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Conserved domains on  [gi|442535505|ref|NP_001259030|]
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matrix metalloproteinase-19 isoform 3 preproprotein [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 ...
 103-174 5.75e-27

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: 103.05  E-value: 5.75e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442535505 103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGA-ADIRLSFhGRQSSYCSNTFDGPG 174
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISF-ARGNHGDGYPFDGPG 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-80 3.87e-06

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: 43.27  E-value: 3.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442535505   31 YLSQYGYLQKPLEGsnNFKPEdITEALRAFQEASELPVSGQLDDATRARM 80
Cdd:pfam01471  11 YLNRLGYYPGPVDG--YFGPS-TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-174 5.75e-27

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: 103.05  E-value: 5.75e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442535505 103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGA-ADIRLSFhGRQSSYCSNTFDGPG 174
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISF-ARGNHGDGYPFDGPG 72
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-174 1.07e-24

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: 97.30  E-value: 1.07e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442535505  103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSFhGRQSSYCSNTFDGPG 174
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGF-GRGDHGDGYPFDGPG 71
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-80 3.87e-06

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: 43.27  E-value: 3.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442535505   31 YLSQYGYLQKPLEGsnNFKPEdITEALRAFQEASELPVSGQLDDATRARM 80
Cdd:pfam01471  11 YLNRLGYYPGPVDG--YFGPS-TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 55-82 8.04e-03

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 34.50  E-value: 8.04e-03
                         10        20
                 ....*....|....*....|....*...
gi 442535505  55 EALRAFQEASELPVSGQLDDATRARMRQ 82
Cdd:COG3409   42 AAVRAFQRANGLPVDGIVGPATWAALRA 69
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-174 5.75e-27

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: 103.05  E-value: 5.75e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442535505 103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGA-ADIRLSFhGRQSSYCSNTFDGPG 174
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISF-ARGNHGDGYPFDGPG 72
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-174 1.07e-24

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: 97.30  E-value: 1.07e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442535505  103 RWRKKHLTFRILNLPSTLPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSFhGRQSSYCSNTFDGPG 174
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGF-GRGDHGDGYPFDGPG 71
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-80 3.87e-06

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: 43.27  E-value: 3.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442535505   31 YLSQYGYLQKPLEGsnNFKPEdITEALRAFQEASELPVSGQLDDATRARM 80
Cdd:pfam01471  11 YLNRLGYYPGPVDG--YFGPS-TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 104-158 3.11e-03

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 38.13  E-value: 3.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442535505 104 WRKKHlTFRILNLPStlPPHTARAALRQAFQDWSNVAPLTFQEVQAGAADIRLSF 158
Cdd:cd04327    3 WRNGT-VLRIAFLGG--PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF 54
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 55-82 8.04e-03

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 34.50  E-value: 8.04e-03
                         10        20
                 ....*....|....*....|....*...
gi 442535505  55 EALRAFQEASELPVSGQLDDATRARMRQ 82
Cdd:COG3409   42 AAVRAFQRANGLPVDGIVGPATWAALRA 69
 
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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