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Conserved domains on  [gi|743718720|ref|XP_010953104|]
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granzyme H-like isoform X3 [Camelus bactrianus]

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 ...
14-208 3.86e-73

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: 221.00  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  14 RCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHPDYNPKDHSSDIMLLQLQRKAKQTAA 89
Cdd:cd00190   26 FCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  90 VRPLRLPGGRARVKPGQACGVAGWGQVAVGVP-ATTLQEAVLTVQEDRVCESLFP-GYYSRATQICVGDPSTVKTSFKGD 167
Cdd:cd00190  106 VRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRAYSyGGTITDNMLCAGGLEGGKDACQGD 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 743718720 168 SGGPLVCK----NLVQGIFSCGKQNGTP--PGVFTKVSHFLPWIKRT 208
Cdd:cd00190  186 SGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
14-208 3.86e-73

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: 221.00  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  14 RCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHPDYNPKDHSSDIMLLQLQRKAKQTAA 89
Cdd:cd00190   26 FCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  90 VRPLRLPGGRARVKPGQACGVAGWGQVAVGVP-ATTLQEAVLTVQEDRVCESLFP-GYYSRATQICVGDPSTVKTSFKGD 167
Cdd:cd00190  106 VRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRAYSyGGTITDNMLCAGGLEGGKDACQGD 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 743718720 168 SGGPLVCK----NLVQGIFSCGKQNGTP--PGVFTKVSHFLPWIKRT 208
Cdd:cd00190  186 SGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-205 4.21e-70

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: 213.31  E-value: 4.21e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720     1 MAFVQFLDQERmrRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGtQQVVPVRRAIPHPDYNPKDHSSDIM 76
Cdd:smart00020  16 QVSLQYGGGRH--FCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHPNYNPSTYDNDIA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720    77 LLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VGVPATTLQEAVLTVQEDRVCESLFPGYYS-RATQIC 153
Cdd:smart00020  93 LLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCRRAYSGGGAiTDNMLC 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 743718720   154 VGDPSTVKTSFKGDSGGPLVCKNL---VQGIFSCGKQNGTP--PGVFTKVSHFLPWI 205
Cdd:smart00020 173 AGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-205 1.68e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.12  E-value: 1.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720    1 MAFVQFldQERMRRCGGVLVQKDFVLTAAHC--RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHPDYNPKDHSSDIMLL 78
Cdd:pfam00089  15 QVSLQL--SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720   79 QLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVPATTLQEAVLTVQEDRVCESLFPGYYSRaTQICVGdpS 158
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTD-TMICAG--A 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 743718720  159 TVKTSFKGDSGGPLVCKN-LVQGIFSCGKQNGTP--PGVFTKVSHFLPWI 205
Cdd:pfam00089 170 GGKDACQGDSGGPLVCSDgELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-212 2.17e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 159.04  E-value: 2.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720   1 MAFVQFLDQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGtqQVVPVRRAIPHPDYNPKDHSSDIM 76
Cdd:COG5640   45 MVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  77 LLQLqrkAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VGVPATTLQEAVLTVQEDRVCESlFPGYYSrATQICV 154
Cdd:COG5640  123 LLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSegPGSQSGTLRKADVPVVSDATCAA-YGGFDG-GTMLCA 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743718720 155 GDPSTVKTSFKGDSGGPLVCKN-----LVqGIFSCGKQNGTP--PGVFTKVSHFLPWIKRTMKRL 212
Cdd:COG5640  198 GYPEGGKDACQGDSGGPLVVKDgggwvLV-GVVSWGGGPCAAgyPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
14-208 3.86e-73

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: 221.00  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  14 RCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHPDYNPKDHSSDIMLLQLQRKAKQTAA 89
Cdd:cd00190   26 FCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  90 VRPLRLPGGRARVKPGQACGVAGWGQVAVGVP-ATTLQEAVLTVQEDRVCESLFP-GYYSRATQICVGDPSTVKTSFKGD 167
Cdd:cd00190  106 VRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRAYSyGGTITDNMLCAGGLEGGKDACQGD 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 743718720 168 SGGPLVCK----NLVQGIFSCGKQNGTP--PGVFTKVSHFLPWIKRT 208
Cdd:cd00190  186 SGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-205 4.21e-70

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: 213.31  E-value: 4.21e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720     1 MAFVQFLDQERmrRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGtQQVVPVRRAIPHPDYNPKDHSSDIM 76
Cdd:smart00020  16 QVSLQYGGGRH--FCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHPNYNPSTYDNDIA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720    77 LLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VGVPATTLQEAVLTVQEDRVCESLFPGYYS-RATQIC 153
Cdd:smart00020  93 LLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCRRAYSGGGAiTDNMLC 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 743718720   154 VGDPSTVKTSFKGDSGGPLVCKNL---VQGIFSCGKQNGTP--PGVFTKVSHFLPWI 205
Cdd:smart00020 173 AGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-205 1.68e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.12  E-value: 1.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720    1 MAFVQFldQERMRRCGGVLVQKDFVLTAAHC--RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHPDYNPKDHSSDIMLL 78
Cdd:pfam00089  15 QVSLQL--SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720   79 QLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVPATTLQEAVLTVQEDRVCESLFPGYYSRaTQICVGdpS 158
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTD-TMICAG--A 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 743718720  159 TVKTSFKGDSGGPLVCKN-LVQGIFSCGKQNGTP--PGVFTKVSHFLPWI 205
Cdd:pfam00089 170 GGKDACQGDSGGPLVCSDgELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-212 2.17e-48

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 159.04  E-value: 2.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720   1 MAFVQFLDQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGtqQVVPVRRAIPHPDYNPKDHSSDIM 76
Cdd:COG5640   45 MVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG--TVVKVARIVVHPDYDPATPGNDIA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  77 LLQLqrkAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VGVPATTLQEAVLTVQEDRVCESlFPGYYSrATQICV 154
Cdd:COG5640  123 LLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSegPGSQSGTLRKADVPVVSDATCAA-YGGFDG-GTMLCA 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743718720 155 GDPSTVKTSFKGDSGGPLVCKN-----LVqGIFSCGKQNGTP--PGVFTKVSHFLPWIKRTMKRL 212
Cdd:COG5640  198 GYPEGGKDACQGDSGGPLVVKDgggwvLV-GVVSWGGGPCAAgyPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
14-172 4.04e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 39.66  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  14 RCGGVLVQKDFVLTAAHC--------RGSSINVTLGAHNikkqeGTQQVVPVRRAIPHPDY-NPKDHSSDIMLLQLQRKA 84
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720  85 kqTAAVRPLRLpGGRARVKPGQACGVAGWGQVAVGVPATTLQEAVLTVQEDRVceslfpgYYSratqiCVGDPstvktsf 164
Cdd:COG3591   88 --GDTTGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGNRL-------SYD-----CDTTG------- 145

                 ....*...
gi 743718720 165 kGDSGGPL 172
Cdd:COG3591  146 -GSSGSPV 152
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
17-173 1.94e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.40  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720   17 GVLVQKD-FVLTAAHCRGSSINVTLGAHNIKKQEGTQQVVPVRRAiphpdynpkDHSSDIMLLQLqrkAKQTAAVRPLRL 95
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR---------DPDLDLALLRV---SGDGRGLPPLPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718720   96 pGGRARVKPGQACgvagwgqVAVGVPattLQEAVLTVQEDRVCEslfpgyySRATQICVGDPSTVKTS---FKGDSGGPL 172
Cdd:pfam13365  71 -GDSEPLVGGERV-------YAVGYP---LGGEKLSLSEGIVSG-------VDEGRDGGDDGRVIQTDaalSPGSSGGPV 132

                  .
gi 743718720  173 V 173
Cdd:pfam13365 133 F 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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