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Conserved domains on  [gi|507083466|ref|WP_016154214|]
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MULTISPECIES: aminopeptidase [Citrobacter]

Protein Classification

Zn-dependent exopeptidase M28( domain architecture ID 11484609)

Zn-dependent exopeptidase M28, similar to alkaline phosphatase isozyme conversion aminopeptidase, may be an aminopeptidase or a carboxypeptidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 1-346 0e+00

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


:

Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 719.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466   1 MFSATRPLLAILALGACFILPAQATSSKPGDIANTQARYIATFFPGRVTGSPAEMLSADYIRQQFQQMGYSSDIRTFNSR 80
Cdd:PRK10199   1 MFSALRHRTAALALGVCFILPVQAASPKPGDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGYQSDIRTFNSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  81 YVYTAKNNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAAQSDADSDANLGGLTLQGIDDNAAGLGVMLELAEKLKD 160
Cdd:PRK10199  81 YIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQGMDDNAAGLGVMLELAERLKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 161 VPTQYGIRFIATSGEEEGKLGAENILKRMSAAEKKNTLLVINLDNLIVGDKLYFNSGKKTPEAVRKLTRDRALAIAHSRG 240
Cdd:PRK10199 161 VPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSGVNTPEAVRKLTRDRALAIARRHG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 241 IVASTNPGQNKNYPKGTGCCNDAEVFDNAGIAVLSVEATNWSLGKKDGYQQRAKSASFPAGNSWHDVRLDNQQHIDKALP 320
Cdd:PRK10199 241 IAATTNPGLNKNYPKGTGCCNDAEVFDKAGIPVLSVEATNWNLGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHIDKALP 320

                        330       340
                 ....*....|....*....|....*.
gi 507083466 321 GRIEHRSRDVVRIMLPLVKELAKAGK 346
Cdd:PRK10199 321 GRIERRCRDVVRIMLPLVKELAKASK 346
 
Name Accession Description Interval E-value
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 1-346 0e+00

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 719.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466   1 MFSATRPLLAILALGACFILPAQATSSKPGDIANTQARYIATFFPGRVTGSPAEMLSADYIRQQFQQMGYSSDIRTFNSR 80
Cdd:PRK10199   1 MFSALRHRTAALALGVCFILPVQAASPKPGDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGYQSDIRTFNSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  81 YVYTAKNNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAAQSDADSDANLGGLTLQGIDDNAAGLGVMLELAEKLKD 160
Cdd:PRK10199  81 YIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQGMDDNAAGLGVMLELAERLKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 161 VPTQYGIRFIATSGEEEGKLGAENILKRMSAAEKKNTLLVINLDNLIVGDKLYFNSGKKTPEAVRKLTRDRALAIAHSRG 240
Cdd:PRK10199 161 VPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSGVNTPEAVRKLTRDRALAIARRHG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 241 IVASTNPGQNKNYPKGTGCCNDAEVFDNAGIAVLSVEATNWSLGKKDGYQQRAKSASFPAGNSWHDVRLDNQQHIDKALP 320
Cdd:PRK10199 241 IAATTNPGLNKNYPKGTGCCNDAEVFDKAGIPVLSVEATNWNLGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHIDKALP 320

                        330       340
                 ....*....|....*....|....*.
gi 507083466 321 GRIEHRSRDVVRIMLPLVKELAKAGK 346
Cdd:PRK10199 321 GRIERRCRDVVRIMLPLVKELAKASK 346
Peptidase_M28 pfam04389
Peptidase family M28;
100-331 2.31e-32

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 119.31  E-value: 2.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  100 VIAAHEGKAPQQ-IIIMAHLDTYAAqsdADsdanlggltlqGIDDNAAGLGVMLELAEKLKDVPT-QYGIRFIATSGEEE 177
Cdd:pfam04389   2 VIAKLPGKAPDEvVLLSAHYDSVGT---GP-----------GADDNASGVAALLELARVLAAGQRpKRSVRFLFFDAEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  178 GKLGAENILKrmSAAEKKNTLLVINLDNLIVGDKLY-FNSGKKTPEAVRKLTRdralAIAHSRGIVASTNPGQNKNYPKG 256
Cdd:pfam04389  68 GLLGSHHFAK--SHPPLKKIRAVINLDMIGSGGPALlFQSGPKGSSLLEKYLK----AAAKPYGVTLAEDPFQERGGPGR 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507083466  257 TgccnDAEVFDNAGIAVLSVeatnwslgkkdgyqqraksASFPAGNSWHdVRLDNQQHIDKALPGRIEHRSRDVV 331
Cdd:pfam04389 142 S----DHAPFIKAGIPGLDL-------------------AFTDFGYRYH-TPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 100-346 2.65e-31

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 118.70  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 100 VIAAHEGKAP--QQIIIMAHLDTYaaqsdadsdanlgGLTLQGIDDNAAGLGVMLELAEKLKD--VPTQYGIRFIATSGE 175
Cdd:COG2234   49 VIAEIPGTDPpdEVVVLGAHYDSV-------------GSIGPGADDNASGVAALLELARALAAlgPKPKRTIRFVAFGAE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 176 EEGKLGAENILKRMsAAEKKNTLLVINLDNLIVGD---KLYFNSGKKTPEAVRKLtrdRALAIAHSRGIVASTnpgqnkN 252
Cdd:COG2234  116 EQGLLGSRYYAENL-KAPLEKIVAVLNLDMIGRGGprnYLYVDGDGGSPELADLL---EAAAKAYLPGLGVDP------P 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 253 YPKGTGCCNDAEVFDNAGIAVLSVEATNWSlgkkdgyqqraksaSFPAgnsWHDVRlDNQQHIDkalPGRIEHrsrdVVR 332
Cdd:COG2234  186 EETGGYGRSDHAPFAKAGIPALFLFTGAED--------------YHPD---YHTPS-DTLDKID---LDALAK----VAQ 240

                        250
                 ....*....|....
gi 507083466 333 IMLPLVKELAKAGK 346
Cdd:COG2234  241 LLAALVYELANADE 254
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 46-209 1.45e-20

M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349913 [Multi-domain]  Cd Length: 266  Bit Score: 89.82  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  46 GRVTGSPAEMLSADYIRQQFQQMGYSS--DIRTFNSRYVYTAKnnrknwhnvTGSTVIAAHEGKAPQQ---IIIMAHLDT 120
Cdd:cd05663   11 GRLTGTKGEKLAADYIAQRFEELGLEPglDNGTYFQPFEFTTG---------TGRNVIGVLPGKGDVAdetVVVGAHYDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 121 YA---AQSDADSDANLgglTLQGIDDNAAGLGVMLELAEKLKD----VPTQYGIRFIATSGEEEGKLGAENILKRMSaAE 193
Cdd:cd05663   82 LGyggEGSLARGDESL---IHNGADDNASGVAAMLELAAKLVDsdtsLALSRNLVFIAFSGEELGLLGSKHFVKNPP-FP 157

                        170
                 ....*....|....*.
gi 507083466 194 KKNTLLVINLDnlIVG 209
Cdd:cd05663  158 IKNTVYMINMD--MVG 171
 
Name Accession Description Interval E-value
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 1-346 0e+00

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 719.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466   1 MFSATRPLLAILALGACFILPAQATSSKPGDIANTQARYIATFFPGRVTGSPAEMLSADYIRQQFQQMGYSSDIRTFNSR 80
Cdd:PRK10199   1 MFSALRHRTAALALGVCFILPVQAASPKPGDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGYQSDIRTFNSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  81 YVYTAKNNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAAQSDADSDANLGGLTLQGIDDNAAGLGVMLELAEKLKD 160
Cdd:PRK10199  81 YIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQGMDDNAAGLGVMLELAERLKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 161 VPTQYGIRFIATSGEEEGKLGAENILKRMSAAEKKNTLLVINLDNLIVGDKLYFNSGKKTPEAVRKLTRDRALAIAHSRG 240
Cdd:PRK10199 161 VPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSGVNTPEAVRKLTRDRALAIARRHG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 241 IVASTNPGQNKNYPKGTGCCNDAEVFDNAGIAVLSVEATNWSLGKKDGYQQRAKSASFPAGNSWHDVRLDNQQHIDKALP 320
Cdd:PRK10199 241 IAATTNPGLNKNYPKGTGCCNDAEVFDKAGIPVLSVEATNWNLGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHIDKALP 320

                        330       340
                 ....*....|....*....|....*.
gi 507083466 321 GRIEHRSRDVVRIMLPLVKELAKAGK 346
Cdd:PRK10199 321 GRIERRCRDVVRIMLPLVKELAKASK 346
Peptidase_M28 pfam04389
Peptidase family M28;
100-331 2.31e-32

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 119.31  E-value: 2.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  100 VIAAHEGKAPQQ-IIIMAHLDTYAAqsdADsdanlggltlqGIDDNAAGLGVMLELAEKLKDVPT-QYGIRFIATSGEEE 177
Cdd:pfam04389   2 VIAKLPGKAPDEvVLLSAHYDSVGT---GP-----------GADDNASGVAALLELARVLAAGQRpKRSVRFLFFDAEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  178 GKLGAENILKrmSAAEKKNTLLVINLDNLIVGDKLY-FNSGKKTPEAVRKLTRdralAIAHSRGIVASTNPGQNKNYPKG 256
Cdd:pfam04389  68 GLLGSHHFAK--SHPPLKKIRAVINLDMIGSGGPALlFQSGPKGSSLLEKYLK----AAAKPYGVTLAEDPFQERGGPGR 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507083466  257 TgccnDAEVFDNAGIAVLSVeatnwslgkkdgyqqraksASFPAGNSWHdVRLDNQQHIDKALPGRIEHRSRDVV 331
Cdd:pfam04389 142 S----DHAPFIKAGIPGLDL-------------------AFTDFGYRYH-TPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 100-346 2.65e-31

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 118.70  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 100 VIAAHEGKAP--QQIIIMAHLDTYaaqsdadsdanlgGLTLQGIDDNAAGLGVMLELAEKLKD--VPTQYGIRFIATSGE 175
Cdd:COG2234   49 VIAEIPGTDPpdEVVVLGAHYDSV-------------GSIGPGADDNASGVAALLELARALAAlgPKPKRTIRFVAFGAE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 176 EEGKLGAENILKRMsAAEKKNTLLVINLDNLIVGD---KLYFNSGKKTPEAVRKLtrdRALAIAHSRGIVASTnpgqnkN 252
Cdd:COG2234  116 EQGLLGSRYYAENL-KAPLEKIVAVLNLDMIGRGGprnYLYVDGDGGSPELADLL---EAAAKAYLPGLGVDP------P 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 253 YPKGTGCCNDAEVFDNAGIAVLSVEATNWSlgkkdgyqqraksaSFPAgnsWHDVRlDNQQHIDkalPGRIEHrsrdVVR 332
Cdd:COG2234  186 EETGGYGRSDHAPFAKAGIPALFLFTGAED--------------YHPD---YHTPS-DTLDKID---LDALAK----VAQ 240

                        250
                 ....*....|....
gi 507083466 333 IMLPLVKELAKAGK 346
Cdd:COG2234  241 LLAALVYELANADE 254
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 46-209 1.45e-20

M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349913 [Multi-domain]  Cd Length: 266  Bit Score: 89.82  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  46 GRVTGSPAEMLSADYIRQQFQQMGYSS--DIRTFNSRYVYTAKnnrknwhnvTGSTVIAAHEGKAPQQ---IIIMAHLDT 120
Cdd:cd05663   11 GRLTGTKGEKLAADYIAQRFEELGLEPglDNGTYFQPFEFTTG---------TGRNVIGVLPGKGDVAdetVVVGAHYDH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 121 YA---AQSDADSDANLgglTLQGIDDNAAGLGVMLELAEKLKD----VPTQYGIRFIATSGEEEGKLGAENILKRMSaAE 193
Cdd:cd05663   82 LGyggEGSLARGDESL---IHNGADDNASGVAAMLELAAKLVDsdtsLALSRNLVFIAFSGEELGLLGSKHFVKNPP-FP 157

                        170
                 ....*....|....*.
gi 507083466 194 KKNTLLVINLDnlIVG 209
Cdd:cd05663  158 IKNTVYMINMD--MVG 171
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 44-235 2.03e-19

M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain.


Pssm-ID: 349912 [Multi-domain]  Cd Length: 268  Bit Score: 86.37  E-value: 2.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  44 FPGRVTGSPAEMLSADYIRQQFQQMGYSSDIRTFNSRYVYTAKNNRKNWHNVTGstVIAAHEgKAPQQIIIMAHLDTYAA 123
Cdd:cd05662   14 FEGRKTGTKGAAKTRAYIIERFKQIGLLPWGDRFEHPFSYTKRFSTRQGVNVLA--VIKGSE-PPTKWRVVSAHYDHLGI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 124 QsdadsdanlGGLTLQGIDDNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLGAENILKRMSAAEKKnTLLVINL 203
Cdd:cd05662   91 R---------GGKIYNGADDNASGVAALLALAEYFKKHPPKHNVIFAATDAEEPGLRGSYAFVEALKVPRAQ-IELNINL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 507083466 204 DnlIVG----DKLYFNSGKKTPEAVRKLTRDRALAI 235
Cdd:cd05662  161 D--MISrperNELYVEGASQFPQLTSILENVKGTCI 194
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 44-204 8.27e-19

M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349910 [Multi-domain]  Cd Length: 290  Bit Score: 85.10  E-value: 8.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  44 FPGRVTGSPAEMLSADYIRQQFQQMGY--SSDIRTFNSRYVYTAKNNRKNWHNVTGstVIAAHEGKApQQIIIMAHLDTY 121
Cdd:cd05660    9 FEGRAPGSEGEKKTVDYLAEQFKELGLkpAGSDGSYLQAVPLVSKIEYSTSHNVVA--ILPGSKLPD-EYIVLSAHWDHL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 122 AAQSDADsdanlGGLTLQGIDDNAAGLGVMLELAEKLK--DVPTQYGIRFIATSGEEEGKLG----AENILkrmsaAEKK 195
Cdd:cd05660   86 GIGPPIG-----GDEIYNGAVDNASGVAAVLELARVFAaqDQRPKRSIVFLAVTAEEKGLLGsryyAANPI-----FPLD 155


                 ....*....
gi 507083466 196 NTLLVINLD 204
Cdd:cd05660  156 KIVANLNID 164
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 47-271 1.40e-18

M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349911 [Multi-domain]  Cd Length: 262  Bit Score: 84.16  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  47 RVTGSPAEMLSADYIRQQFQQMGYSSDIRTFNSRYVY---TAKNNRKNwhnvtgstviaahegkaPQQIIIMAHLDTYAA 123
Cdd:cd05661   28 GVAGTPEELKAARYIEQQLKSLGYEVEVQPFTSHNVIatkKPDNNKNN-----------------NDIIIVTSHYDSVVK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 124 QSdadsdanlggltlqGIDDNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLGAENILKRMSAAEKKNTLLVINL 203
Cdd:cd05661   91 AP--------------GANDNASGTAVTLELARVFKKVKTDKELRFIAFGAEENGLLGSKYYVASLSEDEIKRTIGVFNL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507083466 204 DNLIVGDKLYFNSGKKTPEAVRKLTRDRALAIAHSRGivastnpgqnKNYPKGTGCCNDAEVFDNAGI 271
Cdd:cd05661  157 DMVGTSDAKAGDLYAYTIDGKPNLVTDSGAAASKRLS----------GVLPLVQQGSSDHVPFHEAGI 214
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 97-276 6.86e-17

M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.


Pssm-ID: 349868 [Multi-domain]  Cd Length: 202  Bit Score: 78.15  E-value: 6.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  97 GSTVIAAHEGKAPQQ--IIIMAHLDTYAAQSdadsdanlggltlqGIDDNAAGLGVMLELAEKLKDVPTQ--YGIRFIAT 172
Cdd:cd02690    1 GYNVIATIKGSDKPDevILIGAHYDSVPLSP--------------GANDNASGVAVLLELARVLSKLQLKpkRSIRFAFW 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 173 SGEEEGKLGAENILKRMsAAEKKNTLLVINLDNLIVGDK-LYFNSGKKTPEAVRKLTRdralAIAHSRGIVASTnpGQNK 251
Cdd:cd02690   67 DAEELGLLGSKYYAEQL-LSSLKNIRAALNLDMIGGAGPdLYLQTAPGNDALVEKLLR----ALAHELENVVYT--VVYK 139

                        170       180
                 ....*....|....*....|....*
gi 507083466 252 NYpKGTGcCNDAEVFDNAGIAVLSV 276
Cdd:cd02690  140 ED-GGTG-GSDHRPFLARGIPAASL 162
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 97-204 3.62e-13

M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349874 [Multi-domain]  Cd Length: 206  Bit Score: 67.65  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  97 GSTVIAAHEGKAP--QQIIIMAHLDTYAAQSDADSD--ANlggltlqGIDDNAAGLGVMLELAEKLKDVPT-QYGIRFIA 171
Cdd:cd03877    1 GHNVVGVLEGSDLpdETIVIGAHYDHLGIGGGDSGDkiYN-------GADDNASGVAAVLELARYFAKQKTpKRSIVFAA 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 507083466 172 TSGEEEGKLGAENILKRMSaAEKKNTLLVINLD 204
Cdd:cd03877   74 FTAEEKGLLGSKYFAENPK-FPLDKIVAMLNLD 105
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 57-176 2.17e-10

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 60.54  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  57 SADYIRQQFQQMGYSSDIRTFNsryvytakNNRKNWHNVtgstvIAAHEGKAPQ--QIIIMAHLDTYAaqsdadsdanlg 134
Cdd:cd05640   25 AAEYIAQELVGSGYNVTSHFFS--------HQEGVYANL-----IADLPGSYSQdkLILIGAHYDTVP------------ 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 507083466 135 glTLQGIDDNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEE 176
Cdd:cd05640   80 --GSPGADDNASGVAALLELARLLATLDPNHTLRFVAFDLEE 119
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 23-204 1.70e-09

M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures.


Pssm-ID: 349873 [Multi-domain]  Cd Length: 289  Bit Score: 58.08  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  23 QATSSKPGDIANTQARyiatffpGRVTGSPAEMLSADYIRQQFQQMG-YSSDIRTFNSRYVYTaknnrknwHNVTGSTVi 101
Cdd:cd03876    8 MAHLQQLQDIADANGG-------NRAFGSPGYNASVDYVKNELKAAGyYDVTLQPFTSLYRTT--------YNVIAETK- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 102 aahEGKAPQQIIIMAHLDTYAAQSdadsdanlggltlqGIDDNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLG 181
Cdd:cd03876   72 ---GGDPNNVVMLGAHLDSVSAGP--------------GINDNGSGSAALLEVALALAKFKVKNAVRFAWWTAEEFGLLG 134

                        170       180
                 ....*....|....*....|...
gi 507083466 182 AENILKRMSAAEKKNTLLVINLD 204
Cdd:cd03876  135 SKFYVNNLSSEERSKIRLYLNFD 157
M28_like cd08656
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 40-317 2.30e-09

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349943 [Multi-domain]  Cd Length: 287  Bit Score: 57.53  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  40 IATFFPgRVTGSPAEMLSADYIRQQFQQMGyssdIRTFNSRYVYTAKNNRknwhNVTGSTVIAAHEGKAPQQIIIMAHLD 119
Cdd:cd08656   11 QVDFGP-RVPNTAAHKACGEYLAGKLEAFG----AKVYNQYADLIAYDGT----ILKARNIIGAYNPESKKRVLLCAHWD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 120 T--YAaqsDADSDANLGGLTLQGIDDNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEE-------EGK-------LGAE 183
Cdd:cd08656   82 SrpYA---DNDADPKKHHTPILGANDGASGVGALLEIARQIQQQAPAIGIDIIFFDAEDygtpefyEGKyksdtwcLGSQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 184 nILKRMSAAEKKNTLLVINLDnlIVGDK-LYFNSGKKTPEAVRKLTRdRALAIAHSRGIvastnpgqNKNY-PKGTGCCN 261
Cdd:cd08656  159 -YWARNPHVQGYNARYGILLD--*VGGKnATFLKEQYSLRTARDIVK-KIWKTAKRLGY--------GKYFvPEAGGTIT 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 507083466 262 DAEVFDNAGIAVLSVEATNWSLGKKDGyqqraksasfpAGNSWHDVRlDNQQHIDK 317
Cdd:cd08656  227 DDHLYVNQLARIPTIDIINYDPERPTG-----------FPSYWHTIQ-DN*ENIDK 270
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 49-194 2.48e-07

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 51.81  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  49 TGSPAEMLSADYIRQQFQQMGYSSDIrtfnsryvYTAKNNRKNwhnvtgstVIAAHEGKAPQQ-IIIMAHLDT--YAAQS 125
Cdd:COG0624   26 SVSGEEAAAAELLAELLEALGFEVER--------LEVPPGRPN--------LVARRPGDGGGPtLLLYGHLDVvpPGDLE 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507083466 126 DADSDA--------NLGGLtlqGIDDNAAGLGVMLELAEKLKD--VPTQYGIRFIATSGEEEGKLGAENILKRMSAAEK 194
Cdd:COG0624   90 LWTSDPfeptiedgRLYGR---GAADMKGGLAAMLAALRALLAagLRLPGNVTLLFTGDEEVGSPGARALVEELAEGLK 165
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 50-276 7.70e-07

M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor (TfR) and prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase or GCP-II) subfamily. TfR and PSMA are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants. While related in sequence to peptidase M28 GCP-II, TfR lacks the metal ion coordination centers and protease activity.


Pssm-ID: 349871 [Multi-domain]  Cd Length: 278  Bit Score: 49.99  E-value: 7.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  50 GSPAEMLSADYIRQQFQQMGYSSDIRTFNSRYvytaknnrknwHNVTGSTviaahEGK--APQQIIIMAHLDTyaaqsda 127
Cdd:cd03874   26 GTKGDAALAKYIENSFKNNGLFEVELEEYSPI-----------TNVVGKI-----EGIeqPDRAIIIGAHRDS------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 128 dsdANLGGLtlqgidDNAAGLGVMLELAEKLKDVPTQYG------IRFIATSGEEEGKLGAENILKRMSAAEKKNTLLVI 201
Cdd:cd03874   83 ---WGYGAG------YPNSGTAVLLEIARLFQQLKKKFGwkplrtIYFISWDGSEFGLAGSTELGEDRKASLKDEVYAYI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 202 NLDNLIVGDKlYFNsgkktPEA---VRKLTRDRALAIAHSR-GIVASTNPGQNKNYPKGTGccnDAEVFDNA-GIAVLSV 276
Cdd:cd03874  154 NIDQLVIGNS-ELD-----VDAhplLQSLFRKASKKVKFPGnEDWWKHSPNAKVSNLHQYG---DWTPFLNHlGIPVAVF 224
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 59-225 1.22e-06

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349894 [Multi-domain]  Cd Length: 347  Bit Score: 49.80  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  59 DYIRQQFQQMGYSSDIRTFNSRYVYTAKNNRKNWHNVTGSTVIAAHEG-KAPQQIIIMA-HLDTYAAQS-DADSDAnlgg 135
Cdd:cd05642   50 DWIAEEFREYAAASGGRMTVEVPSYVQGPASRIPFPVNISNVVATLKGsEDPDRVYVVSgHYDSRVSDVmDYESDA---- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 136 ltlQGIDDNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLGAENILKRMSAAeKKNTLLVINLDnlIVGDKLYfN 215
Cdd:cd05642  126 ---PGANDDASGVAVSMELARIFAKHRPKATIVFTAVAGEEQGLYGSTFLAQTYRNN-SVNVEGMLNND--IVGSSTG-D 198

                        170
                 ....*....|
gi 507083466 216 SGKKTPEAVR 225
Cdd:cd05642  199 DGTKDPHTIR 208
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 47-204 1.87e-05

M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.


Pssm-ID: 349872 [Multi-domain]  Cd Length: 307  Bit Score: 45.66  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  47 RVTGSPAEMLSADYIRQQFQQMGYSSDIR---------TFNSRYVYTAKNNRKNWHNVTgsTVIAAHEGKAPQQ---III 114
Cdd:cd03875   22 HPYGSHNNDKVRDYLLARVEEIKERANANglevevqddTGSGSFNFLSSGMTLVYFEVT--NIVVRISGKNSNSlpaLLL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 115 MAHLDtyaaqsdadSDANLGGLTlqgidDNAAGLGVMLELAEKLKDVPTQ--YGIRFIATSGEEEGKLGAENILKRMSAA 192
Cdd:cd03875  100 NAHFD---------SVPTSPGAT-----DDGMGVAVMLEVLRYLSKSGHQpkRDIIFLFNGAEENGLLGAHAFITQHPWA 165

                        170
                 ....*....|..
gi 507083466 193 ekKNTLLVINLD 204
Cdd:cd03875  166 --KNVRAFINLE 175
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 51-209 2.48e-05

Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of 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 family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.


Pssm-ID: 349944 [Multi-domain]  Cd Length: 361  Bit Score: 45.75  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  51 SPAEMLSADYIRQQFQQMGYssDIRTFNSryvytakNNRKNwhnvtgstVIAAHEGKAPQQIIIMAHLDTYAAQ------ 124
Cdd:cd08659   13 NPPEAEVAEYLAELLAKRGY--GIESTIV-------EGRGN--------LVATVGGGDGPVLLLNGHIDTVPPGdgdkws 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 125 ----SDADSDANLGGLtlqGIDDNAAGLGVMLELAEKLKD--VPTQYGIRFIATSGEEEGKLGAENILkrmsaaekkNTL 198
Cdd:cd08659   76 fppfSGRIRDGRLYGR---GACDMKGGLAAMVAALIELKEagALLGGRVALLATVDEEVGSDGARALL---------EAG 143

                        170
                 ....*....|.
gi 507083466 199 LVINLDNLIVG 209
Cdd:cd08659  144 YADRLDALIVG 154
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
 54-209 5.78e-05

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 44.49  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  54 EMLSADYIRQQFQQMGYSSDIRTFNSRyvytaknnRKNwhnvtgstvIAAHEGKAPQQIIIMAHLDTYAA------QSDA 127
Cdd:PRK08588  21 EIEVANYLQDLFAKHGIESKIVKVNDG--------RAN---------LVAEIGSGSPVLALSGHMDVVAAgdvdkwTYDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 128 ----DSDANLGGltlQGIDDNAAGLG----VMLELAEKlkDVPTQYGIRFIATSGEEEGKLGAENILKRMSAAekkntll 199
Cdd:PRK08588  84 feltEKDGKLYG---RGATDMKSGLAalviAMIELKEQ--GQLLNGTIRLLATAGEEVGELGAKQLTEKGYAD------- 151

                        170
                 ....*....|
gi 507083466 200 viNLDNLIVG 209
Cdd:PRK08588 152 --DLDALIIG 159
Peptidase_M42 pfam05343
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ...
 143-242 1.98e-04

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: 42.56  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  143 DNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLGAENilkrmsAAEKKNTLLVINLDNLIVGDklyfnsGKKTPE 222
Cdd:pfam05343 134 DDRAGVAVLLELLKELKDEDLPADVYFVATVQEEVGLRGAKT------SAFKIKPDEAIAVDVTAAGD------TPGSDE 201

                          90       100
                  ....*....|....*....|
gi 507083466  223 AVRKLTRDRALAIAHSRGIV 242
Cdd:pfam05343 202 YEAPLGKGPAIRVKDASGIY 221
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
 143-248 3.27e-04

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


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 42.04  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 143 DNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLGAenilkrMSAAEKKNTLLVINLDNLIVGDKLYFNsgkktPE 222
Cdd:COG1363  179 DDRAGCAVLLELLKALKDEDLPVTVYFVFTVQEEVGLRGA------STAAYDIKPDEAIAVDVTPAGDTPGVN-----EE 247

                         90       100
                 ....*....|....*....|....*.
gi 507083466 223 AVRKLTRDRALAIAHSRGIvasTNPG 248
Cdd:COG1363  248 AVTKLGKGPAIRAKDSSGI---YDPG 270
M28_nicalin_like cd03882
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ...
 78-219 1.07e-03

M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development.


Pssm-ID: 349878  Cd Length: 296  Bit Score: 40.43  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  78 NSRYVYTAKNN----RKNWH--NVTGSTVIAAHEGKAPQqIIIMAHLDTYAAQSDADSdanlggltlqGIDDNAAGLGVM 151
Cdd:cd03882   53 ANGFKIVVSGNspkaISDWKitTIEGRLTGLGDGEKLPT-IVIVAHYDTFGVAPWLSS----------GADSNGSGVAAL 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507083466 152 LELAE---KL---KDVPTQYGIRFIATSGEEEGKLGAENILKRMSAAEKKNTLLVINLDNLIVGD-KLYFNSGKK 219
Cdd:cd03882  122 LELMRlfsRLysnPRTRAKYNLLFLLTGGGKLNYQGTKHWLESNLDHFLDNVEFVLCLDSIGSKDsDLYLHVSKP 196
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 53-183 1.31e-03

M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.


Pssm-ID: 349879 [Multi-domain]  Cd Length: 425  Bit Score: 40.37  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466  53 AEMLSADYIRQQfqqmgyssdirtfnsRYVYTAKNNRKNWHNVTGSTVIAAHEG-KAPQQIIIM-AHLDTYAAQsdadsd 130
Cdd:cd03883  197 AEMLSRMAARGQ---------------KIVIELKMEAKTYPDATSRNVIAEITGsKYPDEVVLVgGHLDSWDVG------ 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507083466 131 anlggltlQGIDDNAAGLGVMLELAEKLKDVPTQ--YGIRFIATSGEEEGKLGAE 183
Cdd:cd03883  256 --------TGAMDDGGGVAISWEALKLIKDLGLKpkRTIRVVLWTGEEQGLVGAK 302
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 106-205 1.99e-03

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349937 [Multi-domain]  Cd Length: 218  Bit Score: 39.12  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 106 GKAPQQIIIMAHLDTYAAQSdadsdanlggltlqGIDDNAAGLGVMLELAEKLKDVPTQ--YGIRFIATSGEEEGKLGAE 183
Cdd:cd08015   12 DKKDEVVILGAHLDSWHGAT--------------GATDNGAGTAVMMEAMRILKAIGSKpkRTIRVALWGSEEQGLHGSR 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 507083466 184 NILKRMSAAEK--------KNTLLVINLDN 205
Cdd:cd08015   78 AYVEKHFGDPPtmqlqrdhKKISAYFNLDN 107
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 140-195 3.01e-03

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 38.87  E-value: 3.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 507083466  140 GIDDNAAGLGVMLELAEKLKDVPTQYG-IRFIATSGEEEGKLGAENILKRMSAAEKK 195
Cdd:pfam01546  31 GHDDMKGGLLAALEALRALKEEGLKKGtVKLLFQPDEEGGMGGARALIEDGLLEREK 87
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
112-185 5.11e-03

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


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 38.49  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083466 112 IIIMAHLDTyAAQSDAD------------SDanlgGLTLQGIDDnAAGLGVMLELAEKLKDVPTQYG-IRFIATSGEEEG 178
Cdd:COG2195   63 IGLQAHMDT-VPQFPGDgikpqidgglitAD----GTTTLGADD-KAGVAAILAALEYLKEPEIPHGpIEVLFTPDEEIG 136


                 ....*..
gi 507083466 179 KLGAENI 185
Cdd:COG2195  137 LRGAKAL 143
M42_Frv cd05656
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 ...
 143-182 6.38e-03

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: 37.93  E-value: 6.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 507083466 143 DNAAGLGVMLELAEKLKDVPTQYGIRFIATSGEEEGKLGA 182
Cdd:cd05656  173 DNRAGCAVLLEVLRELKDEELPNDLYFVATVQEEVGLRGA 212
 
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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