NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|50363237|ref|NP_001002231|]
View 

kallikrein-2 isoform 2 preproprotein [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-209 1.68e-69

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: 212.14  E-value: 1.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237  25 IVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCL----KKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237 100 LYNMSllkhqslrpdeDSSHDLMLLRLSEPAKITDVVKVLGLPTQ--EPALGTTCYASGWGSIEPEEFLrPRSLQCVSLH 177
Cdd:cd00190  81 NYNPS-----------TYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190
                ....*....|....*....|....*....|....
gi 50363237 178 LLSNDMCARAYS--EKVTEFMLCAGLWTGGKDTC 209
Cdd:cd00190 149 IVSNAECKRAYSygGTITDNMLCAGGLEGGKDAC 182
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-209 1.68e-69

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: 212.14  E-value: 1.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237  25 IVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCL----KKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237 100 LYNMSllkhqslrpdeDSSHDLMLLRLSEPAKITDVVKVLGLPTQ--EPALGTTCYASGWGSIEPEEFLrPRSLQCVSLH 177
Cdd:cd00190  81 NYNPS-----------TYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190
                ....*....|....*....|....*....|....
gi 50363237 178 LLSNDMCARAYS--EKVTEFMLCAGLWTGGKDTC 209
Cdd:cd00190 149 IVSNAECKRAYSygGTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-209 1.92e-69

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: 212.15  E-value: 1.92e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237     24 RIVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCL----KKNSQVWLGRHNLFEPEDtGQRVPVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVrgsdPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237     99 PLYNMSLLkhqslrpdedsSHDLMLLRLSEPAKITDVVKVLGLPT--QEPALGTTCYASGWGSIEPEEFLRPRSLQCVSL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 50363237    177 HLLSNDMCARAYS--EKVTEFMLCAGLWTGGKDTC 209
Cdd:smart00020 149 PIVSNATCRRAYSggGAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
25-209 1.71e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 173.78  E-value: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237    25 IVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCLK--KNSQVWLGRHNLFEPEDTGQRVPVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237   102 NmsllkhqslrpDEDSSHDLMLLRLSEPAKITDVVKVLGLPTQEP--ALGTTCYASGWGSiePEEFLRPRSLQCVSLHLL 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVV 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 50363237   180 SNDMCARAYSEKVTEFMLCAGlwTGGKDTC 209
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAG--AGGKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-209 2.87e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 138.63  E-value: 2.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237   4 LVLSIALSVGCTgAVPLIQSRIVGGWECEKHSQPWQVAVYSHGWA---HCGGVLVHPQWVLTAAHCLKKNS----QVWLG 76
Cdd:COG5640  11 AAAALALALAAA-PAADAAPAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGpsdlRVVIG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237  77 RHNLFepEDTGQRVPVSHSFPHPLYNmsllkhqslrpDEDSSHDLMLLRLSEPAKITDVVKVLGlPTQEPALGTTCYASG 156
Cdd:COG5640  90 STDLS--TSGGTVVKVARIVVHPDYD-----------PATPGNDIALLKLATPVPGVAPAPLAT-SADAAAPGTPATVAG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 50363237 157 WGSIEPEEFLRPRSLQCVSLHLLSNDMCArAYSEKVTEFMLCAGLWTGGKDTC 209
Cdd:COG5640 156 WGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDAC 207
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-209 1.68e-69

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: 212.14  E-value: 1.68e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237  25 IVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCL----KKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHfCGGSLISPRWVLTAAHCVyssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237 100 LYNMSllkhqslrpdeDSSHDLMLLRLSEPAKITDVVKVLGLPTQ--EPALGTTCYASGWGSIEPEEFLrPRSLQCVSLH 177
Cdd:cd00190  81 NYNPS-----------TYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190
                ....*....|....*....|....*....|....
gi 50363237 178 LLSNDMCARAYS--EKVTEFMLCAGLWTGGKDTC 209
Cdd:cd00190 149 IVSNAECKRAYSygGTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-209 1.92e-69

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: 212.15  E-value: 1.92e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237     24 RIVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCL----KKNSQVWLGRHNLFEPEDtGQRVPVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHfCGGSLISPRWVLTAAHCVrgsdPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237     99 PLYNMSLLkhqslrpdedsSHDLMLLRLSEPAKITDVVKVLGLPT--QEPALGTTCYASGWGSIEPEEFLRPRSLQCVSL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 50363237    177 HLLSNDMCARAYS--EKVTEFMLCAGLWTGGKDTC 209
Cdd:smart00020 149 PIVSNATCRRAYSggGAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
25-209 1.71e-54

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 173.78  E-value: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237    25 IVGGWECEKHSQPWQVAVYSHGWAH-CGGVLVHPQWVLTAAHCLK--KNSQVWLGRHNLFEPEDTGQRVPVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237   102 NmsllkhqslrpDEDSSHDLMLLRLSEPAKITDVVKVLGLPTQEP--ALGTTCYASGWGSiePEEFLRPRSLQCVSLHLL 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVV 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 50363237   180 SNDMCARAYSEKVTEFMLCAGlwTGGKDTC 209
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAG--AGGKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-209 2.87e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 138.63  E-value: 2.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237   4 LVLSIALSVGCTgAVPLIQSRIVGGWECEKHSQPWQVAVYSHGWA---HCGGVLVHPQWVLTAAHCLKKNS----QVWLG 76
Cdd:COG5640  11 AAAALALALAAA-PAADAAPAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGDGpsdlRVVIG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237  77 RHNLFepEDTGQRVPVSHSFPHPLYNmsllkhqslrpDEDSSHDLMLLRLSEPAKITDVVKVLGlPTQEPALGTTCYASG 156
Cdd:COG5640  90 STDLS--TSGGTVVKVARIVVHPDYD-----------PATPGNDIALLKLATPVPGVAPAPLAT-SADAAAPGTPATVAG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 50363237 157 WGSIEPEEFLRPRSLQCVSLHLLSNDMCArAYSEKVTEFMLCAGLWTGGKDTC 209
Cdd:COG5640 156 WGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDAC 207
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
46-163 2.08e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.29  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237  46 GWAHCGGVLVHPQWVLTAAHCLK--------KNSQVWLGRHNLFEPEDTGQRVPVshsfphplynmsllkHQSLRPDEDS 117
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVYdgagggwaTNIVFVPGYNGGPYGTATATRFRV---------------PPGWVASGDA 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 50363237 118 SHDLMLLRLSEPakITDVVKVLGL-PTQEPALGTTCYASGWGSIEPE 163
Cdd:COG3591  75 GYDYALLRLDEP--LGDTTGWLGLaFNDAPLAGEPVTIIGYPGDRPK 119
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
52-159 2.63e-04

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 39.71  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50363237    52 GVLVHPQ-WVLTAAHCLKKNSQVWLGRHNLFEPEDTGQRVPVSHSfphplynmsllkhqslrpdeDSSHDLMLLRLSEPA 130
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR--------------------DPDLDLALLRVSGDG 62
                          90       100
                  ....*....|....*....|....*....
gi 50363237   131 KITDVVKvLGlPTQEPALGTTCYASGWGS 159
Cdd:pfam13365  63 RGLPPLP-LG-DSEPLVGGERVYAVGYPL 89
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH