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Conserved domains on  [gi|194373559|dbj|BAG56875|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 super family cl37987
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-167 3.39e-25

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


The actual alignment was detected with superfamily member pfam00413:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 95.38  E-value: 3.39e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194373559  103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWDKEIPLHFRKVVWGTADIMIGFARGGKKDSC 167
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGY 65
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-82 6.63e-10

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: 52.52  E-value: 6.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194373559   31 QWEQAQDYLKRFYLYDSE--TKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIM 82
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPvdGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-167 3.39e-25

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: 95.38  E-value: 3.39e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194373559  103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWDKEIPLHFRKVVWGTADIMIGFARGGKKDSC 167
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGY 65
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-168 3.04e-21

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: 85.33  E-value: 3.04e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194373559 103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWDKEIPLHFRKVVWG-TADIMIGFARGGKKDSCR 168
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYP 67
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-82 6.63e-10

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: 52.52  E-value: 6.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194373559   31 QWEQAQDYLKRFYLYDSE--TKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIM 82
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPvdGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 100-161 1.73e-08

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: 51.20  E-value: 1.73e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194373559   100 NSPKWTSKVVTYRIvsYTRDLPHiTVDRLVSKALNMWDKEIPLHFRKVVwGTADIMIGFARG 161
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSG 58
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 103-167 3.39e-25

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: 95.38  E-value: 3.39e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194373559  103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWDKEIPLHFRKVVWGTADIMIGFARGGKKDSC 167
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGY 65
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 103-168 3.04e-21

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: 85.33  E-value: 3.04e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194373559 103 KWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWDKEIPLHFRKVVWG-TADIMIGFARGGKKDSCR 168
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYP 67
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-82 6.63e-10

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: 52.52  E-value: 6.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 194373559   31 QWEQAQDYLKRFYLYDSE--TKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIM 82
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPvdGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 100-161 1.73e-08

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: 51.20  E-value: 1.73e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194373559   100 NSPKWTSKVVTYRIvsYTRDLPHiTVDRLVSKALNMWDKEIPLHFRKVVwGTADIMIGFARG 161
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSG 58
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 107-168 2.55e-06

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: 45.59  E-value: 2.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194373559 107 KVVTYRIVSYTR----DLPHITVDRLVSKALNMWDKEIPLHFRKVVWG--TADIMIGFARGGKKDSCR 168
Cdd:cd00203    1 KVIPYVVVADDRdveeENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQDFDGGTG 68
 
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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