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Conserved domains on  [gi|2462550265|ref|XP_054169654|]
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matrix metalloproteinase-25 isoform X4 [Homo sapiens]

Protein Classification

PG_binding_1 and ZnMc domain-containing protein( domain architecture ID 10478046)

PG_binding_1 and ZnMc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 115-219 7.50e-45

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.


The actual alignment was detected with superfamily member cd04278:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 157  Bit Score: 149.28  E-value: 7.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550265 115 WKKRTLTWRVRSFPQSsqLSQETVRVLMSYALMAWGMESGLTFHEVDSpqGQEPDILIDFARAFHQDSYPFDGLGGTLAH 194
Cdd:cd04278     2 WSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTS--GQEADIRISFARGNHGDGYPFDGPGGTLAH 77

                          90       100
                  ....*....|....*....|....*
gi 2462550265 195 AFFPGEhpISGDTHFDDEETWTFGS 219
Cdd:cd04278    78 AFFPGG--IGGDIHFDDDEQWTLGS 100
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 25-85 5.52e-09

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 51.36  E-value: 5.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462550265  25 SAQDVSLGVDWLTRYGYLPPPhpaqAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATM 85
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-219 7.50e-45

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: 149.28  E-value: 7.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550265 115 WKKRTLTWRVRSFPQSsqLSQETVRVLMSYALMAWGMESGLTFHEVDSpqGQEPDILIDFARAFHQDSYPFDGLGGTLAH 194
Cdd:cd04278     2 WSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTS--GQEADIRISFARGNHGDGYPFDGPGGTLAH 77

                          90       100
                  ....*....|....*....|....*
gi 2462550265 195 AFFPGEhpISGDTHFDDEETWTFGS 219
Cdd:cd04278    78 AFFPGG--IGGDIHFDDDEQWTLGS 100
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-221 4.56e-38

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: 131.59  E-value: 4.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550265 115 WKKRTLTWRVrsFPQSSQLSQETVRVLMSYALMAWGMESGLTFHEVDSPqgqEPDILIDFARAFHQDSYPFDGLGGTLAH 194
Cdd:pfam00413   2 WRKKNLTYRI--LNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG---EADIMIGFGRGDHGDGYPFDGPGGVLAH 76

                          90       100
                  ....*....|....*....|....*..
gi 2462550265 195 AFFPGEHpISGDTHFDDEETWTFGSKD 221
Cdd:pfam00413  77 AFFPGPG-LGGDIHFDDDETWTVGSDP 102
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 25-85 5.52e-09

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 51.36  E-value: 5.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462550265  25 SAQDVSLGVDWLTRYGYLPPPhpaqAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATM 85
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-219 7.50e-45

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: 149.28  E-value: 7.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550265 115 WKKRTLTWRVRSFPQSsqLSQETVRVLMSYALMAWGMESGLTFHEVDSpqGQEPDILIDFARAFHQDSYPFDGLGGTLAH 194
Cdd:cd04278     2 WSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTS--GQEADIRISFARGNHGDGYPFDGPGGTLAH 77

                          90       100
                  ....*....|....*....|....*
gi 2462550265 195 AFFPGEhpISGDTHFDDEETWTFGS 219
Cdd:cd04278    78 AFFPGG--IGGDIHFDDDEQWTLGS 100
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-221 4.56e-38

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: 131.59  E-value: 4.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462550265 115 WKKRTLTWRVrsFPQSSQLSQETVRVLMSYALMAWGMESGLTFHEVDSPqgqEPDILIDFARAFHQDSYPFDGLGGTLAH 194
Cdd:pfam00413   2 WRKKNLTYRI--LNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG---EADIMIGFGRGDHGDGYPFDGPGGVLAH 76

                          90       100
                  ....*....|....*....|....*..
gi 2462550265 195 AFFPGEHpISGDTHFDDEETWTFGSKD 221
Cdd:pfam00413  77 AFFPGPG-LGGDIHFDDDETWTVGSDP 102
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 25-85 5.52e-09

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 51.36  E-value: 5.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462550265  25 SAQDVSLGVDWLTRYGYLPPPhpaqAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATM 85
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
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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