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Conserved domains on  [gi|119368636|sp|Q148C8|]
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RecName: Full=Migration and invasion enhancer 1; Flags: Precursor

Protein Classification

CXXU_selWTH family protein (domain architecture ID 10020357)

CXXU_selWTH family protein

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 ...
25-95 3.28e-31

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: 105.44  E-value: 3.28e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119368636   25 IVVEYCEPCGFEATYLELASAVKEQYPGIEIE--SRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIRR 95
Cdd:TIGR02174   1 VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEgeNTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 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 ...
25-95 3.28e-31

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: 105.44  E-value: 3.28e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119368636   25 IVVEYCEPCGFEATYLELASAVKEQYPGIEIE--SRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIRR 95
Cdd:TIGR02174   1 VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEgeNTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
Rdx pfam10262
Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved ...
24-94 3.82e-24

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: 402052  Cd Length: 74  Bit Score: 87.58  E-value: 3.82e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119368636   24 RIVVEYCEPCGFEATYLELASAVKEQYPG--IEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIR 94
Cdd:pfam10262   1 RVTIEYCTQCGWLLRAAWLAQELLQTFPDelGEVALIPGTGGAFEVTLDGELIWSRKEDGGFPEPKELKQRVR 73
COG3526 COG3526
Predicted selenoprotein, Rdx family [Function unknown];
24-94 3.83e-05

Predicted selenoprotein, Rdx family [Function unknown];


Pssm-ID: 226057  Cd Length: 99  Bit Score: 39.47  E-value: 3.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119368636  24 RIVVEYCEPCGF--EATYL--ELASAVKEQYPgiEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIR 94
Cdd:COG3526    7 RIEITYCTQCNWllRAAWMaqELLSTFADDLG--EVALIPGTGGVFEITCDGVLIWERKRDGGFPEAKVLKQRVR 79
 
Name Accession Description Interval E-value
CXXU_selWTH TIGR02174
selT/selW/selH selenoprotein domain; This model represents a domain found in both bacteria and ...
25-95 3.28e-31

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: 105.44  E-value: 3.28e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119368636   25 IVVEYCEPCGFEATYLELASAVKEQYPGIEIE--SRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIRR 95
Cdd:TIGR02174   1 VEVEYCGSCGYKPRAAELKQALLEEFPDLEIEgeNTPPTTGAFEVEVNGQLVWSKLEGGGFPEPEELKQLIRD 73
Rdx pfam10262
Rdx family; This entry is an approximately 100 residue region of selenoprotein-T, conserved ...
24-94 3.82e-24

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: 402052  Cd Length: 74  Bit Score: 87.58  E-value: 3.82e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119368636   24 RIVVEYCEPCGFEATYLELASAVKEQYPG--IEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIR 94
Cdd:pfam10262   1 RVTIEYCTQCGWLLRAAWLAQELLQTFPDelGEVALIPGTGGAFEVTLDGELIWSRKEDGGFPEPKELKQRVR 73
COG3526 COG3526
Predicted selenoprotein, Rdx family [Function unknown];
24-94 3.83e-05

Predicted selenoprotein, Rdx family [Function unknown];


Pssm-ID: 226057  Cd Length: 99  Bit Score: 39.47  E-value: 3.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119368636  24 RIVVEYCEPCGF--EATYL--ELASAVKEQYPgiEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIR 94
Cdd:COG3526    7 RIEITYCTQCNWllRAAWMaqELLSTFADDLG--EVALIPGTGGVFEITCDGVLIWERKRDGGFPEAKVLKQRVR 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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