M14 family of metallocarboxypeptidases and related proteins; The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (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. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVS---FKANNPGVFIEGGIHAREWISTATVMYILHKLLKS 140
Cdd:cd03860    1 YHPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWgsgGKGGKPAIVIHGGQHAREWISTSTVEYLAHQLLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 141 --DNPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQYSF-FCYGSDPNRNWGYKWNTGGASNSACSETYAGSA 217
Cdd:cd03860   81 ygSDATITALLDKFDFYIIPVVNPDGYVYTWTTDRLWRKNRQPTGGsSCVGIDLNRNWGYKWGGPGASTNPCSETYRGPS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332031880 218 PFSEIETKTLSKYIDSISD--KLYAYIAFHSYSQLLLIPYGHT-TAHLDNYDDLVS 270
Cdd:cd03860  161 AFSAPETKALADFINALAAgqGIKGFIDLHSYSQLILYPYGYScDAVPPDLENLME 216

Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVS---FKANNPGVFIEGGIHAREWISTATVMYILHKLLKS 140
Cdd:cd03860    1 YHPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWgsgGKGGKPAIVIHGGQHAREWISTSTVEYLAHQLLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 141 --DNPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQYSF-FCYGSDPNRNWGYKWNTGGASNSACSETYAGSA 217
Cdd:cd03860   81 ygSDATITALLDKFDFYIIPVVNPDGYVYTWTTDRLWRKNRQPTGGsSCVGIDLNRNWGYKWGGPGASTNPCSETYRGPS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332031880 218 PFSEIETKTLSKYIDSISD--KLYAYIAFHSYSQLLLIPYGHT-TAHLDNYDDLVS 270
Cdd:cd03860  161 AFSAPETKALADFINALAAgqGIKGFIDLHSYSQLILYPYGYScDAVPPDLENLME 216

Zinc carboxypeptidase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880   70 INKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSFKA-----NNPGVFIEGGIHAREWISTATVMYILHKLLKS--DN 142
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPgehnpGKPAVFIDGGIHAREWIGPATALYLIHQLLTNygRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  143 PEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQY-SFFCYGSDPNRNWGYKWNTGGASNSACSETYAGSAPFSE 221
Cdd:pfam00246  81 PEITELLDDTDIYILPVVNPDGYEYTHTTDRLWRKNRSNAnGSSCIGVDLNRNFPDHWNEVGASSNPCSETYRGPAPFSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332031880  222 IETKTLSKYIDSIsDKLYAYIAFHSYSQLLLIPYGHT-TAHLDNYDDLVSI 271
Cdd:pfam00246 161 PETRAVADFIRSK-KPFVLYISLHSYSQVLLYPYGYTrDEPPPDDEELKSL 210

Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 332031880    1 FSYWIAP-FANKQAELMIAPHKLPEFYEMMKQMQIPYTVFIENVQTLINR 49
Cdd:pfam02244  23 LDFWKPPsKVGKPVDVMVPPSKLEAFEELLEKHGISYEVLIEDVQELIDE 72

Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVS---FKANNPGVFIEGGIHAREWISTATVMYILHKLLKS 140
Cdd:cd03860    1 YHPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWgsgGKGGKPAIVIHGGQHAREWISTSTVEYLAHQLLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 141 --DNPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQYSF-FCYGSDPNRNWGYKWNTGGASNSACSETYAGSA 217
Cdd:cd03860   81 ygSDATITALLDKFDFYIIPVVNPDGYVYTWTTDRLWRKNRQPTGGsSCVGIDLNRNWGYKWGGPGASTNPCSETYRGPS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332031880 218 PFSEIETKTLSKYIDSISD--KLYAYIAFHSYSQLLLIPYGHT-TAHLDNYDDLVS 270
Cdd:cd03860  161 AFSAPETKALADFINALAAgqGIKGFIDLHSYSQLILYPYGYScDAVPPDLENLME 216

Zinc carboxypeptidase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880   70 INKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSFKA-----NNPGVFIEGGIHAREWISTATVMYILHKLLKS--DN 142
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPgehnpGKPAVFIDGGIHAREWIGPATALYLIHQLLTNygRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  143 PEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQY-SFFCYGSDPNRNWGYKWNTGGASNSACSETYAGSAPFSE 221
Cdd:pfam00246  81 PEITELLDDTDIYILPVVNPDGYEYTHTTDRLWRKNRSNAnGSSCIGVDLNRNFPDHWNEVGASSNPCSETYRGPAPFSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332031880  222 IETKTLSKYIDSIsDKLYAYIAFHSYSQLLLIPYGHT-TAHLDNYDDLVSI 271
Cdd:pfam00246 161 PETRAVADFIRSK-KPFVLYISLHSYSQVLLYPYGYTrDEPPPDDEELKSL 210

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B subgroup; Peptidase M14 Carboxypeptidase B (CPB) belongs to the carboxypeptidase A/B 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. Carboxypeptidase B (CPB) enzymes only cleave the basic residues lysine or arginine. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The procarboxypeptidase B (PCPB) is produced by the exocrine pancreas and stored as stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. PCPB has been reported to be a good serum marker for the diagnosis of acute pancreatitis and graft rejection in pancreas transplant recipients. this subfamily also includes thrombin activatable fibrinolysis inhibitor (TAFIa), a carboxypeptidase that stabilizes fibrin clots by removing C-terminal arginines and lysines from partially degraded fibrin. Inhibition of TAFIa stimulates the degradation of fibrin clots and may help in prevention of thrombosis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  59 FDFKNYHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKV-SFKANNPGVFIEGGIHAREWISTATVMYILHKL 137
Cdd:cd03871    1 HSYEKYNNWETIEAWTEQVASKNPDLVSRSQIGTTFEGRPIYLLKVgKPGSNKKAIFMDCGFHAREWISPAFCQWFVREA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 138 LKS--DNPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTR-KQYSFFCYGSDPNRNWGYKWNTGGASNSACSETYA 214
Cdd:cd03871   81 VRTygKEKIMTKLLDRLDFYILPVLNIDGYVYTWTKNRMWRKTRsPNAGSSCIGTDPNRNFNAGWCTVGASSNPCSETYC 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332031880 215 GSAPFSEIETKTLSKYIDSISDKLYAYIAFHSYSQLLLIPYGHTTAHLDNYDDLVSI 271
Cdd:cd03871  161 GSAPESEKETKALANFIRNNLSSIKAYLTIHSYSQMLLYPYSYTYKLAPNHEELNSI 217

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup; Peptidase M14 carboxypeptidase (CP) O (CPO, also known as metallocarboxypeptidase C; EC 3.4.17.) belongs to the carboxypeptidase A/B 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. CPO has not been well characterized as yet, and little is known about it. Based on modeling studies, CPO has been suggested to have specificity for acidic residues rather than aliphatic/aromatic residues as in A-like enzymes or basic residues as in B-like enzymes. It remains to be demonstrated that CPO is functional as an MCP.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  61 FKNYHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSFKANNPG--VFIEGGIHAREWISTATVMYILHKLL 138
Cdd:cd06247    1 YTKYHPMDEIYQWMDQMQEKNSEVVSQHYLGQTYEKRPMYYLKIGWPSDKPKkiIWMDCGIHAREWIAPAFCQWFVKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 139 KS--DNPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQY-SFFCYGSDPNRNWGYKWNTGGASNSACSETYAG 215
Cdd:cd06247   81 QNykTDSRLNKLLKNLDFYVLPVLNIDGYIYSWTTDRLWRKSRSPHnNGTCYGTDLNRNFNSQWCSIGASRNCCSIIFCG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332031880 216 SAPFSEIETKTLSKYIDSISDKLYAYIAFHSYSQLLLIPYGHTTAHLDNYDDLVSI 271
Cdd:cd06247  161 TGPESEPETKAVADLIEKKKSDILCYLTIHSYGQLILLPYGYTKEPSPNHEEMMEV 216

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, and CPU), belongs to the carboxpeptidase A/B 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. CPB2 enzyme displays B-like activity; it only cleaves the basic residues lysine or arginine. It is produced and secreted by the liver as the inactive precursor, procarboxypeptidase U or PCPB2, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). It circulates in plasma as a zymogen bound to plasminogen, and the active enzyme, TAFIa, inhibits fibrinolysis. It is highly regulated, increased TAFI concentrations are thought to increase the risk of thrombosis and coronary artery disease by reducing fibrinolytic activity while low TAFI levels have been correlated with chronic liver disease.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  61 FKNYHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVS--FKANNPGVFIEGGIHAREWISTATVMYILHKLL 138
Cdd:cd06246    2 YEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSgkEQTAKNAIWIDCGIHAREWISPAFCLWFIGHAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 139 K--SDNPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQYS-FFCYGSDPNRNWGYKWNTGGASNSACSETYAG 215
Cdd:cd06246   82 YfyGIIGQHTNLLNLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSKHAnNRCIGTDLNRNFDAGWCGKGASSDSCSETYCG 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 332031880 216 SAPFSEIETKTLSKYIDSISDKLYAYIAFHSYSQLLLIPYGHTTAHLDNYDDLVSI 271
Cdd:cd06246  162 PYPESEPEVKAVASFLRRHKDTIKAYISMHSYSQMVLFPYSYTRNKSKDHDELSLL 217

M14 family of metallocarboxypeptidases and related proteins; The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (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. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 113 VFIEGGIHAREWISTATVMYILHKLLKSD-NPEIRALAESYDWYIFPSFNPDGYVYTHTKNrlWRKTRKqysffcyGSDP 191
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLENYgNDPLKRLLDNVELWIVPLVNPDGFARVIDSG--GRKNAN-------GVDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 192 NRNWGYKWNtGGASNSACSETYAGSAPFSEIETKTLSKYIDSIsdKLYAYIAFHSYSQLLLIPYGHTTAHLDNYDDLVSI 271
Cdd:cd00596   72 NRNFPYNWG-KDGTSGPSSPTYRGPAPFSEPETQALRDLAKSH--RFDLAVSYHSSSEAILYPYGYTNEPPPDFSEFQEL 148

                 .
gi 332031880 272 I 272
Cdd:cd00596  149 A 149

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  50 AAPASASSTFDFKNYHTLDVINKNLDDTAKQySKFVQTVVGGQTYEGRQIKGVKVS-FKANNPGVFIEGGIHAREWISTA 128
Cdd:COG2866    5 ILPATYKEVSSYDRYYTYEELLALLAKLAAA-SPLVELESIGKSVEGRPIYLLKIGdPAEGKPKVLLNAQQHGNEWTGTE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 129 TVMYILHKLLKSDNPEIRALAESYDWYIFPSFNPDGYVythtknRLWRKTRkqysffcYGSDPNRNWGYKWntggasnsa 208
Cdd:COG2866   84 ALLGLLEDLLDNYDPLIRALLDNVTLYIVPMLNPDGAE------RNTRTNA-------NGVDLNRDWPAPW--------- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332031880 209 csetyagsapFSEIETKTLSKYIDSIsdKLYAYIAFHSYSQLLLIPYGHTT 259
Cdd:COG2866  142 ----------LSEPETRALRDLLDEH--DPDFVLDLHGQGELFYWFVGTTE 180

Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (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. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  59 FDFKNYHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSFKA-----NNPGVFIEGGIHAREWISTATVMYI 133
Cdd:cd06905    1 LAFDRYYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGEtgpadEKPALWVDGNIHGNEVTGSEVALYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 134 LHKLLK--SDNPEIRALAESYDWYIFPSFNPDGY--VYTHTKNRLWRKTR------------------------------ 179
Cdd:cd06905   81 AEYLLTnyGKDPEITRLLDTRTFYILPRLNPDGAeaYKLKTERSGRSSPRdddrdgdgdedgpedlngdglitqmrvkdp 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 180 ----------------------KQYSFF----------------CYGSDPNRNWGYKWNTGGASNSacsetyAGSAPFSE 221
Cdd:cd06905  161 tgtwkvdpddprlmvdrekgekGFYRLYpegidndgdgrynedgPGGVDLNRNFPYNWQPFYVQPG------AGPYPLSE 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 332031880 222 IETKTLSKYIDSISDkLYAYIAFHSYSQLLLIPYGH 257
Cdd:cd06905  235 PETRAVADFLLAHPN-IAAVLTFHTSGGMILRPPGT 269

Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 113 VFIEGGIHAREWISTATVMYILHKLLKS-------DNPEIRALAESYDWYIFPSFNPDGYVYT-------HTKNRLWRKT 178
Cdd:cd06229    1 VLYNASFHAREYITTLLLMKFIEDYAKAyvnksyiRGKDVGELLNKVTLHIVPMVNPDGVEISqngsnaiNPYYLRLVAW 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332031880 179 RKQYSFF------CYGSDPNRNWGYKWNTGGASNSAC--SETYAGSAPFSEIETKTLSKYIdsISDKLYAYIAFHS 246
Cdd:cd06229   81 NKKGTDFtgwkanIRGVDLNRNFPAGWEKEKRLGPKApgPRDYPGKEPLSEPETKAMAALT--RQNDFDLVLAYHS 154

Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 332031880    1 FSYWIAP-FANKQAELMIAPHKLPEFYEMMKQMQIPYTVFIENVQTLINR 49
Cdd:pfam02244  23 LDFWKPPsKVGKPVDVMVPPSKLEAFEELLEKHGISYEVLIEDVQELIDE 72

bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial carboxypeptidase (CP) members of the M14 family of metallocarboxypeptidases (MCPs), mostly of which have yet to be characterized. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVS----FKANNPGVFIEGGIHAREWISTATVMYILHKLLK 139
Cdd:cd18173    4 YPTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISdnvnTEEAEPEFKYTSTMHGDETTGYELMLRLIDYLLT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 140 S--DNPEIRALAESYDWYIFPSFNPDGYVYTHTkNRLWRKTRKQYSffcyGSDPNRNwgYKWNTGGASNsacsetyagSA 217
Cdd:cd18173   84 NygTDPRITNLVDNTEIWINPLANPDGTYAGGN-NTVSGATRYNAN----GVDLNRN--FPDPVDGDHP---------DG 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 332031880 218 PFSEIETKTLSKYIDSISDKLYAyiAFHSYSQLLLIPYGHT-TAHLDN 264
Cdd:cd18173  148 NGWQPETQAMMNFADEHNFVLSA--NFHGGAEVVNYPWDTWySRHPDD 193

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSfkaNNPGV---------FIeGGIHAREWISTATVMYIL 134
Cdd:cd03858    1 HHNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEIS---DNPGVhepgepefkYV-ANMHGNEVVGRELLLLLA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332031880 135 HKLLKSD--NPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQYSffcyGSDPNRN 194
Cdd:cd03858   77 EYLCENYgkDPRVTQLVNSTRIHIMPSMNPDGYEKAQEGDCGGLIGRNNAN----GVDLNRN 134

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The first carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain I. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the 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. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. This Domain I family contains two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus regulating intracellular trafficking. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop. In D. melanogaster, the CPD variant 1B short (DmCPD1Bs) is necessary and sufficient for viability of the fruit fly.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSFKANN-----PGVFIEGGIHAREWISTATVMYILHKLL 138
Cdd:cd03868    1 YHNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDNVNRrepgkPMFKYVANMHGDETVGRQLLIYLAQYLL 80

                         90       100
                 ....*....|....*....|....*....
gi 332031880 139 K--SDNPEIRALAESYDWYIFPSFNPDGY 165
Cdd:cd03868   81 EnyGKDERVTRLVNSTDIHLMPSMNPDGF 109

Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar to Pseudomonas aerugnosa CCP (PaCCP); A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP)-like proteins. This subgroup includes PaCCP from Pseudomonas aeruginosa, a carboxypeptidase homologous to M14D subfamily of human CCPs. Structural complexes with well-known inhibitors of metallocarboxypeptidases indicate that PaCCP might only possess C-terminal hydrolase activity against cellular substrates of particular specificity. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (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. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  80 QYSKFVQTVVGGQTYEGRQIKGVKVSFKANNPGVfieGGIHAR--------EWISTAtvmyILHKLLKSDNPEIRALAES 151
Cdd:cd06234   14 QASPGVRLEVLGQTLDGRDIDLLTIGDPGTGKKK---VWIIARqhpgetmaEWFMEG----LLDRLLDEDDPVSRALLEK 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 332031880 152 YDWYIFPSFNPDGYVYTHTK-NRLwrktrkqysffcyGSDPNRNWG 196
Cdd:cd06234   87 AVFYVVPNMNPDGSVRGNLRtNAA-------------GVNLNREWA 119

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase M14-like domain of carboxypeptidase (CP) Z (CPZ), CPZ belongs to the N/E 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. CPZ is a secreted Zn-dependent enzyme whose biological function is largely unknown. Unlike other members of the N/E subfamily, CPZ has a bipartite structure, which consists of an N-terminal cysteine-rich domain (CRD) whose sequence is similar to Wnt-binding proteins, and a C-terminal CP catalytic domain that removes C-terminal Arg residues from substrates. CPZ is enriched in the extracellular matrix and is widely distributed during early embryogenesis. That the CRD of CPZ can bind to Wnt4 suggests that CPZ plays a role in Wnt signaling.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIkgVKVSFKAN-------NPGVFIEGGIHAREWISTATVMYiLHK 136
Cdd:cd03867    1 HHSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDL--LVIEFSSNpgqhellEPEVKYIGNMHGNEVVGREMLIY-LAQ 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 332031880 137 LLKSD----NPEIRALAESYDWYIFPSFNPDGY 165
Cdd:cd03867   78 YLCSEyllgNPRIQTLINTTRIHLLPSMNPDGY 110

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (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. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 113 VFIEGGIHAREWISTATVMYILHKLLKSDNPEIRALAESYDWYIFPSFNPDG---YV--YTHTK-------------NRL 174
Cdd:cd06238    4 LWMGYSIHGNELSGSEAAMQVAYHLAAGQDEATRALLENTVIVIDPNQNPDGrerFVnwFNQNRgavgdpdpqsmehNEP 83

                         90       100
                 ....*....|....*....|.
gi 332031880 175 WRKTRKQYSFFcygsDPNRNW 195
Cdd:cd06238   84 WPGGRTNHYLF----DLNRDW 100

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 Carboxypeptidase (CP) M (CPM) belongs to the N/E 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. CPM is an extracellular glycoprotein, bound to cell membranes via a glycosyl-phosphatidylinositol on the C-terminus of the protein. It specifically removes C-terminal basic residues such as lysine and arginine from peptides and proteins. The highest levels of CPM have been found in human lung and placenta, but significant amounts are present in kidney, blood vessels, intestine, brain, and peripheral nerves. CPM has also been found in soluble form in various body fluids, including amniotic fluid, seminal plasma and urine. Due to its wide distribution in a variety of tissues, it is believed that it plays an important role in the control of peptide hormones and growth factor activity on the cell surface and in the membrane-localized degradation of extracellular proteins, for example it hydrolyses the C-terminal arginine of epidermal growth factor (EGF) resulting in des-Arg-EGF which binds to the EGF receptor (EGFR) with an equal or greater affinity than native EGF. CPM is a required processing enzyme that generates specific agonists for the B1 receptor.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880  64 YHTLDVINKNLDDTAKQYSKFVQTVVGGQTYEGRQIKGVKVSFKANNPGVFIE-----GGIHAREWISTATVMYILHKLL 138
Cdd:cd03866    1 YHNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLVLGRFPTKHRIGIPefkyvANMHGDEVVGRELLLHLIEFLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332031880 139 KSD--NPEIRALAESYDWYIFPSFNPDGYVYTHTKNRLWRKTRKQYSffcyGSDPNRNW--GYKWN-------TGGASNS 207
Cdd:cd03866   81 TSYgsDPVITRLINSTRIHIMPSMNPDGFEATKKPDCYYTKGRYNKN----GYDLNRNFpdAFEENnvqrqpeTRAVMDW 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332031880 208 ACSETYAGSA-----------PFSEIETKTLSKYIDSIS--DKLYAYIAfHSYSqlllipYGHTT 259
Cdd:cd03866  157 IKNETFVLSAnlhggalvasyPFDNGNSGTGQLGYYSVSpdDDVFIYLA-KTYS------YNHTN 214