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Conserved domains on  [gi|1953328464|ref|XP_038285728|]
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N-acetylated-alpha-linked acidic dipeptidase 2 isoform X5 [Canis lupus familiaris]

Protein Classification

M28_PSMA_like and TFR_dimer domain-containing protein( domain architecture ID 10168803)

M28_PSMA_like and TFR_dimer domain-containing 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 ...
 37-331 3.78e-125

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: 366.17  E-value: 3.78e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  37 KYYYGMSHMGGTGppddswkGSLNVDYNIGPGF--AGHESFRKVRMHVhntnkitRIYNVIGTIRGSVEPDRYVILGGHR 114
Cdd:cd08022    18 RYYTSGPHLAGTE-------GNLELAQWTEDKWreFGLDDVELEEYDV-------PIWNVIGTIRGSEEPDEYIILGNHR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 115 DSWVFGAIDPTSGAAVLQEIVQSFGKLMSRGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKTLQERSIAYINSDSSIEG 194
Cdd:cd08022    84 DAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWLQERAVAYLNVDVAVSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 195 nYTLRVDCTPLLYQLVYKLTKEISSPDDGFESKSLYESWLEKDpssentnfPRINKLGSGSDFEAYFQRLGIASGRARYT 274
Cdd:cd08022   164 -STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDTG--------GEIGNLGSGSDYTPFLDHLGIASIDFGFS 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953328464 275 KNRKtekySSYPVYHTIYETFELVENFYDPTFKKQLSVAQLRAALVYELADSKIIPF 331
Cdd:cd08022   235 GGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPILPF 287
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 363-482 6.82e-44

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: 150.43  E-value: 6.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 363 VSFDSLFSAVKNFSDAASDFHRR---LRQVDLNNPIAVRIMNDQLMLLERAFIDPLGLPGRRFYRHIIFAPSSHNKYAGE 439
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWakkWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1953328464 440 SFPGIYDAmfdIENKDdprsaWTEVKKHISIAAFTIQAAAGTL 482
Cdd:pfam04253  81 TFPGIRDA---IEAGD-----WELAQKQISIVAKAIQSAAETL 115
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 37-331 3.78e-125

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: 366.17  E-value: 3.78e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  37 KYYYGMSHMGGTGppddswkGSLNVDYNIGPGF--AGHESFRKVRMHVhntnkitRIYNVIGTIRGSVEPDRYVILGGHR 114
Cdd:cd08022    18 RYYTSGPHLAGTE-------GNLELAQWTEDKWreFGLDDVELEEYDV-------PIWNVIGTIRGSEEPDEYIILGNHR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 115 DSWVFGAIDPTSGAAVLQEIVQSFGKLMSRGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKTLQERSIAYINSDSSIEG 194
Cdd:cd08022    84 DAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWLQERAVAYLNVDVAVSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 195 nYTLRVDCTPLLYQLVYKLTKEISSPDDGFESKSLYESWLEKDpssentnfPRINKLGSGSDFEAYFQRLGIASGRARYT 274
Cdd:cd08022   164 -STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDTG--------GEIGNLGSGSDYTPFLDHLGIASIDFGFS 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953328464 275 KNRKtekySSYPVYHTIYETFELVENFYDPTFKKQLSVAQLRAALVYELADSKIIPF 331
Cdd:cd08022   235 GGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPILPF 287
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 363-482 6.82e-44

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: 150.43  E-value: 6.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 363 VSFDSLFSAVKNFSDAASDFHRR---LRQVDLNNPIAVRIMNDQLMLLERAFIDPLGLPGRRFYRHIIFAPSSHNKYAGE 439
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWakkWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1953328464 440 SFPGIYDAmfdIENKDdprsaWTEVKKHISIAAFTIQAAAGTL 482
Cdd:pfam04253  81 TFPGIRDA---IEAGD-----WELAQKQISIVAKAIQSAAETL 115
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 46-326 4.52e-35

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: 131.41  E-value: 4.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  46 GGTGPPDDSWKGSLNVDYNIGPGFAGHESFRKVRMHVHNTNKITRIYNVIGTIRGSVEPDRYVILGGHRDSWVF---GAI 122
Cdd:COG2234     1 ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSigpGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 123 DPTSGAAVLQEIVQSFGKLmsrGWRPRRTIIFASWDAEEFGLLGSTEWAeENVKTLQERSIAYINSDSSIEGNYTLRvdc 202
Cdd:COG2234    81 DNASGVAALLELARALAAL---GPKPKRTIRFVAFGAEEQGLLGSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNY--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 203 tpllyqlVYKLTKEISSpddgfESKSLYESWLEKDPSSENTNFPRINKLGSGSDFeAYFQRLGIASGRARytknrkTEKY 282
Cdd:COG2234   154 -------LYVDGDGGSP-----ELADLLEAAAKAYLPGLGVDPPEETGGYGRSDH-APFAKAGIPALFLF------TGAE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1953328464 283 SSYPVYHTIYETFELVenfyDPTFKKQlsVAQLRAALVYELADS 326
Cdd:COG2234   215 DYHPDYHTPSDTLDKI----DLDALAK--VAQLLAALVYELANA 252
Peptidase_M28 pfam04389
Peptidase family M28;
93-296 3.88e-23

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 96.59  E-value: 3.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTIRGSvEPDRYVILGGHRDSWVF--GAIDPTSGAAVLQEIVQSFGKlmsrGWRPRRTIIFASWDAEEFGLLGSTEW 170
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTgpGADDNASGVAALLELARVLAA----GQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 171 AEENvkTLQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEISSPddgfeskslYESWLEKDPSSENTNFprink 250
Cdd:pfam04389  76 AKSH--PPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKP---------YGVTLAEDPFQERGGP----- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953328464 251 lgSGSDFEAyFQRLGIASGRARYTKNRktekyssyPVYHTIYETFE 296
Cdd:pfam04389 140 --GRSDHAP-FIKAGIPGLDLAFTDFG--------YRYHTPADTID 174
PRK09133 PRK09133
hypothetical protein; Provisional
 93-209 2.35e-04

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 43.45  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTIRGSvEPDRYVILGGH-------RDSWV---F------------GAIDPTSGAAVLqeiVQSFGKLMSRGWRPRR 150
Cdd:PRK09133   90 NLVARLRGT-DPKKPILLLAHmdvveakREDWTrdpFklveengyfygrGTSDDKADAAIW---VATLIRLKREGFKPKR 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953328464 151 TIIFASWDAEEFGLLGSTEWAEENVKTLQERSIAyINSDssieGNYTLRVDCTPLLYQL 209
Cdd:PRK09133  166 DIILALTGDEEGTPMNGVAWLAENHRDLIDAEFA-LNEG----GGGTLDEDGKPVLLTV 219
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 37-331 3.78e-125

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: 366.17  E-value: 3.78e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  37 KYYYGMSHMGGTGppddswkGSLNVDYNIGPGF--AGHESFRKVRMHVhntnkitRIYNVIGTIRGSVEPDRYVILGGHR 114
Cdd:cd08022    18 RYYTSGPHLAGTE-------GNLELAQWTEDKWreFGLDDVELEEYDV-------PIWNVIGTIRGSEEPDEYIILGNHR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 115 DSWVFGAIDPTSGAAVLQEIVQSFGKLMSRGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKTLQERSIAYINSDSSIEG 194
Cdd:cd08022    84 DAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWLQERAVAYLNVDVAVSG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 195 nYTLRVDCTPLLYQLVYKLTKEISSPDDGFESKSLYESWLEKDpssentnfPRINKLGSGSDFEAYFQRLGIASGRARYT 274
Cdd:cd08022   164 -STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDTG--------GEIGNLGSGSDYTPFLDHLGIASIDFGFS 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953328464 275 KNRKtekySSYPVYHTIYETFELVENFYDPTFKKQLSVAQLRAALVYELADSKIIPF 331
Cdd:cd08022   235 GGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPILPF 287
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 86-330 5.93e-76

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: 239.89  E-value: 5.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  86 NKITRIYNVIGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGAAVLQEIVQSFGKLMSR-GWRPRRTIIFASWDAEEFGL 164
Cdd:cd03874    52 EEYSPITNVVGKIEGIEQPDRAIIIGAHRDSWGYGAGYPNSGTAVLLEIARLFQQLKKKfGWKPLRTIYFISWDGSEFGL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 165 LGSTEWAEENVKTLQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEISSPDDGFESKSLYEswlekdpssentn 244
Cdd:cd03874   132 AGSTELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEDWWKHSPN------------- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 245 fPRINKLGSGSDFEAYFQRLGIASGRARYTKNRktekySSYPVYHTIYETFELVENFYDPTFKKQLSVAQLRAALVYELA 324
Cdd:cd03874   199 -AKVSNLHQYGDWTPFLNHLGIPVAVFSFKNDR-----NASYPINSSYDTFEWLEKFLDPDFELHSTLAEFVGLLVLSLA 272


                  ....*.
gi 1953328464 325 DSKIIP 330
Cdd:cd03874   273 EDPLLP 278
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 363-482 6.82e-44

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: 150.43  E-value: 6.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 363 VSFDSLFSAVKNFSDAASDFHRR---LRQVDLNNPIAVRIMNDQLMLLERAFIDPLGLPGRRFYRHIIFAPSSHNKYAGE 439
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWakkWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1953328464 440 SFPGIYDAmfdIENKDdprsaWTEVKKHISIAAFTIQAAAGTL 482
Cdd:pfam04253  81 TFPGIRDA---IEAGD-----WELAQKQISIVAKAIQSAAETL 115
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 72-324 3.52e-41

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: 148.68  E-value: 3.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  72 HESFRKVRMHVHNTNKITRIYNVIGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGAAVLQEIVQSFGKLMS-RGWRPRR 150
Cdd:cd09848    37 MNEFKNLKLMKVWTDEHYKIHNIFGVIKGFVEPDRYVVIGAQRDAWGPGAAKSGVGTALLLELARTFSDMVKnDGFKPRR 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 151 TIIFASWDAEEFGLLGSTEWAEENVKTLQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEISSPDDGfeskslY 230
Cdd:cd09848   117 SIVFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYISLDGAVLGDDSFKASASPLLYTLIESTMKQVKSPVHS------G 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 231 ESWLEKDPSSENTNfprINKLGSGSDFEAYFQRLGIASGRARYTKNRKtekysSYPVYHTIYETFELVENFydpTFKKQL 310
Cdd:cd09848   191 QSYYETRSSWWASI---VEPLGLDSAAYPFLAFSGIPSVSFHFTEDDE-----DYPFLGTKEDTKENLDKF---TNGELW 259

                         250
                  ....*....|....
gi 1953328464 311 SVAQLRAALVYELA 324
Cdd:cd09848   260 EVAAAAAEVAGQMA 273
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 46-326 4.52e-35

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: 131.41  E-value: 4.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  46 GGTGPPDDSWKGSLNVDYNIGPGFAGHESFRKVRMHVHNTNKITRIYNVIGTIRGSVEPDRYVILGGHRDSWVF---GAI 122
Cdd:COG2234     1 ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSigpGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 123 DPTSGAAVLQEIVQSFGKLmsrGWRPRRTIIFASWDAEEFGLLGSTEWAeENVKTLQERSIAYINSDSSIEGNYTLRvdc 202
Cdd:COG2234    81 DNASGVAALLELARALAAL---GPKPKRTIRFVAFGAEEQGLLGSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNY--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 203 tpllyqlVYKLTKEISSpddgfESKSLYESWLEKDPSSENTNFPRINKLGSGSDFeAYFQRLGIASGRARytknrkTEKY 282
Cdd:COG2234   154 -------LYVDGDGGSP-----ELADLLEAAAKAYLPGLGVDPPEETGGYGRSDH-APFAKAGIPALFLF------TGAE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1953328464 283 SSYPVYHTIYETFELVenfyDPTFKKQlsVAQLRAALVYELADS 326
Cdd:COG2234   215 DYHPDYHTPSDTLDKI----DLDALAK--VAQLLAALVYELANA 252
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 91-296 4.83e-27

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: 107.81  E-value: 4.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  91 IYNVIGTIRGSVEPDRYVILGGHRDSWVF--GAIDPTSGAAVLQEIVQSFGKLmsrGWRPRRTIIFASWDAEEFGLLGST 168
Cdd:cd02690     1 GYNVIATIKGSDKPDEVILIGAHYDSVPLspGANDNASGVAVLLELARVLSKL---QLKPKRSIRFAFWDAEELGLLGSK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 169 EWAEENvKTLQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEISSPDDgfeskslyeswlekdpSSENTNFPRI 248
Cdd:cd02690    78 YYAEQL-LSSLKNIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELE----------------NVVYTVVYKE 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953328464 249 NKLGSGSDFEaYFQRLGIASGRARYTknrkteKYSSYPVYHTIYETFE 296
Cdd:cd02690   141 DGGTGGSDHR-PFLARGIPAASLIQS------ESYNFPYYHTTQDTLE 181
Peptidase_M28 pfam04389
Peptidase family M28;
93-296 3.88e-23

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 96.59  E-value: 3.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTIRGSvEPDRYVILGGHRDSWVF--GAIDPTSGAAVLQEIVQSFGKlmsrGWRPRRTIIFASWDAEEFGLLGSTEW 170
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTgpGADDNASGVAALLELARVLAA----GQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 171 AEENvkTLQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEISSPddgfeskslYESWLEKDPSSENTNFprink 250
Cdd:pfam04389  76 AKSH--PPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKP---------YGVTLAEDPFQERGGP----- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953328464 251 lgSGSDFEAyFQRLGIASGRARYTKNRktekyssyPVYHTIYETFE 296
Cdd:pfam04389 140 --GRSDHAP-FIKAGIPGLDLAFTDFG--------YRYHTPADTID 174
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 80-327 8.20e-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: 85.44  E-value: 8.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  80 MHVHNTNKITRiYNVIGTIRGSVEPDRYVILGGHRDSWVF--GAIDPTSGAAVLQEIVQSFGKLmsrGWRPRRTIIFASW 157
Cdd:cd03883   216 MEAKTYPDATS-RNVIAEITGSKYPDEVVLVGGHLDSWDVgtGAMDDGGGVAISWEALKLIKDL---GLKPKRTIRVVLW 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 158 DAEEFGLLGSTEWAEENVKTLQERSIAyINSDSSIEGNYTLRVDCTP---LLYQLVYKLTKEISspddgfeskslyeswl 234
Cdd:cd03883   292 TGEEQGLVGAKAYAEAHKDELENHVFA-MESDIGTFTPYGLQFTGSDtarAIVKEVMKLLSPLG---------------- 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464 235 ekdpsseNTNFPriNKLGSGSDFEAYfQRLGIASGRARYtknrKTEKYSSYpvYHTIYETFELVenfyDPtfkKQLSV-A 313
Cdd:cd03883   355 -------ITQVL--PKAGVGPDISFL-KAAGVPGASLIQ----DNSDYFDY--HHTAGDTMDVM----DP---KQLDQnV 411

                         250
                  ....*....|....
gi 1953328464 314 QLRAALVYELADSK 327
Cdd:cd03883   412 AAWASLAYVIADMD 425
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 92-190 1.19e-16

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: 78.79  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  92 YNVIGTIRGSVEPDRYVILGGHRDSW--VFGAIDPTSGAAVLQEIVQSFGKLmsrGWRPRRTIIFASWDAEEFGLLGSTE 169
Cdd:cd08015     2 YNVIAEIPGSDKKDEVVILGAHLDSWhgATGATDNGAGTAVMMEAMRILKAI---GSKPKRTIRVALWGSEEQGLHGSRA 78

                          90       100
                  ....*....|....*....|....*....
gi 1953328464 170 WAE---ENVKTLQERSI-----AYINSDS 190
Cdd:cd08015    79 YVEkhfGDPPTMQLQRDhkkisAYFNLDN 107
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 92-189 1.33e-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: 69.58  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  92 YNVIGTIRGSVEPDRYVILGGHRDSWVF-----------GAIDPTSGAAVLQEIVQSFGKlmsrGWRPRRTIIFASWDAE 160
Cdd:cd03877     2 HNVVGVLEGSDLPDETIVIGAHYDHLGIgggdsgdkiynGADDNASGVAAVLELARYFAK----QKTPKRSIVFAAFTAE 77

                          90       100
                  ....*....|....*....|....*....
gi 1953328464 161 EFGLLGSTEWAeENVKTLQERSIAYINSD 189
Cdd:cd03877    78 EKGLLGSKYFA-ENPKFPLDKIVAMLNLD 105
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 67-190 3.88e-13

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: 69.70  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  67 PGFAGHESFRKVRMhVHNTNKITRiYNVIGTIRGSVEPDRYVILGGHRDSW----------VF-GAIDPTSGAAVLQEIV 135
Cdd:cd05660    37 PAGSDGSYLQAVPL-VSKIEYSTS-HNVVAILPGSKLPDEYIVLSAHWDHLgigppiggdeIYnGAVDNASGVAAVLELA 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953328464 136 QSFGKlmsRGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKTLqERSIAYINSDS 190
Cdd:cd05660   115 RVFAA---QDQRPKRSIVFLAVTAEEKGLLGSRYYAANPIFPL-DKIVANLNIDM 165
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 89-172 2.89e-11

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: 64.82  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  89 TRIYNVIGTIRGSVEPDRYVILGGHRDSWVF----------GAIDPTSGAAVLQEIVQSFGKlmsrgWRPRRTIIFASWD 158
Cdd:cd05642    86 VNISNVVATLKGSEDPDRVYVVSGHYDSRVSdvmdyesdapGANDDASGVAVSMELARIFAK-----HRPKATIVFTAVA 160

                          90
                  ....*....|....
gi 1953328464 159 AEEFGLLGSTEWAE 172
Cdd:cd05642   161 GEEQGLYGSTFLAQ 174
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 92-167 2.07e-10

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: 61.49  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  92 YNVIGTIRGSVEPDRYVILGGHRDS---WVF------GAIDPTSGAAVLQEivqSFGKLMSRGWRPRRTIIFASWDAEEF 162
Cdd:cd03879    75 PSIIATIPGSEKSDEIVVIGAHQDSingSNPsngrapGADDDGSGTVTILE---ALRVLLESGFQPKNTIEFHWYAAEEG 151


                  ....*
gi 1953328464 163 GLLGS 167
Cdd:cd03879   152 GLLGS 156
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 73-178 1.71e-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: 59.14  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  73 ESFRKVRMHVHNTNKITRIYNVIGTIRGSV-EPDRYVILGGHRDSWV--FGAIDPTSGAAVLQEIVQSFGKlmsRGWRPR 149
Cdd:cd03875    61 GSGSFNFLSSGMTLVYFEVTNIVVRISGKNsNSLPALLLNAHFDSVPtsPGATDDGMGVAVMLEVLRYLSK---SGHQPK 137

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1953328464 150 RTIIFASWDAEEFGLLGST-----EWAEENVKTL 178
Cdd:cd03875   138 RDIIFLFNGAEENGLLGAHafitqHPWAKNVRAF 171
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 92-196 6.89e-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: 56.92  E-value: 6.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  92 YNVIGTIRGSvEPDRYVILGGHRDSwVF---GAIDPTSGAAVLQEIVQSFGKlmsrgWRPRRTIIFASWDAEEFGLLGST 168
Cdd:cd03876    64 YNVIAETKGG-DPNNVVMLGAHLDS-VSagpGINDNGSGSAALLEVALALAK-----FKVKNAVRFAWWTAEEFGLLGSK 136

                          90       100
                  ....*....|....*....|....*...
gi 1953328464 169 EWAEENVKTLQERSIAYINSDSSIEGNY 196
Cdd:cd03876   137 FYVNNLSSEERSKIRLYLNFDMIASPNY 164
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 92-189 3.64e-07

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: 51.42  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  92 YNVIGTIR--GSVEPDRYVILGGHRDSWVF--GAIDPTSGAAVLQEIVQSFGKLMSRgwrprRTIIFASWDAEEFGLLGS 167
Cdd:cd05661    61 HNVIATKKpdNNKNNNDIIIVTSHYDSVVKapGANDNASGTAVTLELARVFKKVKTD-----KELRFIAFGAEENGLLGS 135

                          90       100
                  ....*....|....*....|..
gi 1953328464 168 TEWAEENVKTLQERSIAYINSD 189
Cdd:cd05661   136 KYYVASLSEDEIKRTIGVFNLD 157
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 93-179 7.07e-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: 50.91  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTIRGSVEPDRYVILGGHRDSW--VFGAIDPTSGAAVLQEIVQSFGKLmsrgwRPRRTIIFASWDAEEF-----GLL 165
Cdd:cd05640    54 NLIADLPGSYSQDKLILIGAHYDTVpgSPGADDNASGVAALLELARLLATL-----DPNHTLRFVAFDLEEYpffarGLM 128

                          90
                  ....*....|....
gi 1953328464 166 GSTEWAEENVKTLQ 179
Cdd:cd05640   129 GSHAYAEDLLRPLT 142
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 93-189 7.50e-07

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: 50.53  E-value: 7.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTI-RGSVEPDRYVILGGHRDSWVFG----------------AIDPTSGAAVLQEIVQsfgKLMSRGWRP--RRTII 153
Cdd:cd05663    57 NVIGVLpGKGDVADETVVVGAHYDHLGYGgegslargdeslihngADDNASGVAAMLELAA---KLVDSDTSLalSRNLV 133

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1953328464 154 FASWDAEEFGLLGSTEWAEENVKTLqERSIAYINSD 189
Cdd:cd05663   134 FIAFSGEELGLLGSKHFVKNPPFPI-KNTVYMINMD 168
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 93-172 9.72e-07

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: 50.16  E-value: 9.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTIRGSVEPDRYVILGGHRD------SWVF-GAIDPTSGAAVLQEIVQSFGKlmsrgWRPRRTIIFASWDAEEFGLL 165
Cdd:cd05662    64 NVLAVIKGSEPPTKWRVVSAHYDhlgirgGKIYnGADDNASGVAALLALAEYFKK-----HPPKHNVIFAATDAEEPGLR 138


                  ....*..
gi 1953328464 166 GSTEWAE 172
Cdd:cd05662   139 GSYAFVE 145
PRK09133 PRK09133
hypothetical protein; Provisional
 93-209 2.35e-04

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 43.45  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953328464  93 NVIGTIRGSvEPDRYVILGGH-------RDSWV---F------------GAIDPTSGAAVLqeiVQSFGKLMSRGWRPRR 150
Cdd:PRK09133   90 NLVARLRGT-DPKKPILLLAHmdvveakREDWTrdpFklveengyfygrGTSDDKADAAIW---VATLIRLKREGFKPKR 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953328464 151 TIIFASWDAEEFGLLGSTEWAEENVKTLQERSIAyINSDssieGNYTLRVDCTPLLYQL 209
Cdd:PRK09133  166 DIILALTGDEEGTPMNGVAWLAENHRDLIDAEFA-LNEG----GGGTLDEDGKPVLLTV 219
PRK08262 PRK08262
M20 family peptidase;
117-183 4.21e-04

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 42.62  E-value: 4.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953328464 117 WVFGAIDPTSGAAVLQEIVQSfgkLMSRGWRPRRTIIFASWDAEEFGLLGstewAEENVKTLQERSI 183
Cdd:PRK08262  148 WGRGALDDKGSLVAILEAAEA---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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