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Conserved domains on  [gi|15529990|ref|NP_219491|]
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granzyme H isoform 1 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

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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 ...
21-242 5.19e-91

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: 267.99  E-value: 5.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  21 IIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERTQQFIPVKRPIP 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  97 HPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS-MSTLATTLQEVLLTVQKDCQCERL 175
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15529990 176 F-HGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKD----VAQGILSYGNKKGTP--PGVYIKVSHFLPWIKRT 242
Cdd:cd00190 159 YsYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 5.19e-91

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: 267.99  E-value: 5.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  21 IIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERTQQFIPVKRPIP 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  97 HPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS-MSTLATTLQEVLLTVQKDCQCERL 175
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15529990 176 F-HGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKD----VAQGILSYGNKKGTP--PGVYIKVSHFLPWIKRT 242
Cdd:cd00190 159 YsYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 8.21e-84

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: 249.52  E-value: 8.21e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990     20 EIIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERtQQFIPVKRPI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY--GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990     96 PHPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS--MSTLATTLQEVLLTVQKDCQCE 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15529990    174 RLFHGNYS-RATEICVGDPKKTQTGFKGDSGGPLVCKD---VAQGILSYGNKKGTP--PGVYIKVSHFLPWI 239
Cdd:smart00020 158 RAYSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 7.42e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 221.16  E-value: 7.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990    21 IIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC--QGSSINVTLGAHNIKEQERTQQFIPVKRPIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990    99 AYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVSMSTLATTLQEVLLTVQKDCQCERlFHG 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS-AYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15529990   179 NYSRATEICVGDPKKTQtgFKGDSGGPLVCKDV-AQGILSYGNKKGTP--PGVYIKVSHFLPWI 239
Cdd:pfam00089 158 GTVTDTMICAGAGGKDA--CQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-246 1.46e-53

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 173.68  E-value: 1.46e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  13 TPGAGTEEIIGGHEAKPHSRPYMAFVQFLQEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERTQqf 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGGTV-- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  89 IPVKRPIPHPAYNPKNFSNDIMLLQLERKAkwtTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS--MSTLATTLQEVLLTV 166
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSegPGSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990 167 QKDCQCERlfHGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKDVAQ----GILSYGNKKGTP--PGVYIKVSHFLPWIK 240
Cdd:COG5640 178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGwvlvGVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                ....*.
gi 15529990 241 RTMKRL 246
Cdd:COG5640 256 STAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 5.19e-91

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: 267.99  E-value: 5.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  21 IIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERTQQFIPVKRPIP 96
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  97 HPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS-MSTLATTLQEVLLTVQKDCQCERL 175
Cdd:cd00190  79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15529990 176 F-HGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKD----VAQGILSYGNKKGTP--PGVYIKVSHFLPWIKRT 242
Cdd:cd00190 159 YsYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 8.21e-84

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: 249.52  E-value: 8.21e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990     20 EIIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERtQQFIPVKRPI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY--GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990     96 PHPAYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS--MSTLATTLQEVLLTVQKDCQCE 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15529990    174 RLFHGNYS-RATEICVGDPKKTQTGFKGDSGGPLVCKD---VAQGILSYGNKKGTP--PGVYIKVSHFLPWI 239
Cdd:smart00020 158 RAYSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 7.42e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 221.16  E-value: 7.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990    21 IIGGHEAKPHSRPYMAFVQFlqEKSRKRCGGILVRKDFVLTAAHC--QGSSINVTLGAHNIKEQERTQQFIPVKRPIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990    99 AYNPKNFSNDIMLLQLERKAKWTTAVRPLRLPSSKAQVKPGQLCSVAGWGYVSMSTLATTLQEVLLTVQKDCQCERlFHG 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS-AYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15529990   179 NYSRATEICVGDPKKTQtgFKGDSGGPLVCKDV-AQGILSYGNKKGTP--PGVYIKVSHFLPWI 239
Cdd:pfam00089 158 GTVTDTMICAGAGGKDA--CQGDSGGPLVCSDGeLIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-246 1.46e-53

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 173.68  E-value: 1.46e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  13 TPGAGTEEIIGGHEAKPHSRPYMAFVQFLQEKSRKRCGGILVRKDFVLTAAHC----QGSSINVTLGAHNIKEQERTQqf 88
Cdd:COG5640  23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGGTV-- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  89 IPVKRPIPHPAYNPKNFSNDIMLLQLERKAkwtTAVRPLRLPSSKAQVKPGQLCSVAGWGYVS--MSTLATTLQEVLLTV 166
Cdd:COG5640 101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSegPGSQSGTLRKADVPV 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990 167 QKDCQCERlfHGNYSRATEICVGDPKKTQTGFKGDSGGPLVCKDVAQ----GILSYGNKKGTP--PGVYIKVSHFLPWIK 240
Cdd:COG5640 178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGwvlvGVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                ....*.
gi 15529990 241 RTMKRL 246
Cdd:COG5640 256 STAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
36-245 1.36e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 44.67  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990  36 AFVQFLQEKSRKRCGGILVRKDFVLTAAHC--------QGSSINVTLGAHNikeqeRTQQFIPVKRPIPHPAY-NPKNFS 106
Cdd:COG3591   1 AVGRLETDGGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15529990 107 NDIMLLQLERKAkwTTAVRPLRLPSSkAQVKPGQLCSVAGWGYVSMSTlattlqevlLTVQKDCQC-----ERLFHGnys 181
Cdd:COG3591  76 YDYALLRLDEPL--GDTTGWLGLAFN-DAPLAGEPVTIIGYPGDRPKD---------LSLDCSGRVtgvqgNRLSYD--- 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15529990 182 rateiCVGDPkktqtgfkGDSGGPLVCKDVAQ----GILSYGNKKGTPPGVYIkVSHFLPWIKRTMKR 245
Cdd:COG3591 141 -----CDTTG--------GSSGSPVLDDSDGGgrvvGVHSAGGADRANTGVRL-TSAIVAALRAWASA 194
 
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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