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Conserved domains on  [gi|966954355|ref|XP_014998955|]
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granzyme H isoform X1 [Macaca mulatta]

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

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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 1.84e-90

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: 266.45  E-value: 1.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  21 IIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCLGSS----INVTLGAHNIKEQERTQQIIPVKRAIP 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  97 HPAYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVS-TGTLATTLQEVLLTVQKDWECERL 175
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966954355 176 FHANYS-KATEICVGDPKTTKTGFKGDSGGPLVCKR----VAQGIFSHGRINGTP--PGVYMKVSHFLPWIKRT 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 1.84e-90

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: 266.45  E-value: 1.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  21 IIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCLGSS----INVTLGAHNIKEQERTQQIIPVKRAIP 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  97 HPAYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVS-TGTLATTLQEVLLTVQKDWECERL 175
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966954355 176 FHANYS-KATEICVGDPKTTKTGFKGDSGGPLVCKR----VAQGIFSHGRINGTP--PGVYMKVSHFLPWIKRT 242
Cdd:cd00190  159 YSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 1.37e-85

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: 254.14  E-value: 1.37e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355    20 EIIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCLG----SSINVTLGAHNIKEQERtQQIIPVKRAI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY--GGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355    96 PHPAYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVS--TGTLATTLQEVLLTVQKDWECE 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966954355   174 RLFHANYS-KATEICVGDPKTTKTGFKGDSGGPLVCK---RVAQGIFSHGRINGTP--PGVYMKVSHFLPWI 239
Cdd:smart00020 158 RAYSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 2.64e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.00  E-value: 2.64e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355   21 IIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCL--GSSINVTLGAHNIKEQERTQQIIPVKRAIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355   99 AYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVSTGTLATTLQEVLLTVQKDWECERlFHA 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS-AYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966954355  179 NYSKATEICVGDpkTTKTGFKGDSGGPLVC-KRVAQGIFSHGRINGTP--PGVYMKVSHFLPWI 239
Cdd:pfam00089 158 GTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-243 5.17e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 179.85  E-value: 5.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  13 TPGAGTEEIIGGHEAKPHSRPYMAFVQFLDEKSKKRCGGILVRKDFVLTAAHCL----GSSINVTLGAHNIKEQERtqQI 88
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  89 IPVKRAIPHPAYNPKNFSNDIMLLQLERKAkrtTAVQPLRLPSSKVQVKPGQVCSVAGWGRVST--GTLATTLQEVLLTV 166
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEgpGSQSGTLRKADVPV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355 167 QKDWECERlfHANYSKATEICVGDPKTTKTGFKGDSGGPLVCKRVAQGI------FSHGRINGTPPGVYMKVSHFLPWIK 240
Cdd:COG5640  178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVlvgvvsWGGGPCAAGYPGVYTRVSAYRDWIK 255

                 ...
gi 966954355 241 RTM 243
Cdd:COG5640  256 STA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-242 1.84e-90

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: 266.45  E-value: 1.84e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  21 IIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCLGSS----INVTLGAHNIKEQERTQQIIPVKRAIP 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  97 HPAYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVS-TGTLATTLQEVLLTVQKDWECERL 175
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966954355 176 FHANYS-KATEICVGDPKTTKTGFKGDSGGPLVCKR----VAQGIFSHGRINGTP--PGVYMKVSHFLPWIKRT 242
Cdd:cd00190  159 YSYGGTiTDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-239 1.37e-85

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: 254.14  E-value: 1.37e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355    20 EIIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCLG----SSINVTLGAHNIKEQERtQQIIPVKRAI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY--GGGRHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355    96 PHPAYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVS--TGTLATTLQEVLLTVQKDWECE 173
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966954355   174 RLFHANYS-KATEICVGDPKTTKTGFKGDSGGPLVCK---RVAQGIFSHGRINGTP--PGVYMKVSHFLPWI 239
Cdd:smart00020 158 RAYSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-239 2.64e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.00  E-value: 2.64e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355   21 IIGGHEAKPHSRPYMAFVQFldEKSKKRCGGILVRKDFVLTAAHCL--GSSINVTLGAHNIKEQERTQQIIPVKRAIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355   99 AYNPKNFSNDIMLLQLERKAKRTTAVQPLRLPSSKVQVKPGQVCSVAGWGRVSTGTLATTLQEVLLTVQKDWECERlFHA 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS-AYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966954355  179 NYSKATEICVGDpkTTKTGFKGDSGGPLVC-KRVAQGIFSHGRINGTP--PGVYMKVSHFLPWI 239
Cdd:pfam00089 158 GTVTDTMICAGA--GGKDACQGDSGGPLVCsDGELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
13-243 5.17e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 179.85  E-value: 5.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  13 TPGAGTEEIIGGHEAKPHSRPYMAFVQFLDEKSKKRCGGILVRKDFVLTAAHCL----GSSINVTLGAHNIKEQERtqQI 88
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCVdgdgPSDLRVVIGSTDLSTSGG--TV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  89 IPVKRAIPHPAYNPKNFSNDIMLLQLERKAkrtTAVQPLRLPSSKVQVKPGQVCSVAGWGRVST--GTLATTLQEVLLTV 166
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEgpGSQSGTLRKADVPV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355 167 QKDWECERlfHANYSKATEICVGDPKTTKTGFKGDSGGPLVCKRVAQGI------FSHGRINGTPPGVYMKVSHFLPWIK 240
Cdd:COG5640  178 VSDATCAA--YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVlvgvvsWGGGPCAAGYPGVYTRVSAYRDWIK 255

                 ...
gi 966954355 241 RTM 243
Cdd:COG5640  256 STA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
36-243 6.87e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 42.36  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  36 AFVQFLDEKSKKRCGGILVRKDFVLTAAHCLGS--------SINVTLGAHNikeqeRTQQIIPVKRAIPHPAY-NPKNFS 106
Cdd:COG3591    1 AVGRLETDGGGGVCTGTLIGPNLVLTAGHCVYDgagggwatNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355 107 NDIMLLQLERKAKRTTAVQPLRLPSSKVqvkPGQVCSVAGWGRVSTGTLATTLQEVLLTVQKDweceRLFHAnyskatei 186
Cdd:COG3591   76 YDYALLRLDEPLGDTTGWLGLAFNDAPL---AGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGN----RLSYD-------- 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966954355 187 CVGDPkttktgfkGDSGGPLV----CKRVAQGIFSHGRINGTPPGVYMkVSHFLPWIKRTM 243
Cdd:COG3591  141 CDTTG--------GSSGSPVLddsdGGGRVVGVHSAGGADRANTGVRL-TSAIVAALRAWA 192
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
51-207 4.82e-04

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 39.33  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355   51 GILVRKD-FVLTAAHCLGSSINVTLGAhnIKEQERTQQIIPVKRAIPHPAYnpknfsnDIMLLQLErkaKRTTAVQPLRL 129
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVEL--VSVVLADGREYPATVVARDPDL-------DLALLRVS---GDGRGLPPLPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966954355  130 pSSKVQVKPGQVCSVAGWGR------VSTGTLATtlqevLLTVQKDWECERLFHANYSkateicvgdpkttktGFKGDSG 203
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGYPLggeklsLSEGIVSG-----VDEGRDGGDDGRVIQTDAA---------------LSPGSSG 129

                  ....
gi 966954355  204 GPLV 207
Cdd:pfam13365 130 GPVF 133
 
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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