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Conserved domains on  [gi|743718718|ref|XP_010953103|]
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granzyme H-like isoform X2 [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 ...
25-246 2.09e-83

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: 248.73  E-value: 2.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  25 IIGGHEAKPHSRPYMAFVQFldQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGTQQVVPVRRAIP 100
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718 101 HPDYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVP-ATTLQEAVLTVQEDRVCESL 179
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743718718 180 FP-GYYSRATQICVGDPSTVKTSFKGDSGGPLVCK----NLVQGIFSCGKQNGTP--PGVFTKVSHFLPWIKRT 246
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 ...
25-246 2.09e-83

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: 248.73  E-value: 2.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  25 IIGGHEAKPHSRPYMAFVQFldQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGTQQVVPVRRAIP 100
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718 101 HPDYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVP-ATTLQEAVLTVQEDRVCESL 179
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743718718 180 FP-GYYSRATQICVGDPSTVKTSFKGDSGGPLVCK----NLVQGIFSCGKQNGTP--PGVFTKVSHFLPWIKRT 246
Cdd:cd00190  159 YSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-243 1.39e-80

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: 241.43  E-value: 1.39e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718    24 EIIGGHEAKPHSRPYMAFVQFLDQERmrRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGtQQVVPVRRAI 99
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRH--FCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   100 PHPDYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VGVPATTLQEAVLTVQEDRVCE 177
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743718718   178 SLFPGYYS-RATQICVGDPSTVKTSFKGDSGGPLVCKNL---VQGIFSCGKQNGTP--PGVFTKVSHFLPWI 243
Cdd:smart00020 158 RAYSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
25-243 5.43e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 216.92  E-value: 5.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   25 IIGGHEAKPHSRPYMAFVQFldQERMRRCGGVLVQKDFVLTAAHC--RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHP 102
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  103 DYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVPATTLQEAVLTVQEDRVCESLFPG 182
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743718718  183 YYSRaTQICVGdpSTVKTSFKGDSGGPLVCKN-LVQGIFSCGKQNGTP--PGVFTKVSHFLPWI 243
Cdd:pfam00089 159 TVTD-TMICAG--AGGKDACQGDSGGPLVCSDgELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-250 3.72e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 3.72e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   4 LLLVMAVLLPAGRGQPSLSGEIIGGHEAKPHSRPYMAFVQFLDQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLG 79
Cdd:COG5640   10 LAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  80 AHNIKKQEGtqQVVPVRRAIPHPDYNPKDHSSDIMLLQLqrkAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VG 157
Cdd:COG5640   90 STDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSegPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718 158 VPATTLQEAVLTVQEDRVCESlFPGYYSrATQICVGDPSTVKTSFKGDSGGPLVCKN-----LVqGIFSCGKQNGTP--P 230
Cdd:COG5640  165 SQSGTLRKADVPVVSDATCAA-YGGFDG-GTMLCAGYPEGGKDACQGDSGGPLVVKDgggwvLV-GVVSWGGGPCAAgyP 241
                        250       260
                 ....*....|....*....|
gi 743718718 231 GVFTKVSHFLPWIKRTMKRL 250
Cdd:COG5640  242 GVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-246 2.09e-83

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: 248.73  E-value: 2.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  25 IIGGHEAKPHSRPYMAFVQFldQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGTQQVVPVRRAIP 100
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQY--TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718 101 HPDYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVP-ATTLQEAVLTVQEDRVCESL 179
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743718718 180 FP-GYYSRATQICVGDPSTVKTSFKGDSGGPLVCK----NLVQGIFSCGKQNGTP--PGVFTKVSHFLPWIKRT 246
Cdd:cd00190  159 YSyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-243 1.39e-80

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: 241.43  E-value: 1.39e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718    24 EIIGGHEAKPHSRPYMAFVQFLDQERmrRCGGVLVQKDFVLTAAHC----RGSSINVTLGAHNIKKQEGtQQVVPVRRAI 99
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRH--FCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   100 PHPDYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VGVPATTLQEAVLTVQEDRVCE 177
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSegAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743718718   178 SLFPGYYS-RATQICVGDPSTVKTSFKGDSGGPLVCKNL---VQGIFSCGKQNGTP--PGVFTKVSHFLPWI 243
Cdd:smart00020 158 RAYSGGGAiTDNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
25-243 5.43e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 216.92  E-value: 5.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   25 IIGGHEAKPHSRPYMAFVQFldQERMRRCGGVLVQKDFVLTAAHC--RGSSINVTLGAHNIKKQEGTQQVVPVRRAIPHP 102
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL--SSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  103 DYNPKDHSSDIMLLQLQRKAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVAVGVPATTLQEAVLTVQEDRVCESLFPG 182
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743718718  183 YYSRaTQICVGdpSTVKTSFKGDSGGPLVCKN-LVQGIFSCGKQNGTP--PGVFTKVSHFLPWI 243
Cdd:pfam00089 159 TVTD-TMICAG--AGGKDACQGDSGGPLVCSDgELIGIVSWGYGCASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
4-250 3.72e-56

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 3.72e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   4 LLLVMAVLLPAGRGQPSLSGEIIGGHEAKPHSRPYMAFVQFLDQERMRRCGGVLVQKDFVLTAAHC----RGSSINVTLG 79
Cdd:COG5640   10 LAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  80 AHNIKKQEGtqQVVPVRRAIPHPDYNPKDHSSDIMLLQLqrkAKQTAAVRPLRLPGGRARVKPGQACGVAGWGQVA--VG 157
Cdd:COG5640   90 STDLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSegPG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718 158 VPATTLQEAVLTVQEDRVCESlFPGYYSrATQICVGDPSTVKTSFKGDSGGPLVCKN-----LVqGIFSCGKQNGTP--P 230
Cdd:COG5640  165 SQSGTLRKADVPVVSDATCAA-YGGFDG-GTMLCAGYPEGGKDACQGDSGGPLVVKDgggwvLV-GVVSWGGGPCAAgyP 241
                        250       260
                 ....*....|....*....|
gi 743718718 231 GVFTKVSHFLPWIKRTMKRL 250
Cdd:COG5640  242 GVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
52-210 4.81e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 40.04  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  52 RCGGVLVQKDFVLTAAHC--------RGSSINVTLGAHNikkqeGTQQVVPVRRAIPHPDY-NPKDHSSDIMLLQLQRKA 122
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718 123 kqTAAVRPLRLpGGRARVKPGQACGVAGWGQVAVGVPATTLQEAVLTVQEDRVceslfpgYYSratqiCVGDPstvktsf 202
Cdd:COG3591   88 --GDTTGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGRVTGVQGNRL-------SYD-----CDTTG------- 145

                 ....*...
gi 743718718 203 kGDSGGPL 210
Cdd:COG3591  146 -GSSGSPV 152
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
55-211 2.80e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.02  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718   55 GVLVQKD-FVLTAAHCRGSSINVTLGAHNIKKQEGTQQVVPVRRAiphpdynpkDHSSDIMLLQLqrkAKQTAAVRPLRL 133
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVAR---------DPDLDLALLRV---SGDGRGLPPLPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743718718  134 pGGRARVKPGQACgvagwgqVAVGVPattLQEAVLTVQEDRVCEslfpgyySRATQICVGDPSTVKTS---FKGDSGGPL 210
Cdd:pfam13365  71 -GDSEPLVGGERV-------YAVGYP---LGGEKLSLSEGIVSG-------VDEGRDGGDDGRVIQTDaalSPGSSGGPV 132

                  .
gi 743718718  211 V 211
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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