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Conserved domains on  [gi|632794820|ref|NP_001278844|]
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complement factor D isoform 2 preproprotein [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
25-251 2.77e-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: 2.77e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  25 ILGGQEAAAHARPYMASVQVN-GTHVCGGTLLDEQWVLSAAHCMDGvTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 103
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820 104 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRT 183
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 632794820 184 YHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA----VEGVVTWGSRvCGNGKKPGVYTRVSSYRMWIENI 251
Cdd:cd00190  160 SYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-251 2.77e-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: 2.77e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  25 ILGGQEAAAHARPYMASVQVN-GTHVCGGTLLDEQWVLSAAHCMDGvTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 103
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820 104 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRT 183
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 632794820 184 YHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA----VEGVVTWGSRvCGNGKKPGVYTRVSSYRMWIENI 251
Cdd:cd00190  160 SYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-248 9.43e-79

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: 237.19  E-value: 9.43e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820    24 RILGGQEAAAHARPYMASVQVNG-THVCGGTLLDEQWVLSAAHCMDGVtDDDSVQVLLGAHSLSAPEPYKRwYDVQSVVP 102
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   103 HPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTH-AGRRPDVLHQLRVSIMNRTTCNL 181
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 632794820   182 RTYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA---VEGVVTWGSrVCGNGKKPGVYTRVSSYRMWI 248
Cdd:smart00020 159 AYSGGGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
25-248 4.56e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.31  E-value: 4.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   25 ILGGQEAAAHARPYMASVQV-NGTHVCGGTLLDEQWVLSAAHCmdgVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 103
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  104 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGvVTHAGRRPDVLHQLRVSIMNRTTCnlRT 183
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETC--RS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 632794820  184 YHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDA-VEGVVTWGsRVCGNGKKPGVYTRVSSYRMWI 248
Cdd:pfam00089 155 AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
7-255 1.89e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 186.39  E-value: 1.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   7 FVALVILGAAVCAQPRGRILGGQEAAAHARPYMASVQVNG---THVCGGTLLDEQWVLSAAHCMDGVTDDDsVQVLLGAH 83
Cdd:COG5640   13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD-LRVVIGST 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  84 SLSAPEPykRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNAslgPHVRPLPLQYEDKEVEPGTLCDVAGWGVV-THAGRR 162
Cdd:COG5640   92 DLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820 163 PDVLHQLRVSIMNRTTCNlrtYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDAVE----GVVTWGSRVCGnGKKPG 236
Cdd:COG5640  167 SGTLRKADVPVVSDATCA---AYGGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGwvlvGVVSWGGGPCA-AGYPG 242
                        250
                 ....*....|....*....
gi 632794820 237 VYTRVSSYRMWIENITNGN 255
Cdd:COG5640  243 VYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-251 2.77e-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: 2.77e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  25 ILGGQEAAAHARPYMASVQVN-GTHVCGGTLLDEQWVLSAAHCMDGvTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 103
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820 104 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRT 183
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 632794820 184 YHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA----VEGVVTWGSRvCGNGKKPGVYTRVSSYRMWIENI 251
Cdd:cd00190  160 SYGGTITDNMLCAggLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-248 9.43e-79

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: 237.19  E-value: 9.43e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820    24 RILGGQEAAAHARPYMASVQVNG-THVCGGTLLDEQWVLSAAHCMDGVtDDDSVQVLLGAHSLSAPEPYKRwYDVQSVVP 102
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGEEGQV-IKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   103 HPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTH-AGRRPDVLHQLRVSIMNRTTCNL 181
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 632794820   182 RTYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDA---VEGVVTWGSrVCGNGKKPGVYTRVSSYRMWI 248
Cdd:smart00020 159 AYSGGGAITDNMLCAggLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGS-GCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
25-248 4.56e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 217.31  E-value: 4.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   25 ILGGQEAAAHARPYMASVQV-NGTHVCGGTLLDEQWVLSAAHCmdgVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPH 103
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  104 PGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGvVTHAGRRPDVLHQLRVSIMNRTTCnlRT 183
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSDTLQEVTVPVVSRETC--RS 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 632794820  184 YHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDA-VEGVVTWGsRVCGNGKKPGVYTRVSSYRMWI 248
Cdd:pfam00089 155 AYGGTVTDTMICAGAGGKDACQGDSGGPLVCSDGeLIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
7-255 1.89e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 186.39  E-value: 1.89e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   7 FVALVILGAAVCAQPRGRILGGQEAAAHARPYMASVQVNG---THVCGGTLLDEQWVLSAAHCMDGVTDDDsVQVLLGAH 83
Cdd:COG5640   13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSD-LRVVIGST 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  84 SLSAPEPykRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNAslgPHVRPLPLQYEDKEVEPGTLCDVAGWGVV-THAGRR 162
Cdd:COG5640   92 DLSTSGG--TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTsEGPGSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820 163 PDVLHQLRVSIMNRTTCNlrtYHDGVVTINMMCA--ESNRRDTCRGDSGSPLVCGDAVE----GVVTWGSRVCGnGKKPG 236
Cdd:COG5640  167 SGTLRKADVPVVSDATCA---AYGGFDGGTMLCAgyPEGGKDACQGDSGGPLVVKDGGGwvlvGVVSWGGGPCA-AGYPG 242
                        250
                 ....*....|....*....
gi 632794820 237 VYTRVSSYRMWIENITNGN 255
Cdd:COG5640  243 VYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
45-231 6.09e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.30  E-value: 6.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820  45 NGTHVCGGTLLDEQWVLSAAHCMDGVTDD---DSVQVLLGAHSlsapEPYKRWYDVQSVVpHPGSRPD-SLEDDLILFKL 120
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGgwaTNIVFVPGYNG----GPYGTATATRFRV-PPGWVASgDAGYDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820 121 sqNASLGPHVRPLPLQYEDKEVEPGTlcdvagWGVVTHAGRRPDVLHQlrvsimnRTTCNLRTYHDGVVTINMmcaesnr 200
Cdd:COG3591   84 --DEPLGDTTGWLGLAFNDAPLAGEP------VTIIGYPGDRPKDLSL-------DCSGRVTGVQGNRLSYDC------- 141
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 632794820 201 rDTCRGDSGSPLV----CGDAVEGVVTWGSRVCGN 231
Cdd:COG3591  142 -DTTGGSSGSPVLddsdGGGRVVGVHSAGGADRAN 175
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
37-132 1.37e-05

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 43.31  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 632794820   37 PYMASVQVNGTHVCGGTLLDEQWVLSAAHCMDGVTDDDS-VQVLLGAHS--LSAPEPYKRWYDVQsvvphpgSRPDSLED 113
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQyISVVLGGAKtlKSIEGPYEQIVRVD-------CRHDIPES 74
                          90
                  ....*....|....*....
gi 632794820  114 DLILFKLSQNASLGPHVRP 132
Cdd:pfam09342  75 EISLLHLASPASFSNHVLP 93
 
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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