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Conserved domains on  [gi|70887655|ref|NP_001020685|]
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uncharacterized protein LOC561476 precursor [Danio rerio]

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 ...
59-308 4.69e-96

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: 283.40  E-value: 4.69e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655  59 IVSGNEARPHSWPWQVSLQVRPRGskhyvHVCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERFFP 138
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-----HFCGGSLISPRWVLTAAHCVYSS---APSNYTVRLGSHDLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 139 VKRIYRHEHFRYpahSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRggkENVSLAEALNQAR 218
Cdd:cd00190  73 VKKVIVHPNYNP---STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS---EGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 219 LPIIDYKTCRQKKFWGDRVRDSMICAGfrDTEGTPAACQGDSGGPLLCQVgRDRWEVHGIVSFGpIGCTVENKPSVFTRT 298
Cdd:cd00190 147 VPIVSNAECKRAYSYGGTITDNMLCAG--GLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWG-SGCARPNYPGVYTRV 222
                       250
                ....*....|
gi 70887655 299 AAYIPWIEAT 308
Cdd:cd00190 223 SSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
59-308 4.69e-96

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: 283.40  E-value: 4.69e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655  59 IVSGNEARPHSWPWQVSLQVRPRGskhyvHVCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERFFP 138
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-----HFCGGSLISPRWVLTAAHCVYSS---APSNYTVRLGSHDLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 139 VKRIYRHEHFRYpahSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRggkENVSLAEALNQAR 218
Cdd:cd00190  73 VKKVIVHPNYNP---STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS---EGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 219 LPIIDYKTCRQKKFWGDRVRDSMICAGfrDTEGTPAACQGDSGGPLLCQVgRDRWEVHGIVSFGpIGCTVENKPSVFTRT 298
Cdd:cd00190 147 VPIVSNAECKRAYSYGGTITDNMLCAG--GLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWG-SGCARPNYPGVYTRV 222
                       250
                ....*....|
gi 70887655 299 AAYIPWIEAT 308
Cdd:cd00190 223 SSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
58-305 2.61e-93

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: 276.48  E-value: 2.61e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655     58 RIVSGNEARPHSWPWQVSLQVRprgskHYVHVCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERFf 137
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGS---DPSNIRVRLGSHDLSSGEEGQVI- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    138 PVKRIYRHEHFRYpahSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRGGkeNVSLAEALNQA 217
Cdd:smart00020  72 KVSKVIIHPNYNP---STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG--AGSLPDTLQEV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    218 RLPIIDYKTCRQKKFWGDRVRDSMICAGfrDTEGTPAACQGDSGGPLLCQVGrdRWEVHGIVSFGpIGCTVENKPSVFTR 297
Cdd:smart00020 147 NVPIVSNATCRRAYSGGGAITDNMLCAG--GLEGGKDACQGDSGGPLVCNDG--RWVLVGIVSWG-SGCARPGKPGVYTR 221

                   ....*...
gi 70887655    298 TAAYIPWI 305
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
59-305 1.59e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.80  E-value: 1.59e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    59 IVSGNEARPHSWPWQVSLQVRprgskHYVHVCGGTLIHKNWVLTAAHCFqkgkaEDASSWRIVLGKHQLKRSETAERFFP 138
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS-----SGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655   139 VKRIYRHEHFRypaHSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRGGKenvsLAEALNQAR 218
Cdd:pfam00089  71 VEKIIVHPNYN---PDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG----PSDTLQEVT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655   219 LPIIDYKTCRQkkFWGDRVRDSMICAGFrdteGTPAACQGDSGGPLLCQVGrdrwEVHGIVSFGpIGCTVENKPSVFTRT 298
Cdd:pfam00089 144 VPVVSRETCRS--AYGGTVTDTMICAGA----GGKDACQGDSGGPLVCSDG----ELIGIVSWG-YGCASGNYPGVYTPV 212

                  ....*..
gi 70887655   299 AAYIPWI 305
Cdd:pfam00089 213 SSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
58-308 5.38e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 5.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655  58 RIVSGNEARPHSWPWQVSLQVRPRGSKHYvhvCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERff 137
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCVDGD---GPSDLRVVIGSTDLSTSGGTVV-- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 138 PVKRIYRHEHFRypaHSELDYDIALVKAATdiqPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRGGKENVSlaEALNQA 217
Cdd:COG5640 102 KVARIVVHPDYD---PATPGNDIALLKLAT---PVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQS--GTLRKA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 218 RLPIIDYKTCRQkkfWGDRVRDSMICAGFrdTEGTPAACQGDSGGPLLCQVGrDRWEVHGIVSFGPIGCtVENKPSVFTR 297
Cdd:COG5640 174 DVPVVSDATCAA---YGGFDGGTMLCAGY--PEGGKDACQGDSGGPLVVKDG-GGWVLVGVVSWGGGPC-AAGYPGVYTR 246
                       250
                ....*....|.
gi 70887655 298 TAAYIPWIEAT 308
Cdd:COG5640 247 VSAYRDWIKST 257
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
59-308 4.69e-96

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: 283.40  E-value: 4.69e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655  59 IVSGNEARPHSWPWQVSLQVRPRGskhyvHVCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERFFP 138
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-----HFCGGSLISPRWVLTAAHCVYSS---APSNYTVRLGSHDLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 139 VKRIYRHEHFRYpahSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRggkENVSLAEALNQAR 218
Cdd:cd00190  73 VKKVIVHPNYNP---STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTS---EGGPLPDVLQEVN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 219 LPIIDYKTCRQKKFWGDRVRDSMICAGfrDTEGTPAACQGDSGGPLLCQVgRDRWEVHGIVSFGpIGCTVENKPSVFTRT 298
Cdd:cd00190 147 VPIVSNAECKRAYSYGGTITDNMLCAG--GLEGGKDACQGDSGGPLVCND-NGRGVLVGIVSWG-SGCARPNYPGVYTRV 222
                       250
                ....*....|
gi 70887655 299 AAYIPWIEAT 308
Cdd:cd00190 223 SSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
58-305 2.61e-93

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: 276.48  E-value: 2.61e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655     58 RIVSGNEARPHSWPWQVSLQVRprgskHYVHVCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERFf 137
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGS---DPSNIRVRLGSHDLSSGEEGQVI- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    138 PVKRIYRHEHFRYpahSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRGGkeNVSLAEALNQA 217
Cdd:smart00020  72 KVSKVIIHPNYNP---STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG--AGSLPDTLQEV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    218 RLPIIDYKTCRQKKFWGDRVRDSMICAGfrDTEGTPAACQGDSGGPLLCQVGrdRWEVHGIVSFGpIGCTVENKPSVFTR 297
Cdd:smart00020 147 NVPIVSNATCRRAYSGGGAITDNMLCAG--GLEGGKDACQGDSGGPLVCNDG--RWVLVGIVSWG-SGCARPGKPGVYTR 221

                   ....*...
gi 70887655    298 TAAYIPWI 305
Cdd:smart00020 222 VSSYLDWI 229
Trypsin pfam00089
Trypsin;
59-305 1.59e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 235.80  E-value: 1.59e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    59 IVSGNEARPHSWPWQVSLQVRprgskHYVHVCGGTLIHKNWVLTAAHCFqkgkaEDASSWRIVLGKHQLKRSETAERFFP 138
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS-----SGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655   139 VKRIYRHEHFRypaHSELDYDIALVKAATDIQPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRGGKenvsLAEALNQAR 218
Cdd:pfam00089  71 VEKIIVHPNYN---PDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG----PSDTLQEVT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655   219 LPIIDYKTCRQkkFWGDRVRDSMICAGFrdteGTPAACQGDSGGPLLCQVGrdrwEVHGIVSFGpIGCTVENKPSVFTRT 298
Cdd:pfam00089 144 VPVVSRETCRS--AYGGTVTDTMICAGA----GGKDACQGDSGGPLVCSDG----ELIGIVSWG-YGCASGNYPGVYTPV 212

                  ....*..
gi 70887655   299 AAYIPWI 305
Cdd:pfam00089 213 SSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
58-308 5.38e-65

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 205.27  E-value: 5.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655  58 RIVSGNEARPHSWPWQVSLQVRPRGSKHYvhvCGGTLIHKNWVLTAAHCFQKGkaeDASSWRIVLGKHQLKRSETAERff 137
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGPSGQF---CGGTLIAPRWVLTAAHCVDGD---GPSDLRVVIGSTDLSTSGGTVV-- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 138 PVKRIYRHEHFRypaHSELDYDIALVKAATdiqPSNFIRYACLPRKQINLNPGHYCWVTGWGDTRGGKENVSlaEALNQA 217
Cdd:COG5640 102 KVARIVVHPDYD---PATPGNDIALLKLAT---PVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQS--GTLRKA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 218 RLPIIDYKTCRQkkfWGDRVRDSMICAGFrdTEGTPAACQGDSGGPLLCQVGrDRWEVHGIVSFGPIGCtVENKPSVFTR 297
Cdd:COG5640 174 DVPVVSDATCAA---YGGFDGGTMLCAGY--PEGGKDACQGDSGGPLVVKDG-GGWVLVGVVSWGGGPC-AAGYPGVYTR 246
                       250
                ....*....|.
gi 70887655 298 TAAYIPWIEAT 308
Cdd:COG5640 247 VSAYRDWIKST 257
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
88-286 6.00e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.85  E-value: 6.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655  88 HVCGGTLIHKNWVLTAAHC-FQKGKAEDASSWRIVLGkhqlkRSETAERFFPVKRIYRHEhfRYPAHSELDYDIALVKAA 166
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCvYDGAGGGWATNIVFVPG-----YNGGPYGTATATRFRVPP--GWVASGDAGYDYALLRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655 167 TDIQPSN-FIRYACLPRKQinlnPGHYCWVTGWGDTRGGKENVslaealnqarlpiidYKTCRQKKFWGDRVRDSMicag 245
Cdd:COG3591  85 EPLGDTTgWLGLAFNDAPL----AGEPVTIIGYPGDRPKDLSL---------------DCSGRVTGVQGNRLSYDC---- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 70887655 246 frDTEGtpaacqGDSGGPLLCQVGrDRWEVHGIVSFGPIGC 286
Cdd:COG3591 142 --DTTG------GSSGSPVLDDSD-GGGRVVGVHSAGGADR 173
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
92-270 6.57e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 36.25  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655    92 GTLIHKN-WVLTAAHCFQKGKAEDASSWRIVLGkhqlkrsetAERFFPVKRIYRHEhfrypahselDYDIALVKAATDIQ 170
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLA---------DGREYPATVVARDP----------DLDLALLRVSGDGR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887655   171 PsnfirYACLP-RKQINLNPGHYCWVTGWGDtrgGKENVSLAEAlnqarlpIIdyktCRQKKFWGDRVRDSMICAgfrDT 249
Cdd:pfam13365  64 G-----LPPLPlGDSEPLVGGERVYAVGYPL---GGEKLSLSEG-------IV----SGVDEGRDGGDDGRVIQT---DA 121
                         170       180
                  ....*....|....*....|.
gi 70887655   250 EGTPaacqGDSGGPLLCQVGR 270
Cdd:pfam13365 122 ALSP----GSSGGPVFDADGR 138
 
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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