIKKGEGAAEASPDEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499245618   82 ARQGRTVMLITSDRLGDGPEDLGRLLMKSFIITLLDQESLPDRMMFLNSGVLLTTEGSEVLQALEQLGNRGVEVLSCGVC 161
Cdd:TIGR03527  81 AKEGKLVVVITSDKLGEGDEELGRILMKGFIYTLSELDPLPKRIIFVNGGVKLTTEGSEVLEDLKELEKKGVEILSCGTC 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 499245618  162 LDFFHCKEKLAAGTVTNMFTTAEALLTAGSVIRL 195
Cdd:TIGR03527 161 LDFYGLKDKLKVGTITNMYDIVEALTTADKVIRL 194
SirA_like_N cd03421
SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, ...
 3-67 5.87e-28

SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, YedF, YeeD protein family is present in bacteria as well as archaea. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.


Pssm-ID: 239513  Cd Length: 67  Bit Score: 99.97  E-value: 5.87e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499245618   3 TIDCRNMACPAPVVTTKRALEEAGGETVRVLVDAGAPRENVARFAANRGFRVAVEEADGGFAITI 67
Cdd:cd03421    1 TIDARGLACPQPVIKTKKALELEAGGEIEVLVDNEVAKENVSRFAESRGYEVSVEEKGGEFEITI 65
TusA COG0425
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ...
 4-67 3.22e-17

Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440194  Cd Length: 70  Bit Score: 72.15  E-value: 3.22e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499245618   4 IDCRNMACPAPVVTTKRALEE-AGGETVRVLVDAGAPRENVARFAANRGFRV-AVEEADGGFAITI 67
Cdd:COG0425    1 LDARGLSCPLPVLKTKKALEElKPGEVLEVLADDPGAVEDIPAWCRETGHELlSVEEEGGVYRILI 66
TusA pfam01206
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.
 3-63 4.84e-16

Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.


Pssm-ID: 426125  Cd Length: 64  Bit Score: 69.14  E-value: 4.84e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499245618    3 TIDCRNMACPAPVVTTKRALEEAG-GETVRVLVDAGAPRENVARFAANRGFRV-AVEEADGGF 63
Cdd:pfam01206   1 TLDLRGLACPMPLLKTKKALKKLKpGEVLEVLADDPGAVEDIPRWAKETGHEVlEVEEEDGEY 63
 
Name Accession Description Interval E-value
selenium_YedF TIGR03527
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ...
 4-195 3.05e-97

selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis.


Pssm-ID: 274630 [Multi-domain]  Cd Length: 194  Bit Score: 279.89  E-value: 3.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499245618    4 IDCRNMACPAPVVTTKRALEEAGGETV-RVLVDAGAPRENVARFAANRGFRVAVEEADGGFA-ITIGSGEGAPSAPAENP 81
Cdd:TIGR03527   1 IDARGLACPQPVILTKKALDELGEEGVlTVIVDNEAAKENVSKFATSLGYEVEVEEKEEGYWiLIIKKGEGAAEASPDEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499245618   82 ARQGRTVMLITSDRLGDGPEDLGRLLMKSFIITLLDQESLPDRMMFLNSGVLLTTEGSEVLQALEQLGNRGVEVLSCGVC 161
Cdd:TIGR03527  81 AKEGKLVVVITSDKLGEGDEELGRILMKGFIYTLSELDPLPKRIIFVNGGVKLTTEGSEVLEDLKELEKKGVEILSCGTC 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 499245618  162 LDFFHCKEKLAAGTVTNMFTTAEALLTAGSVIRL 195
Cdd:TIGR03527 161 LDFYGLKDKLKVGTITNMYDIVEALTTADKVIRL 194
SirA_like_N cd03421
SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, ...
 3-67 5.87e-28

SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, YedF, YeeD protein family is present in bacteria as well as archaea. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.


Pssm-ID: 239513  Cd Length: 67  Bit Score: 99.97  E-value: 5.87e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499245618   3 TIDCRNMACPAPVVTTKRALEEAGGETVRVLVDAGAPRENVARFAANRGFRVAVEEADGGFAITI 67
Cdd:cd03421    1 TIDARGLACPQPVIKTKKALELEAGGEIEVLVDNEVAKENVSRFAESRGYEVSVEEKGGEFEITI 65
SirA_YedF_YeeD cd00291
SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and ...
 3-67 2.34e-17

SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.


Pssm-ID: 238180  Cd Length: 69  Bit Score: 72.59  E-value: 2.34e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499245618   3 TIDCRNMACPAPVVTTKRALEE-AGGETVRVLVDAGAPRENVARFAANRGFRV-AVEEADGGFAITI 67
Cdd:cd00291    1 TLDLRGLPCPLPVLKTKKALEKlKSGEVLEVLLDDPGAVEDIPAWAKETGHEVlEVEEEGGVYRILI 67
TusA COG0425
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ...
 4-67 3.22e-17

Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440194  Cd Length: 70  Bit Score: 72.15  E-value: 3.22e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499245618   4 IDCRNMACPAPVVTTKRALEE-AGGETVRVLVDAGAPRENVARFAANRGFRV-AVEEADGGFAITI 67
Cdd:COG0425    1 LDARGLSCPLPVLKTKKALEElKPGEVLEVLADDPGAVEDIPAWCRETGHELlSVEEEGGVYRILI 66
TusA pfam01206
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.
 3-63 4.84e-16

Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.


Pssm-ID: 426125  Cd Length: 64  Bit Score: 69.14  E-value: 4.84e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499245618    3 TIDCRNMACPAPVVTTKRALEEAG-GETVRVLVDAGAPRENVARFAANRGFRV-AVEEADGGF 63
Cdd:pfam01206   1 TLDLRGLACPMPLLKTKKALKKLKpGEVLEVLADDPGAVEDIPRWAKETGHEVlEVEEEDGEY 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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