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Conserved domains on  [gi|1562380476|ref|WP_128799288|]
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zinc-dependent metalloprotease [Corallococcus coralloides]

Protein Classification

zinc-dependent metalloprotease( domain architecture ID 10574850)

zinc-dependent metalloprotease similar to Myxococcus xanthus protease B (prtB)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
51-255 5.07e-118

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


:

Pssm-ID: 432518  Cd Length: 212  Bit Score: 336.02  E-value: 5.07e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476  51 VYVGRDAHVSLDASREMLQADSETAEQYRTTNLVGTSVTKICII--PTSQFNSYSRLSAGLDLAIENYNSQGLRLTFA-- 126
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSVTVIKICvnPTSNFNSYSRLSTGLDLAIANYNRLGLRFTFRlt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 127 ---RGSASDC-TATISAKTTSGTGGSAGFPKGGKPYGTINIGTGLQSYSVDVNEHVITHELGHTIGFRHSDYYDRSISCG 202
Cdd:pfam12388  81 fgpNTGNSDMvTYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1562380476 203 SGGNEGASNVGAIHIPGTPTTATrGGSVMNSCFSSNESGEWTSSDRTALDYLY 255
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
 
Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
51-255 5.07e-118

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 336.02  E-value: 5.07e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476  51 VYVGRDAHVSLDASREMLQADSETAEQYRTTNLVGTSVTKICII--PTSQFNSYSRLSAGLDLAIENYNSQGLRLTFA-- 126
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSVTVIKICvnPTSNFNSYSRLSTGLDLAIANYNRLGLRFTFRlt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 127 ---RGSASDC-TATISAKTTSGTGGSAGFPKGGKPYGTINIGTGLQSYSVDVNEHVITHELGHTIGFRHSDYYDRSISCG 202
Cdd:pfam12388  81 fgpNTGNSDMvTYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1562380476 203 SGGNEGASNVGAIHIPGTPTTATrGGSVMNSCFSSNESGEWTSSDRTALDYLY 255
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
141-255 1.15e-06

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 47.49  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 141 TTSGTGGSAGFPKGGKPY-GTINIGTGLQSYSVDVNEHVITHELGHTIGFRHSDYYDRSIScgsggnegasnvgaihIPG 219
Cdd:cd04268    59 GTWSYGPSQVDPLTGEILlARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRDD----------------NVD 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1562380476 220 TPTTATRGGSVMNsCFSSNESGE--------WTSSDRTALDYLY 255
Cdd:cd04268   123 LLAEKGDTSSVMD-YAPSNFSIQlgdgqkytIGPYDIAAIKKLY 165
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
123-197 4.03e-05

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 42.34  E-value: 4.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562380476  123 LTFARGSASDcTATIS-AKTTSGTGGS-AGFPKGGkpyGTINIGTGlqsysvDVNEHVITHELGHTIGFRHS-DYYDR 197
Cdd:smart00235  40 IRFVERTGTA-DIYISfGSGDSGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEqSRSDR 107
 
Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
51-255 5.07e-118

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 336.02  E-value: 5.07e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476  51 VYVGRDAHVSLDASREMLQADSETAEQYRTTNLVGTSVTKICII--PTSQFNSYSRLSAGLDLAIENYNSQGLRLTFA-- 126
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSVTVIKICvnPTSNFNSYSRLSTGLDLAIANYNRLGLRFTFRlt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 127 ---RGSASDC-TATISAKTTSGTGGSAGFPKGGKPYGTINIGTGLQSYSVDVNEHVITHELGHTIGFRHSDYYDRSISCG 202
Cdd:pfam12388  81 fgpNTGNSDMvTYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1562380476 203 SGGNEGASNVGAIHIPGTPTTATrGGSVMNSCFSSNESGEWTSSDRTALDYLY 255
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
141-255 1.15e-06

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 47.49  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 141 TTSGTGGSAGFPKGGKPY-GTINIGTGLQSYSVDVNEHVITHELGHTIGFRHSDYYDRSIScgsggnegasnvgaihIPG 219
Cdd:cd04268    59 GTWSYGPSQVDPLTGEILlARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRDD----------------NVD 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1562380476 220 TPTTATRGGSVMNsCFSSNESGE--------WTSSDRTALDYLY 255
Cdd:cd04268   123 LLAEKGDTSSVMD-YAPSNFSIQlgdgqkytIGPYDIAAIKKLY 165
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
123-197 4.03e-05

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 42.34  E-value: 4.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562380476  123 LTFARGSASDcTATIS-AKTTSGTGGS-AGFPKGGkpyGTINIGTGlqsysvDVNEHVITHELGHTIGFRHS-DYYDR 197
Cdd:smart00235  40 IRFVERTGTA-DIYISfGSGDSGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEqSRSDR 107
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
127-238 3.99e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 37.40  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 127 RGSASDCTATISAKTTSGTGG------SAGFPKGGKPYGTINIGTGLQSYSVDVneHVITHELGHTIGFRHSDYYDRSIS 200
Cdd:pfam13688  85 RGTQNDDLAYLFLMTNCSGGGlawlgqLCNSGSAGSVSTRVSGNNVVVSTATEW--QVFAHEIGHNFGAVHDCDSSTSSQ 162
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1562380476 201 CGSggnegasnvgaihiPGTPTTATRGGSVMNSCFSSN 238
Cdd:pfam13688 163 CCP--------------PSNSTCPAGGRYIMNPSSSPN 186
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
123-255 4.39e-03

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 37.01  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 123 LTF---ARGSASDCTATISAKTTSGTGGSAGFPK---GGKPYGTINIGTGLQSYSVDVNEH---VITHELGHTIGFRHSd 193
Cdd:cd04277    52 IDFvevSDNSGADIRFGNSSDPDGNTAGYAYYPGsgsGTAYGGDIWFNSSYDTNSDSPGSYgyqTIIHEIGHALGLEHP- 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562380476 194 yydrsiscgsgGNEGASNVgaihIPGTPTTATRGGSVMnSCFSSNESGEWTSS---------DRTALDYLY 255
Cdd:cd04277   131 -----------GDYNGGDP----VPPTYALDSREYTVM-SYNSGYGNGASAGGgypqtpmllDIAALQYLY 185
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
144-255 6.91e-03

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 36.35  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 144 GTGGSAGFPKGGKPY-GTINIGTGlqSYSVDVNEHVITHELGHTIGFRHSdyydrsiscgSGGNEGASNVGAihIPGTPT 222
Cdd:cd00203    66 GTGGWAYLGRVCDSLrGVGVLQDN--QSGTKEGAQTIAHELGHALGFYHD----------HDRKDRDDYPTI--DDTLNA 131
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1562380476 223 TATRGGSVMnSCFSSNESGE----WTSSDRTALDYLY 255
Cdd:cd00203   132 EDDDYYSVM-SYTKGSFSDGqrkdFSQCDIDQINKLY 167
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
123-212 8.60e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 36.45  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562380476 123 LTFARGSASDCTATISAKTTSGtGGSAGFPKGG----KPYGTINIGTGL-------QSYSVDVNEHVITHELGHTIGFRH 191
Cdd:pfam13574  62 LSQWRGEQDYCLAHLVTMGTFS-GGELGLAYVGqicqKGASSPKTNTGLstttnygSFNYPTQEWDVVAHEVGHNFGATH 140
                          90       100
                  ....*....|....*....|.
gi 1562380476 192 SDyyDRSISCGSGGNEGASNV 212
Cdd:pfam13574 141 DC--DGSQYASSGCERNAATS 159
 
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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