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Conserved domains on  [gi|119592333|gb|EAW71927|]
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kallikrein 3, (prostate specific antigen), isoform CRA_f [Homo sapiens]

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

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 ...
 25-90 1.03e-22

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 cd00190:

Pssm-ID: 473915 [Multi-domain]  Cd Length: 232  Bit Score: 86.95  E-value: 1.03e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119592333  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQAR 90
Cdd:cd00190    1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVI 71
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 25-90 1.03e-22

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: 86.95  E-value: 1.03e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119592333  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQAR 90
Cdd:cd00190    1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVI 71
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 24-86 1.60e-21

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: 83.88  E-value: 1.60e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119592333    24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDT 86
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEEG 68
Trypsin pfam00089
Trypsin;
25-88 1.12e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 73.63  E-value: 1.12e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119592333   25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRNKS--VILLGRHSLFHPEDTGQ 88
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQ 67
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 23-90 1.24e-11

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 58.12  E-value: 1.24e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119592333  23 SRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFhpEDTGQAR 90
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVIGSTDLS--TSGGTVV 101
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 25-90 1.03e-22

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: 86.95  E-value: 1.03e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119592333  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQAR 90
Cdd:cd00190    1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVI 71
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 24-86 1.60e-21

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: 83.88  E-value: 1.60e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119592333    24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDT 86
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEEG 68
Trypsin pfam00089
Trypsin;
25-88 1.12e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 73.63  E-value: 1.12e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119592333   25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRNKS--VILLGRHSLFHPEDTGQ 88
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQ 67
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 23-90 1.24e-11

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 58.12  E-value: 1.24e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119592333  23 SRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFhpEDTGQAR 90
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVIGSTDLS--TSGGTVV 101
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 41-71 7.18e-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: 7.18e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 119592333  41 LVASRGRAVCGGVLVHPQWVLTAAHCIRNKS 71
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGA 35
 
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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