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Conserved domains on  [gi|2101239085|ref|WP_223759908|]
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zinc-dependent metalloprotease [Myxococcus sp. RHSTA-1-4]

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 ...
55-259 3.53e-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: 336.41  E-value: 3.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085  55 VYVGRDAHVTLEASREMLQPAEVSAEQYRTTNLVGTS--VTKICVNPTSQFNSYSRLSAGLDLAIENYNSMGLRLTF--V 130
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSvtVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRFTFrlT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 131 RGPATDC----TASISARTTSGVGGSAGFPKGGKPYGTINIGTGLQNYSVDVNEHVITHELGHTIGFRHSDYYDRSISCG 206
Cdd:pfam12388  81 FGPNTGNsdmvTYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2101239085 207 SGGNEGEAGVGAIHIPGTPTTATrGGSVMNSCFSSNESGEWTSSDRTALDYLY 259
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 ...
55-259 3.53e-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: 336.41  E-value: 3.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085  55 VYVGRDAHVTLEASREMLQPAEVSAEQYRTTNLVGTS--VTKICVNPTSQFNSYSRLSAGLDLAIENYNSMGLRLTF--V 130
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSvtVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRFTFrlT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 131 RGPATDC----TASISARTTSGVGGSAGFPKGGKPYGTINIGTGLQNYSVDVNEHVITHELGHTIGFRHSDYYDRSISCG 206
Cdd:pfam12388  81 FGPNTGNsdmvTYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2101239085 207 SGGNEGEAGVGAIHIPGTPTTATrGGSVMNSCFSSNESGEWTSSDRTALDYLY 259
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
145-259 7.45e-07

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: 47.88  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 145 TTSGVGGSAGFPKGGKPY-GTINIGTGLQNYSVDVNEHVITHELGHTIGFRHSDyydrsiscgsggnegeAGVGAIHIPG 223
Cdd:cd04268    59 GTWSYGPSQVDPLTGEILlARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNF----------------AASDRDDNVD 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2101239085 224 TPTTATRGGSVMNsCFSSNESGE--------WTSSDRTALDYLY 259
Cdd:cd04268   123 LLAEKGDTSSVMD-YAPSNFSIQlgdgqkytIGPYDIAAIKKLY 165
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
127-201 1.43e-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: 43.88  E-value: 1.43e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2101239085  127 LTFVRGPATDcTASIS-ARTTSGVGGS-AGFPKGGkpyGTINIGTGlqnysvDVNEHVITHELGHTIGFRHS-DYYDR 201
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 ...
55-259 3.53e-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: 336.41  E-value: 3.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085  55 VYVGRDAHVTLEASREMLQPAEVSAEQYRTTNLVGTS--VTKICVNPTSQFNSYSRLSAGLDLAIENYNSMGLRLTF--V 130
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSvtVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRFTFrlT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 131 RGPATDC----TASISARTTSGVGGSAGFPKGGKPYGTINIGTGLQNYSVDVNEHVITHELGHTIGFRHSDYYDRSISCG 206
Cdd:pfam12388  81 FGPNTGNsdmvTYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISCG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2101239085 207 SGGNEGEAGVGAIHIPGTPTTATrGGSVMNSCFSSNESGEWTSSDRTALDYLY 259
Cdd:pfam12388 161 SGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
145-259 7.45e-07

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: 47.88  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 145 TTSGVGGSAGFPKGGKPY-GTINIGTGLQNYSVDVNEHVITHELGHTIGFRHSDyydrsiscgsggnegeAGVGAIHIPG 223
Cdd:cd04268    59 GTWSYGPSQVDPLTGEILlARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNF----------------AASDRDDNVD 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2101239085 224 TPTTATRGGSVMNsCFSSNESGE--------WTSSDRTALDYLY 259
Cdd:cd04268   123 LLAEKGDTSSVMD-YAPSNFSIQlgdgqkytIGPYDIAAIKKLY 165
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
127-201 1.43e-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: 43.88  E-value: 1.43e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2101239085  127 LTFVRGPATDcTASIS-ARTTSGVGGS-AGFPKGGkpyGTINIGTGlqnysvDVNEHVITHELGHTIGFRHS-DYYDR 201
Cdd:smart00235  40 IRFVERTGTA-DIYISfGSGDSGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEqSRSDR 107
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
127-259 4.34e-04

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: 40.09  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 127 LTFVRGPATDCTA---SISARTTSGVGGSAGFPK---GGKPYGTINIGTGLQNYSVDVNEH---VITHELGHTIGFRHSd 197
Cdd:cd04277    52 IDFVEVSDNSGADirfGNSSDPDGNTAGYAYYPGsgsGTAYGGDIWFNSSYDTNSDSPGSYgyqTIIHEIGHALGLEHP- 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2101239085 198 yydrsiscgsggneGEAGVGAihiPGTPTTA--TRGGSVMnSCFSSNESGEWTSS---------DRTALDYLY 259
Cdd:cd04277   131 --------------GDYNGGD---PVPPTYAldSREYTVM-SYNSGYGNGASAGGgypqtpmllDIAALQYLY 185
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
94-259 6.95e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 38.98  E-value: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085  94 KICVNPTSQFNS--YSRLSAGLDLAIENYNSmGLRLTFVRGPATDCTASI--------SARTTSGVGGSAGFPKGGKPYG 163
Cdd:cd04279     5 RVYIDPTPAPPDsrAQSWLQAVKQAAAEWEN-VGPLKFVYNPEEDNDADIviffdrppPVGGAGGGLARAGFPLISDGNR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 164 ------TINIGTGLQNYSVDVnEHVITHELGHTIGFRHSDyydrsiscgsggnegeagvgaihipgtpttaTRGGSVMNS 237
Cdd:cd04279    84 klfnrtDINLGPGQPRGAENL-QAIALHELGHALGLWHHS-------------------------------DRPEDAMYP 131
                         170       180
                  ....*....|....*....|....
gi 2101239085 238 CFSSNESGEW--TSSDRTALDYLY 259
Cdd:cd04279   132 SQGQGPDGNPtlSARDVATLKRLY 155
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
182-259 6.62e-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: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101239085 182 VITHELGHTIGFRHSDYYdrsiscgsggnegEAGVGAIHIPGT-PTTATRGGSVMnSCFSSNESGE----WTSSDRTALD 256
Cdd:cd00203    99 TIAHELGHALGFYHDHDR-------------KDRDDYPTIDDTlNAEDDDYYSVM-SYTKGSFSDGqrkdFSQCDIDQIN 164

                  ...
gi 2101239085 257 YLY 259
Cdd:cd00203   165 KLY 167
 
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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