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Conserved domains on  [gi|488283805|ref|WP_002355013|]
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MULTISPECIES: glutamyl aminopeptidase [Enterococcus]

Protein Classification

glutamyl aminopeptidase( domain architecture ID 10022127)

glutamyl aminopeptidase is a zinc-dependent membrane-bound aminopeptidase that catalyzes the cleavage of glutamatic and aspartatic amino acid residues from the N-terminus of polypeptides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
glu_aminopep TIGR03107
glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 ...
6-355 0e+00

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: 668.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805    6 FQRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKVEAAPRVMVAAHMDEVGFMLTQINDNGLFQ 85
Cdd:TIGR03107   1 FNKIKEVTELQGTSGFEHPIRDYLRQDITPLVDQVETDGLGGIFGIKESQVENAPRVMVAAHMDEVGFMVSQIKPDGTFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   86 VVPLGGWNPYVVSAQRFTLKTSKGN-YPCISSSIPPHLLRGTSGQKQL-EVSDVLFDAGFSSKEEAESFGVRPGDSIVPQ 163
Cdd:TIGR03107  81 VVELGGWNPLVVSSQRFTLFTRKGKkYPVISGSVPPHLLRGSSGGPQLpAVSDILFDGGFTNKDEAWSFGVRPGDVIVPQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  164 TETIKTANGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDI 243
Cdd:TIGR03107 161 TETILTANGKNVISKAWDNRYGVLMILELLESLKDQELPNTLIAGANVQEEVGLRGAHVSTTKFNPDIFFAVDCSPAGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  244 HTKKGtyGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFVSKGGTDAGAAHTTNNGVPSTVIGVCGRYIHTH 323
Cdd:TIGR03107 241 YGDQG--GKLGEGTLLRFFDPGHIMLPRMKDFLLTTAEEAGIKYQYYVAKGGTDAGAAHLKNSGVPSTTIGVCARYIHSH 318
                         330       340       350
                  ....*....|....*....|....*....|..
gi 488283805  324 QTMFSIADYEAAREMLLQALRGLDKSTVNTIV 355
Cdd:TIGR03107 319 QTLYSIDDFLAAQAFLQAIVKKLDRSTVDTIK 350
 
Name Accession Description Interval E-value
glu_aminopep TIGR03107
glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 ...
6-355 0e+00

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: 668.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805    6 FQRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKVEAAPRVMVAAHMDEVGFMLTQINDNGLFQ 85
Cdd:TIGR03107   1 FNKIKEVTELQGTSGFEHPIRDYLRQDITPLVDQVETDGLGGIFGIKESQVENAPRVMVAAHMDEVGFMVSQIKPDGTFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   86 VVPLGGWNPYVVSAQRFTLKTSKGN-YPCISSSIPPHLLRGTSGQKQL-EVSDVLFDAGFSSKEEAESFGVRPGDSIVPQ 163
Cdd:TIGR03107  81 VVELGGWNPLVVSSQRFTLFTRKGKkYPVISGSVPPHLLRGSSGGPQLpAVSDILFDGGFTNKDEAWSFGVRPGDVIVPQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  164 TETIKTANGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDI 243
Cdd:TIGR03107 161 TETILTANGKNVISKAWDNRYGVLMILELLESLKDQELPNTLIAGANVQEEVGLRGAHVSTTKFNPDIFFAVDCSPAGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  244 HTKKGtyGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFVSKGGTDAGAAHTTNNGVPSTVIGVCGRYIHTH 323
Cdd:TIGR03107 241 YGDQG--GKLGEGTLLRFFDPGHIMLPRMKDFLLTTAEEAGIKYQYYVAKGGTDAGAAHLKNSGVPSTTIGVCARYIHSH 318
                         330       340       350
                  ....*....|....*....|....*....|..
gi 488283805  324 QTMFSIADYEAAREMLLQALRGLDKSTVNTIV 355
Cdd:TIGR03107 319 QTLYSIDDFLAAQAFLQAIVKKLDRSTVDTIK 350
M42_Frv cd05656
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 ...
7-343 1.15e-164

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: 463.19  E-value: 1.15e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   7 QRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKvEAAPRVMVAAHMDEVGFMLTQINDNGLFQV 86
Cdd:cd05656    1 ELLKKLTEAPGPSGYEEEVRDVIKEELKPYVDEVKVDGLGNLIARKKGK-GEAPKVMIAAHMDEIGFMVTHIDDDGFLRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  87 VPLGGWNPYVVSAQRFTLKTSKGNYPCISSSIPPHLLRGTSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTET 166
Cdd:cd05656   80 EPIGGWDPQVLLGQRVRILTDKGEVPGVIGSKPPHLLKPEERKKVPKIDDLFIDIGASSKEEAAEMGVRVGDPVVPDTEF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 167 IKTaNGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDIHT- 245
Cdd:cd05656  160 TEL-GGNRVVGKALDNRAGCAVLLEVLRELKDEELPNDLYFVATVQEEVGLRGAKTAAFRIDPDIAIAVDVTIAGDTPGi 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 246 KKGTYGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFVSK-GGTDAGAAHTTNNGVPSTVIGVCGRYIHTHQ 324
Cdd:cd05656  239 KHKGEVKLGKGPVIRIGDRSLIPHPKLREFLIETAEKNNIPYQLEVSPgGGTDAGAIHLTREGVPTAVISIPARYIHSPV 318
                        330
                 ....*....|....*....
gi 488283805 325 TMFSIADYEAAREMLLQAL 343
Cdd:cd05656  319 EVVDLRDVENAVKLLTALI 337
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
3-353 3.08e-162

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


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 457.67  E-value: 3.08e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   3 EKTFQRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKvEAAPRVMVAAHMDEVGFMLTQINDNG 82
Cdd:COG1363    2 DYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETDRLGNLIATKKGK-GDGPKVMLAAHMDEIGFMVKHITDNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  83 LFQVVPLGGWNPYVVSAQRFTLKTSKGNYPCISSSIPPHLLRGTSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVP 162
Cdd:COG1363   81 FLRFTPLGGWDPRVLEGQRVTIHTRDGDIPGVIGSKPPHVLTPEERKKPVDIEELFIDIGASSKEEAEALGIRVGDFVVF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 163 QTETIKTANGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADD 242
Cdd:COG1363  161 DPEFEELTNSGFIKSKALDDRAGCAVLLELLKALKDEDLPVTVYFVFTVQEEVGLRGASTAAYDIKPDEAIAVDVTPAGD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 243 IHTKKGTY-GHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQY-FVSKGGTDAGAAHTTNNGVPSTVIGVCGRYI 320
Cdd:COG1363  241 TPGVNEEAvTKLGKGPAIRAKDSSGIYDPGLRRFLIELAEENGIPYQRdVLPGGGTDAGAAHLAGEGVPTALIGIPTRYI 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 488283805 321 HTHQTMFSIADYEAAREMLLQALRGLDKSTVNT 353
Cdd:COG1363  321 HSPYERIHLDDLEATVKLLVAYLESLDAETVEG 353
Peptidase_M42 pfam05343
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ...
46-338 7.90e-125

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: 360.35  E-value: 7.90e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   46 GGIFGIKRSKVEAaPRVMVAAHMDEVGFMLTQINDNGLFQVVPLGGWNPYVVSAQRFTLKTSKGNYPCISSSIPPHLLRG 125
Cdd:pfam05343   1 GNLIATKKGKNKG-PKVMIAAHMDEIGFMVTEIKDNGFLRFTPVGGWDPRVLEGQRVTIHTDKGKIPGVIGSKPPHLLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  126 TSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTETIKTANGKnIISKSWDNRYGCTLVLDALETLQNEELGHTL 205
Cdd:pfam05343  80 EERKKPIDIDELFIDIGASSKEEAEELGISVGDFVVFDPEFVELGNGR-IKSKALDDRAGVAVLLELLKELKDEDLPADV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  206 IAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDIHTKKGTYGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNI 285
Cdd:pfam05343 159 YFVATVQEEVGLRGAKTSAFKIKPDEAIAVDVTAAGDTPGSDEYEAPLGKGPAIRVKDASGIYHPKLRKFLVELAKKNNI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488283805  286 PYQYFV-SKGGTDAGAAHTTNNGVPSTVIGVCGRYIHTHQTMFSIADYEAAREM 338
Cdd:pfam05343 239 PYQVDVyPGGGTDAGAAHLTGGGVPTALISIPTRYIHSPVEVAHLDDLEATVKL 292
PRK09961 PRK09961
aminopeptidase;
9-351 1.37e-65

aminopeptidase;


Pssm-ID: 182170  Cd Length: 344  Bit Score: 211.15  E-value: 1.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   9 IKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIfgIKRSKVEAAPRVMVAAHMDEVGFMLTQINDNGLFQVVP 88
Cdd:PRK09961   6 LKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSV--LIRLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  89 LGGWNPYVVSAQRFTLKTSKGnypcisSSIPPhLLRGTSGQKqlEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTETIK 168
Cdd:PRK09961  84 VGNVRMAARQLQPVRITTREE------CKIPG-LLNGDRQGN--DVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 169 TANgKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAaddiHTKKG 248
Cdd:PRK09961 155 LPH-QRVMGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTAC----WAKNF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 249 TYGH-----LGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQY-FVSKGGTDAGAAHTTNNGVPSTVIGVCGRYIHT 322
Cdd:PRK09961 230 DYGAanhrqIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGIPLQAdMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHC 309
                        330       340
                 ....*....|....*....|....*....
gi 488283805 323 HQTMFSIADYEAAREMLLQALRGLDKSTV 351
Cdd:PRK09961 310 AASIADCRDILQMIQLLSALIQRLTRETV 338
 
Name Accession Description Interval E-value
glu_aminopep TIGR03107
glutamyl aminopeptidase; This model represents the M42.001 clade within MEROPS family M42. M42 ...
6-355 0e+00

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: 668.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805    6 FQRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKVEAAPRVMVAAHMDEVGFMLTQINDNGLFQ 85
Cdd:TIGR03107   1 FNKIKEVTELQGTSGFEHPIRDYLRQDITPLVDQVETDGLGGIFGIKESQVENAPRVMVAAHMDEVGFMVSQIKPDGTFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   86 VVPLGGWNPYVVSAQRFTLKTSKGN-YPCISSSIPPHLLRGTSGQKQL-EVSDVLFDAGFSSKEEAESFGVRPGDSIVPQ 163
Cdd:TIGR03107  81 VVELGGWNPLVVSSQRFTLFTRKGKkYPVISGSVPPHLLRGSSGGPQLpAVSDILFDGGFTNKDEAWSFGVRPGDVIVPQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  164 TETIKTANGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDI 243
Cdd:TIGR03107 161 TETILTANGKNVISKAWDNRYGVLMILELLESLKDQELPNTLIAGANVQEEVGLRGAHVSTTKFNPDIFFAVDCSPAGDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  244 HTKKGtyGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFVSKGGTDAGAAHTTNNGVPSTVIGVCGRYIHTH 323
Cdd:TIGR03107 241 YGDQG--GKLGEGTLLRFFDPGHIMLPRMKDFLLTTAEEAGIKYQYYVAKGGTDAGAAHLKNSGVPSTTIGVCARYIHSH 318
                         330       340       350
                  ....*....|....*....|....*....|..
gi 488283805  324 QTMFSIADYEAAREMLLQALRGLDKSTVNTIV 355
Cdd:TIGR03107 319 QTLYSIDDFLAAQAFLQAIVKKLDRSTVDTIK 350
M42_Frv cd05656
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 ...
7-343 1.15e-164

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: 463.19  E-value: 1.15e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   7 QRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKvEAAPRVMVAAHMDEVGFMLTQINDNGLFQV 86
Cdd:cd05656    1 ELLKKLTEAPGPSGYEEEVRDVIKEELKPYVDEVKVDGLGNLIARKKGK-GEAPKVMIAAHMDEIGFMVTHIDDDGFLRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  87 VPLGGWNPYVVSAQRFTLKTSKGNYPCISSSIPPHLLRGTSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTET 166
Cdd:cd05656   80 EPIGGWDPQVLLGQRVRILTDKGEVPGVIGSKPPHLLKPEERKKVPKIDDLFIDIGASSKEEAAEMGVRVGDPVVPDTEF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 167 IKTaNGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDIHT- 245
Cdd:cd05656  160 TEL-GGNRVVGKALDNRAGCAVLLEVLRELKDEELPNDLYFVATVQEEVGLRGAKTAAFRIDPDIAIAVDVTIAGDTPGi 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 246 KKGTYGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFVSK-GGTDAGAAHTTNNGVPSTVIGVCGRYIHTHQ 324
Cdd:cd05656  239 KHKGEVKLGKGPVIRIGDRSLIPHPKLREFLIETAEKNNIPYQLEVSPgGGTDAGAIHLTREGVPTAVISIPARYIHSPV 318
                        330
                 ....*....|....*....
gi 488283805 325 TMFSIADYEAAREMLLQAL 343
Cdd:cd05656  319 EVVDLRDVENAVKLLTALI 337
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
3-353 3.08e-162

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


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 457.67  E-value: 3.08e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   3 EKTFQRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKvEAAPRVMVAAHMDEVGFMLTQINDNG 82
Cdd:COG1363    2 DYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETDRLGNLIATKKGK-GDGPKVMLAAHMDEIGFMVKHITDNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  83 LFQVVPLGGWNPYVVSAQRFTLKTSKGNYPCISSSIPPHLLRGTSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVP 162
Cdd:COG1363   81 FLRFTPLGGWDPRVLEGQRVTIHTRDGDIPGVIGSKPPHVLTPEERKKPVDIEELFIDIGASSKEEAEALGIRVGDFVVF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 163 QTETIKTANGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADD 242
Cdd:COG1363  161 DPEFEELTNSGFIKSKALDDRAGCAVLLELLKALKDEDLPVTVYFVFTVQEEVGLRGASTAAYDIKPDEAIAVDVTPAGD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 243 IHTKKGTY-GHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQY-FVSKGGTDAGAAHTTNNGVPSTVIGVCGRYI 320
Cdd:COG1363  241 TPGVNEEAvTKLGKGPAIRAKDSSGIYDPGLRRFLIELAEENGIPYQRdVLPGGGTDAGAAHLAGEGVPTALIGIPTRYI 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 488283805 321 HTHQTMFSIADYEAAREMLLQALRGLDKSTVNT 353
Cdd:COG1363  321 HSPYERIHLDDLEATVKLLVAYLESLDAETVEG 353
Peptidase_M42 pfam05343
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ...
46-338 7.90e-125

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: 360.35  E-value: 7.90e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   46 GGIFGIKRSKVEAaPRVMVAAHMDEVGFMLTQINDNGLFQVVPLGGWNPYVVSAQRFTLKTSKGNYPCISSSIPPHLLRG 125
Cdd:pfam05343   1 GNLIATKKGKNKG-PKVMIAAHMDEIGFMVTEIKDNGFLRFTPVGGWDPRVLEGQRVTIHTDKGKIPGVIGSKPPHLLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  126 TSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTETIKTANGKnIISKSWDNRYGCTLVLDALETLQNEELGHTL 205
Cdd:pfam05343  80 EERKKPIDIDELFIDIGASSKEEAEELGISVGDFVVFDPEFVELGNGR-IKSKALDDRAGVAVLLELLKELKDEDLPADV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  206 IAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDIHTKKGTYGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNI 285
Cdd:pfam05343 159 YFVATVQEEVGLRGAKTSAFKIKPDEAIAVDVTAAGDTPGSDEYEAPLGKGPAIRVKDASGIYHPKLRKFLVELAKKNNI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488283805  286 PYQYFV-SKGGTDAGAAHTTNNGVPSTVIGVCGRYIHTHQTMFSIADYEAAREM 338
Cdd:pfam05343 239 PYQVDVyPGGGTDAGAAHLTGGGVPTALISIPTRYIHSPVEVAHLDDLEATVKL 292
M42 cd05638
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, ...
9-343 3.25e-115

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: 337.51  E-value: 3.25e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   9 IKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSkvEAAPRVMVAAHMDEVGFMLTQINDNGLFQVVP 88
Cdd:cd05638    3 LKELVEIPAISGYEAKIRNFIIEEIKDWVDEVKVDGLGNLILTLKE--ENAPRVLIAAH*DEVGF*VTEIKPDGRLRVSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  89 LGGWNPYVVSAQRFTLKTSKGN-YPCISSSIPPHLLRGTSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTETI 167
Cdd:cd05638   81 IGGVRPNSVEGQRVKIETRKGKtIPGVIGSVPPHLHVYDAGKAKPDWKDIVVDIGARSKEEVEELGIRPGDFVVFDPRFQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 168 KTaNGKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDIHTKK 247
Cdd:cd05638  161 VL-ESKYIKSRALDDRVSVYILLELIKRLQDAELPAEVYFVASVQEEVGLRGASTSTEAVEPDVALAVD*GAAGDGFAGQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 248 gtyGHLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFV-SKGGTDAGAAHTTNNGVPSTVIGVCGRYIHTHQTM 326
Cdd:cd05638  240 ---AKIGKGPSIRAKDSSGIYHPALRRWLETLAKENGIEYQVDIyPYGGTDAGAAHLTGFGVPTLAIGVPIRYIHSFAER 316
                        330
                 ....*....|....*..
gi 488283805 327 FSIADYEAArEMLLQAL 343
Cdd:cd05638  317 THERDILHT-EALLYAL 332
PRK09961 PRK09961
aminopeptidase;
9-351 1.37e-65

aminopeptidase;


Pssm-ID: 182170  Cd Length: 344  Bit Score: 211.15  E-value: 1.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   9 IKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIfgIKRSKVEAAPRVMVAAHMDEVGFMLTQINDNGLFQVVP 88
Cdd:PRK09961   6 LKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSV--LIRLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  89 LGGWNPYVVSAQRFTLKTSKGnypcisSSIPPhLLRGTSGQKqlEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTETIK 168
Cdd:PRK09961  84 VGNVRMAARQLQPVRITTREE------CKIPG-LLNGDRQGN--DVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 169 TANgKNIISKSWDNRYGCTLVLDALETLQNEELGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAaddiHTKKG 248
Cdd:PRK09961 155 LPH-QRVMGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTAC----WAKNF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 249 TYGH-----LGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQY-FVSKGGTDAGAAHTTNNGVPSTVIGVCGRYIHT 322
Cdd:PRK09961 230 DYGAanhrqIGNGPMLVLSDKSLIAPPKLTAWIETVAAEIGIPLQAdMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHC 309
                        330       340
                 ....*....|....*....|....*....
gi 488283805 323 HQTMFSIADYEAAREMLLQALRGLDKSTV 351
Cdd:PRK09961 310 AASIADCRDILQMIQLLSALIQRLTRETV 338
PRK09864 PRK09864
aminopeptidase;
9-352 7.39e-55

aminopeptidase;


Pssm-ID: 182122  Cd Length: 356  Bit Score: 183.76  E-value: 7.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   9 IKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKveaAPRVMVAAHMDEVGFMLTQINDNGLFQVVP 88
Cdd:PRK09864   6 LQQLCEASAVSGDEQEVRDILINTLEPCVNEITFDGLGSFVARKGNK---GPKVAVVGHMDEVGFMVTHIDESGFLRFTT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  89 LGGWNPYVVSAQRFTLKTSKG-NYPCISSSIPPHLLRGTSGQKQLEVSDVLFDAGFSSKEEAESFGVRPGDSIVPQTETI 167
Cdd:PRK09864  83 IGGWWNQSMLNHRVTIRTHKGvKIPGVIGSVAPHALTEKQKQQPLSFDEMFIDIGANSREEVEKRGVEIGDFISPEANFA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 168 KTANGKnIISKSWDNRYGCTLVLDALETLQNEelGHTLIAGANVQEEVGLRGSKPSVHKFNPDIFFAVDCSAADDIHTKK 247
Cdd:PRK09864 163 CWGEDK-VVGKALDNRIGCAMMAELLQTVNNP--EITLYGVGSVEEEVGLRGAQTSAEHIKPDVVIVLDTAVAGDVPGID 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 248 GTYG--HLGEGTLLRIFDPGLITLPRLREYLLDTAATHNIPYQYFVSK-GGTDAGAAHTTNNGVPSTVIGVCGRYIHTHQ 324
Cdd:PRK09864 240 NIKYplKLGQGPGLMLFDKRYFPNQKLVAALKSCAAHNDLPLQFSTMKtGATDGGRYNVMGGGRPVVALCLPTRYLHANS 319
                        330       340
                 ....*....|....*....|....*...
gi 488283805 325 TMFSIADYEAAREMLLQALRGLDKSTVN 352
Cdd:PRK09864 320 GMISKADYDALLTLIRDFLTTLTAEKVN 347
M42_glucanase_like cd05657
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ...
4-301 4.94e-25

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: 103.51  E-value: 4.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805   4 KTFQRIKELTELQGTSGFEDDIRAYMKEHITPLVDDVQYDGLGGIFGIKRSKVEAAPRvMVAAHMDEVGFMLTQINDNGL 83
Cdd:cd05657    1 YLLDLLKELLAIPSPTGYTDEAVRYLKKELEGLGVETELTNKGALIATIPGKDSRKAR-ALSAHVDTLGAIVKEIKPDGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805  84 FQVVPLGGWNPYVVSAQRFTLKTSKGNypCISSSIPPHL----LRGTSGQKQ---LEVSDVLFDAGFSSKEEAESFGVRP 156
Cdd:cd05657   80 LRLTPIGGFAWNSAEGENVTIITRDGK--TYTGTVLPLKasvhVYGDAPEAQertWDNMEVRLDEKVKSKEDVLALGIRV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 157 GDSIVPQTETIKTANGkNIISKSWDNRYGCTLVLDALETLQNE--ELGHTLIAGANVQEEVGLRGSkpSVHKFNPDIFFA 234
Cdd:cd05657  158 GDFVAFDPRPEVTESG-FIKSRHLDDKASVAILLALARALKENklKLPVDTHFLFSNYEEVGHGAS--FAPPEDTDELLA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283805 235 VD-CSAADDIHT-----------KKGTYGHlgegtllrifdpglitlpRLREYLLDTAATHNIPYQYFVSKG-GTDAGAA 301
Cdd:cd05657  235 VDmGPVGPGQNSdeytvsicakdSGGPYDY------------------HLRKRLVNLAERNGIDYQVDVYPFyGSDASAA 296
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
181-243 2.77e-04

Di- or tripeptidase [Amino acid transport and metabolism];


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 42.35  E-value: 2.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488283805 181 DNRYGCTLVLDALETLQNEELGH-TLIAGANVQEEVGLRGSK---PSvhKFNPDIFFAVDCSAADDI 243
Cdd:COG2195  100 DDKAGVAAILAALEYLKEPEIPHgPIEVLFTPDEEIGLRGAKaldVS--KLGADFAYTLDGGEEGEL 164
PRK13381 PRK13381
peptidase T; Provisional
165-237 9.08e-04

peptidase T; Provisional


Pssm-ID: 237371 [Multi-domain]  Cd Length: 404  Bit Score: 41.06  E-value: 9.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488283805 165 ETIKTANGKNIISKswDNRYGCTLVLDALETLQNEELGHTLIAGANV-QEEVGLRGSKP-SVHKFNPDIFFAVDC 237
Cdd:PRK13381 124 EDIIFSDGTSVLGA--DNKAAIAVVMTLLENLTENEVEHGDIVVAFVpDEEIGLRGAKAlDLARFPVDFAYTIDC 196
 
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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