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Conserved domains on  [gi|2982082|pdb|1AZZ|A]
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Chain A, COLLAGENASE

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 ...
1-221 2.80e-86

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: 254.89  E-value: 2.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A        1 IVGGVEAVPNSWPHQAALFIDD-MYFCGGSLISPEWILTAAHCMDG--AGFVDVVLGAHNIREDEATQVTIQSTDFTVHE 77
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSsaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       78 NYNSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPSDSAlGISDVLRQVDVPIMSNADCDAVY 155
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1AZZ_A      156 ---GIVTDGNICI-DSTGGKGTCNGDSGGPLNYNGLT----YGITSFGaaAGC-EAGYPDAFTRVTYFLDWIQTQ 221
Cdd:cd00190 160 sygGTITDNMLCAgGLEGGKDACQGDSGGPLVCNDNGrgvlVGIVSWG--SGCaRPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-221 2.80e-86

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: 254.89  E-value: 2.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A        1 IVGGVEAVPNSWPHQAALFIDD-MYFCGGSLISPEWILTAAHCMDG--AGFVDVVLGAHNIREDEATQVTIQSTDFTVHE 77
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSsaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       78 NYNSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPSDSAlGISDVLRQVDVPIMSNADCDAVY 155
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1AZZ_A      156 ---GIVTDGNICI-DSTGGKGTCNGDSGGPLNYNGLT----YGITSFGaaAGC-EAGYPDAFTRVTYFLDWIQTQ 221
Cdd:cd00190 160 sygGTITDNMLCAgGLEGGKDACQGDSGGPLVCNDNGrgvlVGIVSWG--SGCaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-218 2.04e-85

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: 252.60  E-value: 2.04e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A           1 IVGGVEAVPNSWPHQAALFIDDMY-FCGGSLISPEWILTAAHCMDG--AGFVDVVLGAHNIREDEATQVtIQSTDFTVHE 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A          78 NYNSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPSDSALGISDVLRQVDVPIMSNADCDAVY 155
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1AZZ_A         156 G---IVTDGNICI-DSTGGKGTCNGDSGGPLNYNGLTY---GITSFGaaAGC-EAGYPDAFTRVTYFLDWI 218
Cdd:smart00020 161 SgggAITDNMLCAgGLEGGKDACQGDSGGPLVCNDGRWvlvGIVSWG--SGCaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-218 1.18e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 212.30  E-value: 1.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A          1 IVGGVEAVPNSWPHQAALFI-DDMYFCGGSLISPEWILTAAHCMDGAGFVDVVLGAHNIREDEATQVTIQSTDFTVHENY 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A         80 NSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPsdSALGISDVLRQVDVPIMSNADCDAVYGI 157
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNT--KTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1AZZ_A        158 -VTDGNICIDsTGGKGTCNGDSGGPL-NYNGLTYGITSFGaaAGC-EAGYPDAFTRVTYFLDWI 218
Cdd:pfam00089 159 tVTDTMICAG-AGGKDACQGDSGGPLvCSDGELIGIVSWG--YGCaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-226 4.66e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.88  E-value: 4.66e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A        1 IVGGVEAVPNSWPHQAALFIDD---MYFCGGSLISPEWILTAAHCMDGAGF--VDVVLGAHNIREDEATQVTIqsTDFTV 75
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdLRVVIGSTDLSTSGGTVVKV--ARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       76 HENYNSFVISNDIAVIRLPVPVTlTAAIATVGLPSTDVGVGTVVTPTGWGLPSDSALGISDVLRQVDVPIMSNADCDAVY 155
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP-GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAYG 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1AZZ_A      156 GIVTDGNICID-STGGKGTCNGDSGGPL----NYNGLTYGITSFGaAAGCEAGYPDAFTRVTYFLDWIQTQTGITP 226
Cdd:COG5640 188 GFDGGTMLCAGyPEGGKDACQGDSGGPLvvkdGGGWVLVGVVSWG-GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-221 2.80e-86

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: 254.89  E-value: 2.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A        1 IVGGVEAVPNSWPHQAALFIDD-MYFCGGSLISPEWILTAAHCMDG--AGFVDVVLGAHNIREDEATQVTIQSTDFTVHE 77
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYSsaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       78 NYNSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPSDSAlGISDVLRQVDVPIMSNADCDAVY 155
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1AZZ_A      156 ---GIVTDGNICI-DSTGGKGTCNGDSGGPLNYNGLT----YGITSFGaaAGC-EAGYPDAFTRVTYFLDWIQTQ 221
Cdd:cd00190 160 sygGTITDNMLCAgGLEGGKDACQGDSGGPLVCNDNGrgvlVGIVSWG--SGCaRPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-218 2.04e-85

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: 252.60  E-value: 2.04e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A           1 IVGGVEAVPNSWPHQAALFIDDMY-FCGGSLISPEWILTAAHCMDG--AGFVDVVLGAHNIREDEATQVtIQSTDFTVHE 77
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCVRGsdPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A          78 NYNSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPSDSALGISDVLRQVDVPIMSNADCDAVY 155
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAY 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1AZZ_A         156 G---IVTDGNICI-DSTGGKGTCNGDSGGPLNYNGLTY---GITSFGaaAGC-EAGYPDAFTRVTYFLDWI 218
Cdd:smart00020 161 SgggAITDNMLCAgGLEGGKDACQGDSGGPLVCNDGRWvlvGIVSWG--SGCaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-218 1.18e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 212.30  E-value: 1.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A          1 IVGGVEAVPNSWPHQAALFI-DDMYFCGGSLISPEWILTAAHCMDGAGFVDVVLGAHNIREDEATQVTIQSTDFTVHENY 79
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A         80 NSFVISNDIAVIRLPVPVTLTAAIATVGLPSTD--VGVGTVVTPTGWGLPsdSALGISDVLRQVDVPIMSNADCDAVYGI 157
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNT--KTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1AZZ_A        158 -VTDGNICIDsTGGKGTCNGDSGGPL-NYNGLTYGITSFGaaAGC-EAGYPDAFTRVTYFLDWI 218
Cdd:pfam00089 159 tVTDTMICAG-AGGKDACQGDSGGPLvCSDGELIGIVSWG--YGCaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-226 4.66e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 204.88  E-value: 4.66e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A        1 IVGGVEAVPNSWPHQAALFIDD---MYFCGGSLISPEWILTAAHCMDGAGF--VDVVLGAHNIREDEATQVTIqsTDFTV 75
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdLRVVIGSTDLSTSGGTVVKV--ARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       76 HENYNSFVISNDIAVIRLPVPVTlTAAIATVGLPSTDVGVGTVVTPTGWGLPSDSALGISDVLRQVDVPIMSNADCDAVY 155
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP-GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDATCAAYG 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1AZZ_A      156 GIVTDGNICID-STGGKGTCNGDSGGPL----NYNGLTYGITSFGaAAGCEAGYPDAFTRVTYFLDWIQTQTGITP 226
Cdd:COG5640 188 GFDGGTMLCAGyPEGGKDACQGDSGGPLvvkdGGGWVLVGVVSWG-GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
24-197 1.05e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 53.14  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       24 YFCGGSLISPEWILTAAHCMDG------AGFVDVVLGAHNiredeATQVTIQSTDFTVHENY-NSFVISNDIAVIRLPVP 96
Cdd:COG3591  12 GVCTGTLIGPNLVLTAGHCVYDgagggwATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZZ_A       97 VTLTAAIATVGlPSTDVGVGTVVTPTGWglPSDSALGISdvlrqvdvpimsnADCDAVYGIVTDGNICIDSTggkgTCNG 176
Cdd:COG3591  87 LGDTTGWLGLA-FNDAPLAGEPVTIIGY--PGDRPKDLS-------------LDCSGRVTGVQGNRLSYDCD----TTGG 146
                       170       180
                ....*....|....*....|....*
1AZZ_A      177 DSGGPL----NYNGLTYGITSFGAA 197
Cdd:COG3591 147 SSGSPVlddsDGGGRVVGVHSAGGA 171
 
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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