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Conserved domains on  [gi|45766933|gb|AAH26350|]
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Selenoprotein T [Homo sapiens]

Protein Classification

SelT/SelW/SelH family protein( domain architecture ID 10020357)

SelT/SelW/SelH family protein is a selenoprotein that possesses a thioredoxin-like fold and a conserved CXXC or CxxU (U is selenocysteine) motif near the N terminus, suggesting a redox function

CATH:  3.40.30.10
Gene Ontology:  GO:0016020
PubMed:  17503775|1400197|22479358
SCOP:  4002953

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
 41-179 2.57e-19

selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam.


:

Pssm-ID: 274013  Cd Length: 73  Bit Score: 77.71  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45766933    41 LKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPqpiyrhiasflsvfklvligliivgkdpfaffgmqapsiwqw 120
Cdd:TIGR02174   1 VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEGENTPP------------------------------------------ 38

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45766933   121 gqenkvyacmmvfflsnmienqcmSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDN 179
Cdd:TIGR02174  39 ------------------------TTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
 
Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
 41-179 2.57e-19

selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam.


Pssm-ID: 274013  Cd Length: 73  Bit Score: 77.71  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45766933    41 LKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPqpiyrhiasflsvfklvligliivgkdpfaffgmqapsiwqw 120
Cdd:TIGR02174   1 VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEGENTPP------------------------------------------ 38

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45766933   121 gqenkvyacmmvfflsnmienqcmSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDN 179
Cdd:TIGR02174  39 ------------------------TTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
Rdx pfam10262
Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved ...
 41-179 9.00e-11

Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved from plants to humans. The protein binds to UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which is known to be involved in the quality control of protein folding. Selenium (Se) plays an essential role in cell survival and most of the effects of Se are probably mediated by selenoproteins, including selenoprotein T. However, despite its binding to UGTR and that its mRNA is up-regulated in extended asphyxia, the function of the protein and hence of this region of it is unknown. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium.


Pssm-ID: 463032  Cd Length: 74  Bit Score: 55.61  E-value: 9.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45766933    41 LKFQICVSUGYRRVFEEYMRVISQRYPDIRIEgenylpqpiyrhiasflsvfklvligliivgkdpfaffgmqapsiwqw 120
Cdd:pfam10262   2 VTIEYCTQCGWLLRAAWLAQELLSTFPDELGE------------------------------------------------ 33

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45766933   121 gqenkvyacmmvfflsnmIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDN 179
Cdd:pfam10262  34 ------------------VALIPGTGGAFEVTLDGELVWSRKEDGGFPEPKELKQLVRD 74
COG3526 COG3526
Predicted selenoprotein, Rdx family [General function prediction only];
147-188 4.23e-03

Predicted selenoprotein, Rdx family [General function prediction only];


Pssm-ID: 442748  Cd Length: 93  Bit Score: 35.18  E-value: 4.23e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 45766933 147 GAFEITLNDVPVWSKLESGHLPSMQQLVQ----ILDNEMKLNvHMD 188
Cdd:COG3526  46 GVFEVRVDGELIWDRKEDGGFPEAKELKQrvrdRIAPERDLG-HSD 90
 
Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
 41-179 2.57e-19

selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and animals, including animal proteins SelT, SelW, and SelH, all of which are selenoproteins. In a CXXC motif near the N-terminus of the domain, selenocysteine may replace the second Cys. Proteins with this domain may include an insert of about 70 amino acids. This model is broader than the current SelW model pfam05169 in Pfam.


Pssm-ID: 274013  Cd Length: 73  Bit Score: 77.71  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45766933    41 LKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPqpiyrhiasflsvfklvligliivgkdpfaffgmqapsiwqw 120
Cdd:TIGR02174   1 VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEGENTPP------------------------------------------ 38

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45766933   121 gqenkvyacmmvfflsnmienqcmSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDN 179
Cdd:TIGR02174  39 ------------------------TTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
Rdx pfam10262
Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved ...
 41-179 9.00e-11

Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved from plants to humans. The protein binds to UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which is known to be involved in the quality control of protein folding. Selenium (Se) plays an essential role in cell survival and most of the effects of Se are probably mediated by selenoproteins, including selenoprotein T. However, despite its binding to UGTR and that its mRNA is up-regulated in extended asphyxia, the function of the protein and hence of this region of it is unknown. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium.


Pssm-ID: 463032  Cd Length: 74  Bit Score: 55.61  E-value: 9.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45766933    41 LKFQICVSUGYRRVFEEYMRVISQRYPDIRIEgenylpqpiyrhiasflsvfklvligliivgkdpfaffgmqapsiwqw 120
Cdd:pfam10262   2 VTIEYCTQCGWLLRAAWLAQELLSTFPDELGE------------------------------------------------ 33

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45766933   121 gqenkvyacmmvfflsnmIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDN 179
Cdd:pfam10262  34 ------------------VALIPGTGGAFEVTLDGELVWSRKEDGGFPEPKELKQLVRD 74
COG3526 COG3526
Predicted selenoprotein, Rdx family [General function prediction only];
147-188 4.23e-03

Predicted selenoprotein, Rdx family [General function prediction only];


Pssm-ID: 442748  Cd Length: 93  Bit Score: 35.18  E-value: 4.23e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 45766933 147 GAFEITLNDVPVWSKLESGHLPSMQQLVQ----ILDNEMKLNvHMD 188
Cdd:COG3526  46 GVFEVRVDGELIWDRKEDGGFPEAKELKQrvrdRIAPERDLG-HSD 90
 
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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