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Conserved domains on  [gi|918588655|ref|XP_013367545|]
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PREDICTED: putative N-acetylated-alpha-linked acidic dipeptidase [Chinchilla lanigera]

Protein Classification

M28 family metallopeptidase( domain architecture ID 10329992)

M28 family metallopeptidase similar to Homo sapiens glutamate carboxypeptidase 2, N-acetylated-alpha-linked acidic dipeptidase 2 and N-acetylated-alpha-linked acidic dipeptidase-like protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 353-594 2.46e-123

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: 370.02  E-value: 2.46e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 353 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEYGLLGSTE 432
Cdd:cd08022   59 PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 433 WAEENSRLLQERGVAYINADSSIEGnYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLYESWSEKspssalsgKPRIS 512
Cdd:cd08022  139 WVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDT--------GGEIG 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 513 KLGSGNDFEVFFQRLGIASGRARYTKNWEtnkfSNYPLYHSVYETYELVERFYDPTFKYHLTVAQVRGGLVFELATSVLL 592
Cdd:cd08022  210 NLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPIL 285


                 ..
gi 918588655 593 PF 594
Cdd:cd08022  286 PF 287
PA_GCPII_like cd02121
PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II ...
 119-345 8.96e-98

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: 301.52  E-value: 8.96e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 119 PNETHPNYISVISDDGNEVFNTSLSEPPPPGyenvsgVVPPFSAFSPQGVPEGDLVYVNYARTEDFFKLErDMKINCAGK 198
Cdd:cd02121    1 PVKRSLILTKPDGATGKLIEDTVLEEPPSPD------VVPPFHAYSASGNVTAELVYANYGSPEDFEYLE-DLGIDVKGK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 199 IVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADYFAPGVAS---YPDGWNLPGGGVQRGNILNL-NGAGDPLTPGYPAN 274
Cdd:cd02121   74 IVIARYGGIFRGLKVKNAQLAGAVGVIIYSDPADDGYITGENgktYPDGPARPPSGVQRGSVLFMsIGPGDPLTPGYPSK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918588655 275 EYAYRREITEAVGIPNIPVHPIGYYDAQRLLERMGGSAPPdSSWKGGLRVPYNVGPgftGNFSTQKVRMHI 345
Cdd:cd02121  154 PGAERRDKEESKGLPKIPSLPISYRDAQPLLKALGGPGAP-SDWQGGLPVTYRLGF---GGPSPGKVRVNL 220
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 626-746 7.92e-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: 153.51  E-value: 7.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  626 VSFDSLFSAVNNFTEIASQFNKRLQHLE---ESNPILLRIMNDQLMFLERAFIDPLGLPDRPFYRHIIYAPSSHNKYAGE 702
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWAKKWEdikEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 918588655  703 SFPGIYDALFDieskadpsKAWAEVKRQISIAAFTVQAAAGTLR 746
Cdd:pfam04253  81 TFPGIRDAIEA--------GDWELAQKQISIVAKAIQSAAETLK 116
Zinc_peptidase_like super family cl14876
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 57-114 1.09e-17

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


The actual alignment was detected with superfamily member cd08022:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 287  Bit Score: 84.20  E-value: 1.09e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 918588655  57 KKAFLSELKAENIKEFLYNFTRVPHLAGTEQNLHLTKQIQSQWKEFGLDSVELVHYDV 114
Cdd:cd08022    1 EKILLDEPDAENIREWLRYYTSGPHLAGTEGNLELAQWTEDKWREFGLDDVELEEYDV 58
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 353-594 2.46e-123

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: 370.02  E-value: 2.46e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 353 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEYGLLGSTE 432
Cdd:cd08022   59 PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 433 WAEENSRLLQERGVAYINADSSIEGnYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLYESWSEKspssalsgKPRIS 512
Cdd:cd08022  139 WVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDT--------GGEIG 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 513 KLGSGNDFEVFFQRLGIASGRARYTKNWEtnkfSNYPLYHSVYETYELVERFYDPTFKYHLTVAQVRGGLVFELATSVLL 592
Cdd:cd08022  210 NLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPIL 285


                 ..
gi 918588655 593 PF 594
Cdd:cd08022  286 PF 287
PA_GCPII_like cd02121
PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II ...
 119-345 8.96e-98

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: 301.52  E-value: 8.96e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 119 PNETHPNYISVISDDGNEVFNTSLSEPPPPGyenvsgVVPPFSAFSPQGVPEGDLVYVNYARTEDFFKLErDMKINCAGK 198
Cdd:cd02121    1 PVKRSLILTKPDGATGKLIEDTVLEEPPSPD------VVPPFHAYSASGNVTAELVYANYGSPEDFEYLE-DLGIDVKGK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 199 IVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADYFAPGVAS---YPDGWNLPGGGVQRGNILNL-NGAGDPLTPGYPAN 274
Cdd:cd02121   74 IVIARYGGIFRGLKVKNAQLAGAVGVIIYSDPADDGYITGENgktYPDGPARPPSGVQRGSVLFMsIGPGDPLTPGYPSK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918588655 275 EYAYRREITEAVGIPNIPVHPIGYYDAQRLLERMGGSAPPdSSWKGGLRVPYNVGPgftGNFSTQKVRMHI 345
Cdd:cd02121  154 PGAERRDKEESKGLPKIPSLPISYRDAQPLLKALGGPGAP-SDWQGGLPVTYRLGF---GGPSPGKVRVNL 220
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 626-746 7.92e-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: 153.51  E-value: 7.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  626 VSFDSLFSAVNNFTEIASQFNKRLQHLE---ESNPILLRIMNDQLMFLERAFIDPLGLPDRPFYRHIIYAPSSHNKYAGE 702
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWAKKWEdikEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 918588655  703 SFPGIYDALFDieskadpsKAWAEVKRQISIAAFTVQAAAGTLR 746
Cdd:pfam04253  81 TFPGIRDAIEA--------GDWELAQKQISIVAKAIQSAAETLK 116
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 309-563 2.13e-27

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: 111.76  E-value: 2.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 309 GGSAPPDSSWKGGLRVPYNVGPGFTGNFSTQKVRMHIHSDSKVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGG---I 385
Cdd:COG2234    1 ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSIGpgaD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 386 DPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEYGLLGSTEWAeENSRLLQERGVAYINADSSIEGNYTLRVDC 465
Cdd:COG2234   81 DNASGVAALLELAR---ALAALGPKPKRTIRFVAFGAEEQGLLGSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNYLYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 466 TPLMYSLvynltkelqspdegfEGKSLYESWSEKSPSSALSGKPRISKLGSGNDFEVFFQRlGIASGrarytkNWETNKF 545
Cdd:COG2234  157 DGDGGSP---------------ELADLLEAAAKAYLPGLGVDPPEETGGYGRSDHAPFAKA-GIPAL------FLFTGAE 214

                        250
                 ....*....|....*...
gi 918588655 546 SNYPLYHSVYETYELVER 563
Cdd:COG2234  215 DYHPDYHTPSDTLDKIDL 232
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 170-260 5.17e-19

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 82.18  E-value: 5.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  170 EGDLVYVNYARTEDFFKLERDMKincaGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADYFAP----GVASYPDGW 245
Cdd:pfam02225   1 TGPLVLAPGCYAGDGIPADFDVK----GKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPpgagGNELYPDGI 76

                          90
                  ....*....|....*
gi 918588655  246 NLPGGGVQRGNILNL 260
Cdd:pfam02225  77 YIPAVGVSRADGEAL 91
Peptidase_M28 pfam04389
Peptidase family M28;
356-453 5.00e-18

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 82.72  E-value: 5.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  356 NVIGTLRGAvEPDRYVILGGHRDSWVFG-GI-DPQSGAAVVHEIVRSFgtlkKEGWRPRRTILFASWDAEEYGLLGSTEW 433
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTGpGAdDNASGVAALLELARVL----AAGQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100
                  ....*....|....*....|
gi 918588655  434 AEENSRLlqERGVAYINADS 453
Cdd:pfam04389  76 AKSHPPL--KKIRAVINLDM 93
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 57-114 1.09e-17

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: 84.20  E-value: 1.09e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 918588655  57 KKAFLSELKAENIKEFLYNFTRVPHLAGTEQNLHLTKQIQSQWKEFGLDSVELVHYDV 114
Cdd:cd08022    1 EKILLDEPDAENIREWLRYYTSGPHLAGTEGNLELAQWTEDKWREFGLDDVELEEYDV 58
PRK09133 PRK09133
hypothetical protein; Provisional
 356-472 2.93e-05

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 47.30  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 356 NVIGTLRGAvEPDRYVILGGH-------RDSWV---F------------GGIDPQSGAAVVheiVRSFGTLKKEGWRPRR 413
Cdd:PRK09133  90 NLVARLRGT-DPKKPILLLAHmdvveakREDWTrdpFklveengyfygrGTSDDKADAAIW---VATLIRLKREGFKPKR 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918588655 414 TILFASWDAEEYGLLGSTEWAEENSRLLqergvayINADSSIE--GNYTLRVDCTPLMYSL 472
Cdd:PRK09133 166 DIILALTGDEEGTPMNGVAWLAENHRDL-------IDAEFALNegGGGTLDEDGKPVLLTV 219
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 196-267 1.40e-03

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 42.33  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918588655 196 AGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDpadyfAPGvASYPDGWNLPGGGVQRGNILNLNGAGDPL 267
Cdd:NF038113 468 AGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNN-----VPG-EPIVMGGGDTGPPITIPSIMISQADGEAI 533
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 353-594 2.46e-123

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: 370.02  E-value: 2.46e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 353 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEYGLLGSTE 432
Cdd:cd08022   59 PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 433 WAEENSRLLQERGVAYINADSSIEGnYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLYESWSEKspssalsgKPRIS 512
Cdd:cd08022  139 WVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWWDDT--------GGEIG 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 513 KLGSGNDFEVFFQRLGIASGRARYTKNWEtnkfSNYPLYHSVYETYELVERFYDPTFKYHLTVAQVRGGLVFELATSVLL 592
Cdd:cd08022  210 NLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPIL 285


                 ..
gi 918588655 593 PF 594
Cdd:cd08022  286 PF 287
PA_GCPII_like cd02121
PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II ...
 119-345 8.96e-98

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: 301.52  E-value: 8.96e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 119 PNETHPNYISVISDDGNEVFNTSLSEPPPPGyenvsgVVPPFSAFSPQGVPEGDLVYVNYARTEDFFKLErDMKINCAGK 198
Cdd:cd02121    1 PVKRSLILTKPDGATGKLIEDTVLEEPPSPD------VVPPFHAYSASGNVTAELVYANYGSPEDFEYLE-DLGIDVKGK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 199 IVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADYFAPGVAS---YPDGWNLPGGGVQRGNILNL-NGAGDPLTPGYPAN 274
Cdd:cd02121   74 IVIARYGGIFRGLKVKNAQLAGAVGVIIYSDPADDGYITGENgktYPDGPARPPSGVQRGSVLFMsIGPGDPLTPGYPSK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918588655 275 EYAYRREITEAVGIPNIPVHPIGYYDAQRLLERMGGSAPPdSSWKGGLRVPYNVGPgftGNFSTQKVRMHI 345
Cdd:cd02121  154 PGAERRDKEESKGLPKIPSLPISYRDAQPLLKALGGPGAP-SDWQGGLPVTYRLGF---GGPSPGKVRVNL 220
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 353-593 1.21e-84

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: 269.55  E-value: 1.21e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 353 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTL-KKEGWRPRRTILFASWDAEEYGLLGST 431
Cdd:cd03874   56 PITNVVGKIEGIEQPDRAIIIGAHRDSWGYGAGYPNSGTAVLLEIARLFQQLkKKFGWKPLRTIYFISWDGSEFGLAGST 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 432 EWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEgfegkslyESWSEKSPSsalsgkPRI 511
Cdd:cd03874  136 ELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGN--------EDWWKHSPN------AKV 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 512 SKLGSGNDFEVFFQRLGIASGRARYTKNWetnkfSNYPLYHSVYETYELVERFYDPTFKYHLTVAQVRGGLVFELATSVL 591
Cdd:cd03874  202 SNLHQYGDWTPFLNHLGIPVAVFSFKNDR-----NASYPINSSYDTFEWLEKFLDPDFELHSTLAEFVGLLVLSLAEDPL 276


                 ..
gi 918588655 592 LP 593
Cdd:cd03874  277 LP 278
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 626-746 7.92e-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: 153.51  E-value: 7.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  626 VSFDSLFSAVNNFTEIASQFNKRLQHLE---ESNPILLRIMNDQLMFLERAFIDPLGLPDRPFYRHIIYAPSSHNKYAGE 702
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAWAKKWEdikEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 918588655  703 SFPGIYDALFDieskadpsKAWAEVKRQISIAAFTVQAAAGTLR 746
Cdd:pfam04253  81 TFPGIRDAIEA--------GDWELAQKQISIVAKAIQSAAETLK 116
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 334-595 2.04e-40

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: 150.22  E-value: 2.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 334 GNFSTQKVrMHIHSDSKVtRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKE-GWRPR 412
Cdd:cd09848   38 NEFKNLKL-MKVWTDEHY-KIHNIFGVIKGFVEPDRYVVIGAQRDAWGPGAAKSGVGTALLLELARTFSDMVKNdGFKPR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 413 RTILFASWDAEEYGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGfeGKSL 492
Cdd:cd09848  116 RSIVFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYISLDGAVLGDDSFKASASPLLYTLIESTMKQVKSPVHS--GQSY 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 493 YES----WSEKspssalsgkprISKLGSGNDFEVFFQRLGIASGRARYTKNWETnkfsnYPLYHSVYETYE-LVERFYDP 567
Cdd:cd09848  194 YETrsswWASI-----------VEPLGLDSAAYPFLAFSGIPSVSFHFTEDDED-----YPFLGTKEDTKEnLDKFTNGE 257

                        250       260
                 ....*....|....*....|....*...
gi 918588655 568 TFKYHLTVAQVRGGLVFELATSVLLPFN 595
Cdd:cd09848  258 LWEVAAAAAEVAGQMALRLVHDHLLPLD 285
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 309-563 2.13e-27

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: 111.76  E-value: 2.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 309 GGSAPPDSSWKGGLRVPYNVGPGFTGNFSTQKVRMHIHSDSKVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGG---I 385
Cdd:COG2234    1 ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSIGpgaD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 386 DPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEYGLLGSTEWAeENSRLLQERGVAYINADSSIEGNYTLRVDC 465
Cdd:COG2234   81 DNASGVAALLELAR---ALAALGPKPKRTIRFVAFGAEEQGLLGSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNYLYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 466 TPLMYSLvynltkelqspdegfEGKSLYESWSEKSPSSALSGKPRISKLGSGNDFEVFFQRlGIASGrarytkNWETNKF 545
Cdd:COG2234  157 DGDGGSP---------------ELADLLEAAAKAYLPGLGVDPPEETGGYGRSDHAPFAKA-GIPAL------FLFTGAE 214

                        250
                 ....*....|....*...
gi 918588655 546 SNYPLYHSVYETYELVER 563
Cdd:COG2234  215 DYHPDYHTPSDTLDKIDL 232
PA_TfR cd02128
PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This ...
 151-345 3.66e-26

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: 105.94  E-value: 3.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 151 ENVSGVVPPFSAFSPQGVPEGDLVYVNYARTEDFFKLeRDMKINCAGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDP 230
Cdd:cd02128   11 NELVENPGGYVAYSAAGTVTGKLVYANYGRKKDFEDL-QSVGVSVNGSVVLVRAGKISFAEKVANAEKLGAVGVLIYPDP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 231 ADYfaPGVASYpdgwNLPGGGVQRgnilnlnGAGDPLTPGYPA-NEYAYrrEITEAVGIPNIPVHPIGYYDAQRLLERMG 309
Cdd:cd02128   90 ADF--PIDPSE----TALFGHVHL-------GTGDPYTPGFPSfNHTQF--PPSQSSGLPNIPAQTISAAAAAKLLSKMG 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 918588655 310 GSAPPdSSWKGGLrVPYNVGPGftgnfSTQKVRMHI 345
Cdd:cd02128  155 GPVCP-SGWKGGD-STCRLGTS-----SSKNVKLTV 183
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 354-559 8.41e-25

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: 102.81  E-value: 8.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 354 IYNVIGTLRGAVEPDRYVILGGHRDSWVF--GGIDPQSGAAVVHEIVRSFGTLKKegwRPRRTILFASWDAEEYGLLGST 431
Cdd:cd02690    1 GYNVIATIKGSDKPDEVILIGAHYDSVPLspGANDNASGVAVLLELARVLSKLQL---KPKRSIRFAFWDAEELGLLGSK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 432 EWAEENSRLLQeRGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEgfegkslyeswsekspSSALSGKPRI 511
Cdd:cd02690   78 YYAEQLLSSLK-NIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELE----------------NVVYTVVYKE 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 918588655 512 SKLGSGNDFEVFfQRLGIASGRARytknweTNKFSNYPLYHSVYETYE 559
Cdd:cd02690  141 DGGTGGSDHRPF-LARGIPAASLI------QSESYNFPYYHTTQDTLE 181
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 170-260 5.17e-19

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 82.18  E-value: 5.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  170 EGDLVYVNYARTEDFFKLERDMKincaGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADYFAP----GVASYPDGW 245
Cdd:pfam02225   1 TGPLVLAPGCYAGDGIPADFDVK----GKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPpgagGNELYPDGI 76

                          90
                  ....*....|....*
gi 918588655  246 NLPGGGVQRGNILNL 260
Cdd:pfam02225  77 YIPAVGVSRADGEAL 91
Peptidase_M28 pfam04389
Peptidase family M28;
356-453 5.00e-18

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 82.72  E-value: 5.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655  356 NVIGTLRGAvEPDRYVILGGHRDSWVFG-GI-DPQSGAAVVHEIVRSFgtlkKEGWRPRRTILFASWDAEEYGLLGSTEW 433
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTGpGAdDNASGVAALLELARVL----AAGQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100
                  ....*....|....*....|
gi 918588655  434 AEENSRLlqERGVAYINADS 453
Cdd:pfam04389  76 AKSHPPL--KKIRAVINLDM 93
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 57-114 1.09e-17

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: 84.20  E-value: 1.09e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 918588655  57 KKAFLSELKAENIKEFLYNFTRVPHLAGTEQNLHLTKQIQSQWKEFGLDSVELVHYDV 114
Cdd:cd08022    1 EKILLDEPDAENIREWLRYYTSGPHLAGTEGNLELAQWTEDKWREFGLDDVELEEYDV 58
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 355-453 2.42e-17

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


Pssm-ID: 349937 [Multi-domain]  Cd Length: 218  Bit Score: 81.49  E-value: 2.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 355 YNVIGTLRGAVEPDRYVILGGHRDSW--VFGGIDPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEYGLLGSTE 432
Cdd:cd08015    2 YNVIAEIPGSDKKDEVVILGAHLDSWhgATGATDNGAGTAVMMEAMR---ILKAIGSKPKRTIRVALWGSEEQGLHGSRA 78

                         90       100
                 ....*....|....*....|....*....
gi 918588655 433 WAE---ENSRLLQ-----ERGVAYINADS 453
Cdd:cd08015   79 YVEkhfGDPPTMQlqrdhKKISAYFNLDN 107
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 157-311 3.59e-17

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.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 78.33  E-value: 3.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 157 VPPFSAFSPQGVPEGDLVYVNYARTEDFfklerdmKINCAGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADyfap 236
Cdd:cd00538   14 LLFNPPSSPVGVVAGPLVGCGYGTTDDS-------GADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGDD---- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918588655 237 gvasypdgwnlpgGGVQRGNILNLNGAgdpltpgypaneyayrreiteavgiPNIPVHPIGYYDAQRLLERMGGS 311
Cdd:cd00538   83 -------------PGPQMGSVGLESTD-------------------------PSIPTVGISYADGEALLSLLEAG 119
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 164-438 2.03e-16

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: 82.36  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 164 SPQGVPEGDLVYVNYARTEDFFKLERDmkiNCAGKIVI-----ARYGK--IFRGNKVKNAQLAGAKGVILYSdpadyfap 236
Cdd:cd03883   96 SVGTPVEGIEAEVVVVFSFEELQAKAD---EVKGKIVVynqpfKGYGEtvKYRGQGAVEAAKYGAVAVLIRS-------- 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 237 gVASYPDgwNLPGGGVQRgnilnlngagdpltpgypaneyayrreitEAVGIPNIPVHPIGYYDAQrLLERMggsappds 316
Cdd:cd03883  165 -ITPFSI--YSPHTGIMR-----------------------------YQDGVTKIPAAAITVEDAE-MLSRM-------- 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 317 swkgglrvpYNVGpgftgnfstQKVRMHIHSDSKV---TRIYNVIGTLRGAVEPDRYVILGGHRDSWVF--GGIDPQSGA 391
Cdd:cd03883  204 ---------AARG---------QKIVIELKMEAKTypdATSRNVIAEITGSKYPDEVVLVGGHLDSWDVgtGAMDDGGGV 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 918588655 392 AVVHEIVRSfgtLKKEGWRPRRTILFASWDAEEYGLLGSTEWAEENS 438
Cdd:cd03883  266 AISWEALKL---IKDLGLKPKRTIRVVLWTGEEQGLVGAKAYAEAHK 309
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 329-453 5.53e-14

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: 73.16  E-value: 5.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 329 GPGFTGNFsTQKVRMHIHSDSKVTriYNVIGTLRGAVEPDRYVILGGHRDSW----------VF-GGIDPQSGAAVVHEI 397
Cdd:cd05660   37 PAGSDGSY-LQAVPLVSKIEYSTS--HNVVAILPGSKLPDEYIVLSAHWDHLgigppiggdeIYnGAVDNASGVAAVLEL 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 918588655 398 VRSFgtlKKEGWRPRRTILFASWDAEEYGLLGSTEWAEENSRLLqERGVAYINADS 453
Cdd:cd05660  114 ARVF---AAQDQRPKRSIVFLAVTAEEKGLLGSRYYAANPIFPL-DKIVANLNIDM 165
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 355-452 1.82e-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: 69.96  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 355 YNVIGTLRGAVEPDRYVILGGHRDSWVFGG-----------IDPQSGAAVVHEIVRSFgtlkKEGWRPRRTILFASWDAE 423
Cdd:cd03877    2 HNVVGVLEGSDLPDETIVIGAHYDHLGIGGgdsgdkiyngaDDNASGVAAVLELARYF----AKQKTPKRSIVFAAFTAE 77

                         90       100
                 ....*....|....*....|....*....
gi 918588655 424 EYGLLGSTEWAeENSRLLQERGVAYINAD 452
Cdd:cd03877   78 EKGLLGSKYFA-ENPKFPLDKIVAMLNLD 105
PA_hNAALADL2_like cd02131
PA_hNAALADL2_like: Protease-associated domain containing proteins like human N-acetylated ...
 159-320 5.26e-12

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: 64.19  E-value: 5.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 159 PFSAFSPQGVPEGDLVYVNYARTEDFFKLERDMkiNCAGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDPADyFAPGV 238
Cdd:cd02131    5 SYAAYSAKGTLQAEVVDVQYGSVEDLRRIRDNM--NVTNQIALLKLGQAPLLYKLSLLEEAGFGGVLLYVDPCD-LPKTR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 239 ASYPDGWnlpgggvqrgnILNLNGAGDPLTPGYPANEYAYRReitEAVGIPNIPVHPIGYYDAQRLLermggSAPPDSSW 318
Cdd:cd02131   82 HTWHQAF-----------MVSLNPGGDPSTPGYPSADQSCRQ---CRGNLTSLLVQPISAYLAKKLL-----SAPPSRRK 142


                 ..
gi 918588655 319 KG 320
Cdd:cd02131  143 EG 144
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 68-113 1.81e-11

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: 65.40  E-value: 1.81e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 918588655  68 NIKEFLYNFTRVPHLAGTEQNLHLTKQIQSQWKEFGLDSVELVHYD 113
Cdd:cd03874   10 KIKEDLEYLSSMPHMAGTKGDAALAKYIENSFKNNGLFEVELEEYS 55
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 352-435 5.05e-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: 5.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 352 TRIYNVIGTLRGAVEPDRYVILGGHRDSWVF----------GGIDPQSGAAVVHEIVRSFGTlkkegWRPRRTILFASWD 421
Cdd:cd05642   86 VNISNVVATLKGSEDPDRVYVVSGHYDSRVSdvmdyesdapGANDDASGVAVSMELARIFAK-----HRPKATIVFTAVA 160

                         90
                 ....*....|....
gi 918588655 422 AEEYGLLGSTEWAE 435
Cdd:cd05642  161 GEEQGLYGSTFLAQ 174
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 356-452 3.74e-08

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


Pssm-ID: 349913 [Multi-domain]  Cd Length: 266  Bit Score: 55.15  E-value: 3.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 356 NVIGTL-RGAVEPDRYVILGGHRDSWVFGGI----------------DPQSGAAVVHEIVRSFGTLKKEGWRPRRtILFA 418
Cdd:cd05663   57 NVIGVLpGKGDVADETVVVGAHYDHLGYGGEgslargdeslihngadDNASGVAAMLELAAKLVDSDTSLALSRN-LVFI 135

                         90       100       110
                 ....*....|....*....|....*....|....
gi 918588655 419 SWDAEEYGLLGSTEWAeENSRLLQERGVAYINAD 452
Cdd:cd05663  136 AFSGEELGLLGSKHFV-KNPPFPIKNTVYMINMD 168
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 355-505 5.64e-08

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: 54.50  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 355 YNVIGTLR--GAVEPDRYVILGGHRDSWVF--GGIDPQSGAAVVHEIVRSFGTLKKEgwrprRTILFASWDAEEYGLLGS 430
Cdd:cd05661   61 HNVIATKKpdNNKNNNDIIIVTSHYDSVVKapGANDNASGTAVTLELARVFKKVKTD-----KELRFIAFGAEENGLLGS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 431 TEWAEENSRLLQERGVAYINAD------SSIEGNYTLRVDCTPlmySLVYNLTKE-----LQSPDEGFEGKSLYESWSEK 499
Cdd:cd05661  136 KYYVASLSEDEIKRTIGVFNLDmvgtsdAKAGDLYAYTIDGKP---NLVTDSGAAaskrlSGVLPLVQQGSSDHVPFHEA 212


                 ....*.
gi 918588655 500 SPSSAL 505
Cdd:cd05661  213 GIPAAL 218
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 355-459 6.29e-08

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: 55.00  E-value: 6.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 355 YNVIGTLRGAvEPDRYVILGGHRDSWVFG-GI-DPQSGAAVVHEIvrsFGTLKKegWRPRRTILFASWDAEEYGLLGSTE 432
Cdd:cd03876   64 YNVIAETKGG-DPNNVVMLGAHLDSVSAGpGInDNGSGSAALLEV---ALALAK--FKVKNAVRFAWWTAEEFGLLGSKF 137

                         90       100
                 ....*....|....*....|....*..
gi 918588655 433 WAEENSRLLQERGVAYINADSSIEGNY 459
Cdd:cd03876  138 YVNNLSSEERSKIRLYLNFDMIASPNY 164
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 355-430 7.25e-08

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: 54.56  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 355 YNVIGTLRGAVEPDRYVILGGHRDS---WVF------GGIDPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEY 425
Cdd:cd03879   75 PSIIATIPGSEKSDEIVVIGAHQDSingSNPsngrapGADDDGSGTVTILEALR---VLLESGFQPKNTIEFHWYAAEEG 151


                 ....*
gi 918588655 426 GLLGS 430
Cdd:cd03879  152 GLLGS 156
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 356-442 8.15e-08

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: 54.38  E-value: 8.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 356 NVIGTLRGAVEPDRYVILGGHRDSW--VFGGIDPQSGAAVVHEIVRSFGTLkkegwRPRRTILFASWDAEEY-----GLL 428
Cdd:cd05640   54 NLIADLPGSYSQDKLILIGAHYDTVpgSPGADDNASGVAALLELARLLATL-----DPNHTLRFVAFDLEEYpffarGLM 128

                         90
                 ....*....|....
gi 918588655 429 GSTEWAEENSRLLQ 442
Cdd:cd05640  129 GSHAYAEDLLRPLT 142
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
 172-227 1.31e-06

PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins 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: 239048 [Multi-domain]  Cd Length: 143  Bit Score: 48.44  E-value: 1.31e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 918588655 172 DLVYVNYARTEDFFKLerDMKincaGKIV-IARyGKIFRGNKVKNAQLAGAKGVILY 227
Cdd:cd02133   29 ELVDAGLGTPEDFEGK--DVK----GKIAlIQR-GEITFVEKIANAKAAGAVGVIIY 78
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 344-430 6.53e-06

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: 48.74  E-value: 6.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 344 HIHSDSKVTRIY----NVIGTLRGAV-EPDRYVILGGHRDSWV--FGGIDPQSGAAVVHEIVRSFgtlKKEGWRPRRTIL 416
Cdd:cd03875   65 FNFLSSGMTLVYfevtNIVVRISGKNsNSLPALLLNAHFDSVPtsPGATDDGMGVAVMLEVLRYL---SKSGHQPKRDII 141

                         90
                 ....*....|....
gi 918588655 417 FASWDAEEYGLLGS 430
Cdd:cd03875  142 FLFNGAEENGLLGA 155
PRK09133 PRK09133
hypothetical protein; Provisional
 356-472 2.93e-05

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 47.30  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 356 NVIGTLRGAvEPDRYVILGGH-------RDSWV---F------------GGIDPQSGAAVVheiVRSFGTLKKEGWRPRR 413
Cdd:PRK09133  90 NLVARLRGT-DPKKPILLLAHmdvveakREDWTrdpFklveengyfygrGTSDDKADAAIW---VATLIRLKREGFKPKR 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918588655 414 TILFASWDAEEYGLLGSTEWAEENSRLLqergvayINADSSIE--GNYTLRVDCTPLMYSL 472
Cdd:PRK09133 166 DIILALTGDEEGTPMNGVAWLAENHRDL-------IDAEFALNegGGGTLDEDGKPVLLTV 219
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
 152-252 5.31e-05

PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. The significance of the PA domain to these proteins 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: 239045 [Multi-domain]  Cd Length: 122  Bit Score: 43.40  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 152 NVSGVVPPFSAF--SPQGVPEGDLVYVNYARTEdffklERDMKINCAGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSD 229
Cdd:cd02130    3 SANGEAIPTTAFtySPAGEVTGPLVVVPNLGCD-----AADYPASVAGNIALIERGECPFGDKSALAGAAGAAAAIIYNN 77

                         90       100
                 ....*....|....*....|...
gi 918588655 230 PADYFAPGVASYPDGWNLPGGGV 252
Cdd:cd02130   78 VPAGGLSGTLGEPSGPYVPTVGI 100
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 196-244 9.86e-05

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins 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: 239035 [Multi-domain]  Cd Length: 126  Bit Score: 42.79  E-value: 9.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 918588655 196 AGKIVIARYGKIF-RGNKVKNAQLAGAKGVILYSDPAD--------YFAPGVA-SYPDG 244
Cdd:cd02120   51 KGKIVLCDRGGNTsRVAKGDAVKAAGGAGMILANDPTDgldvvadaHVLPAVHvDYEDG 109
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
 159-227 2.48e-04

PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like 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 subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.


Pssm-ID: 240122 [Multi-domain]  Cd Length: 118  Bit Score: 41.16  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 159 PFSAFSPQGVPE-GDLVYVNYARTEDF-----FKLERDMkincAGKIVIarygkIFRGN-----KVKNAQLAGAKGVILY 227
Cdd:cd04818    1 VSAGFGPALTNVtADVVLAGAAPASNTdgctaFTNAAAF----AGKIAL-----IDRGTcnftvKVLNAQNAGAIAVIVA 71
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 343-430 4.09e-04

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 43.61  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 343 MHIHSDskvtRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGI-DPQSG--AAVvhEIVRsfgTLKKEGWRPRRTILFAS 419
Cdd:PRK09290  52 LTVRVD----AVGNLFGRLEGRDPDAPAVLTGSHLDTVPNGGRfDGPLGvlAGL--EAVR---TLNERGIRPRRPIEVVA 122

                         90
                 ....*....|....*.
gi 918588655 420 WDAEE-----YGLLGS 430
Cdd:PRK09290 123 FTNEEgsrfgPAMLGS 138
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 353-430 5.25e-04

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 42.97  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 353 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGI-DPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEE---YG-- 426
Cdd:PRK12890  59 AAGNLFGRLPGRDPDLPPLMTGSHLDTVPNGGRyDGILGVLAGLEVVA---ALREAGIRPPHPLEVIAFTNEEgvrFGps 135


                 ....
gi 918588655 427 LLGS 430
Cdd:PRK12890 136 MIGS 139
PRK12892 PRK12892
allantoate amidohydrolase; Reviewed
 343-430 9.60e-04

allantoate amidohydrolase; Reviewed


Pssm-ID: 183817 [Multi-domain]  Cd Length: 412  Bit Score: 42.39  E-value: 9.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 343 MHIHSDskvtRIYNVIGTLRGAvEPDRYVILGGHRDSWVFGG-IDPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWD 421
Cdd:PRK12892  54 LAVRID----GIGNVFGRLPGP-GPGPALLVGSHLDSQNLGGrYDGALGVVAGLEAAR---ALNEHGIATRHPLDVVAWC 125

                         90
                 ....*....|....
gi 918588655 422 AEE-----YGLLGS 430
Cdd:PRK12892 126 DEEgsrftPGFLGS 139
PRK08262 PRK08262
M20 family peptidase;
404-446 1.15e-03

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 42.24  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 918588655 404 LKKEGWRPRRTILFASWDAEEYGLLGstewAEENSRLLQERGV 446
Cdd:PRK08262 169 LLAQGFQPRRTIYLAFGHDEEVGGLG----ARAIAELLKERGV 207
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 196-267 1.40e-03

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 42.33  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918588655 196 AGKIVIARYGKIFRGNKVKNAQLAGAKGVILYSDpadyfAPGvASYPDGWNLPGGGVQRGNILNLNGAGDPL 267
Cdd:NF038113 468 AGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNN-----VPG-EPIVMGGGDTGPPITIPSIMISQADGEAI 533
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 356-452 2.71e-03

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: 40.53  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918588655 356 NVIGTLRGAVEPDRYVILGGHRD------SWVFGGIDPQ-SGAAVVHEIVRSFgtlKKEgwRPRRTILFASWDAEEYGLL 428
Cdd:cd05662   64 NVLAVIKGSEPPTKWRVVSAHYDhlgirgGKIYNGADDNaSGVAALLALAEYF---KKH--PPKHNVIFAATDAEEPGLR 138

                         90       100
                 ....*....|....*....|....
gi 918588655 429 GSTEWAEENSRLLQERGVAyINAD 452
Cdd:cd05662  139 GSYAFVEALKVPRAQIELN-INLD 161
PA_2 cd04819
PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. ...
 163-229 2.82e-03

PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. 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 in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup.


Pssm-ID: 240123 [Multi-domain]  Cd Length: 127  Bit Score: 38.53  E-value: 2.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918588655 163 FSPQGVPEGDLVYVNYARTEDFFKLErdmkinCAGKIVIARYGK--IFRGNKVKNAQLAGAKGVILYSD 229
Cdd:cd04819   17 RSPSGEAKGEPVDAGYGLPKDFDGLD------LEGKIAVVKRDDpdVDRKEKYAKAVAAGAAAFVVVNT 79
 
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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