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Conserved domains on  [gi|749111179|gb|AJE76317|]
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acrosin, partial [Apomys sierrae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 21-45 2.67e-07

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


The actual alignment was detected with superfamily member smart00020:

Pssm-ID: 473915  Cd Length: 229  Bit Score: 44.21  E-value: 2.67e-07
                           10        20
                   ....*....|....*....|....*
gi 749111179    21 RIVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR 25
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 21-45 2.67e-07

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 44.21  E-value: 2.67e-07
                           10        20
                   ....*....|....*....|....*
gi 749111179    21 RIVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR 25
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 22-45 4.72e-06

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 40.72  E-value: 4.72e-06
                         10        20
                 ....*....|....*....|....
gi 749111179  22 IVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGR 24
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 21-47 8.80e-06

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 40.02  E-value: 8.80e-06
                         10        20
                 ....*....|....*....|....*..
gi 749111179  21 RIVGGQTAQPGAWPWMVSLQIFTSHNS 47
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNGPSG 56
Trypsin pfam00089
Trypsin;
22-45 5.37e-05

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 37.81  E-value: 5.37e-05
                          10        20
                  ....*....|....*....|....
gi 749111179   22 IVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK 24
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 21-45 2.67e-07

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 44.21  E-value: 2.67e-07
                           10        20
                   ....*....|....*....|....*
gi 749111179    21 RIVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR 25
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 22-45 4.72e-06

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 40.72  E-value: 4.72e-06
                         10        20
                 ....*....|....*....|....
gi 749111179  22 IVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGR 24
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 21-47 8.80e-06

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 40.02  E-value: 8.80e-06
                         10        20
                 ....*....|....*....|....*..
gi 749111179  21 RIVGGQTAQPGAWPWMVSLQIFTSHNS 47
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNGPSG 56
Trypsin pfam00089
Trypsin;
22-45 5.37e-05

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 37.81  E-value: 5.37e-05
                          10        20
                  ....*....|....*....|....
gi 749111179   22 IVGGQTAQPGAWPWMVSLQIFTSH 45
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK 24
 
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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