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Conserved domains on  [gi|45552791|ref|NP_995920|]
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uncharacterized protein Dmel_CG9294 [Drosophila melanogaster]

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 ...
101-334 8.93e-91

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: 271.46  E-value: 8.93e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 101 IVGGQETRVHQYPWMAVILIY-NRFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRShSNDDIVIQRYVSRVKVH 179
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 180 ELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREGGFGTDTLREVDVVVLPQSECRNg 258
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDN-VRPICLPSSGYNLpAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552791 259 TTYRPGQITDNMMCAGYiSEGGKDACSGDSGGPLqttFDEQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLRWL 334
Cdd:cd00190 158 AYSYGGTITDNMLCAGG-LEGGKDACQGDSGGPL---VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
101-334 8.93e-91

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: 271.46  E-value: 8.93e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 101 IVGGQETRVHQYPWMAVILIY-NRFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRShSNDDIVIQRYVSRVKVH 179
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 180 ELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREGGFGTDTLREVDVVVLPQSECRNg 258
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDN-VRPICLPSSGYNLpAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552791 259 TTYRPGQITDNMMCAGYiSEGGKDACSGDSGGPLqttFDEQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLRWL 334
Cdd:cd00190 158 AYSYGGTITDNMLCAGG-LEGGKDACQGDSGGPL---VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
100-333 6.58e-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: 264.15  E-value: 6.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791    100 KIVGGQETRVHQYPWMAVILIYN-RFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRSHSNDDIVIQryVSRVKV 178
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK--VSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791    179 HELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREG-GFGTDTLREVDVVVLPQSECR 256
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDN-VRPICLPSSNYNVpAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552791    257 NgTTYRPGQITDNMMCAGYiSEGGKDACSGDSGGPLQTtfdeQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLRW 333
Cdd:smart00020 158 R-AYSGGGAITDNMLCAGG-LEGGKDACQGDSGGPLVC----NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
100-340 1.19e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.05  E-value: 1.19e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 100 KIVGGQETRVHQYPWMAVILI---YNRFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRSHSNDDiviQRYVSRV 176
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT---VVKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 177 KVHELYNPRSFDNDLAVLRLNQPLDmrhhRLRPICLPVQSYSFdhELG---IVAGWGAQREG-GFGTDTLREVDVVVLPQ 252
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVP----GVAPAPLATSADAA--APGtpaTVAGWGRTSEGpGSQSGTLRKADVPVVSD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 253 SECRNGTTYrpgqITDNMMCAGYiSEGGKDACSGDSGGPLqttFDEQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLR 332
Cdd:COG5640 181 ATCAAYGGF----DGGTMLCAGY-PEGGKDACQGDSGGPL---VVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252

                ....*...
gi 45552791 333 WLGSNTPG 340
Cdd:COG5640 253 WIKSTAGG 260
Trypsin pfam00089
Trypsin;
101-334 4.89e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 4.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791   101 IVGGQETRVHQYPWMAVILIYNRFY-CSGSLINDLYVLTAAHCVEGvpPELITLRFLEHNRSHSNDDIVIqRYVSRVKVH 179
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREGGEQK-FDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791   180 ELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREGGFgTDTLREVDVVVLPQSECRNg 258
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDT-VRPICLPDASSDLpVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552791   259 ttYRPGQITDNMMCAGYiseGGKDACSGDSGGPLQTtfdeqPGQYqLAGIVSWGVGCARPQSPGVYTRVNQYLRWL 334
Cdd:pfam00089 155 --AYGGTVTDTMICAGA---GGKDACQGDSGGPLVC-----SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
101-334 8.93e-91

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: 271.46  E-value: 8.93e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 101 IVGGQETRVHQYPWMAVILIY-NRFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRShSNDDIVIQRYVSRVKVH 179
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 180 ELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREGGFGTDTLREVDVVVLPQSECRNg 258
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDN-VRPICLPSSGYNLpAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR- 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552791 259 TTYRPGQITDNMMCAGYiSEGGKDACSGDSGGPLqttFDEQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLRWL 334
Cdd:cd00190 158 AYSYGGTITDNMLCAGG-LEGGKDACQGDSGGPL---VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
100-333 6.58e-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: 264.15  E-value: 6.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791    100 KIVGGQETRVHQYPWMAVILIYN-RFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRSHSNDDIVIQryVSRVKV 178
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIK--VSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791    179 HELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREG-GFGTDTLREVDVVVLPQSECR 256
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDN-VRPICLPSSNYNVpAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552791    257 NgTTYRPGQITDNMMCAGYiSEGGKDACSGDSGGPLQTtfdeQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLRW 333
Cdd:smart00020 158 R-AYSGGGAITDNMLCAGG-LEGGKDACQGDSGGPLVC----NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
100-340 1.19e-68

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 216.05  E-value: 1.19e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 100 KIVGGQETRVHQYPWMAVILI---YNRFYCSGSLINDLYVLTAAHCVEGVPPELITLRFLEHNRSHSNDDiviQRYVSRV 176
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGT---VVKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 177 KVHELYNPRSFDNDLAVLRLNQPLDmrhhRLRPICLPVQSYSFdhELG---IVAGWGAQREG-GFGTDTLREVDVVVLPQ 252
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATPVP----GVAPAPLATSADAA--APGtpaTVAGWGRTSEGpGSQSGTLRKADVPVVSD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 253 SECRNGTTYrpgqITDNMMCAGYiSEGGKDACSGDSGGPLqttFDEQPGQYQLAGIVSWGVGCARPQSPGVYTRVNQYLR 332
Cdd:COG5640 181 ATCAAYGGF----DGGTMLCAGY-PEGGKDACQGDSGGPL---VVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252

                ....*...
gi 45552791 333 WLGSNTPG 340
Cdd:COG5640 253 WIKSTAGG 260
Trypsin pfam00089
Trypsin;
101-334 4.89e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 4.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791   101 IVGGQETRVHQYPWMAVILIYNRFY-CSGSLINDLYVLTAAHCVEGvpPELITLRFLEHNRSHSNDDIVIqRYVSRVKVH 179
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSG--ASDVKVVLGAHNIVLREGGEQK-FDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791   180 ELYNPRSFDNDLAVLRLNQPLDMRHHrLRPICLPVQSYSF-DHELGIVAGWGAQREGGFgTDTLREVDVVVLPQSECRNg 258
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDT-VRPICLPDASSDLpVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552791   259 ttYRPGQITDNMMCAGYiseGGKDACSGDSGGPLQTtfdeqPGQYqLAGIVSWGVGCARPQSPGVYTRVNQYLRWL 334
Cdd:pfam00089 155 --AYGGTVTDTMICAGA---GGKDACQGDSGGPLVC-----SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
122-314 1.06e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 63.16  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 122 NRFYCSGSLINDLYVLTAAHCVE----GVPPELITLRFLEHNRSHSnddiviQRYVSRVKVHELY-NPRSFDNDLAVLRL 196
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVYdgagGGWATNIVFVPGYNGGPYG------TATATRFRVPPGWvASGDAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 197 NQPLDmrhhrlrpiclpvqsysfdhelgivagwgaQREGGFG----TDTLREVDVVVL--PQSECRNGTTYRPGQITDNm 270
Cdd:COG3591  84 DEPLG------------------------------DTTGWLGlafnDAPLAGEPVTIIgyPGDRPKDLSLDCSGRVTGV- 132
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 45552791 271 mcAGYISEGGKDACSGDSGGPLqttFDEQPGQYQLAGIVSWGVG 314
Cdd:COG3591 133 --QGNRLSYDCDTTGGSSGSPV---LDDSDGGGRVVGVHSAGGA 171
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
255-335 4.04e-03

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 37.67  E-value: 4.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552791 255 CRNGTT--YRPGQITDNMMCAGYisEGGK-------DACS--GDSGGPLQTTfdeqpgqYQLAGIVSWGVG-CARPQSPG 322
Cdd:cd21112 105 CKSGRTtgWTCGTVTAVNVTVNY--PGGTvtgltrtNACAepGDSGGPVFSG-------TQALGITSGGSGnCGSGGGTS 175
                        90
                ....*....|...
gi 45552791 323 VYTRVNQYLRWLG 335
Cdd:cd21112 176 YFQPVNPVLSAYG 188
 
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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