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Conserved domains on  [gi|637155854|ref|WP_024423288|]
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MULTISPECIES: zinc metallopeptidase [Bacillus]

Protein Classification

zinc metallopeptidase( domain architecture ID 10006578)

zinc metallopeptidase similar to Bacillus subtilis membrane protease YugP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YugP COG2738
Zn-dependent membrane protease YugP [Posttranslational modification, protein turnover, ...
1-223 5.84e-113

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


:

Pssm-ID: 442040  Cd Length: 226  Bit Score: 322.43  E-value: 5.84e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854   1 MFF---YFLTFAALGLSFWAQFKVKNNFEKYSKVEASSMKTGAETARYILDRNGLYDVPVEPVRGTLTDHYDPTQRVVRL 77
Cdd:COG2738    1 MFFdpyIILLIPALLLSLWAQAKVKSTFKKYSKVPSSSGLTGAEVARKMLDDNGLYDVRVESVPGQLTDHYDPRNKVVRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854  78 SEPVYYGHSISAISVASHEVGHALQHQESYGALVLRHKIFPVVNFASGVAPLLFLGGILLSSLNLIGLGIILFSAAVFFQ 157
Cdd:COG2738   81 SEDVYNGRSVAAAAVAAHEVGHAIQHAEGYAPLKLRSALVPVANFGSNLSWILILIGLLLGSPGLLLIGIILFAAAVLFQ 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637155854 158 LVTLPVEFNASSRAKDIIVSEGIIRSSEERGVNKVLNAAALTYVAAALVSLFELLRFVMIFLNGRN 223
Cdd:COG2738  161 LVTLPVEFDASRRALAWLESGGILTQEELPGAKKVLNAAALTYVAAALVALLQLLRLLLIFGGRRD 226
 
Name Accession Description Interval E-value
YugP COG2738
Zn-dependent membrane protease YugP [Posttranslational modification, protein turnover, ...
1-223 5.84e-113

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


Pssm-ID: 442040  Cd Length: 226  Bit Score: 322.43  E-value: 5.84e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854   1 MFF---YFLTFAALGLSFWAQFKVKNNFEKYSKVEASSMKTGAETARYILDRNGLYDVPVEPVRGTLTDHYDPTQRVVRL 77
Cdd:COG2738    1 MFFdpyIILLIPALLLSLWAQAKVKSTFKKYSKVPSSSGLTGAEVARKMLDDNGLYDVRVESVPGQLTDHYDPRNKVVRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854  78 SEPVYYGHSISAISVASHEVGHALQHQESYGALVLRHKIFPVVNFASGVAPLLFLGGILLSSLNLIGLGIILFSAAVFFQ 157
Cdd:COG2738   81 SEDVYNGRSVAAAAVAAHEVGHAIQHAEGYAPLKLRSALVPVANFGSNLSWILILIGLLLGSPGLLLIGIILFAAAVLFQ 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637155854 158 LVTLPVEFNASSRAKDIIVSEGIIRSSEERGVNKVLNAAALTYVAAALVSLFELLRFVMIFLNGRN 223
Cdd:COG2738  161 LVTLPVEFDASRRALAWLESGGILTQEELPGAKKVLNAAALTYVAAALVALLQLLRLLLIFGGRRD 226
Zn_peptidase_2 pfam04298
Putative neutral zinc metallopeptidase; Zinc metallopeptidase zinc binding regions have been ...
4-218 1.22e-104

Putative neutral zinc metallopeptidase; Zinc metallopeptidase zinc binding regions have been predicted in some family members by a pattern match (Prosite:PS00142), of the characteriztic HEXXH motif.


Pssm-ID: 461253  Cd Length: 217  Bit Score: 300.86  E-value: 1.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854    4 YFLTFAALGLSFWAQFKVKNNFEKYSKVEASSMKTGAETARYILDRNGLYDVPVEPVRGTLTDHYDPTQRVVRLSEPVYY 83
Cdd:pfam04298   1 YILVIPALLLSLWAQLKVKSTFKKYSKVRSSSGLTGAEVARRILDDNGLYDVRVERVPGNLTDHYDPRNKVVRLSESVYN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854   84 GHSISAISVASHEVGHALQHQESYGALVLRHKIFPVVNFASGVAPLLFLGGILLSSLN-LIGLGIILFSAAVFFQLVTLP 162
Cdd:pfam04298  81 GRSVAAVAVAAHEVGHAIQHAEGYAPLKLRSALVPVANFGSNLSWPLLLIGLLLGATGlLLLLGIILFAAAVLFQLVTLP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 637155854  163 VEFNASSRAKDIIVSEGIIRSSEERGVNKVLNAAALTYVAAALVSLFELLRFVMIF 218
Cdd:pfam04298 161 VEFDASRRALAILEEGGILSGDELRGAKKVLRAAALTYVAAALSSLLQLLRLLLIF 216
 
Name Accession Description Interval E-value
YugP COG2738
Zn-dependent membrane protease YugP [Posttranslational modification, protein turnover, ...
1-223 5.84e-113

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


Pssm-ID: 442040  Cd Length: 226  Bit Score: 322.43  E-value: 5.84e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854   1 MFF---YFLTFAALGLSFWAQFKVKNNFEKYSKVEASSMKTGAETARYILDRNGLYDVPVEPVRGTLTDHYDPTQRVVRL 77
Cdd:COG2738    1 MFFdpyIILLIPALLLSLWAQAKVKSTFKKYSKVPSSSGLTGAEVARKMLDDNGLYDVRVESVPGQLTDHYDPRNKVVRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854  78 SEPVYYGHSISAISVASHEVGHALQHQESYGALVLRHKIFPVVNFASGVAPLLFLGGILLSSLNLIGLGIILFSAAVFFQ 157
Cdd:COG2738   81 SEDVYNGRSVAAAAVAAHEVGHAIQHAEGYAPLKLRSALVPVANFGSNLSWILILIGLLLGSPGLLLIGIILFAAAVLFQ 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 637155854 158 LVTLPVEFNASSRAKDIIVSEGIIRSSEERGVNKVLNAAALTYVAAALVSLFELLRFVMIFLNGRN 223
Cdd:COG2738  161 LVTLPVEFDASRRALAWLESGGILTQEELPGAKKVLNAAALTYVAAALVALLQLLRLLLIFGGRRD 226
Zn_peptidase_2 pfam04298
Putative neutral zinc metallopeptidase; Zinc metallopeptidase zinc binding regions have been ...
4-218 1.22e-104

Putative neutral zinc metallopeptidase; Zinc metallopeptidase zinc binding regions have been predicted in some family members by a pattern match (Prosite:PS00142), of the characteriztic HEXXH motif.


Pssm-ID: 461253  Cd Length: 217  Bit Score: 300.86  E-value: 1.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854    4 YFLTFAALGLSFWAQFKVKNNFEKYSKVEASSMKTGAETARYILDRNGLYDVPVEPVRGTLTDHYDPTQRVVRLSEPVYY 83
Cdd:pfam04298   1 YILVIPALLLSLWAQLKVKSTFKKYSKVRSSSGLTGAEVARRILDDNGLYDVRVERVPGNLTDHYDPRNKVVRLSESVYN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637155854   84 GHSISAISVASHEVGHALQHQESYGALVLRHKIFPVVNFASGVAPLLFLGGILLSSLN-LIGLGIILFSAAVFFQLVTLP 162
Cdd:pfam04298  81 GRSVAAVAVAAHEVGHAIQHAEGYAPLKLRSALVPVANFGSNLSWPLLLIGLLLGATGlLLLLGIILFAAAVLFQLVTLP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 637155854  163 VEFNASSRAKDIIVSEGIIRSSEERGVNKVLNAAALTYVAAALVSLFELLRFVMIF 218
Cdd:pfam04298 161 VEFDASRRALAILEEGGILSGDELRGAKKVLRAAALTYVAAALSSLLQLLRLLLIF 216
 
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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