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Conserved domains on  [gi|2737752488|ref|WP_347879226|]
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M35 family metallo-endopeptidase [Burkholderia sp. BCC0405]

Protein Classification

M35_like_1 domain-containing protein( domain architecture ID 10181111)

M35_like_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M35_like_1 cd11007
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar ...
 1-115 1.17e-30

Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar to the M35 Zn2+-metallopeptidases, also known as the deuterolysin family, presumably these are bacterial metalloendopeptidases that have yet to be characterized. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand; however, members of this family do not contain the GTXDXXYG motif C-terminal to the His zinc ligands that is typical for the M35 proteases. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Many members of the M35 peptidases display unusual thermostabilities.


:

Pssm-ID: 199913  Cd Length: 183  Bit Score: 107.54  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737752488   1 MRSFNEKNVVRTGSAADlATGCTPNPvgTDGEAAHVCAPDTtthtIAISVRFCTMRPWTANA----DSHVSTIIHEATHF 76
Cdd:cd11007    69 LNSLTPENFVRSDSEKD-TCGCVPND--GDGEAAFVCGPDT----ISIHVIFCELGAFFDAAsnglDSQASTIIHELSHF 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737752488  77 HDTMSSTDDQYTIT--RFLPEWGRSHPALAINNADSIAGYV 115
Cdd:cd11007   142 EDTFGTDDHRYGDQglDPCAAAFRDNPDKAIENADSIAGYI 182
 
Name Accession Description Interval E-value
M35_like_1 cd11007
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar ...
 1-115 1.17e-30

Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar to the M35 Zn2+-metallopeptidases, also known as the deuterolysin family, presumably these are bacterial metalloendopeptidases that have yet to be characterized. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand; however, members of this family do not contain the GTXDXXYG motif C-terminal to the His zinc ligands that is typical for the M35 proteases. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Many members of the M35 peptidases display unusual thermostabilities.


Pssm-ID: 199913  Cd Length: 183  Bit Score: 107.54  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737752488   1 MRSFNEKNVVRTGSAADlATGCTPNPvgTDGEAAHVCAPDTtthtIAISVRFCTMRPWTANA----DSHVSTIIHEATHF 76
Cdd:cd11007    69 LNSLTPENFVRSDSEKD-TCGCVPND--GDGEAAFVCGPDT----ISIHVIFCELGAFFDAAsnglDSQASTIIHELSHF 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737752488  77 HDTMSSTDDQYTIT--RFLPEWGRSHPALAINNADSIAGYV 115
Cdd:cd11007   142 EDTFGTDDHRYGDQglDPCAAAFRDNPDKAIENADSIAGYI 182
 
Name Accession Description Interval E-value
M35_like_1 cd11007
Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar ...
 1-115 1.17e-30

Peptidase M35-like domain of uncharacterized proteins; This family contains proteins similar to the M35 Zn2+-metallopeptidases, also known as the deuterolysin family, presumably these are bacterial metalloendopeptidases that have yet to be characterized. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand; however, members of this family do not contain the GTXDXXYG motif C-terminal to the His zinc ligands that is typical for the M35 proteases. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Many members of the M35 peptidases display unusual thermostabilities.


Pssm-ID: 199913  Cd Length: 183  Bit Score: 107.54  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737752488   1 MRSFNEKNVVRTGSAADlATGCTPNPvgTDGEAAHVCAPDTtthtIAISVRFCTMRPWTANA----DSHVSTIIHEATHF 76
Cdd:cd11007    69 LNSLTPENFVRSDSEKD-TCGCVPND--GDGEAAFVCGPDT----ISIHVIFCELGAFFDAAsnglDSQASTIIHELSHF 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737752488  77 HDTMSSTDDQYTIT--RFLPEWGRSHPALAINNADSIAGYV 115
Cdd:cd11007   142 EDTFGTDDHRYGDQglDPCAAAFRDNPDKAIENADSIAGYI 182
M35_like cd11005
Peptidase M35 family; Family M35 Zn2+-metallopeptidase domain, also known as the deuterolysin ...
 21-115 7.97e-09

Peptidase M35 family; Family M35 Zn2+-metallopeptidase domain, also known as the deuterolysin family, contains fungal as well as bacterial metalloendopeptidases that include deuterolysin (EC2.4.24.39), peptidyl-Lys metalloendopeptidase (MEP), penicillolysin, as well as uncharacterized sequences. Typically, members of this family of extracellular peptidases contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG motif C-terminal to the His zinc ligands. Deuterolysins are highly active towards basic nuclear proteins such as histones and protamines, with a preference for a Lys or Arg residue in the P1' subsite. MEPs specifically cleave peptidyl-lysine bonds (-X-Lys-) in proteins and peptides. Penicillolysin, a thermolabile protease from Penicillium citrinum, strongly hydrolyzes nuclear proteins such as clupeine, salmine and histone. Many members of the M35 peptidases display unusual thermostabilities.


Pssm-ID: 199911  Cd Length: 167  Bit Score: 50.74  E-value: 7.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737752488  21 GCTPNpvgtdGEAAHVCAPdttthtIAISVRFCTMRpWTA---NADSHVSTIIHEATHFHDTMSSTDDQYTITRFLPEWg 97
Cdd:cd11005    82 GCVPN-----MEFAYVYPP------ISIAVYLCTNF-WGApptGADSQAGTVVHEVTHFVDTFGTGDLGYGQDAAAALA- 148

                          90
                  ....*....|....*...
gi 2737752488  98 RSHPALAINNADSIAGYV 115
Cdd:cd11005   149 AADPDKALNNADNHEYFA 166
M35_peptidyl-Lys cd11306
Peptidase M35 domain of peptidyl-Lys metalloendopeptidases; This family M35 Zn2 ...
 58-110 4.92e-03

Peptidase M35 domain of peptidyl-Lys metalloendopeptidases; This family M35 Zn2+-metallopeptidase extracellular domain is mostly found in proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20), including some well-characterized domains in Aeromonas salmonicida subsp. Achromogenes (AsaP1) and Grifola frondosa (GfMEP). These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response. Members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands.


Pssm-ID: 199915  Cd Length: 160  Bit Score: 34.73  E-value: 4.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2737752488  58 WTANA---DSHVSTIIHEATHFhDTMSSTDDQYTITRFLPEWGRSHPALAINNADS 110
Cdd:cd11306    99 WQAPTtgtDSKAGTLIHELSHF-TVVAGTDDHVYGQSGAKSLARSNPAQAINNADN 153
M35_peptidyl-Lys_like cd11006
Peptidase M35 domain of peptidyl-Lys metalloendopeptidases and related proteins; This family ...
 52-110 6.30e-03

Peptidase M35 domain of peptidyl-Lys metalloendopeptidases and related proteins; This family M35 Zn2+-metallopeptidase extracellular domain is mostly found in proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20), including some well-characterized domains in Aeromonas salmonicida subsp. Achromogenes (AsaP1) and Grifola frondosa (GfMEP). These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response. Members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands.


Pssm-ID: 199912  Cd Length: 163  Bit Score: 34.33  E-value: 6.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2737752488  52 FCTMRPWTANaDSHVSTIIHEATHFhDTMSSTDDQYTITRFLPEWGRSHPALAINNADS 110
Cdd:cd11006   100 FFQLPTRTGN-DSRAGTIVHELSHF-RGVAGTDDHCYGQANAQELALTDPEAAVENADS 156
 
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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