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Conserved domains on  [gi|50404537|gb|AAT76938|]
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neuropsin type 1, partial [Homo sapiens]

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 ...
 8-50 7.64e-18

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: 72.71  E-value: 7.64e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 50404537      8 KVLGGHECQPHSQPWQAAL-FQGQQLLCGGVLVGGNWVLTAAHC 50
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHC 44
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 8-50 7.64e-18

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: 72.71  E-value: 7.64e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 50404537      8 KVLGGHECQPHSQPWQAAL-FQGQQLLCGGVLVGGNWVLTAAHC 50
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHC 44
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 9-50 2.27e-17

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: 71.54  E-value: 2.27e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 50404537   9 VLGGHECQPHSQPWQAALFQGQ-QLLCGGVLVGGNWVLTAAHC 50
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHC 43
Trypsin pfam00089
Trypsin;
11-50 6.93e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 67.47  E-value: 6.93e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 50404537    11 GGHECQPHSQPWQAAL-FQGQQLLCGGVLVGGNWVLTAAHC 50
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHC 43
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 8-50 2.84e-10

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 52.73  E-value: 2.84e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 50404537   8 KVLGGHECQPHSQPWQAALFQ---GQQLLCGGVLVGGNWVLTAAHC 50
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHC 75
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 8-50 7.64e-18

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: 72.71  E-value: 7.64e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 50404537      8 KVLGGHECQPHSQPWQAAL-FQGQQLLCGGVLVGGNWVLTAAHC 50
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHC 44
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 9-50 2.27e-17

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: 71.54  E-value: 2.27e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 50404537   9 VLGGHECQPHSQPWQAALFQGQ-QLLCGGVLVGGNWVLTAAHC 50
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHC 43
Trypsin pfam00089
Trypsin;
11-50 6.93e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 67.47  E-value: 6.93e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 50404537    11 GGHECQPHSQPWQAAL-FQGQQLLCGGVLVGGNWVLTAAHC 50
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHC 43
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 8-50 2.84e-10

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 52.73  E-value: 2.84e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 50404537   8 KVLGGHECQPHSQPWQAALFQ---GQQLLCGGVLVGGNWVLTAAHC 50
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHC 75
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 33-50 2.02e-04

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 36.19  E-value: 2.02e-04
                        10
                ....*....|....*...
gi 50404537  33 LCGGVLVGGNWVLTAAHC 50
Cdd:COG3591  13 VCTGTLIGPNLVLTAGHC 30
 
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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