NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24652993|ref|NP_725143|]
View 

uncharacterized protein Dmel_CG30043 [Drosophila melanogaster]

Protein Classification

M28 family metallopeptidase( domain architecture ID 10133732)

M28 family metallopeptidase is a zinc-dependent peptidase that may be an aminopeptidase or a carboxypeptidase with co-catalytic zinc ions; similar to Homo sapiens endoplasmic reticulum metallopeptidase 1 that is required for the organization of somatic cells and oocytes into discrete follicular structures

CATH:  3.40.630.10
EC:  3.-.-.-
Gene Ontology:  GO:0008237|GO:0006508|GO:0008270
MEROPS:  M28
PubMed:  7674922|10493853|12773192|18429165

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_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 71-377 5.19e-141

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: 420.46  E-value: 5.19e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993  71 PGEFVAERAQQYLYTYDRIGPKVTGSyANEVTTVEFLVNETEKIRAEMRSDLYDLELDVQSPTG--GYVFNDMVNMYQGI 148
Cdd:cd03875   1 PGGFSLERAWEDLQVLISIGPHPYGS-HNNDKVRDYLLARVEEIKERANANGLEVEVQDDTGSGsfNFLSSGMTLVYFEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 149 HNVIVKLSSKSSQSESYLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFI 228
Cdd:cd03875  80 TNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAFI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 229 TQHKWAEKCKAFINLEVGGSGGRDLLFQSGPnnPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRDYGNIAGL 308
Cdd:cd03875 160 TQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPGL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 309 DIAQIENGYVYHTAFDTYENVPGRSIQNSGNNVLALVRAYSNASELYNTESD-DSHAVFFDFLGLFFVYY 377
Cdd:cd03875 238 DIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYrGGPAVFFDLLGLFFVYY 307
YfcC super family cl42750
Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction ...
 534-615 6.53e-03

Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction only];


The actual alignment was detected with superfamily member COG1288:

Pssm-ID: 440899 [Multi-domain]  Cd Length: 464  Bit Score: 40.12  E-value: 6.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 534 ALLINLVSTLHDRGYYWVPIVMFLqvlpFSYFCYLFYM------FLVIFIPVLGRNGYstnpDLIVGL---LCGVCVffa 604
Cdd:COG1288 103 AGIGALVRKLKGKEKLLIPVLMLL----FALGGTTFGMaeetiaFYPILVPLAIALGY----DAITGVaiiFLGAGI--- 171

                        90
                ....*....|.
gi 24652993 605 lGFAAQLINMF 615
Cdd:COG1288 172 -GFAASTINPF 181
 
Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 71-377 5.19e-141

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: 420.46  E-value: 5.19e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993  71 PGEFVAERAQQYLYTYDRIGPKVTGSyANEVTTVEFLVNETEKIRAEMRSDLYDLELDVQSPTG--GYVFNDMVNMYQGI 148
Cdd:cd03875   1 PGGFSLERAWEDLQVLISIGPHPYGS-HNNDKVRDYLLARVEEIKERANANGLEVEVQDDTGSGsfNFLSSGMTLVYFEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 149 HNVIVKLSSKSSQSESYLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFI 228
Cdd:cd03875  80 TNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAFI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 229 TQHKWAEKCKAFINLEVGGSGGRDLLFQSGPnnPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRDYGNIAGL 308
Cdd:cd03875 160 TQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPGL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 309 DIAQIENGYVYHTAFDTYENVPGRSIQNSGNNVLALVRAYSNASELYNTESD-DSHAVFFDFLGLFFVYY 377
Cdd:cd03875 238 DIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYrGGPAVFFDLLGLFFVYY 307
Peptidase_M28 pfam04389
Peptidase family M28;
150-345 1.50e-62

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 209.45  E-value: 1.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993   150 NVIVKLSSKSSQSesYLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMsISEIPFEHPIVFLFNGAEENPLQASHGFIT 229
Cdd:pfam04389   1 NVIAKLPGKAPDE--VVLLSAHYDSVGTGPGADDNASGVAALLELARVL-AAGQRPKRSVRFLFFDAEEAGLLGSHHFAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993   230 QHKWAEKCKAFINLEVGGSGGRDLLFQSGPNNPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRDYGnIAGLD 309
Cdd:pfam04389  78 SHPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERGGPGRSDHAPFIKAG-IPGLD 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 24652993   310 IAQIENGYVYHTAFDTYENVPGRSIQNSGNNVLALV 345
Cdd:pfam04389 157 LAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 165-355 1.64e-25

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: 106.75  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 165 YLLLNSHFDSKP-GSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFITQHKWA-EKCKAFIN 242
Cdd:COG2234  62 VVVLGAHYDSVGsIGPGADDNASGVAALLELARALAALGPKPKRTIRFVAFGAEEQGLLGSRYYAENLKAPlEKIVAVLN 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 243 LEVGGSGG--RDLLFQSGPNNPWLMKYYRQHAKHPFATTMAEEIFQSGvLPSDSDFRIFRDYGnIAGLDIAQIENGY--V 318
Cdd:COG2234 142 LDMIGRGGprNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPEETG-GYGRSDHAPFAKAG-IPALFLFTGAEDYhpD 219

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24652993 319 YHTAFDTYENVPGRSIQNSGNNVLALVRAYSNASELY 355
Cdd:COG2234 220 YHTPSDTLDKIDLDALAKVAQLLAALVYELANADERW 256
YfcC COG1288
Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction ...
 534-615 6.53e-03

Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction only];


Pssm-ID: 440899 [Multi-domain]  Cd Length: 464  Bit Score: 40.12  E-value: 6.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 534 ALLINLVSTLHDRGYYWVPIVMFLqvlpFSYFCYLFYM------FLVIFIPVLGRNGYstnpDLIVGL---LCGVCVffa 604
Cdd:COG1288 103 AGIGALVRKLKGKEKLLIPVLMLL----FALGGTTFGMaeetiaFYPILVPLAIALGY----DAITGVaiiFLGAGI--- 171

                        90
                ....*....|.
gi 24652993 605 lGFAAQLINMF 615
Cdd:COG1288 172 -GFAASTINPF 181
 
Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 71-377 5.19e-141

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: 420.46  E-value: 5.19e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993  71 PGEFVAERAQQYLYTYDRIGPKVTGSyANEVTTVEFLVNETEKIRAEMRSDLYDLELDVQSPTG--GYVFNDMVNMYQGI 148
Cdd:cd03875   1 PGGFSLERAWEDLQVLISIGPHPYGS-HNNDKVRDYLLARVEEIKERANANGLEVEVQDDTGSGsfNFLSSGMTLVYFEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 149 HNVIVKLSSKSSQSESYLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFI 228
Cdd:cd03875  80 TNIVVRISGKNSNSLPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAFI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 229 TQHKWAEKCKAFINLEVGGSGGRDLLFQSGPnnPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRDYGNIAGL 308
Cdd:cd03875 160 TQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPGL 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 309 DIAQIENGYVYHTAFDTYENVPGRSIQNSGNNVLALVRAYSNASELYNTESD-DSHAVFFDFLGLFFVYY 377
Cdd:cd03875 238 DIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYrGGPAVFFDLLGLFFVYY 307
Peptidase_M28 pfam04389
Peptidase family M28;
150-345 1.50e-62

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 209.45  E-value: 1.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993   150 NVIVKLSSKSSQSesYLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMsISEIPFEHPIVFLFNGAEENPLQASHGFIT 229
Cdd:pfam04389   1 NVIAKLPGKAPDE--VVLLSAHYDSVGTGPGADDNASGVAALLELARVL-AAGQRPKRSVRFLFFDAEEAGLLGSHHFAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993   230 QHKWAEKCKAFINLEVGGSGGRDLLFQSGPNNPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRDYGnIAGLD 309
Cdd:pfam04389  78 SHPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERGGPGRSDHAPFIKAG-IPGLD 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 24652993   310 IAQIENGYVYHTAFDTYENVPGRSIQNSGNNVLALV 345
Cdd:pfam04389 157 LAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 148-346 3.49e-35

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: 132.85  E-value: 3.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 148 IHNVIVKLSSKSSQSEsYLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGF 227
Cdd:cd02690   1 GYNVIATIKGSDKPDE-VILIGAHYDSVPLSPGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDAEELGLLGSKYY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 228 ITQHKW-AEKCKAFINLEVGGSGGRDLLFQSGPNNPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRDyGNIA 306
Cdd:cd02690  80 AEQLLSsLKNIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELENVVYTVVYKEDGGTGGSDHRPFLA-RGIP 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24652993 307 GLDIAQIE--NGYVYHTAFDTYENVPGRSIQNSGNNVLALVR 346
Cdd:cd02690 159 AASLIQSEsyNFPYYHTTQDTLENIDKDTLKRAGDILASFLY 200
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 165-355 1.64e-25

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: 106.75  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 165 YLLLNSHFDSKP-GSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFITQHKWA-EKCKAFIN 242
Cdd:COG2234  62 VVVLGAHYDSVGsIGPGADDNASGVAALLELARALAALGPKPKRTIRFVAFGAEEQGLLGSRYYAENLKAPlEKIVAVLN 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 243 LEVGGSGG--RDLLFQSGPNNPWLMKYYRQHAKHPFATTMAEEIFQSGvLPSDSDFRIFRDYGnIAGLDIAQIENGY--V 318
Cdd:COG2234 142 LDMIGRGGprNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPEETG-GYGRSDHAPFAKAG-IPALFLFTGAEDYhpD 219

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24652993 319 YHTAFDTYENVPGRSIQNSGNNVLALVRAYSNASELY 355
Cdd:COG2234 220 YHTPSDTLDKIDLDALAKVAQLLAALVYELANADERW 256
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 170-345 1.40e-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: 53.73  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 170 SHFDSKPGSPGSGDDGTMVVVMMEVLRQMsiSEIPFEHPIVFLFNGAEENPLQASHGFITQ--HKWAEKCKAFINLEVGG 247
Cdd:cd05661  83 SHYDSVVKAPGANDNASGTAVTLELARVF--KKVKTDKELRFIAFGAEENGLLGSKYYVASlsEDEIKRTIGVFNLDMVG 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 248 SG---GRDLLFQS---GPNNPWlmkyyrqhakhPFATTMAEEIfqSGVLP----SDSDFRIFRDYGNIAGLDI-AQIENG 316
Cdd:cd05661 161 TSdakAGDLYAYTidgKPNLVT-----------DSGAAASKRL--SGVLPlvqqGSSDHVPFHEAGIPAALFIhMDPETE 227

                       170       180       190
                ....*....|....*....|....*....|..
gi 24652993 317 YV---YHTAFDTYENVPGRSIQNSGNNVLALV 345
Cdd:cd05661 228 PVepwYHTPNDTVENISKERLDNALDIVGTAV 259
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 165-329 2.10e-06

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: 49.52  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 165 YLLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFITQH----------KWA 234
Cdd:cd08015  17 VVILGAHLDSWHGATGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVALWGSEEQGLHGSRAYVEKHfgdpptmqlqRDH 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 235 EKCKAFINLEVGGSGGRDLLFQ----SGPN-NPWLMKYYRQhakhpFATTMAEEIFQSgvlpsdSDFRIFrDYGNIAGLD 309
Cdd:cd08015  97 KKISAYFNLDNGTGRIRGIYLQgnlaAYPIfSAWLYPFHDL-----GATTVIERNTGG------TDHAAF-DAVGIPAFQ 164

                       170       180
                ....*....|....*....|...
gi 24652993 310 IAQIE---NGYVYHTAFDTYENV 329
Cdd:cd08015 165 FIQDPwdyWTRTHHTNRDTYDRL 187
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 166-301 3.61e-06

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: 49.75  E-value: 3.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 166 LLLNSHFDSKPGSPGSGDDGTMVVVMMEVLRqmSISEIPFEHPIVFLFNGAEENP-----LQASHGFITQ-HKWAEKCKA 239
Cdd:cd05640  69 ILIGAHYDTVPGSPGADDNASGVAALLELAR--LLATLDPNHTLRFVAFDLEEYPffargLMGSHAYAEDlLRPLTPIVG 146

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652993 240 FINLEVGGSggrdllFQSGPNNpwlmKYYRQHAKHPFATTMAEEIFQSGVLPSDSDFRIFRD 301
Cdd:cd05640 147 MLSLEMIGY------YDPFPHS----QAYPAGFELHFYPHMGDFIAVVGRLRSRKLVRAFKR 198
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 179-250 1.88e-05

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 47.96  E-value: 1.88e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652993 179 PGSGDDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHGFITQHKWAEKCKAFINLEVGGSGG 250
Cdd:COG0624 108 RGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARALVEELAEGLKADAAIVGEPTGVPT 179
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 73-327 1.76e-04

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: 44.53  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993  73 EFVAERAQQYLYTYDRiGPKVTGSYANEVTtVEFLVNETEKIraemrsDLYDLELDVQSPTggyvfndmvnmyqgIHNVI 152
Cdd:cd08022   7 EPDAENIREWLRYYTS-GPHLAGTEGNLEL-AQWTEDKWREF------GLDDVELEEYDVP--------------IWNVI 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 153 VKLSSKSSQSESYLLLNsHFDSkpGSPGSGDDGTMVVVMMEVLRQMS--ISE--IPFEhPIVFLFNGAEENPLQASHGFI 228
Cdd:cd08022  65 GTIRGSEEPDEYIILGN-HRDA--WVFGAGDPNSGTAVLLEVARALGtlLKKgwRPRR-TIIFASWDAEEYGLIGSTEWV 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 229 TQHkwAEKCK----AFINLEVGGSGGRdlLFQSGpnNPWLMKYYRQHAK---HP--------FATTMAEEIFQSGVLPSD 293
Cdd:cd08022 141 EEN--ADWLQeravAYLNVDVAVSGST--LRAAG--SPLLQNLLREAAKevqDPdegatlkyLPSWWDDTGGEIGNLGSG 214

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 24652993 294 SDFRIFRDYGNIAGLDI----AQIENGYVYHTAFDTYE 327
Cdd:cd08022 215 SDYTPFLDHLGIASIDFgfsgGPTDPYPHYHSNYDSFE 252
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 167-250 2.57e-04

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 43.87  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993   167 LLNSHFDSKP-----GSP------------GSGDDGTMVVVMMEVLRQMsISEIPFEHPIVFLFNGAEENPLQASHGFIT 229
Cdd:pfam01546   1 LLRGHMDVVPdeetwGWPfkstedgklygrGHDDMKGGLLAALEALRAL-KEEGLKKGTVKLLFQPDEEGGMGGARALIE 79

                          90       100
                  ....*....|....*....|..
gi 24652993   230 QHKWA-EKCKAFINLEVGGSGG 250
Cdd:pfam01546  80 DGLLErEKVDAVFGLHIGEPTL 101
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 165-273 3.72e-04

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


Pssm-ID: 349910 [Multi-domain]  Cd Length: 290  Bit Score: 43.50  E-value: 3.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 165 YLLLNSHFDSKPGSPGSG---------DDGTMVVVMMEVLRQMSISEIPFEHPIVFLFNGAEENPLQASHgFITQHKWA- 234
Cdd:cd05660  75 YIVLSAHWDHLGIGPPIGgdeiyngavDNASGVAAVLELARVFAAQDQRPKRSIVFLAVTAEEKGLLGSR-YYAANPIFp 153

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24652993 235 -EKCKAFINLEV-GGSGGRDLLFQSGPNNPWLMKYYRQHAK 273
Cdd:cd05660 154 lDKIVANLNIDMiGRIGPTKDVLLIGSGSSELENILKEAAK 194
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 115-346 8.48e-04

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: 42.28  E-value: 8.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 115 RAEMRSDLYDLeLDVQSPTGG--------YVFNDMVNM---------YQGIHNVIVKLSSKSSQSEsYLLLNSHFDSKPG 177
Cdd:cd03874   8 LAKIKEDLEYL-SSMPHMAGTkgdaalakYIENSFKNNglfeveleeYSPITNVVGKIEGIEQPDR-AIIIGAHRDSWGY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 178 SPGSGDDGTMVvvMMEVLRQMSISEIPF----EHPIVFLFNGAEENPLQASHGFITQHKWAEKCK--AFINLEVGGSGGR 251
Cdd:cd03874  86 GAGYPNSGTAV--LLEIARLFQQLKKKFgwkpLRTIYFISWDGSEFGLAGSTELGEDRKASLKDEvyAYINIDQLVIGNS 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 252 DLLFQSgpnNPWLMKYYRQHAK---HPFATTMAEEIFQSGV--LPSDSDFRIFRDYGNIAGLDIAQIENG---YVYHTAF 323
Cdd:cd03874 164 ELDVDA---HPLLQSLFRKASKkvkFPGNEDWWKHSPNAKVsnLHQYGDWTPFLNHLGIPVAVFSFKNDRnasYPINSSY 240

                       250       260
                ....*....|....*....|...
gi 24652993 324 DTYENVPgRSIQNSGNNVLALVR 346
Cdd:cd03874 241 DTFEWLE-KFLDPDFELHSTLAE 262
YfcC COG1288
Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction ...
 534-615 6.53e-03

Predicted membrane transporter YfcC, affects glyoxylate shunt [General function prediction only];


Pssm-ID: 440899 [Multi-domain]  Cd Length: 464  Bit Score: 40.12  E-value: 6.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 534 ALLINLVSTLHDRGYYWVPIVMFLqvlpFSYFCYLFYM------FLVIFIPVLGRNGYstnpDLIVGL---LCGVCVffa 604
Cdd:COG1288 103 AGIGALVRKLKGKEKLLIPVLMLL----FALGGTTFGMaeetiaFYPILVPLAIALGY----DAITGVaiiFLGAGI--- 171

                        90
                ....*....|.
gi 24652993 605 lGFAAQLINMF 615
Cdd:COG1288 172 -GFAASTINPF 181
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 179-293 8.11e-03

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: 38.76  E-value: 8.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652993 179 PGSGDDGTMVVVMMEVLRQMSISEIPfEHPIVFLFNGAEENPLQASHGFITQHKWA-EKCKAFINLE-VGGSGGRDLLFQ 256
Cdd:cd03877  40 NGADDNASGVAAVLELARYFAKQKTP-KRSIVFAAFTAEEKGLLGSKYFAENPKFPlDKIVAMLNLDmIGRLGRSKDVYL 118

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 24652993 257 SGPNNPWLMKYYRQHAKHPFATTMAEEIFQSGVLPSD 293
Cdd:cd03877 119 IGSGSSELENLLKKANKAAGRVLSKDPLPEWGFFRSD 155
 
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