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Conserved domains on  [gi|15832518|ref|NP_311291|]
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aminopeptidase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

M42 family metallopeptidase( domain architecture ID 10013388)

M42 family metallopeptidase is an aminopeptidase similar to Escherichia coli aminopeptidase YpdE that has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09961 PRK09961
aminopeptidase;
1-344 0e+00

aminopeptidase;


:

Pssm-ID: 182170  Cd Length: 344  Bit Score: 660.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAID 80
Cdd:PRK09961   1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   81 VLPVGNVRMAARQLQPVRITTREECKIPGLLDGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRV 160
Cdd:PRK09961  81 VLPVGNVRMAARQLQPVRITTREECKIPGLLNGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  161 MGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFNYGAANHRQIG 240
Cdd:PRK09961 161 MGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFDYGAANHRQIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  241 NGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDIL 320
Cdd:PRK09961 241 NGPMLVLSDKSLIAPPKLTAWIETVAAEIGIPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDIL 320
                        330       340
                 ....*....|....*....|....
gi 15832518  321 QMEQLLSALIQRLTRETVVQLTDF 344
Cdd:PRK09961 321 QMIQLLSALIQRLTRETVVQLTDF 344
 
Name Accession Description Interval E-value
PRK09961 PRK09961
aminopeptidase;
1-344 0e+00

aminopeptidase;


Pssm-ID: 182170  Cd Length: 344  Bit Score: 660.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAID 80
Cdd:PRK09961   1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   81 VLPVGNVRMAARQLQPVRITTREECKIPGLLDGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRV 160
Cdd:PRK09961  81 VLPVGNVRMAARQLQPVRITTREECKIPGLLNGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  161 MGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFNYGAANHRQIG 240
Cdd:PRK09961 161 MGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFDYGAANHRQIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  241 NGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDIL 320
Cdd:PRK09961 241 NGPMLVLSDKSLIAPPKLTAWIETVAAEIGIPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDIL 320
                        330       340
                 ....*....|....*....|....
gi 15832518  321 QMEQLLSALIQRLTRETVVQLTDF 344
Cdd:PRK09961 321 QMIQLLSALIQRLTRETVVQLTDF 344
M42 cd05638
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, ...
4-329 8.26e-162

M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, also known as glutamyl aminopeptidases (GAP), are co-catalytic metallopeptidases, found in archaea and bacteria. They typically bind two zinc or cobalt atoms and include cellulase and endo-1,4-beta-glucanase (endoglucanase). Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. GAP removes glutamyl residues from the N-terminus of peptide substrates, but is also effective against aspartyl and, to a lesser extent, seryl residues. Lactococcus lactis glutamyl aminopeptidase (PepA; aminopeptidase A) has high thermal stability and aids growth of the organism in milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family, used commercially for N-terminal protein sequencing.


Pssm-ID: 193517 [Multi-domain]  Cd Length: 332  Bit Score: 455.38  E-value: 8.26e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   4 SLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLP 83
Cdd:cd05638   1 ELLKELVEIPAISGYEAKIRNFIIEEIKDWVDEVKVDGLGNLILTLKEENAPRVLIAAH*DEVGF*VTEIKPDGRLRVSP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  84 VGNVRMAARQLQPVRITTREECKIPGLLDGDRQ----------GNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQ 153
Cdd:cd05638  81 IGGVRPNSVEGQRVKIETRKGKTIPGVIGSVPPhlhvydagkaKPDWKDIVVDIGARSKEEVEELGIRPGDFVVFDPRFQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 154 VLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFnyga 233
Cdd:cd05638 161 VLESKYIKSRALDDRVSVYILLELIKRLQDAELPAEVYFVASVQEEVGLRGASTSTEAVEPDVALAVD*GAAGDGF---- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 234 ANHRQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASI 313
Cdd:cd05638 237 AGQAKIGKGPSIRAKDSSGIYHPALRRWLETLAKENGIEYQVDIYPYGGTDAGAAHLTGFGVPTLAIGVPIRYIHSFAER 316
                       330
                ....*....|....*.
gi 15832518 314 ADCRDILQMEQLLSAL 329
Cdd:cd05638 317 THERDILHTEALLYAL 332
Peptidase_M42 pfam05343
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ...
43-325 2.25e-110

M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example in Lactococcus lactis, PepA, aids growth on milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family used commercially for N-terminal protein sequencing.


Pssm-ID: 428431 [Multi-domain]  Cd Length: 292  Bit Score: 323.37  E-value: 2.25e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    43 GSVLIRLN-ESTGPKVMICAHMDEVGFMVRSISREGAIDVLPVGNVRMAARQLQPVRITTREEcKIPGLL---------- 111
Cdd:pfam05343   1 GNLIATKKgKNKGPKVMIAAHMDEIGFMVTEIKDNGFLRFTPVGGWDPRVLEGQRVTIHTDKG-KIPGVIgskpphllkd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   112 DGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVW 191
Cdd:pfam05343  80 EERKKPIDIDELFIDIGASSKEEAEELGISVGDFVVFDPEFVELGNGRIKSKALDDRAGVAVLLELLKELKDEDLPADVY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   192 LVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFNYGAANHrQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGV 271
Cdd:pfam05343 160 FVATVQEEVGLRGAKTSAFKIKPDEAIAVDVTAAGDTPGSDEYEA-PLGKGPAIRVKDASGIYHPKLRKFLVELAKKNNI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15832518   272 PLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDILQMEQL 325
Cdd:pfam05343 239 PYQVDVYPGGGTDAGAAHLTGGGVPTALISIPTRYIHSPVEVAHLDDLEATVKL 292
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
1-338 4.92e-109

Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 322.08  E-value: 4.92e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLN-ESTGPKVMICAHMDEVGFMVRSISREGAI 79
Cdd:COG1363   3 YLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETDRLGNLIATKKgKGDGPKVMLAAHMDEIGFMVKHITDNGFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  80 DVLPVGNVRMAARQLQPVRITTREEcKIPGLL----------DGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFD 149
Cdd:COG1363  83 RFTPLGGWDPRVLEGQRVTIHTRDG-DIPGVIgskpphvltpEERKKPVDIEELFIDIGASSKEEAEALGIRVGDFVVFD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 150 TTFQVL-PHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKN 228
Cdd:COG1363 162 PEFEELtNSGFIKSKALDDRAGCAVLLELLKALKDEDLPVTVYFVFTVQEEVGLRGASTAAYDIKPDEAIAVDVTPAGDT 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 229 FNYGAANHRQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGH 308
Cdd:COG1363 242 PGVNEEAVTKLGKGPAIRAKDSSGIYDPGLRRFLIELAEENGIPYQRDVLPGGGTDAGAAHLAGEGVPTALIGIPTRYIH 321
                       330       340       350
                ....*....|....*....|....*....|
gi 15832518 309 CAASIADCRDILQMEQLLSALIQRLTRETV 338
Cdd:COG1363 322 SPYERIHLDDLEATVKLLVAYLESLDAETV 351
glu_aminopep TIGR03107
glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 ...
6-338 2.37e-59

glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 includes glutamyl aminopeptidase as in the present model, deblocking aminopeptidases as from Pyrococcus horikoshii and related species, and endo-1,4-beta-glucanase (cellulase M) as from Clostridium thermocellum. The current family includes [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 132151  Cd Length: 350  Bit Score: 194.65  E-value: 2.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518     6 LKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLI--RLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLP 83
Cdd:TIGR03107   4 IKEVTELQGTSGFEHPIRDYLRQDITPLVDQVETDGLGGIFGikESQVENAPRVMVAAHMDEVGFMVSQIKPDGTFRVVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    84 VGNVRMAARQLQPVRITTREECKI--------PGLLDGDRQGN---DVSAMRVDIGARSYDEVMQAGIRPGDRVTFDT-T 151
Cdd:TIGR03107  84 LGGWNPLVVSSQRFTLFTRKGKKYpvisgsvpPHLLRGSSGGPqlpAVSDILFDGGFTNKDEAWSFGVRPGDVIVPQTeT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   152 FQVLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDtaCWAKNFNY 231
Cdd:TIGR03107 164 ILTANGKNVISKAWDNRYGVLMILELLESLKDQELPNTLIAGANVQEEVGLRGAHVSTTKFNPDIFFAVD--CSPAGDIY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   232 GAANHRqIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMfSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAA 311
Cdd:TIGR03107 242 GDQGGK-LGEGTLLRFFDPGHIMLPRMKDFLLTTAEEAGIKYQYYV-AKGGTDAGAAHLKNSGVPSTTIGVCARYIHSHQ 319
                         330       340
                  ....*....|....*....|....*..
gi 15832518   312 SIADCRDILQMEQLLSALIQRLTRETV 338
Cdd:TIGR03107 320 TLYSIDDFLAAQAFLQAIVKKLDRSTV 346
 
Name Accession Description Interval E-value
PRK09961 PRK09961
aminopeptidase;
1-344 0e+00

aminopeptidase;


Pssm-ID: 182170  Cd Length: 344  Bit Score: 660.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAID 80
Cdd:PRK09961   1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   81 VLPVGNVRMAARQLQPVRITTREECKIPGLLDGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRV 160
Cdd:PRK09961  81 VLPVGNVRMAARQLQPVRITTREECKIPGLLNGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  161 MGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFNYGAANHRQIG 240
Cdd:PRK09961 161 MGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFDYGAANHRQIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  241 NGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDIL 320
Cdd:PRK09961 241 NGPMLVLSDKSLIAPPKLTAWIETVAAEIGIPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDIL 320
                        330       340
                 ....*....|....*....|....
gi 15832518  321 QMEQLLSALIQRLTRETVVQLTDF 344
Cdd:PRK09961 321 QMIQLLSALIQRLTRETVVQLTDF 344
M42 cd05638
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, ...
4-329 8.26e-162

M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, also known as glutamyl aminopeptidases (GAP), are co-catalytic metallopeptidases, found in archaea and bacteria. They typically bind two zinc or cobalt atoms and include cellulase and endo-1,4-beta-glucanase (endoglucanase). Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. GAP removes glutamyl residues from the N-terminus of peptide substrates, but is also effective against aspartyl and, to a lesser extent, seryl residues. Lactococcus lactis glutamyl aminopeptidase (PepA; aminopeptidase A) has high thermal stability and aids growth of the organism in milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family, used commercially for N-terminal protein sequencing.


Pssm-ID: 193517 [Multi-domain]  Cd Length: 332  Bit Score: 455.38  E-value: 8.26e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   4 SLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLP 83
Cdd:cd05638   1 ELLKELVEIPAISGYEAKIRNFIIEEIKDWVDEVKVDGLGNLILTLKEENAPRVLIAAH*DEVGF*VTEIKPDGRLRVSP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  84 VGNVRMAARQLQPVRITTREECKIPGLLDGDRQ----------GNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQ 153
Cdd:cd05638  81 IGGVRPNSVEGQRVKIETRKGKTIPGVIGSVPPhlhvydagkaKPDWKDIVVDIGARSKEEVEELGIRPGDFVVFDPRFQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 154 VLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFnyga 233
Cdd:cd05638 161 VLESKYIKSRALDDRVSVYILLELIKRLQDAELPAEVYFVASVQEEVGLRGASTSTEAVEPDVALAVD*GAAGDGF---- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 234 ANHRQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASI 313
Cdd:cd05638 237 AGQAKIGKGPSIRAKDSSGIYHPALRRWLETLAKENGIEYQVDIYPYGGTDAGAAHLTGFGVPTLAIGVPIRYIHSFAER 316
                       330
                ....*....|....*.
gi 15832518 314 ADCRDILQMEQLLSAL 329
Cdd:cd05638 317 THERDILHTEALLYAL 332
M42_Frv cd05656
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 ...
4-330 4.16e-138

M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation.


Pssm-ID: 349906 [Multi-domain]  Cd Length: 337  Bit Score: 395.39  E-value: 4.16e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   4 SLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNEST-GPKVMICAHMDEVGFMVRSISREGAIDVL 82
Cdd:cd05656   1 ELLKKLTEAPGPSGYEEEVRDVIKEELKPYVDEVKVDGLGNLIARKKGKGeAPKVMIAAHMDEIGFMVTHIDDDGFLRFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  83 PVGNVRMAARQLQPVRITTREeCKIPG--------LLDGDR--QGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTF 152
Cdd:cd05656  81 PIGGWDPQVLLGQRVRILTDK-GEVPGvigskpphLLKPEErkKVPKIDDLFIDIGASSKEEAAEMGVRVGDPVVPDTEF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 153 QVLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFNYG 232
Cdd:cd05656 160 TELGGNRVVGKALDNRAGCAVLLEVLRELKDEELPNDLYFVATVQEEVGLRGAKTAAFRIDPDIAIAVDVTIAGDTPGIK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 233 AANHRQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAAS 312
Cdd:cd05656 240 HKGEVKLGKGPVIRIGDRSLIPHPKLREFLIETAEKNNIPYQLEVSPGGGTDAGAIHLTREGVPTAVISIPARYIHSPVE 319
                       330
                ....*....|....*...
gi 15832518 313 IADCRDILQMEQLLSALI 330
Cdd:cd05656 320 VVDLRDVENAVKLLTALI 337
Peptidase_M42 pfam05343
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ...
43-325 2.25e-110

M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example in Lactococcus lactis, PepA, aids growth on milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family used commercially for N-terminal protein sequencing.


Pssm-ID: 428431 [Multi-domain]  Cd Length: 292  Bit Score: 323.37  E-value: 2.25e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    43 GSVLIRLN-ESTGPKVMICAHMDEVGFMVRSISREGAIDVLPVGNVRMAARQLQPVRITTREEcKIPGLL---------- 111
Cdd:pfam05343   1 GNLIATKKgKNKGPKVMIAAHMDEIGFMVTEIKDNGFLRFTPVGGWDPRVLEGQRVTIHTDKG-KIPGVIgskpphllkd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   112 DGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVW 191
Cdd:pfam05343  80 EERKKPIDIDELFIDIGASSKEEAEELGISVGDFVVFDPEFVELGNGRIKSKALDDRAGVAVLLELLKELKDEDLPADVY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   192 LVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFNYGAANHrQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGV 271
Cdd:pfam05343 160 FVATVQEEVGLRGAKTSAFKIKPDEAIAVDVTAAGDTPGSDEYEA-PLGKGPAIRVKDASGIYHPKLRKFLVELAKKNNI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15832518   272 PLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDILQMEQL 325
Cdd:pfam05343 239 PYQVDVYPGGGTDAGAAHLTGGGVPTALISIPTRYIHSPVEVAHLDDLEATVKL 292
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
1-338 4.92e-109

Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 322.08  E-value: 4.92e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLN-ESTGPKVMICAHMDEVGFMVRSISREGAI 79
Cdd:COG1363   3 YLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETDRLGNLIATKKgKGDGPKVMLAAHMDEIGFMVKHITDNGFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  80 DVLPVGNVRMAARQLQPVRITTREEcKIPGLL----------DGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFD 149
Cdd:COG1363  83 RFTPLGGWDPRVLEGQRVTIHTRDG-DIPGVIgskpphvltpEERKKPVDIEELFIDIGASSKEEAEALGIRVGDFVVFD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 150 TTFQVL-PHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKN 228
Cdd:COG1363 162 PEFEELtNSGFIKSKALDDRAGCAVLLELLKALKDEDLPVTVYFVFTVQEEVGLRGASTAAYDIKPDEAIAVDVTPAGDT 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 229 FNYGAANHRQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGH 308
Cdd:COG1363 242 PGVNEEAVTKLGKGPAIRAKDSSGIYDPGLRRFLIELAEENGIPYQRDVLPGGGTDAGAAHLAGEGVPTALIGIPTRYIH 321
                       330       340       350
                ....*....|....*....|....*....|
gi 15832518 309 CAASIADCRDILQMEQLLSALIQRLTRETV 338
Cdd:COG1363 322 SPYERIHLDDLEATVKLLVAYLESLDAETV 351
PRK09864 PRK09864
aminopeptidase;
1-345 1.54e-59

aminopeptidase;


Pssm-ID: 182122  Cd Length: 356  Bit Score: 195.31  E-value: 1.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    1 MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRlNESTGPKVMICAHMDEVGFMVRSISREGAID 80
Cdd:PRK09864   1 MNIELLQQLCEASAVSGDEQEVRDILINTLEPCVNEITFDGLGSFVAR-KGNKGPKVAVVGHMDEVGFMVTHIDESGFLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   81 VLPVGNVRMAARQLQPVRITTREECKIPGLLDG----------DRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDT 150
Cdd:PRK09864  80 FTTIGGWWNQSMLNHRVTIRTHKGVKIPGVIGSvaphaltekqKQQPLSFDEMFIDIGANSREEVEKRGVEIGDFISPEA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  151 TFQVLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELpaEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAK--- 227
Cdd:PRK09864 160 NFACWGEDKVVGKALDNRIGCAMMAELLQTVNNPEI--TLYGVGSVEEEVGLRGAQTSAEHIKPDVVIVLDTAVAGDvpg 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  228 --NFNYGAanhrQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATR 305
Cdd:PRK09864 238 idNIKYPL----KLGQGPGLMLFDKRYFPNQKLVAALKSCAAHNDLPLQFSTMKTGATDGGRYNVMGGGRPVVALCLPTR 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 15832518  306 HGHCAASIADCRDILQMEQLLSALIQRLTRETVVQLTDFR 345
Cdd:PRK09864 314 YLHANSGMISKADYDALLTLIRDFLTTLTAEKVNAFSQFR 353
glu_aminopep TIGR03107
glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 ...
6-338 2.37e-59

glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 includes glutamyl aminopeptidase as in the present model, deblocking aminopeptidases as from Pyrococcus horikoshii and related species, and endo-1,4-beta-glucanase (cellulase M) as from Clostridium thermocellum. The current family includes [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 132151  Cd Length: 350  Bit Score: 194.65  E-value: 2.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518     6 LKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLI--RLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLP 83
Cdd:TIGR03107   4 IKEVTELQGTSGFEHPIRDYLRQDITPLVDQVETDGLGGIFGikESQVENAPRVMVAAHMDEVGFMVSQIKPDGTFRVVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518    84 VGNVRMAARQLQPVRITTREECKI--------PGLLDGDRQGN---DVSAMRVDIGARSYDEVMQAGIRPGDRVTFDT-T 151
Cdd:TIGR03107  84 LGGWNPLVVSSQRFTLFTRKGKKYpvisgsvpPHLLRGSSGGPqlpAVSDILFDGGFTNKDEAWSFGVRPGDVIVPQTeT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   152 FQVLPHQRVMGKAFDDRLGCYLLVTLLRELHSAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDtaCWAKNFNY 231
Cdd:TIGR03107 164 ILTANGKNVISKAWDNRYGVLMILELLESLKDQELPNTLIAGANVQEEVGLRGAHVSTTKFNPDIFFAVD--CSPAGDIY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   232 GAANHRqIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMfSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAA 311
Cdd:TIGR03107 242 GDQGGK-LGEGTLLRFFDPGHIMLPRMKDFLLTTAEEAGIKYQYYV-AKGGTDAGAAHLKNSGVPSTTIGVCARYIHSHQ 319
                         330       340
                  ....*....|....*....|....*..
gi 15832518   312 SIADCRDILQMEQLLSALIQRLTRETV 338
Cdd:TIGR03107 320 TLYSIDDFLAAQAFLQAIVKKLDRSTV 346
M42_glucanase_like cd05657
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ...
2-308 1.06e-23

M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.


Pssm-ID: 349907 [Multi-domain]  Cd Length: 337  Bit Score: 99.66  E-value: 1.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   2 DLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLN-ESTGPKVMICAHMDEVGFMVRSISREGAID 80
Cdd:cd05657   2 LLDLLKELLAIPSPTGYTDEAVRYLKKELEGLGVETELTNKGALIATIPgKDSRKARALSAHVDTLGAIVKEIKPDGRLR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518  81 VLPVGNVRMAARQLQPVRITTREECKIPGLL------------DGDRQGNDVSAM--RVDIGARSYDEVMQAGIRPGDRV 146
Cdd:cd05657  82 LTPIGGFAWNSAEGENVTIITRDGKTYTGTVlplkasvhvygdAPEAQERTWDNMevRLDEKVKSKEDVLALGIRVGDFV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 147 TFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLREL--HSAELPAEVWLVASSSEEVGLrGGQTATRAVSpDVAIVLDTAC 224
Cdd:cd05657 162 AFDPRPEVTESGFIKSRHLDDKASVAILLALARALkeNKLKLPVDTHFLFSNYEEVGH-GASFAPPEDT-DELLAVDMGP 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 225 WAKNFNygaanhrQIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPAT 304
Cdd:cd05657 240 VGPGQN-------SDEYTVSICAKDSGGPYDYHLRKRLVNLAERNGIDYQVDVYPFYGSDASAALRAGHDVRHALIGPGV 312

                ....
gi 15832518 305 RHGH 308
Cdd:cd05657 313 DASH 316
M18 cd05639
M18 peptidase aminopeptidase family; Peptidase M18 aminopeptidase family is widely distributed ...
166-329 8.39e-07

M18 peptidase aminopeptidase family; Peptidase M18 aminopeptidase family is widely distributed in bacteria and eukaryotes, but only the yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized to date. Yeast aminopeptidase I is active only in its dodecameric form with broad substrate specificity, acting on N-terminal leucine and most other amino acids. In contrast, the mammalian aspartyl aminopeptidase is highly selective for hydrolysis of N-terminal Asp or Glu residues from peptides. These enzymes have two catalytic zinc ions at the active site.


Pssm-ID: 349892  Cd Length: 430  Bit Score: 50.23  E-value: 8.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 166 DDRLGCYllvTLLRELHSAELPAEVWLVASSSEEVGLRGGQTAT--------RAVSP---DVAIVLDTA----------- 223
Cdd:cd05639 238 DDRLCCF---AALRALLSANPDKSIGVTLYDNEEIGSDSNQGAKgrflekvlRRILK*qgDSPFALDEVienssvisadv 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518 224 CWAKNFNYG---AANHR-QIGNGPMLVLSDKSLIAP-PKLTAWIETVAAEIGVPLQADMFSN---GGTDGGAVHLTGTGV 295
Cdd:cd05639 315 AHAVNPNYKdvhDLNHApKLNYGPVLKKNSNQRYATnAEFVALVREVANEQGVPVQVFTLRNddgCGGTIGPILASQRGS 394
                       170       180       190
                ....*....|....*....|....*....|....
gi 15832518 296 PTVVMGPATRHGHCAASIADCRDILQMEQLLSAL 329
Cdd:cd05639 395 RVIDLGPAQLAMHSIREIAGSADLFETVKAFRGF 428
Peptidase_M18 pfam02127
Aminopeptidase I zinc metalloprotease (M18);
137-328 2.68e-04

Aminopeptidase I zinc metalloprotease (M18);


Pssm-ID: 396619  Cd Length: 430  Bit Score: 42.40  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   137 QAGIRPGDRVTFDTTFqvLPHQRVM----GKAF------DDRLGCYLLVTLLreLHSAELPAE----VWLVAS-SSEEVG 201
Cdd:pfam02127 196 ELGIEVEDIVSMDLIL--YDAQPAKiggfDKEFlfaprlDNKVSCFAAMEAL--IDSAEDESDpddkIRIVALfDNEEIG 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832518   202 LRGGQTA----TRAVSPDVAIVLD------TACWAKNFNYGA---------------ANHR-QIGNGPMLVLSDKSLIAP 255
Cdd:pfam02127 272 STSAQGAdsnfLEYVLERISIAGKksrdfhLAVQAKSFLISAdvahaihpnysskheENHRpLLGKGPVIKVNANQRYAT 351
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832518   256 PKLT-AWIETVAAEIGVPLQADMFSN---GGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDILQMEQLLSA 328
Cdd:pfam02127 352 NSAGaALVKELAQLAGVPLQVFVVRNdspCGSTIGPILAARTGIRTIDLGNPQLSMHSIRETTGSKDVYQAVKLFKA 428
M20_ArgE_DapE-like_fungal cd05652
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
3-66 4.05e-03

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.


Pssm-ID: 349903 [Multi-domain]  Cd Length: 340  Bit Score: 38.79  E-value: 4.05e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832518   3 LSLLKALSEADAIASSEQEVRQILLE---------EADRLQKEVRFDglgsVLIRLNESTGPKVMICAHMDEV 66
Cdd:cd05652   2 LSLHKSLVEIPSISGNEAAVGDFLAEyleslgftvEKQPVENKDRFN----VYAYPGSSRQPRVLLTSHIDTV 70
 
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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