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Conserved domains on  [gi|1862719266|ref|NP_001371668|]
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archaemetzincin-1 isoform 4 [Homo sapiens]

Protein Classification

archaemetzincin( domain architecture ID 10183538)

archaemetzincin is an M54 family zinc-dependent aminopeptidase, similar to human archaemetzincin-1 that exhibits aminopeptidase activity against neurogranin in vitro

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 95-282 1.03e-30

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


:

Pssm-ID: 213029  Cd Length: 173  Bit Score: 117.01  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862719266  95 HIYLQPIDlseePVGSSLLHQLCSCTEAFFlGLRVKCLPSVaaaSIRCSSRPsrDSDRLQLHTDGILSFLKNNKPGDALC 174
Cdd:cd11375     1 KIYLVPIG----SVDPDLLDELKERLSAFF-GLPVEVLPSI---PVPPLEAY--NPSRGQYLADDILDALLKLKPPDADC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862719266 175 VLGLTLSDLYPHEaWSFTFSKFLPGHEVGVCSFARFSGEFPKSGPSAPDL---ALVEAAAdgpEaplqdrgwaLCfSALG 251
Cdd:cd11375    71 VLGVTDVDLYEPG-LNFVFGLADGGSGVAVVSTARLRPEFYGLPPDEGLFlerLLKEAVH---E---------LG-HLFG 136

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1862719266 252 MVQC----C--KGALSLDEALRRPLDLCPICLRKLQH 282
Cdd:cd11375   137 LDHCpyyaCvmNFSNSLEETDRKPPYLCPVCLRKLQR 173
 
Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 95-282 1.03e-30

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 117.01  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862719266  95 HIYLQPIDlseePVGSSLLHQLCSCTEAFFlGLRVKCLPSVaaaSIRCSSRPsrDSDRLQLHTDGILSFLKNNKPGDALC 174
Cdd:cd11375     1 KIYLVPIG----SVDPDLLDELKERLSAFF-GLPVEVLPSI---PVPPLEAY--NPSRGQYLADDILDALLKLKPPDADC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862719266 175 VLGLTLSDLYPHEaWSFTFSKFLPGHEVGVCSFARFSGEFPKSGPSAPDL---ALVEAAAdgpEaplqdrgwaLCfSALG 251
Cdd:cd11375    71 VLGVTDVDLYEPG-LNFVFGLADGGSGVAVVSTARLRPEFYGLPPDEGLFlerLLKEAVH---E---------LG-HLFG 136

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1862719266 252 MVQC----C--KGALSLDEALRRPLDLCPICLRKLQH 282
Cdd:cd11375   137 LDHCpyyaCvmNFSNSLEETDRKPPYLCPVCLRKLQR 173
 
Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 95-282 1.03e-30

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 117.01  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862719266  95 HIYLQPIDlseePVGSSLLHQLCSCTEAFFlGLRVKCLPSVaaaSIRCSSRPsrDSDRLQLHTDGILSFLKNNKPGDALC 174
Cdd:cd11375     1 KIYLVPIG----SVDPDLLDELKERLSAFF-GLPVEVLPSI---PVPPLEAY--NPSRGQYLADDILDALLKLKPPDADC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862719266 175 VLGLTLSDLYPHEaWSFTFSKFLPGHEVGVCSFARFSGEFPKSGPSAPDL---ALVEAAAdgpEaplqdrgwaLCfSALG 251
Cdd:cd11375    71 VLGVTDVDLYEPG-LNFVFGLADGGSGVAVVSTARLRPEFYGLPPDEGLFlerLLKEAVH---E---------LG-HLFG 136

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1862719266 252 MVQC----C--KGALSLDEALRRPLDLCPICLRKLQH 282
Cdd:cd11375   137 LDHCpyyaCvmNFSNSLEETDRKPPYLCPVCLRKLQR 173
 
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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