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Conserved domains on  [gi|1079707385|ref|NP_001333413|]
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archaemetzincin-2 isoform 3 [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 ...
69-263 8.09e-68

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: 209.85  E-value: 8.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385  69 ISEEYIKWLTGYCKAYFYgLRVKLLEPVPVSVTRCsfrvnENTHNLQIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRD 148
Cdd:cd11375    10 VDPDLLDELKERLSAFFG-LPVEVLPSIPVPPLEA-----YNPSRGQYLADDILDALLKLKPPDADCVLGVTDVDLYEPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 149 sWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysifdnyyiPEITSVLLLRSCKTLTHEIGHIFGL 228
Cdd:cd11375    84 -LNFVFGLADGGSGVAVVSTARLRPEFYGL-------------------------PPDEGLFLERLLKEAVHELGHLFGL 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1079707385 229 RHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 263
Cdd:cd11375   138 DHCPYYACVMNFSNSLEETDRKPPYLCPVCLRKLQ 172
 
Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
69-263 8.09e-68

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: 209.85  E-value: 8.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385  69 ISEEYIKWLTGYCKAYFYgLRVKLLEPVPVSVTRCsfrvnENTHNLQIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRD 148
Cdd:cd11375    10 VDPDLLDELKERLSAFFG-LPVEVLPSIPVPPLEA-----YNPSRGQYLADDILDALLKLKPPDADCVLGVTDVDLYEPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 149 sWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysifdnyyiPEITSVLLLRSCKTLTHEIGHIFGL 228
Cdd:cd11375    84 -LNFVFGLADGGSGVAVVSTARLRPEFYGL-------------------------PPDEGLFLERLLKEAVHELGHLFGL 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1079707385 229 RHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 263
Cdd:cd11375   138 DHCPYYACVMNFSNSLEETDRKPPYLCPVCLRKLQ 172
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
85-263 2.20e-39

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 136.63  E-value: 2.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385  85 FYGLRVKLLEPVPVSVTRCSFRVNenthnlQIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVG 164
Cdd:COG1913    26 VFGLPVEVLPPLPLPLEAYDPERG------QYDAEALLDFLSRLKEEDGDKVLGVTDVDLYAPG-LNFVFGLAYLGGRVA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 165 IFSFARYGSDFYSMhykgkvkklkktsSSDYSIFdnyyipeitsvlLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHL 244
Cdd:COG1913    99 VVSTARLRPEFYGL-------------PPDEELF------------LERVLKEAVHELGHLFGLGHCPNPRCVMHFSNSL 153
                         170
                  ....*....|....*....
gi 1079707385 245 EEADRRPLNLCPICLHKLQ 263
Cdd:COG1913   154 EELDRKPPSFCPSCRRKLR 172
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
115-262 1.57e-24

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 97.69  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 115 QIHAGDILKFLKKKKPEDAFCVVGITMIDLYpRDSWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssd 194
Cdd:NF033823   49 QYRADAILDYLLRIRVGGADKVLGVTDVDLY-EPGLNFVFGLAYPGGKVAVVSTARLRNEFYGR---------------- 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079707385 195 ysifdnyyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 262
Cdd:NF033823  112 ---------EPDEDLFLERLAKEAVHELGHLLGLGHCPNPRCVMHFSNSLDDTDRKSKYFCPSCRRKL 170
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
115-262 6.04e-18

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 80.07  E-value: 6.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 115 QIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRdSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktSSSD 194
Cdd:PRK13267   52 QYRAEKFLPLLSRIGRFNGDKNIGITDCDLYYR-GLNFVFGLAYPNLRGAVISTYRLRPEFYG-------------NKPD 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079707385 195 YSIFDNyyipeitsvlllRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 262
Cdd:PRK13267  118 SELFEE------------RVRKEVTHELGHTLGLEHCDNPRCVMNFSNSVRDVDIKEPNFCGSCQRKL 173
Peptidase_M54 pfam07998
Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been ...
136-263 8.20e-13

Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been reported to degrade synthetic substrates and peptides.


Pssm-ID: 191923  Cd Length: 176  Bit Score: 65.59  E-value: 8.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 136 VVGITMIDLYPrDSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktssSDYSIFdnyyipeitsvlLLRSC 215
Cdd:pfam07998  76 ILPLGSRDQYF-DGYNFVFGIQVSIGNYAVLALSRLIKPFYT---------------EDRELF------------IERVV 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1079707385 216 KTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 263
Cdd:pfam07998 128 KEVTHELGHTYGLSHCNNTDCVMNFSNSLKDVDRKAPTFCNNCLRKLK 175
 
Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
69-263 8.09e-68

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: 209.85  E-value: 8.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385  69 ISEEYIKWLTGYCKAYFYgLRVKLLEPVPVSVTRCsfrvnENTHNLQIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRD 148
Cdd:cd11375    10 VDPDLLDELKERLSAFFG-LPVEVLPSIPVPPLEA-----YNPSRGQYLADDILDALLKLKPPDADCVLGVTDVDLYEPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 149 sWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysifdnyyiPEITSVLLLRSCKTLTHEIGHIFGL 228
Cdd:cd11375    84 -LNFVFGLADGGSGVAVVSTARLRPEFYGL-------------------------PPDEGLFLERLLKEAVHELGHLFGL 137
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1079707385 229 RHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 263
Cdd:cd11375   138 DHCPYYACVMNFSNSLEETDRKPPYLCPVCLRKLQ 172
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
85-263 2.20e-39

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 136.63  E-value: 2.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385  85 FYGLRVKLLEPVPVSVTRCSFRVNenthnlQIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVG 164
Cdd:COG1913    26 VFGLPVEVLPPLPLPLEAYDPERG------QYDAEALLDFLSRLKEEDGDKVLGVTDVDLYAPG-LNFVFGLAYLGGRVA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 165 IFSFARYGSDFYSMhykgkvkklkktsSSDYSIFdnyyipeitsvlLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHL 244
Cdd:COG1913    99 VVSTARLRPEFYGL-------------PPDEELF------------LERVLKEAVHELGHLFGLGHCPNPRCVMHFSNSL 153
                         170
                  ....*....|....*....
gi 1079707385 245 EEADRRPLNLCPICLHKLQ 263
Cdd:COG1913   154 EELDRKPPSFCPSCRRKLR 172
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
115-262 1.57e-24

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 97.69  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 115 QIHAGDILKFLKKKKPEDAFCVVGITMIDLYpRDSWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssd 194
Cdd:NF033823   49 QYRADAILDYLLRIRVGGADKVLGVTDVDLY-EPGLNFVFGLAYPGGKVAVVSTARLRNEFYGR---------------- 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079707385 195 ysifdnyyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 262
Cdd:NF033823  112 ---------EPDEDLFLERLAKEAVHELGHLLGLGHCPNPRCVMHFSNSLDDTDRKSKYFCPSCRRKL 170
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
115-262 6.04e-18

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 80.07  E-value: 6.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 115 QIHAGDILKFLKKKKPEDAFCVVGITMIDLYPRdSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktSSSD 194
Cdd:PRK13267   52 QYRAEKFLPLLSRIGRFNGDKNIGITDCDLYYR-GLNFVFGLAYPNLRGAVISTYRLRPEFYG-------------NKPD 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079707385 195 YSIFDNyyipeitsvlllRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 262
Cdd:PRK13267  118 SELFEE------------RVRKEVTHELGHTLGLEHCDNPRCVMNFSNSVRDVDIKEPNFCGSCQRKL 173
Peptidase_M54 pfam07998
Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been ...
136-263 8.20e-13

Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been reported to degrade synthetic substrates and peptides.


Pssm-ID: 191923  Cd Length: 176  Bit Score: 65.59  E-value: 8.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079707385 136 VVGITMIDLYPrDSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktssSDYSIFdnyyipeitsvlLLRSC 215
Cdd:pfam07998  76 ILPLGSRDQYF-DGYNFVFGIQVSIGNYAVLALSRLIKPFYT---------------EDRELF------------IERVV 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1079707385 216 KTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 263
Cdd:pfam07998 128 KEVTHELGHTYGLSHCNNTDCVMNFSNSLKDVDRKAPTFCNNCLRKLK 175
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
216-230 6.49e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 37.32  E-value: 6.49e-03
                          10
                  ....*....|....*
gi 1079707385 216 KTLTHEIGHIFGLRH 230
Cdd:cd04275   139 DTATHEVGHWLGLYH 153
 
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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