NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|317373361|sp|P10144|]
View 

RecName: Full=Granzyme B; AltName: Full=C11; AltName: Full=CTLA-1; AltName: Full=Cathepsin G-like 1; Short=CTSGL1; AltName: Full=Cytotoxic T-lymphocyte proteinase 2; Short=Lymphocyte protease; AltName: Full=Fragmentin-2; AltName: Full=Granzyme-2; AltName: Full=Human lymphocyte protein; Short=HLP; AltName: Full=SECT; AltName: Full=T-cell serine protease 1-3E; Flags: Precursor

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 ...
21-243 1.05e-95

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: 279.93  E-value: 1.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  21 IIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCWGSS----INVTLGAHNIKEQEPTQQFIPVKRPIP 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHF--CGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  97 HPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESd 176
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317373361 177 lRHYYDSTI---ELCVGDPEIKKTSFKGDSGGPLVCNK----VAQGIVSYGRNNGMP--PRACTKVSSFVHWIKKT 243
Cdd:cd00190  158 -AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
21-243 1.05e-95

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: 279.93  E-value: 1.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  21 IIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCWGSS----INVTLGAHNIKEQEPTQQFIPVKRPIP 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHF--CGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  97 HPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESd 176
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317373361 177 lRHYYDSTI---ELCVGDPEIKKTSFKGDSGGPLVCNK----VAQGIVSYGRNNGMP--PRACTKVSSFVHWIKKT 243
Cdd:cd00190  158 -AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-240 1.16e-88

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: 261.84  E-value: 1.16e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361    20 EIIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCWG----SSINVTLGAHNIKEQEPtQQFIPVKRPI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF--CGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361    96 PHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPL-GKHSHTLQEVKMTVQEDRKCE 174
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317373361   175 SDLRHY-YDSTIELCVGDPEIKKTSFKGDSGGPLVCNK---VAQGIVSYGRNNGMP--PRACTKVSSFVHWI 240
Cdd:smart00020 158 RAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-240 1.85e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.70  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361   21 IIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCW--GSSINVTLGAHNIKEQEPTQQFIPVKRPIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF--CGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361   99 AYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGkHSHTLQEVKMTVQEDRKCESDLR 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373361  179 HYYDSTiELCVGdpEIKKTSFKGDSGGPLVCNKV-AQGIVSYGRN--NGMPPRACTKVSSFVHWI 240
Cdd:pfam00089 158 GTVTDT-MICAG--AGGKDACQGDSGGPLVCSDGeLIGIVSWGYGcaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
14-244 1.19e-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: 1.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  14 PRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHC----WGSSINVTLGAHNIKEQEPTQqfI 89
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGGTV--V 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  90 PVKRPIPHPAYNPKNFSNDIMLLQLERKAKrtrAVQPLRLPSNKAQVKPGQTCSVAGWGQTAP-LGKHSHTLQEVKMTVQ 168
Cdd:COG5640  102 KVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361 169 EDRKCESDLRhyYDSTIELCVGDPEIKKTSFKGDSGGPLV-----CNKVAqGIVSYGRNNGMP--PRACTKVSSFVHWIK 241
Cdd:COG5640  179 SDATCAAYGG--FDGGTMLCAGYPEGGKDACQGDSGGPLVvkdggGWVLV-GVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                 ...
gi 317373361 242 KTM 244
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 ...
21-243 1.05e-95

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: 279.93  E-value: 1.05e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  21 IIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCWGSS----INVTLGAHNIKEQEPTQQFIPVKRPIP 96
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHF--CGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLSSNEGGGQVIKVKKVIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  97 HPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESd 176
Cdd:cd00190   79 HPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317373361 177 lRHYYDSTI---ELCVGDPEIKKTSFKGDSGGPLVCNK----VAQGIVSYGRNNGMP--PRACTKVSSFVHWIKKT 243
Cdd:cd00190  158 -AYSYGGTItdnMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARPnyPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
20-240 1.16e-88

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: 261.84  E-value: 1.16e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361    20 EIIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCWG----SSINVTLGAHNIKEQEPtQQFIPVKRPI 95
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHF--CGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361    96 PHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPL-GKHSHTLQEVKMTVQEDRKCE 174
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317373361   175 SDLRHY-YDSTIELCVGDPEIKKTSFKGDSGGPLVCNK---VAQGIVSYGRNNGMP--PRACTKVSSFVHWI 240
Cdd:smart00020 158 RAYSGGgAITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGCARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
21-240 1.85e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.70  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361   21 IIGGHEAKPHSRPYMAYLMIWDQKSLkrCGGFLIRDDFVLTAAHCW--GSSINVTLGAHNIKEQEPTQQFIPVKRPIPHP 98
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHF--CGGSLISENWVLTAAHCVsgASDVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361   99 AYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGkHSHTLQEVKMTVQEDRKCESDLR 178
Cdd:pfam00089  79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAYG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317373361  179 HYYDSTiELCVGdpEIKKTSFKGDSGGPLVCNKV-AQGIVSYGRN--NGMPPRACTKVSSFVHWI 240
Cdd:pfam00089 158 GTVTDT-MICAG--AGGKDACQGDSGGPLVCSDGeLIGIVSWGYGcaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
14-244 1.19e-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: 1.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  14 PRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHC----WGSSINVTLGAHNIKEQEPTQqfI 89
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNGPSGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGGTV--V 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  90 PVKRPIPHPAYNPKNFSNDIMLLQLERKAKrtrAVQPLRLPSNKAQVKPGQTCSVAGWGQTAP-LGKHSHTLQEVKMTVQ 168
Cdd:COG5640  102 KVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361 169 EDRKCESDLRhyYDSTIELCVGDPEIKKTSFKGDSGGPLV-----CNKVAqGIVSYGRNNGMP--PRACTKVSSFVHWIK 241
Cdd:COG5640  179 SDATCAAYGG--FDGGTMLCAGYPEGGKDACQGDSGGPLVvkdggGWVLV-GVVSWGGGPCAAgyPGVYTRVSAYRDWIK 255

                 ...
gi 317373361 242 KTM 244
Cdd:COG5640  256 STA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
48-220 6.69e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.44  E-value: 6.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361  48 RCGGFLIRDDFVLTAAHC--------WGSSINVTLGAHNikeqePTQQFIPVKRPIPHPAY-NPKNFSNDIMLLQLERKA 118
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361 119 KRTRAVQPLRLPSNKAqvkPGQTCSVAGWGQTAPLgkhshtlqevKMTVQEDRKC--ESDLRHYYDstielCVGDPeikk 196
Cdd:COG3591   88 GDTTGWLGLAFNDAPL---AGEPVTIIGYPGDRPK----------DLSLDCSGRVtgVQGNRLSYD-----CDTTG---- 145
                        170       180
                 ....*....|....*....|....*....
gi 317373361 197 tsfkGDSGGPL-----VCNKVAqGIVSYG 220
Cdd:COG3591  146 ----GSSGSPVlddsdGGGRVV-GVHSAG 169
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
51-208 1.06e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 38.17  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317373361   51 GFLIRDD-FVLTAAHCWGSSINVTLGAhnIKEQEPTQQFIPVKRPIPHPAYnpknfsnDIMLLQLErkaKRTRAVQPLRL 129
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVEL--VSVVLADGREYPATVVARDPDL-------DLALLRVS---GDGRGLPPLPL 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 317373361  130 pSNKAQVKPGQTCSVAGWgqtaPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELcvgdpeikktsFKGDSGGPLV 208
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGY----PLGGEKLSLSEGIVSGVDEGRDGGDDGRVIQTDAAL-----------SPGSSGGPVF 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH