NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370459016|ref|XP_024304179|]
View 

glutamate carboxypeptidase 2 isoform X7 [Homo sapiens]

Protein Classification

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

M28_PSMA_like and TFR_dimer domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 46-287 1.01e-127

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


:

Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 369.64  E-value: 1.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  46 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTE 125
Cdd:cd08022    59 PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 126 WAEENSRLLQERGVAYINADSSIEGnYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLyeswtkksPSPEFSGMPRIS 205
Cdd:cd08022   139 WVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYL--------PSWWDDTGGEIG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 206 KLGSGNDFEVFFQRLGIASGRARYTKNWEtnkfSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVL 285
Cdd:cd08022   210 NLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPIL 285


                  ..
gi 1370459016 286 PF 287
Cdd:cd08022   286 PF 287
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 319-408 5.43e-20

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: 84.94  E-value: 5.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 319 VSFDSLFSAVKNFTEIASKFSE---------------------RLQDFDKS-------------KHVIYAPSSHNKYAGE 364
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAwakkwedikepdllavravndKLMLFERAfldpeglpgrpwfKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370459016 365 SFPGIYDALFDieskvdpsKAWGEVKRQIYVAAFTVQAAAETLS 408
Cdd:pfam04253  81 TFPGIRDAIEA--------GDWELAQKQISIVAKAIQSAAETLK 116
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 46-287 1.01e-127

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 369.64  E-value: 1.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  46 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTE 125
Cdd:cd08022    59 PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 126 WAEENSRLLQERGVAYINADSSIEGnYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLyeswtkksPSPEFSGMPRIS 205
Cdd:cd08022   139 WVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYL--------PSWWDDTGGEIG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 206 KLGSGNDFEVFFQRLGIASGRARYTKNWEtnkfSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVL 285
Cdd:cd08022   210 NLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPIL 285


                  ..
gi 1370459016 286 PF 287
Cdd:cd08022   286 PF 287
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 2-282 8.55e-29

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: 113.30  E-value: 8.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016   2 GGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGG---I 78
Cdd:COG2234     1 ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSIGpgaD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  79 DPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAeENSRLLQERGVAYINADSSIEGNYTLRVDC 158
Cdd:COG2234    81 DNASGVAALLELAR---ALAALGPKPKRTIRFVAFGAEEQGLLGSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNYLYV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 159 TPLMYSLvhnltkelkspdegfEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRlGIASGrarytkNWETNKF 238
Cdd:COG2234   157 DGDGGSP---------------ELADLLEAAAKAYLPGLGVDPPEETGGYGRSDHAPFAKA-GIPAL------FLFTGAE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370459016 239 SGYPLYHSVYETYELVEkfydpmFKYHLTVAQVRGGMVFELANS 282
Cdd:COG2234   215 DYHPDYHTPSDTLDKID------LDALAKVAQLLAALVYELANA 252
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 319-408 5.43e-20

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: 84.94  E-value: 5.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 319 VSFDSLFSAVKNFTEIASKFSE---------------------RLQDFDKS-------------KHVIYAPSSHNKYAGE 364
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAwakkwedikepdllavravndKLMLFERAfldpeglpgrpwfKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370459016 365 SFPGIYDALFDieskvdpsKAWGEVKRQIYVAAFTVQAAAETLS 408
Cdd:pfam04253  81 TFPGIRDAIEA--------GDWELAQKQISIVAKAIQSAAETLK 116
Peptidase_M28 pfam04389
Peptidase family M28;
49-252 1.83e-19

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 85.41  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAvEPDRYVILGGHRDSWVFG-GI-DPQSGAAVVHEIVRSFgtlkKEGWRPRRTILFASWDAEEFGLLGSTEW 126
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTGpGAdDNASGVAALLELARVL----AAGQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 127 AEENSRLlqERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPdegfEGKSLYEswtkkSPSPEFSGMprisk 206
Cdd:pfam04389  76 AKSHPPL--KKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKP----YGVTLAE-----DPFQERGGP----- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370459016 207 lgSGNDFEVFFQRlGIASGRARYTKNwetnkfsgYPLYHSVYETYE 252
Cdd:pfam04389 140 --GRSDHAPFIKA-GIPGLDLAFTDF--------GYRYHTPADTID 174
PRK09133 PRK09133
hypothetical protein; Provisional
 49-165 1.29e-05

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 47.30  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAvEPDRYVILGGH-------RDSWV---F------------GGIDPQSGAAVVheiVRSFGTLKKEGWRPRR 106
Cdd:PRK09133   90 NLVARLRGT-DPKKPILLLAHmdvveakREDWTrdpFklveengyfygrGTSDDKADAAIW---VATLIRLKREGFKPKR 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459016 107 TILFASWDAEEFGLLGSTEWAEENSRLLqergvayINADSSIE--GNYTLRVDCTPLMYSL 165
Cdd:PRK09133  166 DIILALTGDEEGTPMNGVAWLAENHRDL-------IDAEFALNegGGGTLDEDGKPVLLTV 219
 
Name Accession Description Interval E-value
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 46-287 1.01e-127

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 369.64  E-value: 1.01e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  46 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTE 125
Cdd:cd08022    59 PIWNVIGTIRGSEEPDEYIILGNHRDAWVFGAGDPNSGTAVLLEVARALGTLLKKGWRPRRTIIFASWDAEEYGLIGSTE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 126 WAEENSRLLQERGVAYINADSSIEGnYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLyeswtkksPSPEFSGMPRIS 205
Cdd:cd08022   139 WVEENADWLQERAVAYLNVDVAVSG-STLRAAGSPLLQNLLREAAKEVQDPDEGATLKYL--------PSWWDDTGGEIG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 206 KLGSGNDFEVFFQRLGIASGRARYTKNWEtnkfSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVL 285
Cdd:cd08022   210 NLGSGSDYTPFLDHLGIASIDFGFSGGPT----DPYPHYHSNYDSFEWMEKFGDPGFKYHVAIAQVWGLLALRLADDPIL 285


                  ..
gi 1370459016 286 PF 287
Cdd:cd08022   286 PF 287
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 28-286 1.51e-93

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: 282.26  E-value: 1.51e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  28 NFSTQKVKMHIHStnevtRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTL-KKEGWRPRR 106
Cdd:cd03874    43 NNGLFEVELEEYS-----PITNVVGKIEGIEQPDRAIIIGAHRDSWGYGAGYPNSGTAVLLEIARLFQQLkKKFGWKPLR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 107 TILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEgfegksly 186
Cdd:cd03874   118 TIYFISWDGSEFGLAGSTELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGN-------- 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 187 ESWTKKSPspefsgMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWetnkfSGYPLYHSVYETYELVEKFYDPMFKYHL 266
Cdd:cd03874   190 EDWWKHSP------NAKVSNLHQYGDWTPFLNHLGIPVAVFSFKNDR-----NASYPINSSYDTFEWLEKFLDPDFELHS 258

                         250       260
                  ....*....|....*....|
gi 1370459016 267 TVAQVRGGMVFELANSIVLP 286
Cdd:cd03874   259 TLAEFVGLLVLSLAEDPLLP 278
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 27-288 2.05e-44

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: 155.61  E-value: 2.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  27 GNFSTQKVkMHIHsTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKE-GWRPR 105
Cdd:cd09848    38 NEFKNLKL-MKVW-TDEHYKIHNIFGVIKGFVEPDRYVVIGAQRDAWGPGAAKSGVGTALLLELARTFSDMVKNdGFKPR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 106 RTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGfeGKSL 185
Cdd:cd09848   116 RSIVFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYISLDGAVLGDDSFKASASPLLYTLIESTMKQVKSPVHS--GQSY 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 186 YE---SWTKKSpspefsgmprISKLGSGNDFEVFFQRLGIASGRARYTKNWETnkfsgYPLYHSVYETYELVEKFyDPMF 262
Cdd:cd09848   194 YEtrsSWWASI----------VEPLGLDSAAYPFLAFSGIPSVSFHFTEDDED-----YPFLGTKEDTKENLDKF-TNGE 257

                         250       260
                  ....*....|....*....|....*...
gi 1370459016 263 KYHLT--VAQVRGGMVFELANSIVLPFD 288
Cdd:cd09848   258 LWEVAaaAAEVAGQMALRLVHDHLLPLD 285
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 2-282 8.55e-29

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: 113.30  E-value: 8.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016   2 GGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGG---I 78
Cdd:COG2234     1 ALAAAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVGSIGpgaD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  79 DPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAeENSRLLQERGVAYINADSSIEGNYTLRVDC 158
Cdd:COG2234    81 DNASGVAALLELAR---ALAALGPKPKRTIRFVAFGAEEQGLLGSRYYA-ENLKAPLEKIVAVLNLDMIGRGGPRNYLYV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 159 TPLMYSLvhnltkelkspdegfEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRlGIASGrarytkNWETNKF 238
Cdd:COG2234   157 DGDGGSP---------------ELADLLEAAAKAYLPGLGVDPPEETGGYGRSDHAPFAKA-GIPAL------FLFTGAE 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370459016 239 SGYPLYHSVYETYELVEkfydpmFKYHLTVAQVRGGMVFELANS 282
Cdd:COG2234   215 DYHPDYHTPSDTLDKID------LDALAKVAQLLAALVYELANA 252
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 47-252 2.51e-26

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: 104.73  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  47 IYNVIGTLRGAVEPDRYVILGGHRDSWVF--GGIDPQSGAAVVHEIVRSFGTLKKegwRPRRTILFASWDAEEFGLLGST 124
Cdd:cd02690     1 GYNVIATIKGSDKPDEVILIGAHYDSVPLspGANDNASGVAVLLELARVLSKLQL---KPKRSIRFAFWDAEELGLLGSK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 125 EWAEENSRLLQeRGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEgfegkslyeswtkkspSPEFSGMPRI 204
Cdd:cd02690    78 YYAEQLLSSLK-NIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELE----------------NVVYTVVYKE 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370459016 205 SKLGSGNDFEVfFQRLGIASGRARytknweTNKFSGYPLYHSVYETYE 252
Cdd:cd02690   141 DGGTGGSDHRP-FLARGIPAASLI------QSESYNFPYYHTTQDTLE 181
TFR_dimer pfam04253
Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the ...
 319-408 5.43e-20

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: 84.94  E-value: 5.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 319 VSFDSLFSAVKNFTEIASKFSE---------------------RLQDFDKS-------------KHVIYAPSSHNKYAGE 364
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDAwakkwedikepdllavravndKLMLFERAfldpeglpgrpwfKHVVFAPGLWTGYAGA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370459016 365 SFPGIYDALFDieskvdpsKAWGEVKRQIYVAAFTVQAAAETLS 408
Cdd:pfam04253  81 TFPGIRDAIEA--------GDWELAQKQISIVAKAIQSAAETLK 116
Peptidase_M28 pfam04389
Peptidase family M28;
49-252 1.83e-19

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 85.41  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAvEPDRYVILGGHRDSWVFG-GI-DPQSGAAVVHEIVRSFgtlkKEGWRPRRTILFASWDAEEFGLLGSTEW 126
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTGpGAdDNASGVAALLELARVL----AAGQRPKRSVRFLFFDAEEAGLLGSHHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016 127 AEENSRLlqERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPdegfEGKSLYEswtkkSPSPEFSGMprisk 206
Cdd:pfam04389  76 AKSHPPL--KKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKP----YGVTLAE-----DPFQERGGP----- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370459016 207 lgSGNDFEVFFQRlGIASGRARYTKNwetnkfsgYPLYHSVYETYE 252
Cdd:pfam04389 140 --GRSDHAPFIKA-GIPGLDLAFTDF--------GYRYHTPADTID 174
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 48-146 1.14e-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: 81.10  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  48 YNVIGTLRGAVEPDRYVILGGHRDSW--VFGGIDPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEFGLLGSTE 125
Cdd:cd08015     2 YNVIAEIPGSDKKDEVVILGAHLDSWhgATGATDNGAGTAVMMEAMR---ILKAIGSKPKRTIRVALWGSEEQGLHGSRA 78

                          90       100
                  ....*....|....*....|....*....
gi 1370459016 126 WAE---ENSRLLQ-----ERGVAYINADS 146
Cdd:cd08015    79 YVEkhfGDPPTMQlqrdhKKISAYFNLDN 107
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 33-131 1.67e-15

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: 77.73  E-value: 1.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  33 KVKMHIHSTNEVTRiYNVIGTLRGAVEPDRYVILGGHRDSWVF--GGIDPQSGAAVVHEIVRSfgtLKKEGWRPRRTILF 110
Cdd:cd03883   213 ELKMEAKTYPDATS-RNVIAEITGSKYPDEVVLVGGHLDSWDVgtGAMDDGGGVAISWEALKL---IKDLGLKPKRTIRV 288

                          90       100
                  ....*....|....*....|.
gi 1370459016 111 ASWDAEEFGLLGSTEWAEENS 131
Cdd:cd03883   289 VLWTGEEQGLVGAKAYAEAHK 309
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 22-146 3.83e-15

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


Pssm-ID: 349910 [Multi-domain]  Cd Length: 290  Bit Score: 75.47  E-value: 3.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  22 GPGFTGNFsTQKVKMhIHSTNEVTRiYNVIGTLRGAVEPDRYVILGGHRDSW----------VF-GGIDPQSGAAVVHEI 90
Cdd:cd05660    37 PAGSDGSY-LQAVPL-VSKIEYSTS-HNVVAILPGSKLPDEYIVLSAHWDHLgigppiggdeIYnGAVDNASGVAAVLEL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370459016  91 VRSFgtlKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLqERGVAYINADS 146
Cdd:cd05660   114 ARVF---AAQDQRPKRSIVFLAVTAEEKGLLGSRYYAANPIFPL-DKIVANLNIDM 165
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 48-145 6.13e-14

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: 70.35  E-value: 6.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  48 YNVIGTLRGAVEPDRYVILGGHRDSWVFGG-----------IDPQSGAAVVHEIVRSFgtlkKEGWRPRRTILFASWDAE 116
Cdd:cd03877     2 HNVVGVLEGSDLPDETIVIGAHYDHLGIGGgdsgdkiyngaDDNASGVAAVLELARYF----AKQKTPKRSIVFAAFTAE 77

                          90       100
                  ....*....|....*....|....*....
gi 1370459016 117 EFGLLGSTEWAeENSRLLQERGVAYINAD 145
Cdd:cd03877    78 EKGLLGSKYFA-ENPKFPLDKIVAMLNLD 105
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 45-128 2.42e-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: 64.44  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  45 TRIYNVIGTLRGAVEPDRYVILGGHRDSWVF----------GGIDPQSGAAVVHEIVRSFGTlkkegWRPRRTILFASWD 114
Cdd:cd05642    86 VNISNVVATLKGSEDPDRVYVVSGHYDSRVSdvmdyesdapGANDDASGVAVSMELARIFAK-----HRPKATIVFTAVA 160

                          90
                  ....*....|....
gi 1370459016 115 AEEFGLLGSTEWAE 128
Cdd:cd05642   161 GEEQGLYGSTFLAQ 174
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 26-152 3.80e-09

M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures.


Pssm-ID: 349873 [Multi-domain]  Cd Length: 289  Bit Score: 57.31  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  26 TGNFSTQKVKMhihsTNEVTRIYNVIGTLRGAvEPDRYVILGGHRDSWVFG-GI-DPQSGAAVVHEIvrsFGTLKKegWR 103
Cdd:cd03876    46 AGYYDVTLQPF----TSLYRTTYNVIAETKGG-DPNNVVMLGAHLDSVSAGpGInDNGSGSAALLEV---ALALAK--FK 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370459016 104 PRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNY 152
Cdd:cd03876   116 VKNAVRFAWWTAEEFGLLGSKFYVNNLSSEERSKIRLYLNFDMIASPNY 164
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 49-145 1.20e-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: 55.54  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTL-RGAVEPDRYVILGGHRDSWVFGGI----------------DPQSGAAVVHEIVRSFGTLKKEGWRPRRtILFA 111
Cdd:cd05663    57 NVIGVLpGKGDVADETVVVGAHYDHLGYGGEgslargdeslihngadDNASGVAAMLELAAKLVDSDTSLALSRN-LVFI 135

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370459016 112 SWDAEEFGLLGSTEWAeENSRLLQERGVAYINAD 145
Cdd:cd05663   136 AFSGEELGLLGSKHFV-KNPPFPIKNTVYMINMD 168
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 48-123 4.37e-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: 54.17  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  48 YNVIGTLRGAVEPDRYVILGGHRDS---WVF------GGIDPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEEF 118
Cdd:cd03879    75 PSIIATIPGSEKSDEIVVIGAHQDSingSNPsngrapGADDDGSGTVTILEALR---VLLESGFQPKNTIEFHWYAAEEG 151


                  ....*
gi 1370459016 119 GLLGS 123
Cdd:cd03879   152 GLLGS 156
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 49-135 1.40e-07

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


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 52.45  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAVEPDRYVILGGHRDSwVFG--GIDPQ-SGAAVVHEIVRSFGTLkkegwRPRRTILFASWDAEEF-----GL 120
Cdd:cd05640    54 NLIADLPGSYSQDKLILIGAHYDT-VPGspGADDNaSGVAALLELARLLATL-----DPNHTLRFVAFDLEEYpffarGL 127

                          90
                  ....*....|....*
gi 1370459016 121 LGSTEWAEENSRLLQ 135
Cdd:cd05640   128 MGSHAYAEDLLRPLT 142
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 37-123 1.96e-07

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: 52.20  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  37 HIHSTNEVTRIY----NVIGTLRGAV-EPDRYVILGGHRDSWV--FGGIDPQSGAAVVHEIVRSFgtlKKEGWRPRRTIL 109
Cdd:cd03875    65 FNFLSSGMTLVYfevtNIVVRISGKNsNSLPALLLNAHFDSVPtsPGATDDGMGVAVMLEVLRYL---SKSGHQPKRDII 141

                          90
                  ....*....|....
gi 1370459016 110 FASWDAEEFGLLGS 123
Cdd:cd03875   142 FLFNGAEENGLLGA 155
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 48-145 2.19e-07

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


Pssm-ID: 349911 [Multi-domain]  Cd Length: 262  Bit Score: 51.80  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  48 YNVIGTLR--GAVEPDRYVILGGHRDSWVF--GGIDPQSGAAVVHEIVRSFGTLKKEgwrprRTILFASWDAEEFGLLGS 123
Cdd:cd05661    61 HNVIATKKpdNNKNNNDIIIVTSHYDSVVKapGANDNASGTAVTLELARVFKKVKTD-----KELRFIAFGAEENGLLGS 135

                          90       100
                  ....*....|....*....|..
gi 1370459016 124 TEWAEENSRLLQERGVAYINAD 145
Cdd:cd05661   136 KYYVASLSEDEIKRTIGVFNLD 157
PRK09133 PRK09133
hypothetical protein; Provisional
 49-165 1.29e-05

hypothetical protein; Provisional


Pssm-ID: 236388 [Multi-domain]  Cd Length: 472  Bit Score: 47.30  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAvEPDRYVILGGH-------RDSWV---F------------GGIDPQSGAAVVheiVRSFGTLKKEGWRPRR 106
Cdd:PRK09133   90 NLVARLRGT-DPKKPILLLAHmdvveakREDWTrdpFklveengyfygrGTSDDKADAAIW---VATLIRLKREGFKPKR 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459016 107 TILFASWDAEEFGLLGSTEWAEENSRLLqergvayINADSSIE--GNYTLRVDCTPLMYSL 165
Cdd:PRK09133  166 DIILALTGDEEGTPMNGVAWLAENHRDL-------IDAEFALNegGGGTLDEDGKPVLLTV 219
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 49-193 1.42e-04

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: 43.22  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAVEPDRYVILGGHRD------SWVFGGIDPQ-SGAAVVHEIVRSFgtlKKEgwRPRRTILFASWDAEEFGLL 121
Cdd:cd05662    64 NVLAVIKGSEPPTKWRVVSAHYDhlgirgGKIYNGADDNaSGVAALLALAEYF---KKH--PPKHNVIFAATDAEEPGLR 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370459016 122 GSTEWAEENSRLLQERGVAyINAD----SSIEGNYTLRVDCTPLMYSLV--HNLTKELKSPDEGFEGKSLYESWTKKS 193
Cdd:cd05662   139 GSYAFVEALKVPRAQIELN-INLDmisrPERNELYVEGASQFPQLTSILenVKGTCIKALHPKDTDGSIGSIDWTRAS 215
PRK08262 PRK08262
M20 family peptidase;
97-139 1.66e-04

M20 family peptidase;


Pssm-ID: 236208 [Multi-domain]  Cd Length: 486  Bit Score: 43.78  E-value: 1.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370459016  97 LKKEGWRPRRTILFASWDAEEFGLLGstewAEENSRLLQERGV 139
Cdd:PRK08262  169 LLAQGFQPRRTIYLAFGHDEEVGGLG----ARAIAELLKERGV 207
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 46-123 1.70e-04

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 43.35  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  46 RIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGI-DPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEE---FG-- 119
Cdd:PRK12890   59 AAGNLFGRLPGRDPDLPPLMTGSHLDTVPNGGRyDGILGVLAGLEVVA---ALREAGIRPPHPLEVIAFTNEEgvrFGps 135


                  ....
gi 1370459016 120 LLGS 123
Cdd:PRK12890  136 MIGS 139
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 49-123 3.78e-04

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 42.45  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAVEPDRYVILGGHRDSWVFGGI-DPQSG--AAVvhEIVRsfgTLKKEGWRPRRTILFASWDAEE---FG--L 120
Cdd:PRK09290   61 NLFGRLEGRDPDAPAVLTGSHLDTVPNGGRfDGPLGvlAGL--EAVR---TLNERGIRPRRPIEVVAFTNEEgsrFGpaM 135


                  ...
gi 1370459016 121 LGS 123
Cdd:PRK09290  136 LGS 138
PRK12892 PRK12892
allantoate amidohydrolase; Reviewed
 46-123 7.35e-04

allantoate amidohydrolase; Reviewed


Pssm-ID: 183817 [Multi-domain]  Cd Length: 412  Bit Score: 41.62  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  46 RIYNVIGTLRGAvEPDRYVILGGHRDSWVFGG-IDPQSGAAVVHEIVRsfgTLKKEGWRPRRTILFASWDAEE---F--G 119
Cdd:PRK12892   60 GIGNVFGRLPGP-GPGPALLVGSHLDSQNLGGrYDGALGVVAGLEAAR---ALNEHGIATRHPLDVVAWCDEEgsrFtpG 135


                  ....
gi 1370459016 120 LLGS 123
Cdd:PRK12892  136 FLGS 139
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 49-127 6.05e-03

M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 38.66  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459016  49 NVIGTLRGAVEPDRYVILGGHRDSWVFGGI-DPQSG--AAVvhEIVRsfgTLKKEGWRPRRTILFASWDAEE-----FGL 120
Cdd:cd03884    53 NLFGRLEGTDPDAPPVLTGSHLDTVPNGGRyDGILGvlAGL--EALR---ALKEAGIRPRRPIEVVAFTNEEgsrfpPSM 127


                  ....*..
gi 1370459016 121 LGSTEWA 127
Cdd:cd03884   128 LGSRAFA 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH