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Conserved domains on  [gi|71993326|ref|NP_497490|]
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Peptidase M28 domain-containing protein [Caenorhabditis elegans]

Protein Classification

M28 family metallopeptidase( domain architecture ID 10145313)

M28 family metallopeptidase contains aminopeptidases as well as carboxypeptidases that have co-catalytic zinc ions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 17-349 2.84e-115

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: 336.34  E-value: 2.84e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  17 LALSLSTIADMDRMKHDLSKFLsisrfneteksvARAAIKRALEAVGL--NSMTHTFIHEESneVGANVIAVQKGPYfgt 94
Cdd:cd05640   1 LRAHLEQLVRMERNPHDPSAFL------------AAAAEYIAQELVGSgyNVTSHFFSHQEG--VYANLIADLPGSY--- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  95 GNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNlysrQNTIVYVFFDMKHK-----ALAGSHAFVEDVLL 169
Cdd:cd05640  64 SQDKLILIGAHYDTVPGSPGADDNASGVAALLELARLLATLDP----NHTLRFVAFDLEEYpffarGLMGSHAYAEDLLR 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326 170 PLmertnTKVVGTVIADGLLHFDPFPASQAMPNEFEsffpeaaqkLHEHSHMGDFIQVSSRSDIdddlvQKYTRAYDRSC 249
Cdd:cd05640 140 PL-----TPIVGMLSLEMIGYYDPFPHSQAYPAGFE---------LHFYPHMGDFIAVVGRLRS-----RKLVRAFKRAF 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326 250 EMlssDWSFHPWSLNLQMNLANITsldrlhPFLYSDHSSFFFHSKQKSVQIPTIYltdtlnlRGVRQYCVQCDGlymMTE 329
Cdd:cd05640 201 RM---LSDFPVESLNLPFNGPGVP------PFRRSDHSSFWDHGYPAIMVTDTAF-------YRNPQYHLPCDT---PDT 261

                       330       340
                ....*....|....*....|
gi 71993326 330 QNMKFLALMTDSLIRLLIDM 349
Cdd:cd05640 262 LNYKFLTRVTAGLAAGLADL 281
 
Name Accession Description Interval E-value
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 17-349 2.84e-115

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: 336.34  E-value: 2.84e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  17 LALSLSTIADMDRMKHDLSKFLsisrfneteksvARAAIKRALEAVGL--NSMTHTFIHEESneVGANVIAVQKGPYfgt 94
Cdd:cd05640   1 LRAHLEQLVRMERNPHDPSAFL------------AAAAEYIAQELVGSgyNVTSHFFSHQEG--VYANLIADLPGSY--- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  95 GNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNlysrQNTIVYVFFDMKHK-----ALAGSHAFVEDVLL 169
Cdd:cd05640  64 SQDKLILIGAHYDTVPGSPGADDNASGVAALLELARLLATLDP----NHTLRFVAFDLEEYpffarGLMGSHAYAEDLLR 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326 170 PLmertnTKVVGTVIADGLLHFDPFPASQAMPNEFEsffpeaaqkLHEHSHMGDFIQVSSRSDIdddlvQKYTRAYDRSC 249
Cdd:cd05640 140 PL-----TPIVGMLSLEMIGYYDPFPHSQAYPAGFE---------LHFYPHMGDFIAVVGRLRS-----RKLVRAFKRAF 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326 250 EMlssDWSFHPWSLNLQMNLANITsldrlhPFLYSDHSSFFFHSKQKSVQIPTIYltdtlnlRGVRQYCVQCDGlymMTE 329
Cdd:cd05640 201 RM---LSDFPVESLNLPFNGPGVP------PFRRSDHSSFWDHGYPAIMVTDTAF-------YRNPQYHLPCDT---PDT 261

                       330       340
                ....*....|....*....|
gi 71993326 330 QNMKFLALMTDSLIRLLIDM 349
Cdd:cd05640 262 LNYKFLTRVTAGLAAGLADL 281
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 44-180 8.88e-18

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: 82.10  E-value: 8.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  44 NETEKSVARAAIKRALEAVGLNSMTHTFIHEESNEVGANVIAVQKGPyfgTGNDKMMILSANYDTL-EGNQGVDDNGSGV 122
Cdd:COG2234  10 GTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGT---DPPDEVVVLGAHYDSVgSIGPGADDNASGV 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71993326 123 AAVLEAARVLSTLDnlYSRQNTIVYVFFDMKHKALAGSHAFVEDvllPLMERTNTKVV 180
Cdd:COG2234  87 AALLELARALAALG--PKPKRTIRFVAFGAEEQGLLGSRYYAEN---LKAPLEKIVAV 139
Peptidase_M28 pfam04389
Peptidase family M28;
82-166 1.41e-13

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 68.47  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326    82 NVIAVQKGpyfgTGNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNLysrQNTIVYVFFDMKHKALAGSH 161
Cdd:pfam04389   1 NVIAKLPG----KAPDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVLAAGQRP---KRSVRFLFFDAEEAGLLGSH 73


                  ....*
gi 71993326   162 AFVED 166
Cdd:pfam04389  74 HFAKS 78
 
Name Accession Description Interval E-value
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 17-349 2.84e-115

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: 336.34  E-value: 2.84e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  17 LALSLSTIADMDRMKHDLSKFLsisrfneteksvARAAIKRALEAVGL--NSMTHTFIHEESneVGANVIAVQKGPYfgt 94
Cdd:cd05640   1 LRAHLEQLVRMERNPHDPSAFL------------AAAAEYIAQELVGSgyNVTSHFFSHQEG--VYANLIADLPGSY--- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  95 GNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNlysrQNTIVYVFFDMKHK-----ALAGSHAFVEDVLL 169
Cdd:cd05640  64 SQDKLILIGAHYDTVPGSPGADDNASGVAALLELARLLATLDP----NHTLRFVAFDLEEYpffarGLMGSHAYAEDLLR 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326 170 PLmertnTKVVGTVIADGLLHFDPFPASQAMPNEFEsffpeaaqkLHEHSHMGDFIQVSSRSDIdddlvQKYTRAYDRSC 249
Cdd:cd05640 140 PL-----TPIVGMLSLEMIGYYDPFPHSQAYPAGFE---------LHFYPHMGDFIAVVGRLRS-----RKLVRAFKRAF 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326 250 EMlssDWSFHPWSLNLQMNLANITsldrlhPFLYSDHSSFFFHSKQKSVQIPTIYltdtlnlRGVRQYCVQCDGlymMTE 329
Cdd:cd05640 201 RM---LSDFPVESLNLPFNGPGVP------PFRRSDHSSFWDHGYPAIMVTDTAF-------YRNPQYHLPCDT---PDT 261

                       330       340
                ....*....|....*....|
gi 71993326 330 QNMKFLALMTDSLIRLLIDM 349
Cdd:cd05640 262 LNYKFLTRVTAGLAAGLADL 281
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 44-180 8.88e-18

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: 82.10  E-value: 8.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  44 NETEKSVARAAIKRALEAVGLNSMTHTFIHEESNEVGANVIAVQKGPyfgTGNDKMMILSANYDTL-EGNQGVDDNGSGV 122
Cdd:COG2234  10 GTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGT---DPPDEVVVLGAHYDSVgSIGPGADDNASGV 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71993326 123 AAVLEAARVLSTLDnlYSRQNTIVYVFFDMKHKALAGSHAFVEDvllPLMERTNTKVV 180
Cdd:COG2234  87 AALLELARALAALG--PKPKRTIRFVAFGAEEQGLLGSRYYAEN---LKAPLEKIVAV 139
Peptidase_M28 pfam04389
Peptidase family M28;
82-166 1.41e-13

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 68.47  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326    82 NVIAVQKGpyfgTGNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNLysrQNTIVYVFFDMKHKALAGSH 161
Cdd:pfam04389   1 NVIAKLPG----KAPDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVLAAGQRP---KRSVRFLFFDAEEAGLLGSH 73


                  ....*
gi 71993326   162 AFVED 166
Cdd:pfam04389  74 HFAKS 78
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 80-186 4.51e-11

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: 61.59  E-value: 4.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  80 GANVIAVQKGpyfGTGNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNLYSRqnTIVYVFFDMKHKALAG 159
Cdd:cd02690   1 GYNVIATIKG---SDKPDEVILIGAHYDSVPLSPGANDNASGVAVLLELARVLSKLQLKPKR--SIRFAFWDAEELGLLG 75

                        90       100
                ....*....|....*....|....*..
gi 71993326 160 SHAFVEDvllplMERTNTKVVGTVIAD 186
Cdd:cd02690  76 SKYYAEQ-----LLSSLKNIRAALNLD 97
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 82-182 2.51e-10

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: 60.28  E-value: 2.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  82 NVIAVQKgPYFGTGNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNlysrQNTIVYVFFDMKHKALAGSH 161
Cdd:cd05661  62 NVIATKK-PDNNKNNNDIIIVTSHYDSVVKAPGANDNASGTAVTLELARVFKKVKT----DKELRFIAFGAEENGLLGSK 136

                        90       100
                ....*....|....*....|....*
gi 71993326 162 AFVEDVLLPLMERT----NTKVVGT 182
Cdd:cd05661 137 YYVASLSEDEIKRTigvfNLDMVGT 161
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 51-173 3.08e-10

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: 60.17  E-value: 3.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  51 ARAAIKRALEAVGLNSMTHTFIH------EESNEVGANVIAVQKGpyfGTGNDKMMILSANYDTLEGN-----QGVDDNG 119
Cdd:cd05662  27 TRAYIIERFKQIGLLPWGDRFEHpfsytkRFSTRQGVNVLAVIKG---SEPPTKWRVVSAHYDHLGIRggkiyNGADDNA 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71993326 120 SGVAAVLEAARVLSTLDNLYSrqntIVYVFFDMKHKALAGSHAFVEDVLLPLME 173
Cdd:cd05662 104 SGVAALLALAEYFKKHPPKHN----VIFAATDAEEPGLRGSYAFVEALKVPRAQ 153
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 80-171 3.35e-10

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: 59.18  E-value: 3.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  80 GANVIAVQKGpyfGTGNDKMMILSANYDTL------EGNQ---GVDDNGSGVAAVLEAARVLSTLDNLysrQNTIVYVFF 150
Cdd:cd03877   1 GHNVVGVLEG---SDLPDETIVIGAHYDHLgigggdSGDKiynGADDNASGVAAVLELARYFAKQKTP---KRSIVFAAF 74

                        90       100
                ....*....|....*....|.
gi 71993326 151 DMKHKALAGSHAFVEDVLLPL 171
Cdd:cd03877  75 TAEEKGLLGSKYFAENPKFPL 95
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 71-171 5.97e-09

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: 56.60  E-value: 5.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  71 FIHEESNEVGANVIAVQKGPYFgtgNDKMMILSANYDTL---------EGNQGVDDNGSGVAAVLEAARVLSTLDNLYSR 141
Cdd:cd05660  50 LVSKIEYSTSHNVVAILPGSKL---PDEYIVLSAHWDHLgigppiggdEIYNGAVDNASGVAAVLELARVFAAQDQRPKR 126

                        90       100       110
                ....*....|....*....|....*....|
gi 71993326 142 qnTIVYVFFDMKHKALAGSHAFVEDVLLPL 171
Cdd:cd05660 127 --SIVFLAVTAEEKGLLGSRYYAANPIFPL 154
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 51-171 1.32e-08

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: 55.15  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  51 ARAAIKRALEAVGLN------SMTHTFihEESNEVGANVIAVQKGPyfGTGNDKMMILSANYD--------------TLE 110
Cdd:cd05663  22 AADYIAQRFEELGLEpgldngTYFQPF--EFTTGTGRNVIGVLPGK--GDVADETVVVGAHYDhlgyggegslargdESL 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71993326 111 GNQGVDDNGSGVAAVLEAARVLSTLDNLYSRQNTIVYVFFDMKHKALAGSHAFVEDVLLPL 171
Cdd:cd05663  98 IHNGADDNASGVAAMLELAAKLVDSDTSLALSRNLVFIAFSGEELGLLGSKHFVKNPPFPI 158
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 80-175 7.22e-08

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: 52.60  E-value: 7.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  80 GANVIAVQKGpyfGTGNDKMMILSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNLYSRqnTIVYVFFDMKHKALAG 159
Cdd:cd08015   1 TYNVIAEIPG---SDKKDEVVILGAHLDSWHGATGATDNGAGTAVMMEAMRILKAIGSKPKR--TIRVALWGSEEQGLHG 75

                        90
                ....*....|....*...
gi 71993326 160 SHAFVEDVL--LPLMERT 175
Cdd:cd08015  76 SRAYVEKHFgdPPTMQLQ 93
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 23-179 1.45e-06

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: 49.22  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  23 TIADMdrMKHdLSKFLSISRFNETEKSVARAA-------IKRALEAVG-----LNSMTHTFIheesneVGANVIAVQKGp 90
Cdd:cd03876   3 TVDNL--MAH-LQQLQDIADANGGNRAFGSPGynasvdyVKNELKAAGyydvtLQPFTSLYR------TTYNVIAETKG- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  91 yfGTGNDKMMiLSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTldnlYSRQNTIVYVFFDMKHKALAGSHAFVEDvlLP 170
Cdd:cd03876  73 --GDPNNVVM-LGAHLDSVSAGPGINDNGSGSAALLEVALALAK----FKVKNAVRFAWWTAEEFGLLGSKFYVNN--LS 143


                ....*....
gi 71993326 171 LMERTNTKV 179
Cdd:cd03876 144 SEERSKIRL 152
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 82-160 2.35e-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: 49.03  E-value: 2.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  82 NVIAVQKGpyfGTGNDKMMILSANYDTLEGN--------QGVDDNGSGVAAVLEAARVLSTldnlYSRQNTIVYVFFDMK 153
Cdd:cd05642  90 NVVATLKG---SEDPDRVYVVSGHYDSRVSDvmdyesdaPGANDDASGVAVSMELARIFAK----HRPKATIVFTAVAGE 162


                ....*..
gi 71993326 154 HKALAGS 160
Cdd:cd05642 163 EQGLYGS 169
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 102-165 1.22e-04

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: 43.35  E-value: 1.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71993326 102 LSANYDTLEGNQGVDDNGSGVAAVLEAARVLSTLDNLYsrQNTIVYVFFDMKHKALAGSHAFVE 165
Cdd:cd03875  99 LNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQP--KRDIIFLFNGAEENGLLGAHAFIT 160
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 26-181 1.32e-04

M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position.


Pssm-ID: 349875 [Multi-domain]  Cd Length: 286  Bit Score: 43.39  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  26 DMDRMKHDLSKFLS-ISRFNETE----------KSVARAAIKRALEAVGLNSMTHTFIHEesnevgaNVIAVQKGPYFgt 94
Cdd:cd03879  16 SKSNMQDTLESLTSfNNRYYKSQtgvesaewllDQVQAIIASSGRSGATVEQFTHSFPQP-------SIIATIPGSEK-- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  95 gNDKMMILSANYDTLEGNQ-------GVDDNGSGVAAVLEAARVLstLDNLYSRQNTIVYVFFDMKHKALAGSHAFVEDv 167
Cdd:cd03879  87 -SDEIVVIGAHQDSINGSNpsngrapGADDDGSGTVTILEALRVL--LESGFQPKNTIEFHWYAAEEGGLLGSQAIATQ- 162

                       170
                ....*....|....
gi 71993326 168 llplMERTNTKVVG 181
Cdd:cd03879 163 ----YKSEGKNVKA 172
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 46-175 2.43e-03

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: 39.20  E-value: 2.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993326  46 TEKSVARAAIKRALEAvgLNSMTH-----------TFIHEESNEVGA------------NVIAVQKGPYFgtgNDKMMIL 102
Cdd:cd03874   2 ARKLVDLAKIKEDLEY--LSSMPHmagtkgdaalaKYIENSFKNNGLfeveleeyspitNVVGKIEGIEQ---PDRAIII 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71993326 103 SANYDTLEGnqGVDDNGSGVAAVLEAARVLSTLDNLY----SRqnTIVYVFFDMKHKALAGSHAFVEDVLLPLMERT 175
Cdd:cd03874  77 GAHRDSWGY--GAGYPNSGTAVLLEIARLFQQLKKKFgwkpLR--TIYFISWDGSEFGLAGSTELGEDRKASLKDEV 149
 
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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