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Conserved domains on  [gi|767926201|ref|XP_011510917|]
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inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2 isoform X4 [Homo sapiens]

Protein Classification

M28_PMSA_TfR_like and TFR_dimer domain-containing protein( domain architecture ID 11978079)

protein containing domains PA, M28_PMSA_TfR_like, and TFR_dimer

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 389-610 7.31e-81

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: 259.54  E-value: 7.31e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 389 KTVTNVVGFVMGLTSPDRYIIVGSHHHTAHsYNGQEWASSTAIITAFIRALMSKVKR-GWRPDRTIVFCSWGGTAFGNIG 467
Cdd:cd03874   55 SPITNVVGKIEGIEQPDRAIIIGAHRDSWG-YGAGYPNSGTAVLLEIARLFQQLKKKfGWKPLRTIYFISWDGSEFGLAG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 468 SYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQ-----CPETNISSIQIQGDADYF 542
Cdd:cd03874  134 STELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEdwwkhSPNAKVSNLHQYGDWTPF 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767926201 543 INHLGVPIVQFAYEDIKtleGPSFLSEARFSTRaTKIEEM-DPSFNLHETITKLSGEVILQIANEPVLP 610
Cdd:cd03874  214 LNHLGIPVAVFSFKNDR---NASYPINSSYDTF-EWLEKFlDPDFELHSTLAEFVGLLVLSLAEDPLLP 278
PA super family cl28883
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 268-374 2.26e-56

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


The actual alignment was detected with superfamily member cd02131:

Pssm-ID: 333703  Cd Length: 153  Bit Score: 189.76  E-value: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 268 DLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKT 347
Cdd:cd02131    1 DLLYSYAAYSAKGTLQAEVVDVQYGSVEDLRRIRDNMNVTNQIALLKLGQAPLLYKLSLLEEAGFGGVLLYVDPCDLPKT 80

                         90       100
                 ....*....|....*....|....*..
gi 767926201 348 VNPSHDTFMVSLNPGGDPSTPGYPSVE 374
Cdd:cd02131   81 RHTWHQAFMVSLNPGGDPSTPGYPSAD 107
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 630-743 3.78e-06

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: 46.42  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  630 NTHQLLAMALRLRESAELFQSDEMRpANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPG--FYRNILY----HLDEKTS 703
Cdd:pfam04253   2 SLEPLRKAIEKFKKAAKEFDAWAKK-WEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGrpWFKHVVFapglWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767926201  704 RF-----SILIEAWehckplasnETLQEALSEVLNSINSAQVYFK 743
Cdd:pfam04253  81 TFpgirdAIEAGDW---------ELAQKQISIVAKAIQSAAETLK 116
 
Name Accession Description Interval E-value
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 389-610 7.31e-81

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: 259.54  E-value: 7.31e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 389 KTVTNVVGFVMGLTSPDRYIIVGSHHHTAHsYNGQEWASSTAIITAFIRALMSKVKR-GWRPDRTIVFCSWGGTAFGNIG 467
Cdd:cd03874   55 SPITNVVGKIEGIEQPDRAIIIGAHRDSWG-YGAGYPNSGTAVLLEIARLFQQLKKKfGWKPLRTIYFISWDGSEFGLAG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 468 SYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQ-----CPETNISSIQIQGDADYF 542
Cdd:cd03874  134 STELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEdwwkhSPNAKVSNLHQYGDWTPF 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767926201 543 INHLGVPIVQFAYEDIKtleGPSFLSEARFSTRaTKIEEM-DPSFNLHETITKLSGEVILQIANEPVLP 610
Cdd:cd03874  214 LNHLGIPVAVFSFKNDR---NASYPINSSYDTF-EWLEKFlDPDFELHSTLAEFVGLLVLSLAEDPLLP 278
PA_hNAALADL2_like cd02131
PA_hNAALADL2_like: Protease-associated domain containing proteins like human N-acetylated ...
 268-374 2.26e-56

PA_hNAALADL2_like: Protease-associated domain containing proteins like human N-acetylated alpha-linked acidic dipeptidase-like 2 protein (hNAALADL2). This group contains various PA domain-containing proteins similar to hNAALADL2. The function of hNAALADL2 is unknown. This gene has been mapped to a chromosomal region associated with Cornelia de Lange syndrome. The significance of the PA domain to hNAALADL2 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239046  Cd Length: 153  Bit Score: 189.76  E-value: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 268 DLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKT 347
Cdd:cd02131    1 DLLYSYAAYSAKGTLQAEVVDVQYGSVEDLRRIRDNMNVTNQIALLKLGQAPLLYKLSLLEEAGFGGVLLYVDPCDLPKT 80

                         90       100
                 ....*....|....*....|....*..
gi 767926201 348 VNPSHDTFMVSLNPGGDPSTPGYPSVE 374
Cdd:cd02131   81 RHTWHQAFMVSLNPGGDPSTPGYPSAD 107
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 369-557 3.56e-15

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: 75.94  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 369 GYPSVEIRVVSMQVQTVTKLKTVTNVVGFVMGLTSPDRYIIVGSHH-HTAHSYNGqewA----SSTAIITAFIRALMskv 443
Cdd:COG2234   24 AAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYdSVGSIGPG---AddnaSGVAALLELARALA--- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 444 KRGWRPDRTIVFCSWGGTAFGNIGSYEWGEDFkKVLQKNVVAYISLHSPIRGNSSLY-----PVASPSLQQLvVEKNNFN 518
Cdd:COG2234   98 ALGPKPKRTIRFVAFGAEEQGLLGSRYYAENL-KAPLEKIVAVLNLDMIGRGGPRNYlyvdgDGGSPELADL-LEAAAKA 175

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767926201 519 CTRRAQCPETNISSIQIQGDADYFINHlGVPIVQFAYED 557
Cdd:COG2234  176 YLPGLGVDPPEETGGYGRSDHAPFAKA-GIPALFLFTGA 213
Peptidase_M28 pfam04389
Peptidase family M28;
393-557 7.93e-08

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 53.06  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  393 NVVGFVMGlTSPDRYIIVGSHH-HTAHSY----NgqewASSTAIITAFIRALmskvKRGWRPDRTIVFCSWGGTAFGNIG 467
Cdd:pfam04389   1 NVIAKLPG-KAPDEVVLLSAHYdSVGTGPgaddN----ASGVAALLELARVL----AAGQRPKRSVRFLFFDAEEAGLLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  468 SYEWGEdfKKVLQKNVVAYISLHSPIRGNSSLYPVASP----SLQQLVVEKNNFNCTRRAQCPETNISsiqIQGDADYFI 543
Cdd:pfam04389  72 SHHFAK--SHPPLKKIRAVINLDMIGSGGPALLFQSGPkgssLLEKYLKAAAKPYGVTLAEDPFQERG---GPGRSDHAP 146

                         170
                  ....*....|....*
gi 767926201  544 -NHLGVPIVQFAYED 557
Cdd:pfam04389 147 fIKAGIPGLDLAFTD 161
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 630-743 3.78e-06

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: 46.42  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  630 NTHQLLAMALRLRESAELFQSDEMRpANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPG--FYRNILY----HLDEKTS 703
Cdd:pfam04253   2 SLEPLRKAIEKFKKAAKEFDAWAKK-WEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGrpWFKHVVFapglWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767926201  704 RF-----SILIEAWehckplasnETLQEALSEVLNSINSAQVYFK 743
Cdd:pfam04253  81 TFpgirdAIEAGDW---------ELAQKQISIVAKAIQSAAETLK 116
 
Name Accession Description Interval E-value
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 389-610 7.31e-81

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: 259.54  E-value: 7.31e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 389 KTVTNVVGFVMGLTSPDRYIIVGSHHHTAHsYNGQEWASSTAIITAFIRALMSKVKR-GWRPDRTIVFCSWGGTAFGNIG 467
Cdd:cd03874   55 SPITNVVGKIEGIEQPDRAIIIGAHRDSWG-YGAGYPNSGTAVLLEIARLFQQLKKKfGWKPLRTIYFISWDGSEFGLAG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 468 SYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQ-----CPETNISSIQIQGDADYF 542
Cdd:cd03874  134 STELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEdwwkhSPNAKVSNLHQYGDWTPF 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767926201 543 INHLGVPIVQFAYEDIKtleGPSFLSEARFSTRaTKIEEM-DPSFNLHETITKLSGEVILQIANEPVLP 610
Cdd:cd03874  214 LNHLGIPVAVFSFKNDR---NASYPINSSYDTF-EWLEKFlDPDFELHSTLAEFVGLLVLSLAEDPLLP 278
PA_hNAALADL2_like cd02131
PA_hNAALADL2_like: Protease-associated domain containing proteins like human N-acetylated ...
 268-374 2.26e-56

PA_hNAALADL2_like: Protease-associated domain containing proteins like human N-acetylated alpha-linked acidic dipeptidase-like 2 protein (hNAALADL2). This group contains various PA domain-containing proteins similar to hNAALADL2. The function of hNAALADL2 is unknown. This gene has been mapped to a chromosomal region associated with Cornelia de Lange syndrome. The significance of the PA domain to hNAALADL2 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239046  Cd Length: 153  Bit Score: 189.76  E-value: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 268 DLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKT 347
Cdd:cd02131    1 DLLYSYAAYSAKGTLQAEVVDVQYGSVEDLRRIRDNMNVTNQIALLKLGQAPLLYKLSLLEEAGFGGVLLYVDPCDLPKT 80

                         90       100
                 ....*....|....*....|....*..
gi 767926201 348 VNPSHDTFMVSLNPGGDPSTPGYPSVE 374
Cdd:cd02131   81 RHTWHQAFMVSLNPGGDPSTPGYPSAD 107
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 390-611 1.71e-43

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: 158.93  E-value: 1.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 390 TVTNVVGFVMGLTSPDRYIIVGSHHhTAHSYNGQEWASSTAIITAFIRALMSKVKRGWRPDRTIVFCSWGGTAFGNIGSY 469
Cdd:cd08022   59 PIWNVIGTIRGSEEPDEYIILGNHR-DAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGST 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 470 EWGEDFKKVLQKNVVAYISLHSPIRGnSSLYPVASPSLQQLVveknnFNCTRRAQCPETNISSI-----------QIQG- 537
Cdd:cd08022  138 EWVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLL-----REAAKEVQDPDEGATLKylpswwddtggEIGNl 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 538 --DADY--FINHLGVPIVQFAYEDIKTLEGP-------SFLSEARFstratkieeMDPSFNLHETITKLSGEVILQIANE 606
Cdd:cd08022  212 gsGSDYtpFLDHLGIASIDFGFSGGPTDPYPhyhsnydSFEWMEKF---------GDPGFKYHVAIAQVWGLLALRLADD 282


                 ....*
gi 767926201 607 PVLPF 611
Cdd:cd08022  283 PILPF 287
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 393-612 1.41e-22

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: 98.60  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 393 NVVGFVMGLTSPDRYIIVGSHHHT-----AHSYNGqewassTAIITAFIRALMSKVK-RGWRPDRTIVFCSWGGTAFGNI 466
Cdd:cd09848   58 NIFGVIKGFVEPDRYVVIGAQRDAwgpgaAKSGVG------TALLLELARTFSDMVKnDGFKPRRSIVFASWSAGDFGSV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 467 GSYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLV----------VEKNNFNCTRRAQCPETNISSIQIQ 536
Cdd:cd09848  132 GATEWLEGYLSSLHLKAFTYISLDGAVLGDDSFKASASPLLYTLIestmkqvkspVHSGQSYYETRSSWWASIVEPLGLD 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 537 GDADYFINHLGVPIVQFAYEDiktlegpsflSEARFSTRATKieeMDPSFNLHE-----------TITKLSGEVILQIAN 605
Cdd:cd09848  212 SAAYPFLAFSGIPSVSFHFTE----------DDEDYPFLGTK---EDTKENLDKftngelwevaaAAAEVAGQMALRLVH 278


                 ....*..
gi 767926201 606 EPVLPFN 612
Cdd:cd09848  279 DHLLPLD 285
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 369-557 3.56e-15

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: 75.94  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 369 GYPSVEIRVVSMQVQTVTKLKTVTNVVGFVMGLTSPDRYIIVGSHH-HTAHSYNGqewA----SSTAIITAFIRALMskv 443
Cdd:COG2234   24 AAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYdSVGSIGPG---AddnaSGVAALLELARALA--- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 444 KRGWRPDRTIVFCSWGGTAFGNIGSYEWGEDFkKVLQKNVVAYISLHSPIRGNSSLY-----PVASPSLQQLvVEKNNFN 518
Cdd:COG2234   98 ALGPKPKRTIRFVAFGAEEQGLLGSRYYAENL-KAPLEKIVAVLNLDMIGRGGPRNYlyvdgDGGSPELADL-LEAAAKA 175

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767926201 519 CTRRAQCPETNISSIQIQGDADYFINHlGVPIVQFAYED 557
Cdd:COG2234  176 YLPGLGVDPPEETGGYGRSDHAPFAKA-GIPALFLFTGA 213
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 392-602 3.39e-12

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: 66.21  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 392 TNVVGFVMGLTSPDRYIIVGSHH-HTAHSYNGQEWASSTAIITAFIRALmSKVKRgwRPDRTIVFCSWGGTAFGNIGSYE 470
Cdd:cd02690    2 YNVIATIKGSDKPDEVILIGAHYdSVPLSPGANDNASGVAVLLELARVL-SKLQL--KPKRSIRFAFWDAEELGLLGSKY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 471 WGEDFkKVLQKNVVAYISLHSPIRGNSSLY----PVASPSLQQLVVEKNNF--NCTRRAQCPETNISsiqiqGDADYFIN 544
Cdd:cd02690   79 YAEQL-LSSLKNIRAALNLDMIGGAGPDLYlqtaPGNDALVEKLLRALAHEleNVVYTVVYKEDGGT-----GGSDHRPF 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767926201 545 H-LGVPIVQFayediktlegpSFLSEARFSTRATkieEMDPSFNLHETITKLSGEVILQ 602
Cdd:cd02690  153 LaRGIPAASL-----------IQSESYNFPYYHT---TQDTLENIDKDTLKRAGDILAS 197
PA_GCPII_like cd02121
PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II ...
 236-374 3.05e-10

PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II (GCPII)-like. This group contains various PA domain-containing proteins similar to GCPII including, GCPIII (NAALADase2) and NAALADase L. These proteins belong to the peptidase M28 family. GCPII is also known N-acetylated-alpha-linked acidic dipeptidase (NAALDase1), folate hydrolase or prostate-specific membrane antigen (PSMA). GCPII is found in various human tissues including prostate, small intestine, and the central nervous system. In the brain, GCPII is known as NAALDase1, it functions as a NAALDase hydrolyzing the neuropeptide N-acetyl-L-aspartyl-L-glutamate (alpha-NAAG), to release free glutamate. In the small intestine, GCPII releases the terminal glutamate from poly-gamma-glutamated folates. GCPII (PSMA) is a useful cancer marker; its expression is markedly increased in prostate cancer and in tumor-associated neovasculature. GCPIII hydrolyzes alpha-NAAG with a lower efficiency than does GCPII; NAALADase L is not able to hydrolyze alpha-NAAG. The GCPII PA domain (referred to as the apical domain) participates in substrate binding and may act as a protein-protein interaction domain.


Pssm-ID: 239036  Cd Length: 220  Bit Score: 60.77  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 236 PSPSTVTLSSsgqcfhPNGQPCSE-EARKDSSQDLLYS---YAAYSAKGTLKAEVIDVSYGMADDLKRIRKIK-NVTNQI 310
Cdd:cd02121    1 PVKRSLILTK------PDGATGKLiEDTVLEEPPSPDVvppFHAYSASGNVTAELVYANYGSPEDFEYLEDLGiDVKGKI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 311 ALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCD-----------LPKT--VNPSH---DTFMVSLNPGGDPSTPGYPSVE 374
Cdd:cd02121   75 VIARYGGIFRGLKVKNAQLAGAVGVIIYSDPADdgyitgengktYPDGpaRPPSGvqrGSVLFMSIGPGDPLTPGYPSKP 154
PA_TfR cd02128
PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This ...
 273-372 4.46e-09

PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This group contains various PA domain-containing proteins similar to human TfR1 and TfR2. TfR1 and TfR2 are type II membrane proteins, belonging to the peptidase M28 family. TfR1 is homodimeric, widely expressed, and a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and this complex is internalized. In addition to its role in iron uptake, TfR1 may participate in cell growth and proliferation. TfR2 also binds Tf but with a significantly lower affinity than does TfR1. TfR2 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. HFE and TfR2 interact in cells. By one model for serum iron sensing, at low or basal iron concentrations, HFE and TFR1 form a complex at the plasma membrane; at increased Tf, Tf competes with HFE for binding of TfR1, resulting in HFE disassociating from TfR1 and associating with TfR2 . The TfR1-TfR2 association might initiate a signal cascade leading to the induction of hepcidin (a small peptide hormone that controls systemic iron levels). Human mutations in TfR2 are associated with a form of hemochromatosis (HFE3). The significance of the PA domain to TfRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239043 [Multi-domain]  Cd Length: 183  Bit Score: 56.64  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 273 YAAYSAKGTLKAEVIDVSYGMADDLKRIRKIK-NVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKTvnPS 351
Cdd:cd02128   20 YVAYSAAGTVTGKLVYANYGRKKDFEDLQSVGvSVNGSVVLVRAGKISFAEKVANAEKLGAVGVLIYPDPADFPID--PS 97

                         90       100
                 ....*....|....*....|..
gi 767926201 352 HDTFMVSLNPG-GDPSTPGYPS 372
Cdd:cd02128   98 ETALFGHVHLGtGDPYTPGFPS 119
Peptidase_M28 pfam04389
Peptidase family M28;
393-557 7.93e-08

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 53.06  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  393 NVVGFVMGlTSPDRYIIVGSHH-HTAHSY----NgqewASSTAIITAFIRALmskvKRGWRPDRTIVFCSWGGTAFGNIG 467
Cdd:pfam04389   1 NVIAKLPG-KAPDEVVLLSAHYdSVGTGPgaddN----ASGVAALLELARVL----AAGQRPKRSVRFLFFDAEEAGLLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  468 SYEWGEdfKKVLQKNVVAYISLHSPIRGNSSLYPVASP----SLQQLVVEKNNFNCTRRAQCPETNISsiqIQGDADYFI 543
Cdd:pfam04389  72 SHHFAK--SHPPLKKIRAVINLDMIGSGGPALLFQSGPkgssLLEKYLKAAAKPYGVTLAEDPFQERG---GPGRSDHAP 146

                         170
                  ....*....|....*
gi 767926201  544 -NHLGVPIVQFAYED 557
Cdd:pfam04389 147 fIKAGIPGLDLAFTD 161
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 630-743 3.78e-06

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: 46.42  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201  630 NTHQLLAMALRLRESAELFQSDEMRpANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPG--FYRNILY----HLDEKTS 703
Cdd:pfam04253   2 SLEPLRKAIEKFKKAAKEFDAWAKK-WEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGrpWFKHVVFapglWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767926201  704 RF-----SILIEAWehckplasnETLQEALSEVLNSINSAQVYFK 743
Cdd:pfam04253  81 TFpgirdAIEAGDW---------ELAQKQISIVAKAIQSAAETLK 116
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 393-518 4.10e-05

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: 45.31  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 393 NVVGFVMGLTSPDRYIIVGSH--HHTAHS-------YNG-QEWASSTAIITAFIRALMSKVKrgwrPDRTIVFCSWGGTA 462
Cdd:cd03877    3 NVVGVLEGSDLPDETIVIGAHydHLGIGGgdsgdkiYNGaDDNASGVAAVLELARYFAKQKT----PKRSIVFAAFTAEE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 463 FGNIGSYEWGEDFKKVLqKNVVAYISLH--SPIRGNSSLYPV--ASPSLQQLVVEKNNFN 518
Cdd:cd03877   79 KGLLGSKYFAENPKFPL-DKIVAMLNLDmiGRLGRSKDVYLIgsGSSELENLLKKANKAA 137
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 393-541 1.32e-04

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: 44.12  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 393 NVVGFVMGLTSPDRYIIVGSHHHTAHSYNGqewASSTAIITAFIRALMSKVKR-GWRPDRTIVFCSWGGTAFGNIGSY-- 469
Cdd:cd08015    3 NVIAEIPGSDKKDEVVILGAHLDSWHGATG---ATDNGAGTAVMMEAMRILKAiGSKPKRTIRVALWGSEEQGLHGSRay 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 470 ------EWGEDFKKVLQKNVVAYISLHS---PIR-----GNSSLYPVAS------PSLQQLVVEKNNFNCTRRAQCPETN 529
Cdd:cd08015   80 vekhfgDPPTMQLQRDHKKISAYFNLDNgtgRIRgiylqGNLAAYPIFSawlypfHDLGATTVIERNTGGTDHAAFDAVG 159

                        170
                 ....*....|...
gi 767926201 530 ISSIQ-IQGDADY 541
Cdd:cd08015  160 IPAFQfIQDPWDY 172
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 382-468 2.95e-04

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: 43.50  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926201 382 VQTVTKLKTVT--NVVGFVMGLTSPDRYIIVGSH--HHTAHS-------YNGQ-EWASSTAIITAFIRALMSKVKrgwRP 449
Cdd:cd05660   48 VPLVSKIEYSTshNVVAILPGSKLPDEYIVLSAHwdHLGIGPpiggdeiYNGAvDNASGVAAVLELARVFAAQDQ---RP 124

                         90
                 ....*....|....*....
gi 767926201 450 DRTIVFCSWGGTAFGNIGS 468
Cdd:cd05660  125 KRSIVFLAVTAEEKGLLGS 143
 
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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