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Conserved domains on  [gi|643038352|gb|AIA95808|]
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trehalase, partial [uncultured Saccharomyces]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trehalase super family cl17346
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
 2-95 1.21e-21

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


The actual alignment was detected with superfamily member pfam01204:

Pssm-ID: 418443 [Multi-domain]  Cd Length: 509  Bit Score: 87.39  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643038352    2 FLDEARLNEnpVDRLTRLISTQFWKSLTRRIDDKSIALFAKDTKI-PSNPRVYI-PYDCPDQFEYytQAAKAQPDLKLDV 79
Cdd:pfam01204   9 FVDEARLNE--PNRILRLIRAQFWRALTRRIDGEDLRAFVEDYFDePGDELPRIvPYDEKEQPEF--LQKIEDPDLRLWV 84

                          90
                  ....*....|....*.
gi 643038352   80 EYLPKDITPEYCSINQ 95
Cdd:pfam01204  85 EELNALWPALVRKINK 100
 
Name Accession Description Interval E-value
Trehalase pfam01204
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
 2-95 1.21e-21

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


Pssm-ID: 395961 [Multi-domain]  Cd Length: 509  Bit Score: 87.39  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643038352    2 FLDEARLNEnpVDRLTRLISTQFWKSLTRRIDDKSIALFAKDTKI-PSNPRVYI-PYDCPDQFEYytQAAKAQPDLKLDV 79
Cdd:pfam01204   9 FVDEARLNE--PNRILRLIRAQFWRALTRRIDGEDLRAFVEDYFDePGDELPRIvPYDEKEQPEF--LQKIEDPDLRLWV 84

                          90
                  ....*....|....*.
gi 643038352   80 EYLPKDITPEYCSINQ 95
Cdd:pfam01204  85 EELNALWPALVRKINK 100
SR_Res_par cd03767
Serine recombinase (SR) family, Partitioning (par)-Resolvase subfamily, catalytic domain; ...
 3-43 7.99e-03

Serine recombinase (SR) family, Partitioning (par)-Resolvase subfamily, catalytic domain; Serine recombinases catalyze site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme. They are functionally versatile and include resolvases, invertases, integrases, and transposases. This subgroup is composed of proteins similar to the E. coli resolvase found in the par region of the RP4 plasmid, which encodes a highly efficient partitioning system. This protein is part of a complex stabilization system involved in the resolution of plasmid dimers during cell division. Similar to Tn3 and other resolvases, members of this family may contain a C-terminal DNA binding domain.


Pssm-ID: 239736 [Multi-domain]  Cd Length: 146  Bit Score: 33.45  E-value: 7.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 643038352   3 LDEARLNE----NPVDRLTRLiSTQFWKSLTRRIDDKSIALFAKD 43
Cdd:cd03767   54 LDDAQSGDvllvEQIDRLSRL-PLDDWETLKASIAAKGLRVVSLD 97
 
Name Accession Description Interval E-value
Trehalase pfam01204
Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a ...
 2-95 1.21e-21

Trehalase; Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.


Pssm-ID: 395961 [Multi-domain]  Cd Length: 509  Bit Score: 87.39  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643038352    2 FLDEARLNEnpVDRLTRLISTQFWKSLTRRIDDKSIALFAKDTKI-PSNPRVYI-PYDCPDQFEYytQAAKAQPDLKLDV 79
Cdd:pfam01204   9 FVDEARLNE--PNRILRLIRAQFWRALTRRIDGEDLRAFVEDYFDePGDELPRIvPYDEKEQPEF--LQKIEDPDLRLWV 84

                          90
                  ....*....|....*.
gi 643038352   80 EYLPKDITPEYCSINQ 95
Cdd:pfam01204  85 EELNALWPALVRKINK 100
SR_Res_par cd03767
Serine recombinase (SR) family, Partitioning (par)-Resolvase subfamily, catalytic domain; ...
 3-43 7.99e-03

Serine recombinase (SR) family, Partitioning (par)-Resolvase subfamily, catalytic domain; Serine recombinases catalyze site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and the enzyme. They are functionally versatile and include resolvases, invertases, integrases, and transposases. This subgroup is composed of proteins similar to the E. coli resolvase found in the par region of the RP4 plasmid, which encodes a highly efficient partitioning system. This protein is part of a complex stabilization system involved in the resolution of plasmid dimers during cell division. Similar to Tn3 and other resolvases, members of this family may contain a C-terminal DNA binding domain.


Pssm-ID: 239736 [Multi-domain]  Cd Length: 146  Bit Score: 33.45  E-value: 7.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 643038352   3 LDEARLNE----NPVDRLTRLiSTQFWKSLTRRIDDKSIALFAKD 43
Cdd:cd03767   54 LDDAQSGDvllvEQIDRLSRL-PLDDWETLKASIAAKGLRVVSLD 97
 
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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