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Conserved domains on  [gi|87282900|gb|EAQ74857|]
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hypothetical protein WH5701_11619 [Synechococcus sp. WH 5701]

Protein Classification

ZnMc_MMP_like_1 domain-containing protein( domain architecture ID 10136682)

ZnMc_MMP_like_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 9-167 1.01e-42

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: 139.90  E-value: 1.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900   9 PRLDRWCVWVQPlgetGPGSRFDQRWQQAVNGALTSWASELTLVMVSDP---ARAQILIQRRRPPLLDANGRRRASHGRA 85
Cdd:cd04279   1 KSPIRVYIDPTP----APPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPeedNDADIVIFFDRPPPVGGAGGGLARAGFP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  86 LLellevqRQGAWHLEPRVEVLLSPDQ--RLEALQATALHELGHAIGLWGHSDEPADAMAAVPGAQPV--LSLSARDRAT 161
Cdd:cd04279  77 LI------SDGNRKLFNRTDINLGPGQprGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDgnPTLSARDVAT 150


                ....*.
gi 87282900 162 VRWLYQ 167
Cdd:cd04279 151 LKRLYG 156
 
Name Accession Description Interval E-value
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 9-167 1.01e-42

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: 139.90  E-value: 1.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900   9 PRLDRWCVWVQPlgetGPGSRFDQRWQQAVNGALTSWASELTLVMVSDP---ARAQILIQRRRPPLLDANGRRRASHGRA 85
Cdd:cd04279   1 KSPIRVYIDPTP----APPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPeedNDADIVIFFDRPPPVGGAGGGLARAGFP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  86 LLellevqRQGAWHLEPRVEVLLSPDQ--RLEALQATALHELGHAIGLWGHSDEPADAMAAVPGAQPV--LSLSARDRAT 161
Cdd:cd04279  77 LI------SDGNRKLFNRTDINLGPGQprGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDgnPTLSARDVAT 150


                ....*.
gi 87282900 162 VRWLYQ 167
Cdd:cd04279 151 LKRLYG 156
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 1-169 5.61e-37

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 127.49  E-value: 5.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900   1 METTPLG---WPRLDRwCVWVQPlgetgPGSRFDQR---WQQAVNGALTSWASELTLVMVSDPARAQILIQRRRPPLLDA 74
Cdd:COG5549  69 IKPTPVGylvWSQFPV-KVYIDR-----PPSAAQQRaqqWVAAVLQAIAEWNAYLPLEVVENPENADIIIVRSNPPLTAS 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  75 NGRR-RASHGRALLELLEVQRQgawhLEPRVEVLLSPDQRLEALQATALHELGHAIGLWGHSDEPADAM--AAVPGAQPv 151
Cdd:COG5549 143 PNPEtGARSAETTYEFYDTGNI----LSHRFTILLSPNQTGKYLLATARHELGHALGIWGHSPSPTDAMyfSQVRNPPP- 217

                       170
                ....*....|....*...
gi 87282900 152 lsLSARDRATVRWLYQQP 169
Cdd:COG5549 218 --ISPRDINTLKRIYQQP 233
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 117-166 4.43e-06

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 44.53  E-value: 4.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 87282900   117 LQATALHELGHAIGLwGHSDEPADAMAAV--PGAQPVLSLSARDRATVRWLY 166
Cdd:pfam00413 108 LFLVAAHEIGHALGL-GHSSDPGAIMYPTysPLDSKKFRLSQDDIKGIQQLY 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 119-168 4.07e-04

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: 38.49  E-value: 4.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 87282900    119 ATALHELGHAIGLWgHSDEPAD---AMAAVPGAQPV--LSLSARDRATVRWLYQQ 168
Cdd:smart00235  86 GVAAHELGHALGLY-HEQSRSDrdnYMYINYTNIDTrnFDLSEDDSLGIPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 9-167 1.01e-42

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: 139.90  E-value: 1.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900   9 PRLDRWCVWVQPlgetGPGSRFDQRWQQAVNGALTSWASELTLVMVSDP---ARAQILIQRRRPPLLDANGRRRASHGRA 85
Cdd:cd04279   1 KSPIRVYIDPTP----APPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPeedNDADIVIFFDRPPPVGGAGGGLARAGFP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  86 LLellevqRQGAWHLEPRVEVLLSPDQ--RLEALQATALHELGHAIGLWGHSDEPADAMAAVPGAQPV--LSLSARDRAT 161
Cdd:cd04279  77 LI------SDGNRKLFNRTDINLGPGQprGAENLQAIALHELGHALGLWHHSDRPEDAMYPSQGQGPDgnPTLSARDVAT 150


                ....*.
gi 87282900 162 VRWLYQ 167
Cdd:cd04279 151 LKRLYG 156
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 1-169 5.61e-37

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 127.49  E-value: 5.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900   1 METTPLG---WPRLDRwCVWVQPlgetgPGSRFDQR---WQQAVNGALTSWASELTLVMVSDPARAQILIQRRRPPLLDA 74
Cdd:COG5549  69 IKPTPVGylvWSQFPV-KVYIDR-----PPSAAQQRaqqWVAAVLQAIAEWNAYLPLEVVENPENADIIIVRSNPPLTAS 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  75 NGRR-RASHGRALLELLEVQRQgawhLEPRVEVLLSPDQRLEALQATALHELGHAIGLWGHSDEPADAM--AAVPGAQPv 151
Cdd:COG5549 143 PNPEtGARSAETTYEFYDTGNI----LSHRFTILLSPNQTGKYLLATARHELGHALGIWGHSPSPTDAMyfSQVRNPPP- 217

                       170
                ....*....|....*...
gi 87282900 152 lsLSARDRATVRWLYQQP 169
Cdd:COG5549 218 --ISPRDINTLKRIYQQP 233
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 117-166 3.91e-06

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 44.50  E-value: 3.91e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 87282900 117 LQATALHELGHAIGLwGHSDEPADAMAA-VPGAQPVLSLSARDRATVRWLY 166
Cdd:cd04278 107 LFSVAAHEIGHALGL-GHSSDPDSIMYPyYQGPVPKFKLSQDDIRGIQALY 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 117-166 4.43e-06

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 44.53  E-value: 4.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 87282900   117 LQATALHELGHAIGLwGHSDEPADAMAAV--PGAQPVLSLSARDRATVRWLY 166
Cdd:pfam00413 108 LFLVAAHEIGHALGL-GHSSDPGAIMYPTysPLDSKKFRLSQDDIKGIQQLY 158
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 96-166 2.45e-04

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: 39.79  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  96 GAWHLEPRV------EVLLSPDQ--------RLEALQATALHELGHAIGLWGHSDEPADA---------------MAAVP 146
Cdd:cd04268  59 GTWSYGPSQvdpltgEILLARVYlyssfveySGARLRNTAEHELGHALGLRHNFAASDRDdnvdllaekgdtssvMDYAP 138

                        90       100
                ....*....|....*....|....*..
gi 87282900 147 GAQPVLS-------LSARDRATVRWLY 166
Cdd:cd04268 139 SNFSIQLgdgqkytIGPYDIAAIKKLY 165
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 119-168 4.07e-04

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: 38.49  E-value: 4.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 87282900    119 ATALHELGHAIGLWgHSDEPAD---AMAAVPGAQPV--LSLSARDRATVRWLYQQ 168
Cdd:smart00235  86 GVAAHELGHALGLY-HEQSRSDrdnYMYINYTNIDTrnFDLSEDDSLGIPYDYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 24-140 2.00e-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: 37.40  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87282900  24 TGPGSRFDQRWQQAVNGALTSWASE--LTLVMVSDPARAQILIQrrrppllDANGRRRASHGRALL--ELLEVQRQGAWH 99
Cdd:cd04277  25 TTNTAALSAAQQAAARDALEAWEDVadIDFVEVSDNSGADIRFG-------NSSDPDGNTAGYAYYpgSGSGTAYGGDIW 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 87282900 100 LEPrvevllSPDQRLEAL----QATALHELGHAIGLwGHSDEPAD 140
Cdd:cd04277  98 FNS------SYDTNSDSPgsygYQTIIHEIGHALGL-EHPGDYNG 135
 
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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