1H8L,1UWY,2NSM,1QMU,3MN8


Conserved Protein Domain Family
M14_CP_N-E_like

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cd03858: M14_CP_N-E_like (this model, PSSM-Id:199842 is obsolete and has been replaced by 349431)
Click on image for an interactive view with Cn3D
Peptidase M14 carboxypeptidase subfamily N/E-like
Carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.
Statistics
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PSSM-Id: 199842
View PSSM: cd03858
Aligned: 34 rows
Threshold Bit Score: 385.792
Threshold Setting Gi: 115502368
Created: 18-Oct-2005
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteactive site
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Metallocarboxypeptidases share the zinc binding motif HXXE...H, where the zinc ion is penta-coordinated to ND1 atoms of the histidines, OE1 and OE2 atoms of the glutamic acid, and to a water molecule in a slightly distorted tetrahedral manner.
  • Structure:1QMU_A: duck carboxypeptidase D; contacts at 3.5A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                      #  #              
1H8L_A        10 HHHFsDMEIFLRRYANEYPs-ITRLYSVGKSvELRELYVMEISDNPGIHEaGEPEFKYIGNMHGNEVVGRELLLNLIEYL 88   crested duck
1UWY_A         5 YHRQeGMEAFLKTVAQNYSs-VTHLHSIGKSvKGRNLWVLVVGRFPKEHRiGIPEFKYVANMHGDETVGRELLLHLIDYL 83   human
1QMU_A        10 HHHFsDMEIFLRRYANEYPs-ITRLYSVGKSvELRELYVMEISDNPGIHEaGEPEFKYIGNMHGNEVVGRELLLNLIEYL 88   crested duck
3MN8_A        40 YASQeQLEDLFAGLEKAYPn-QAKVHFLGRSlEGRNLLALQISRNTRSRNlLTPPVKYIANMHGDETVGRQLLVYMAQYL 118  fruit fly
EDQ80213       1 YKSNlELEVALKNFTRRCRh-ISRLYTIGNStLGVPLWALEISDKPGVSE-PEPAFKYVGNMHGDEPLGRELVLLLSDWL 78   Physcomitrella...
CAO81643      97 YYTLtEYQNFMQQTADQYPn-ICQLVQFGTSvQNRPLLMLKISDNVTIEE-NEPELKYFGSIHGDEVVGYDMLIRLIQLL 174  Candidatus Clo...
XP_002117288  25 YHHYpEMIAFMRQTQAKYPs-ITYLYNLGKSvQNRDLLVIAIGEQPNVHTpGRPEFKYVGNMHGNEVVGREMLIHLIDLL 103  Trichoplax adh...
XP_002108045  21 YHHYqEMLTFLQSLQHQHPs-ISHLYDIGRSvQGRRLLVLAIGINPNQHVpGRPEFKYVANMHGNEAVGREMLLHLAKYL 99   Trichoplax adh...
XP_002117289   2 YHNYtSMTALLQDLNQKYSh-LTKLYSIGKSvDGRDLNVLAISANPDRHVpGQPEFKYVGNMHGNEVIGRELLLYLSVHL 80   Trichoplax adh...
XP_001812199  24 YHNNtELEKYLKNFTATTRgiKTRLYSIGKS-TKNNDLWVVRLTAAKESKlGVPNIKLIGTVHGNEPVGREILLHFMEFL 102  red flour beetle
Feature 1                                                                                        
1H8L_A        89 CKNFg-tDPEVTDLVQsTRIHIMPSMNPDGYEksqegd---rggtvGRNNs-NNYDLNRNFPDqffqv------tdppQP 157  crested duck
1UWY_A        84 VTSDg-kDPEITNLINsTRIHIMPSMNPDGFEavkkpd---cyysiGRENy-NQYDLNRNFPDafeyn------nvsrQP 152  human
1QMU_A        89 CKNFg-tDPEVTDLVQsTRIHIMPSMNPDGYEksqegd---rggtvGRNNs-NNYDLNRNFPDqffqv------tdppQP 157  crested duck
3MN8_A       119 LGNHe-rISDLGQLVNsTDIYLVPTMNPDGYAlsqegnceslpnyvGRGNa-ANIDLNRDFPDrleqshvhqlraqsrQP 196  fruit fly
EDQ80213      79 CDNYk-kDPMATLIVDkLHLHLLPTMNPDGFAaqk--------pgpTRNNa-HDVDLNRDFPDqffpqn---nneekrQA 145  Physcomitrella...
CAO81643     175 TTQYg-iDPRITNMVNnTEIWINPMLNPDGYAa------------gIRYNa-NGIDLNRNFPMptgvqh---pdggpwAA 237  Candidatus Clo...
XP_002117288 104 VEGYtnnDAEIRNLLKtTRIHILPSMNPDGFEasyegn---ctgviGRRNa-NNVDLNRNFPDrfvai------ntpiQP 173  Trichoplax adh...
XP_002108045 100 LNHYn-iIDDITQLLNtTRIHIMPSMNPDGFEiavqgh---ctgtqGRYNa-NYKDLNRNFDDpyler------kesvQP 168  Trichoplax adh...
XP_002117289  81 LESYg-tDNEITWLLDnTRIHILPSMNPDGFEmsyegn---ctgvlGRYNr-NGVDLNRNFPDqyipvk---nlshplQP 152  Trichoplax adh...
XP_001812199 103 RANYr-tDPKITWLLDnTKIHFLPNLNPDGFAlasenm---cegeyGRNNalRGMDLNRNFPDyfrtn------ripeAP 172  red flour beetle
Feature 1                            #                                                           
1H8L_A       158 ETLAVMSWLKTyPFVLSANLHGGsLVVNYPFDddeqg----iaiySKSPDDAVFQQLALSYSKENKKMYQGspckdlypt 233  crested duck
1UWY_A       153 ETVAVMKWLKTeTFVLSANLHGGaLVASYPFDngvqat-galysrSLTPDDDVFQYLAHTYASRNPNMKKGdeck---nk 228  human
1QMU_A       158 ETLAVMSWLKTyPFVLSANLHGGsLVVNYPFDddeqg----iaiySKSPDDAVFQQLALSYSKENKKMYQGspckdlypt 233  crested duck
3MN8_A       197 ETAALVNWIVSkPFVLSANFHGGaVVASYPYDnslahn--ecceeSLTPDDRVFKQLAHTYSDNHPIMRKGnnc-----n 269  fruit fly
EDQ80213     146 ETRSVMNWIRSsRFTASASFHEGaLVANYPYDgtpdi----stkyAPSPDDSTFKYLAGVYAGNHPLMLKSk-------- 213  Physcomitrella...
CAO81643     238 ETIAVMDFSNAhDFDLALNFHGGsLVINYPWDyt----------tTLTPDNDLLIEMALTYSRENLPMYNSt-------- 299  Candidatus Clo...
XP_002117288 174 ETQAIITWLKQeHFVLSANLHGGtVVANYPYDslapsv-tprntySMAPDDDILIQISKAYSDNHGYMHIGrpncssspn 252  Trichoplax adh...
XP_002108045 169 EVSAIMDWIKKiPFVLSANLHGGtLVANYPYDsvkphl-ihqniySRSPDDDVFIQLSKVYANNHLLMHYGqpncsdnps 247  Trichoplax adh...
XP_002117289 153 ETIAVMQWIQSlPFVLSANLHGGtVVTVYPYDnlpsny-tdrttyNRCPDDELYRTISKIYSYAHPTMHIGmpnctvndt 231  Trichoplax adh...
XP_001812199 173 ETKAVKKWLREvPFILSAALHGGaLVANYPFDtvqeltsfdtyppSETPDNDVFVHLAGVYARNHLKMHKGdacn---kf 249  red flour beetle
Feature 1                                                                         
1H8L_A       234 eYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCvKYPKAEELPKYWEQNRRSLLQFIKQ 298  crested duck
1UWY_A       229 mNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCcKYPREEKLPSFWNNNKASLIEYIKQ 293  human
1QMU_A       234 eYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCvKYPKAEELPKYWEQNRRSLLQFIKQ 298  crested duck
3MN8_A       270 dSFSGGITNGAHWYELSGGMQDFNYAFSNCFELTIELSCcKYPAASTLPQEWQRNKASLLQLLRQ 334  fruit fly
EDQ80213     214 -EFTGGITNGAHWYPLYGGMQDWNYLHGNCMELTLEMNEnKWPPPDQVPRIWGEHRKSMLELAAA 277  Physcomitrella patens subsp. ...
CAO81643     300 -EFLHGIVNGAAWYIVTGSMQDWNYHYTDCIEMTAEISNnKWPPASTLDTYWNENREAMLKYIEF 363  Candidatus Cloacamonas acidam...
XP_002117288 253 eYFADGITNGAAWYSIDGGMQDYNYVDSECFEVTLEISCcKYPTADQLPFFWQANKNALMAYMKS 317  Trichoplax adhaerens
XP_002108045 248 eQFPNGIVNGAKYYPIFGGMQDYVYLNSNGMEITLELGCcKYPNSKQLPELWQENRPALIAYIQA 312  Trichoplax adhaerens
XP_002117289 232 eYFKDGIINGAAWYAIQGSMQDYNYLQSNCFETTIEVSCcKYPTSDQLPQFWQRNQKSLIQYIKA 296  Trichoplax adhaerens
XP_001812199 250 qKFQGGIVNGAAWYPITGGMQDYNYAFHGCMEITLEISCcKYPSAEDLPQFWEENRMALLNYCVE 314  red flour beetle

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