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Conserved domains on  [gi|1958794991|ref|XP_038936920|]
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N-acetylated-alpha-linked acidic dipeptidase 2 isoform X5 [Rattus norvegicus]

Protein Classification

M28 family metallopeptidase( domain architecture ID 10168803)

M28 family metallopeptidase is a zinc-dependent peptidase that may be an aminopeptidase or a carboxypeptidase with co-catalytic zinc ions; contains a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes; similar to Homo sapiens glutamate carboxypeptidase 2, N-acetylated-alpha-linked acidic dipeptidase 2 and N-acetylated-alpha-linked acidic dipeptidase-like protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 1-277 4.46e-127

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). 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 the 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. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


:

Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 368.87  E-value: 4.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991   1 MAHTDG---LPKLIKDNLKKELLDrKVRMHVHNInkitRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGGIDPTTGTAVL 77
Cdd:cd08022    26 LAGTEGnleLAQWTEDKWREFGLD-DVELEEYDV----PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  78 QEIARSFGKLVNGGWKPRRTIIFASWDAEEFGLLGSTEWAEENAKILQERSIAYINSDSAIEGnYTLRVDCTPLLHQLVY 157
Cdd:cd08022   101 LEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 158 KVAREISSPDDGFESKSLYESWLEKDpspenkerPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKtdkySSYPVYHTI 237
Cdd:cd08022   180 EAAKEVQDPDEGATLKYLPSWWDDTG--------GEIGNLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSN 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958794991 238 YETFELVQNFYDPTFKKQLSVAQLRGALVYELADCVVIPF 277
Cdd:cd08022   248 YDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPILPF 287
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 309-428 6.56e-43

Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the transferrin receptor as shown in its crystal structure.


:

Pssm-ID: 461238  Cd Length: 116  Bit Score: 146.58  E-value: 6.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 309 VSFDPLFSAVKNFSEAASDFHRR---LTQVDLNNPTAVRIMNDQQMLLERAFIDPLGLPGRPFYRHIIFAPSSHNKYAGE 385
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWakkWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958794991 386 SFPGIYDAMFDIenkadthlAWAEVKKHISIAAFTIQAAAGTL 428
Cdd:pfam04253  81 TFPGIRDAIEAG--------DWELAQKQISIVAKAIQSAAETL 115
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 1-277 4.46e-127

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). 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 the 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. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 368.87  E-value: 4.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991   1 MAHTDG---LPKLIKDNLKKELLDrKVRMHVHNInkitRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGGIDPTTGTAVL 77
Cdd:cd08022    26 LAGTEGnleLAQWTEDKWREFGLD-DVELEEYDV----PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  78 QEIARSFGKLVNGGWKPRRTIIFASWDAEEFGLLGSTEWAEENAKILQERSIAYINSDSAIEGnYTLRVDCTPLLHQLVY 157
Cdd:cd08022   101 LEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 158 KVAREISSPDDGFESKSLYESWLEKDpspenkerPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKtdkySSYPVYHTI 237
Cdd:cd08022   180 EAAKEVQDPDEGATLKYLPSWWDDTG--------GEIGNLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSN 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958794991 238 YETFELVQNFYDPTFKKQLSVAQLRGALVYELADCVVIPF 277
Cdd:cd08022   248 YDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPILPF 287
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 309-428 6.56e-43

Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the transferrin receptor as shown in its crystal structure.


Pssm-ID: 461238  Cd Length: 116  Bit Score: 146.58  E-value: 6.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 309 VSFDPLFSAVKNFSEAASDFHRR---LTQVDLNNPTAVRIMNDQQMLLERAFIDPLGLPGRPFYRHIIFAPSSHNKYAGE 385
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWakkWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958794991 386 SFPGIYDAMFDIenkadthlAWAEVKKHISIAAFTIQAAAGTL 428
Cdd:pfam04253  81 TFPGIRDAIEAG--------DWELAQKQISIVAKAIQSAAETL 115
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 35-271 7.83e-36

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: 132.56  E-value: 7.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  35 TRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGG---IDPTTGTAVLQEIARSFGKLvngGWKPRRTIIFASWDAEEFGLL 111
Cdd:COG2234    44 GDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSIGpgaDDNASGVAALLELARALAAL---GPKPKRTIRFVAFGAEEQGLL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 112 GSTEWAeENAKILQERSIAYINSDSAIEGNYTLRvdctpllhqlVYKVAREISSpddgfESKSLYESWLEKDPSPENKER 191
Cdd:COG2234   121 GSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNY----------LYVDGDGGSP-----ELADLLEAAAKAYLPGLGVDP 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 192 PRINKLGSGSDFeAYFQRLGIASGRARytknkkTDKYSSYPVYHTIYETFELVqnfyDPTFKKQlsVAQLRGALVYELAD 271
Cdd:COG2234   185 PEETGGYGRSDH-APFAKAGIPALFLF------TGAEDYHPDYHTPSDTLDKI----DLDALAK--VAQLLAALVYELAN 251
Peptidase_M28 pfam04389
Peptidase family M28;
39-242 3.97e-24

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 98.90  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  39 NVIGTIRGSTePDRYVILGGHRDSWVFG-GI-DPTTGTAVLQEIARSFGKlvngGWKPRRTIIFASWDAEEFGLLGSTEW 116
Cdd:pfam04389   1 NVIAKLPGKA-PDEVVLLSAHYDSVGTGpGAdDNASGVAALLELARVLAA----GQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 117 AEEN---AKILqersiAYINSDSAIEGNYTLRVDCTPLLHQLVYKVAREISSPddgfeskslYESWLEKDPSPENKERpr 193
Cdd:pfam04389  76 AKSHpplKKIR-----AVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKP---------YGVTLAEDPFQERGGP-- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958794991 194 inklgSGSDFEAyFQRLGIASGRARYTKNKktdkyssyPVYHTIYETFE 242
Cdd:pfam04389 140 -----GRSDHAP-FIKAGIPGLDLAFTDFG--------YRYHTPADTID 174
PRK08262 PRK08262
M20 family peptidase;
87-129 3.42e-03

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 39.54  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958794991  87 LVNGGWKPRRTIIFASWDAEEFGLLGstewAEENAKILQERSI 129
Cdd:PRK08262  169 LLAQGFQPRRTIYLAFGHDEEVGGLG----ARAIAELLKERGV 207
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 1-277 4.46e-127

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). 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 the 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. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 368.87  E-value: 4.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991   1 MAHTDG---LPKLIKDNLKKELLDrKVRMHVHNInkitRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGGIDPTTGTAVL 77
Cdd:cd08022    26 LAGTEGnleLAQWTEDKWREFGLD-DVELEEYDV----PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  78 QEIARSFGKLVNGGWKPRRTIIFASWDAEEFGLLGSTEWAEENAKILQERSIAYINSDSAIEGnYTLRVDCTPLLHQLVY 157
Cdd:cd08022   101 LEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 158 KVAREISSPDDGFESKSLYESWLEKDpspenkerPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKtdkySSYPVYHTI 237
Cdd:cd08022   180 EAAKEVQDPDEGATLKYLPSWWDDTG--------GEIGNLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSN 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958794991 238 YETFELVQNFYDPTFKKQLSVAQLRGALVYELADCVVIPF 277
Cdd:cd08022   248 YDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPILPF 287
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 32-276 1.03e-77

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: 242.59  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  32 NKITRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGGIDPTTGTAVLQEIARSFGKLV-NGGWKPRRTIIFASWDAEEFGL 110
Cdd:cd03874    52 EEYSPITNVVGKIEGIEQPDRAIIIGAHRDSWGYGAGYPNSGTAVLLEIARLFQQLKkKFGWKPLRTIYFISWDGSEFGL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 111 LGSTEWAEENAKILQERSIAYINSDSAIEGNYTLRVDCTPLLHQLVYKVAREISSPDDGFESKSLYEswlekdpspenke 190
Cdd:cd03874   132 AGSTELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEDWWKHSPN------------- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 191 rPRINKLGSGSDFEAYFQRLGIASGRARYTKNKktdkySSYPVYHTIYETFELVQNFYDPTFKKQLSVAQLRGALVYELA 270
Cdd:cd03874   199 -AKVSNLHQYGDWTPFLNHLGIPVAVFSFKNDR-----NASYPINSSYDTFEWLEKFLDPDFELHSTLAEFVGLLVLSLA 272


                  ....*.
gi 1958794991 271 DCVVIP 276
Cdd:cd03874   273 EDPLLP 278
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 7-278 6.06e-46

M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) subfamily. TfRs 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). While related in sequence to peptidase M28 glutamate carboxypeptidase II (also called prostate-specific membrane antigen or PSMA), TfR lacks the metal ion coordination centers and protease activity of that group.


Pssm-ID: 349946 [Multi-domain]  Cd Length: 285  Bit Score: 160.23  E-value: 6.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991   7 LPKLIKDNLKKELLDrKVRMHVHninkiTRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGGIDPTTGTAVLQEIARSFGK 86
Cdd:cd09848    32 LANYIMNEFKNLKLM-KVWTDEH-----YKIHNIFGVIKGFVEPDRYVVIGAQRDAWGPGAAKSGVGTALLLELARTFSD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  87 LV-NGGWKPRRTIIFASWDAEEFGLLGSTEWAEENAKILQERSIAYINSDSAIEGNYTLRVDCTPLLHQLVYKVAREISS 165
Cdd:cd09848   106 MVkNDGFKPRRSIVFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYISLDGAVLGDDSFKASASPLLYTLIESTMKQVKS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 166 PDDGfeSKSLYEswlekdpSPENKERPRINKLGSGSDFEAYFQRLGIASGRARYTKNkktdkYSSYPVYHTIYETFELVQ 245
Cdd:cd09848   186 PVHS--GQSYYE-------TRSSWWASIVEPLGLDSAAYPFLAFSGIPSVSFHFTED-----DEDYPFLGTKEDTKENLD 251

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958794991 246 NFYDP-TFKKQLSVAQLRGALVYELADCVVIPFN 278
Cdd:cd09848   252 KFTNGeLWEVAAAAAEVAGQMALRLVHDHLLPLD 285
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 309-428 6.56e-43

Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the transferrin receptor as shown in its crystal structure.


Pssm-ID: 461238  Cd Length: 116  Bit Score: 146.58  E-value: 6.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 309 VSFDPLFSAVKNFSEAASDFHRR---LTQVDLNNPTAVRIMNDQQMLLERAFIDPLGLPGRPFYRHIIFAPSSHNKYAGE 385
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWakkWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958794991 386 SFPGIYDAMFDIenkadthlAWAEVKKHISIAAFTIQAAAGTL 428
Cdd:pfam04253  81 TFPGIRDAIEAG--------DWELAQKQISIVAKAIQSAAETL 115
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 35-271 7.83e-36

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: 132.56  E-value: 7.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  35 TRIYNVIGTIRGSTEPDRYVILGGHRDSWVFGG---IDPTTGTAVLQEIARSFGKLvngGWKPRRTIIFASWDAEEFGLL 111
Cdd:COG2234    44 GDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSIGpgaDDNASGVAALLELARALAAL---GPKPKRTIRFVAFGAEEQGLL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 112 GSTEWAeENAKILQERSIAYINSDSAIEGNYTLRvdctpllhqlVYKVAREISSpddgfESKSLYESWLEKDPSPENKER 191
Cdd:COG2234   121 GSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNY----------LYVDGDGGSP-----ELADLLEAAAKAYLPGLGVDP 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 192 PRINKLGSGSDFeAYFQRLGIASGRARytknkkTDKYSSYPVYHTIYETFELVqnfyDPTFKKQlsVAQLRGALVYELAD 271
Cdd:COG2234   185 PEETGGYGRSDH-APFAKAGIPALFLF------TGAEDYHPDYHTPSDTLDKI----DLDALAK--VAQLLAALVYELAN 251
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 37-242 7.93e-29

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: 112.05  E-value: 7.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  37 IYNVIGTIRGSTEPDRYVILGGHRDSWVF--GGIDPTTGTAVLQEIARSFGKLVnggWKPRRTIIFASWDAEEFGLLGST 114
Cdd:cd02690     1 GYNVIATIKGSDKPDEVILIGAHYDSVPLspGANDNASGVAVLLELARVLSKLQ---LKPKRSIRFAFWDAEELGLLGSK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 115 EWAEENaKILQERSIAYINSDSAIEGNYTL----RVDCTPLLHQLVYKVAREISspddgfeskslyeswlekdpSPENKE 190
Cdd:cd02690    78 YYAEQL-LSSLKNIRAALNLDMIGGAGPDLylqtAPGNDALVEKLLRALAHELE--------------------NVVYTV 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958794991 191 RPRINKLGSGSDFEaYFQRLGIASGRARytknkkTDKYSSYPVYHTIYETFE 242
Cdd:cd02690   137 VYKEDGGTGGSDHR-PFLARGIPAASLI------QSESYNFPYYHTTQDTLE 181
Peptidase_M28 pfam04389
Peptidase family M28;
39-242 3.97e-24

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 98.90  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  39 NVIGTIRGSTePDRYVILGGHRDSWVFG-GI-DPTTGTAVLQEIARSFGKlvngGWKPRRTIIFASWDAEEFGLLGSTEW 116
Cdd:pfam04389   1 NVIAKLPGKA-PDEVVLLSAHYDSVGTGpGAdDNASGVAALLELARVLAA----GQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991 117 AEEN---AKILqersiAYINSDSAIEGNYTLRVDCTPLLHQLVYKVAREISSPddgfeskslYESWLEKDPSPENKERpr 193
Cdd:pfam04389  76 AKSHpplKKIR-----AVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKP---------YGVTLAEDPFQERGGP-- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958794991 194 inklgSGSDFEAyFQRLGIASGRARYTKNKktdkyssyPVYHTIYETFE 242
Cdd:pfam04389 140 -----GRSDHAP-FIKAGIPGLDLAFTDFG--------YRYHTPADTID 174
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 18-164 1.48e-18

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: 87.36  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  18 ELLDR------KVR----MHVHNINKITRiYNVIGTIRGSTEPDRYVILGGHRDSWVF--GGIDPTTGTAVLQEIARSFG 85
Cdd:cd03883   198 EMLSRmaargqKIVielkMEAKTYPDATS-RNVIAEITGSKYPDEVVLVGGHLDSWDVgtGAMDDGGGVAISWEALKLIK 276

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794991  86 KLvngGWKPRRTIIFASWDAEEFGLLGSTEWAEENAKILQERSIAyINSDSAIEGNYTLRVDCTPLLHQLVYKVAREIS 164
Cdd:cd03883   277 DL---GLKPKRTIRVVLWTGEEQGLVGAKAYAEAHKDELENHVFA-MESDIGTFTPYGLQFTGSDTARAIVKEVMKLLS 351
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 38-136 7.23e-17

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: 79.18  E-value: 7.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  38 YNVIGTIRGSTEPDRYVILGGHRDSW--VFGGIDPTTGTAVLQEIARSFGKLvngGWKPRRTIIFASWDAEEFGLLGSTE 115
Cdd:cd08015     2 YNVIAEIPGSDKKDEVVILGAHLDSWhgATGATDNGAGTAVMMEAMRILKAI---GSKPKRTIRVALWGSEEQGLHGSRA 78

                          90       100
                  ....*....|....*....|....*....
gi 1958794991 116 WAE---ENAKILQERSI-----AYINSDS 136
Cdd:cd08015    79 YVEkhfGDPPTMQLQRDhkkisAYFNLDN 107
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 38-135 7.29e-16

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: 75.74  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  38 YNVIGTIRGSTEPDRYVILGGHRDSWVFGG-----------IDPTTGTAVLQEIARSFGKlvngGWKPRRTIIFASWDAE 106
Cdd:cd03877     2 HNVVGVLEGSDLPDETIVIGAHYDHLGIGGgdsgdkiyngaDDNASGVAAVLELARYFAK----QKTPKRSIVFAAFTAE 77

                          90       100
                  ....*....|....*....|....*....
gi 1958794991 107 EFGLLGSTEWAeENAKILQERSIAYINSD 135
Cdd:cd03877    78 EKGLLGSKYFA-ENPKFPLDKIVAMLNLD 105
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 28-136 2.17e-15

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: 76.24  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  28 VHNINKITRiYNVIGTIRGSTEPDRYVILGGHRDSW----------VF-GGIDPTTGTAVLQEIARSFGklvNGGWKPRR 96
Cdd:cd05660    51 VSKIEYSTS-HNVVAILPGSKLPDEYIVLSAHWDHLgigppiggdeIYnGAVDNASGVAAVLELARVFA---AQDQRPKR 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958794991  97 TIIFASWDAEEFGLLGSTEWAeENAKILQERSIAYINSDS 136
Cdd:cd05660   127 SIVFLAVTAEEKGLLGSRYYA-ANPIFPLDKIVANLNIDM 165
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 35-118 1.35e-12

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: 68.67  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  35 TRIYNVIGTIRGSTEPDRYVILGGHRDSWVF----------GGIDPTTGTAVLQEIARSFGKlvnggWKPRRTIIFASWD 104
Cdd:cd05642    86 VNISNVVATLKGSEDPDRVYVVSGHYDSRVSdvmdyesdapGANDDASGVAVSMELARIFAK-----HRPKATIVFTAVA 160

                          90
                  ....*....|....
gi 1958794991 105 AEEFGLLGSTEWAE 118
Cdd:cd05642   161 GEEQGLYGSTFLAQ 174
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 38-142 4.01e-11

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: 63.47  E-value: 4.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  38 YNVIGTIRGStEPDRYVILGGHRDSWVFG-GI-DPTTGTAVLQEIARSFGKlvnggWKPRRTIIFASWDAEEFGLLGSTE 115
Cdd:cd03876    64 YNVIAETKGG-DPNNVVMLGAHLDSVSAGpGInDNGSGSAALLEVALALAK-----FKVKNAVRFAWWTAEEFGLLGSKF 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958794991 116 WA-----EENAKILqersiAYINSDSAIEGNY 142
Cdd:cd03876   138 YVnnlssEERSKIR-----LYLNFDMIASPNY 164
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 38-124 5.05e-11

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: 63.03  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  38 YNVIGTIRGSTEPDRYVILGGHRDSwvFGGIDPTT-----------GTAVLQEIARSfgkLVNGGWKPRRTIIFASWDAE 106
Cdd:cd03879    75 PSIIATIPGSEKSDEIVVIGAHQDS--INGSNPSNgrapgadddgsGTVTILEALRV---LLESGFQPKNTIEFHWYAAE 149

                          90       100
                  ....*....|....*....|..
gi 1958794991 107 EFGLLGS----TEWAEENAKIL 124
Cdd:cd03879   150 EGGLLGSqaiaTQYKSEGKNVK 171
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 39-135 8.55e-10

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: 59.39  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  39 NVIGTI-RGSTEPDRYVILGGHRDSWVFGGI----------------DPTTGTAVLQEIARsfgKLVN--GGWKPRRTII 99
Cdd:cd05663    57 NVIGVLpGKGDVADETVVVGAHYDHLGYGGEgslargdeslihngadDNASGVAAMLELAA---KLVDsdTSLALSRNLV 133

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958794991 100 FASWDAEEFGLLGSTEWAeENAKILQERSIAYINSD 135
Cdd:cd05663   134 FIAFSGEELGLLGSKHFV-KNPPFPIKNTVYMINMD 168
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 38-135 4.93e-09

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: 56.81  E-value: 4.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  38 YNVIGTIR--GSTEPDRYVILGGHRDSWVF--GGIDPTTGTAVLQEIARSFGKLvnggwKPRRTIIFASWDAEEFGLLGS 113
Cdd:cd05661    61 HNVIATKKpdNNKNNNDIIIVTSHYDSVVKapGANDNASGTAVTLELARVFKKV-----KTDKELRFIAFGAEENGLLGS 135

                          90       100
                  ....*....|....*....|..
gi 1958794991 114 TEWAEENAKILQERSIAYINSD 135
Cdd:cd05661   136 KYYVASLSEDEIKRTIGVFNLD 157
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 39-113 8.00e-09

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: 56.83  E-value: 8.00e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794991  39 NVIGTIRG-STEPDRYVILGGHRDSWV--FGGIDPTTGTAVLQEIARSFgklVNGGWKPRRTIIFASWDAEEFGLLGS 113
Cdd:cd03875    81 NIVVRISGkNSNSLPALLLNAHFDSVPtsPGATDDGMGVAVMLEVLRYL---SKSGHQPKRDIIFLFNGAEENGLLGA 155
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 39-119 3.79e-07

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: 51.29  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  39 NVIGTIRGSTEPDRYVILGGHRDSW--VFGGIDPTTGTAVLQEIARSFGKLVnggwkPRRTIIFASWDAEEF-----GLL 111
Cdd:cd05640    54 NLIADLPGSYSQDKLILIGAHYDTVpgSPGADDNASGVAALLELARLLATLD-----PNHTLRFVAFDLEEYpffarGLM 128


                  ....*...
gi 1958794991 112 GSTEWAEE 119
Cdd:cd05640   129 GSHAYAED 136
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 39-135 1.67e-06

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: 49.39  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  39 NVIGTIRGSTEPDRYVILGGHRD------SWVFGGIDP-TTGTAVLQEIARSFGKlvnggWKPRRTIIFASWDAEEFGLL 111
Cdd:cd05662    64 NVLAVIKGSEPPTKWRVVSAHYDhlgirgGKIYNGADDnASGVAALLALAEYFKK-----HPPKHNVIFAATDAEEPGLR 138

                          90       100
                  ....*....|....*....|....*
gi 1958794991 112 GSTEWAEenAKILQERSIAY-INSD 135
Cdd:cd05662   139 GSYAFVE--ALKVPRAQIELnINLD 161
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 39-122 8.47e-04

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. 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. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349870 [Multi-domain]  Cd Length: 200  Bit Score: 40.49  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794991  39 NVIGTIRGsTEPDRYVILGGHRDS-------WVF----------------GGIDPTTGTAVLQEIARSFGKLvngGWKPR 95
Cdd:cd03873     1 NLIARLGG-GEGGKSVALGAHLDVvpagegdNRDppfaedteeegrlygrGALDDKGGVAAALEALKRLKEN---GFKPK 76

                          90       100
                  ....*....|....*....|....*..
gi 1958794991  96 RTIIFASWDAEEFGLLGSTEWAEENAK 122
Cdd:cd03873    77 GTIVVAFTADEEVGSGGGKGLLSKFLL 103
PRK08262 PRK08262
M20 family peptidase;
87-129 3.42e-03

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 39.54  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958794991  87 LVNGGWKPRRTIIFASWDAEEFGLLGstewAEENAKILQERSI 129
Cdd:PRK08262  169 LLAQGFQPRRTIYLAFGHDEEVGGLG----ARAIAELLKERGV 207
 
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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