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Conserved domains on  [gi|642928504|ref|XP_008193818|]
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endoplasmic reticulum metallopeptidase 1 isoform X1 [Tribolium castaneum]

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

Graphical summary

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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 ...
73-381 6.85e-140

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: 417.76  E-value: 6.85e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  73 PDRFIAERAHNVLKKLTKIGPRIAGSyANEVTAVQLLKGAVQEIIDNAHENHV-IELDVQKASGDFNlEFLDGMTNVYRD 151
Cdd:cd03875    1 PGGFSLERAWEDLQVLISIGPHPYGS-HNNDKVRDYLLARVEEIKERANANGLeVEVQDDTGSGSFN-FLSSGMTLVYFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 152 VQNVVVKVSSKIKSP-HSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPASHGF 230
Cdd:cd03875   79 VTNIVVRISGKNSNSlPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 231 ITQHKWASEVRTFINLEACGAGGREVLFQAGPnhPWILETYSEEVPYPYASSLAQEIFQSGVIPGDTDYRIFRDFGNVSG 310
Cdd:cd03875  159 ITQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642928504 311 LDFAWSANGYVYHTKFDSIEHIPLGSLQRTGDNILALAKGMAQGHQLSEVDKYRAGNLVFFDFLGAFVVRW 381
Cdd:cd03875  237 LDIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYRGGPAVFFDLLGLFFVYY 307
 
Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
73-381 6.85e-140

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: 417.76  E-value: 6.85e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  73 PDRFIAERAHNVLKKLTKIGPRIAGSyANEVTAVQLLKGAVQEIIDNAHENHV-IELDVQKASGDFNlEFLDGMTNVYRD 151
Cdd:cd03875    1 PGGFSLERAWEDLQVLISIGPHPYGS-HNNDKVRDYLLARVEEIKERANANGLeVEVQDDTGSGSFN-FLSSGMTLVYFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 152 VQNVVVKVSSKIKSP-HSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPASHGF 230
Cdd:cd03875   79 VTNIVVRISGKNSNSlPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 231 ITQHKWASEVRTFINLEACGAGGREVLFQAGPnhPWILETYSEEVPYPYASSLAQEIFQSGVIPGDTDYRIFRDFGNVSG 310
Cdd:cd03875  159 ITQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642928504 311 LDFAWSANGYVYHTKFDSIEHIPLGSLQRTGDNILALAKGMAQGHQLSEVDKYRAGNLVFFDFLGAFVVRW 381
Cdd:cd03875  237 LDIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYRGGPAVFFDLLGLFFVYY 307
Peptidase_M28 pfam04389
Peptidase family M28;
154-348 3.70e-64

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 213.69  E-value: 3.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  154 NVVVKVSSKiKSPHSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKiLRHNIIFLFNGGEENFMPASHGFITQ 233
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVLAAGQR-PKRSVRFLFFDAEEAGLLGSHHFAKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  234 HKWASEVRTFINLEACGAGGREVLFQAGPNHPWILETYSEEVPYPYASSLAQEIFQSGVIPGDTDYRIFRDFGnVSGLDF 313
Cdd:pfam04389  79 HPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERGGPGRSDHAPFIKAG-IPGLDL 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 642928504  314 AWSANGYVYHTKFDSIEHIPLGSLQRTGDNILALA 348
Cdd:pfam04389 158 AFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
133-353 2.80e-24

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: 102.90  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 133 ASGDFNLEFLDGMTNVYRDVQNVVVKVSSKIKSPHSLLINCHFDSV-VDSPGGSDDGAGCAVMLEILRVLSKSPKILRHN 211
Cdd:COG2234   27 AGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVgSIGPGADDNASGVAALLELARALAALGPKPKRT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 212 IIFLFNGGEENFMPASHGFITQHKWASE-VRTFINLEACGAGG-REVLFQAGPNHPWILETYSEEVPYPYASSLAQEIFQ 289
Cdd:COG2234  107 IRFVAFGAEEQGLLGSRYYAENLKAPLEkIVAVLNLDMIGRGGpRNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPE 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 642928504 290 SGVIPGDTDYRIFRDFGnVSGLDFAWSANGY--VYHTKFDSIEHIPLGSLQRTGDNILALAKGMAQ 353
Cdd:COG2234  187 ETGGYGRSDHAPFAKAG-IPALFLFTGAEDYhpDYHTPSDTLDKIDLDALAKVAQLLAALVYELAN 251
 
Name Accession Description Interval E-value
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
73-381 6.85e-140

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: 417.76  E-value: 6.85e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  73 PDRFIAERAHNVLKKLTKIGPRIAGSyANEVTAVQLLKGAVQEIIDNAHENHV-IELDVQKASGDFNlEFLDGMTNVYRD 151
Cdd:cd03875    1 PGGFSLERAWEDLQVLISIGPHPYGS-HNNDKVRDYLLARVEEIKERANANGLeVEVQDDTGSGSFN-FLSSGMTLVYFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 152 VQNVVVKVSSKIKSP-HSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPASHGF 230
Cdd:cd03875   79 VTNIVVRISGKNSNSlPALLLNAHFDSVPTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFNGAEENGLLGAHAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 231 ITQHKWASEVRTFINLEACGAGGREVLFQAGPnhPWILETYSEEVPYPYASSLAQEIFQSGVIPGDTDYRIFRDFGNVSG 310
Cdd:cd03875  159 ITQHPWAKNVRAFINLEAAGAGGRAILFQTGP--PWLVEAYYSAAKHPFASVIAQDVFQSGLIPSDTDYRVFRDYGGLPG 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642928504 311 LDFAWSANGYVYHTKFDSIEHIPLGSLQRTGDNILALAKGMAQGHQLSEVDKYRAGNLVFFDFLGAFVVRW 381
Cdd:cd03875  237 LDIAFYKNRYVYHTKYDTADHISRGSLQHMGDNLLALLRYLANSSELENDSEYRGGPAVFFDLLGLFFVYY 307
Peptidase_M28 pfam04389
Peptidase family M28;
154-348 3.70e-64

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 213.69  E-value: 3.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  154 NVVVKVSSKiKSPHSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKiLRHNIIFLFNGGEENFMPASHGFITQ 233
Cdd:pfam04389   1 NVIAKLPGK-APDEVVLLSAHYDSVGTGPGADDNASGVAALLELARVLAAGQR-PKRSVRFLFFDAEEAGLLGSHHFAKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  234 HKWASEVRTFINLEACGAGGREVLFQAGPNHPWILETYSEEVPYPYASSLAQEIFQSGVIPGDTDYRIFRDFGnVSGLDF 313
Cdd:pfam04389  79 HPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAEDPFQERGGPGRSDHAPFIKAG-IPGLDL 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 642928504  314 AWSANGYVYHTKFDSIEHIPLGSLQRTGDNILALA 348
Cdd:pfam04389 158 AFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
153-351 5.01e-39

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: 143.64  E-value: 5.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 153 QNVVVKVSSKIKSPHSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPASHGFIT 232
Cdd:cd02690    2 YNVIATIKGSDKPDEVILIGAHYDSVPLSPGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDAEELGLLGSKYYAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 233 QHKWASE-VRTFINLEACGAGGREVLFQAGPNHPWILETYSEEVPYPYASSLAQEIFQSGVIPGDTDYRIFRDfGNVSGL 311
Cdd:cd02690   82 QLLSSLKnIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELENVVYTVVYKEDGGTGGSDHRPFLA-RGIPAA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 642928504 312 DFAWSA--NGYVYHTKFDSIEHIPLGSLQRTGDNILALAKGM 351
Cdd:cd02690  161 SLIQSEsyNFPYYHTTQDTLENIDKDTLKRAGDILASFLYRL 202
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
133-353 2.80e-24

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: 102.90  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 133 ASGDFNLEFLDGMTNVYRDVQNVVVKVSSKIKSPHSLLINCHFDSV-VDSPGGSDDGAGCAVMLEILRVLSKSPKILRHN 211
Cdd:COG2234   27 AGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDSVgSIGPGADDNASGVAALLELARALAALGPKPKRT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 212 IIFLFNGGEENFMPASHGFITQHKWASE-VRTFINLEACGAGG-REVLFQAGPNHPWILETYSEEVPYPYASSLAQEIFQ 289
Cdd:COG2234  107 IRFVAFGAEEQGLLGSRYYAENLKAPLEkIVAVLNLDMIGRGGpRNYLYVDGDGGSPELADLLEAAAKAYLPGLGVDPPE 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 642928504 290 SGVIPGDTDYRIFRDFGnVSGLDFAWSANGY--VYHTKFDSIEHIPLGSLQRTGDNILALAKGMAQ 353
Cdd:COG2234  187 ETGGYGRSDHAPFAKAG-IPALFLFTGAEDYhpDYHTPSDTLDKIDLDALAKVAQLLAALVYELAN 251
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
153-344 1.01e-10

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: 63.36  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 153 QNVVVKVSSK--IKSPHSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSP--KILRhniiFLFNGGEENFMPASH 228
Cdd:cd05661   61 HNVIATKKPDnnKNNNDIIIVTSHYDSVVKAPGANDNASGTAVTLELARVFKKVKtdKELR----FIAFGAEENGLLGSK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 229 GFITQHKWASEVRTfinleacgaggrEVLFQA---GPNHPWILETYSEEVP----YPYASSLAQEIFQSGVIP----GDT 297
Cdd:cd05661  137 YYVASLSEDEIKRT------------IGVFNLdmvGTSDAKAGDLYAYTIDgkpnLVTDSGAAASKRLSGVLPlvqqGSS 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 642928504 298 DYRIFRDFGNVSGLdFAWSANGY-----VYHTKFDSIEHIPLGSLQRTGDNI 344
Cdd:cd05661  205 DHVPFHEAGIPAAL-FIHMDPETepvepWYHTPNDTVENISKERLDNALDIV 255
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
154-339 1.76e-09

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: 58.76  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 154 NVVVKVSSKIKSPHSLLINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPASHGFITQ 233
Cdd:cd08015    3 NVIAEIPGSDKKDEVVILGAHLDSWHGATGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVALWGSEEQGLHGSRAYVEK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 234 H----------KWASEVRTFINLEAcGAGGREVLFQAGPNHPW-ILETYSEEVPYPYASSLAQEIFqsgvipGDTDYRIF 302
Cdd:cd08015   83 HfgdpptmqlqRDHKKISAYFNLDN-GTGRIRGIYLQGNLAAYpIFSAWLYPFHDLGATTVIERNT------GGTDHAAF 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 642928504 303 RDFGnVSGLDFA---WSANGYVYHTKFDSIEHIPLGSLQR 339
Cdd:cd08015  156 DAVG-IPAFQFIqdpWDYWTRTHHTNRDTYDRLIPEDLKQ 194
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
74-330 2.25e-09

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: 59.55  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504  74 DRFIAERAHNVLKKLTKiGPRIAGSYANEVTAVQLLKGAVQEIIDNAHenhVIELDVQkasgdfnlefldgmtnvyrdVQ 153
Cdd:cd08022    6 DEPDAENIREWLRYYTS-GPHLAGTEGNLELAQWTEDKWREFGLDDVE---LEEYDVP--------------------IW 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 154 NVVVKVSSKIKSPHSLLINCHFDSVVdsPGGSDDGAGCAVMLEILRVLSKSPK---ILRHNIIFLFNGGEENFMPASHGF 230
Cdd:cd08022   62 NVIGTIRGSEEPDEYIILGNHRDAWV--FGAGDPNSGTAVLLEVARALGTLLKkgwRPRRTIIFASWDAEEYGLIGSTEW 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 231 ITQH-KWASE-VRTFINLEaCGAGGREVLFQAGPNHPWILETYSEEVPYPYASSLAQEIFQS--------GVIPGDTDYR 300
Cdd:cd08022  140 VEENaDWLQErAVAYLNVD-VAVSGSTLRAAGSPLLQNLLREAAKEVQDPDEGATLKYLPSWwddtggeiGNLGSGSDYT 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 642928504 301 IFRDFGNVSGLDFAWSANG----YVYHTKFDSIE 330
Cdd:cd08022  219 PFLDHLGIASIDFGFSGGPtdpyPHYHSNYDSFE 252
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
132-333 1.80e-07

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: 53.45  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 132 KASGDFNLEFldgmtNVYRDVQNVVVKVSSKIKSPHSLLINCHFDSVvdSPGGSDDGAGCAVMLEILRVLSKSP-----K 206
Cdd:cd03874   42 KNNGLFEVEL-----EEYSPITNVVGKIEGIEQPDRAIIIGAHRDSW--GYGAGYPNSGTAVLLEIARLFQQLKkkfgwK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 207 ILRhNIIF-LFNGGEENFMPASHgFITQHKWA--SEVRTFINLEACGAGGREVLFQAGP--NHpwILETYSEEVPYPYAS 281
Cdd:cd03874  115 PLR-TIYFiSWDGSEFGLAGSTE-LGEDRKASlkDEVYAYINIDQLVIGNSELDVDAHPllQS--LFRKASKKVKFPGNE 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 642928504 282 SLAQEIFQSGV--IPGDTDYRIFRDFGNVSGLDFAWSANG---YVYHTKFDSIEHIP 333
Cdd:cd03874  191 DWWKHSPNAKVsnLHQYGDWTPFLNHLGIPVAVFSFKNDRnasYPINSSYDTFEWLE 247
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
154-253 6.62e-07

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: 52.58  E-value: 6.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 154 NVVVKVSSKIKSPHsLLINCHFDsVV--------DSP--------------GGSDDGAGCAVMLEILRVLSKSPKILRHN 211
Cdd:COG0624   60 NLVARRPGDGGGPT-LLLYGHLD-VVppgdlelwTSDpfeptiedgrlygrGAADMKGGLAAMLAALRALLAAGLRLPGN 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 642928504 212 IIFLFNGGEENFMPASHGFITQHKWASEVRTFINLEACGAGG 253
Cdd:COG0624  138 VTLLFTGDEEVGSPGARALVEELAEGLKADAAIVGEPTGVPT 179
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
183-336 9.25e-06

M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. 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).


Pssm-ID: 349948 [Multi-domain]  Cd Length: 198  Bit Score: 47.43  E-value: 9.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 183 GGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPAshGFITQHKWASEvRTF-----INLEACGAGGREVl 257
Cdd:cd18669   50 GALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGA--GKGLLSKDALE-EDLkvdylFVGDATPAPQKGV- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 258 fqagpnhpwiletyseEVPYPY---ASSLAQEIF----QSGVIPGDTDYRIFRDFGnVSGLDFaWSANGYVYHTK--FDS 328
Cdd:cd18669  126 ----------------GIRTPLvdaLSEAARKVFgkpqHAEGTGGGTDGRYLQELG-IPGVTL-GAGGGKGAHSPneRVN 187

                 ....*...
gi 642928504 329 IEHIPLGS 336
Cdd:cd18669  188 LEDLESAL 195
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
182-336 1.38e-05

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).


Pssm-ID: 349870 [Multi-domain]  Cd Length: 200  Bit Score: 47.03  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 182 PGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEENFMPASHGfiTQHKWA----SEVRTFINLEACGAggreVL 257
Cdd:cd03873   49 RGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKG--LLSKFLlaedLKVDAAFVIDATAG----PI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 258 FQAGPnhpwiletyseEVPYPY---ASSLAQEIF----QSGVIPGDTDYRIFRDFGnVSGLDFaWSANGYVYHTKFD--S 328
Cdd:cd03873  123 LQKGV-----------VIRNPLvdaLRKAAREVGgkpqRASVIGGGTDGRLFAELG-IPGVTL-GPPGDKGAHSPNEflN 189

                 ....*...
gi 642928504 329 IEHIPLGS 336
Cdd:cd03873  190 LDDLEKAT 197
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
173-354 1.63e-05

M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically 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 protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.


Pssm-ID: 349895 [Multi-domain]  Cd Length: 290  Bit Score: 47.78  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 173 CHfdsvvDSPGGSDDGAGCAVMLEILRVLSKSPKI-LRHNIIFLfnggeenFMPASHG---FITQH-KWASEVRTFINLE 247
Cdd:cd05643   93 CH-----PKPGANDNASGSALLLEVARVLAKLILNrPKRGICFL-------WVPEYTGtaaYFAQHpDRLKKIIAVINLD 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 248 ACGAGgrevlfQAGPNHPWILETYSEEVPYPYASSLAQEIFQSGVIP------------GDTDYRIFRDFGNVSGLDFAW 315
Cdd:cd05643  161 MVGED------QTKTGSTLMLVPTPLSFPSYLNEELAQKLSNFTGSSlpavrygkepyeGGSDHDVFSDPGIPAVMFNTW 234
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 642928504 316 SaNGYvYHTKFDSIEHIPLGSLQRTGDNILALAKGMAQG 354
Cdd:cd05643  235 P-DRY-YHTSDDTPDKLDPETLKNVGAAVLLTAYALANG 271
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
164-242 9.45e-05

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: 45.13  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 164 KSPHSL-LINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKSpkILRHNIIFLFNGGEE--NFMPASHGfitQHKWASEV 240
Cdd:cd05640   63 YSQDKLiLIGAHYDTVPGSPGADDNASGVAALLELARLLATL--DPNHTLRFVAFDLEEypFFARGLMG---SHAYAEDL 137

                 ..
gi 642928504 241 RT 242
Cdd:cd05640  138 LR 139
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
103-221 9.61e-05

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: 45.31  E-value: 9.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 103 VTAVQLLKGAVQEIIDNAHENHVielDVQKASGDFNlefldgmtnvyrdvQN-VVVKVSSKIKSPHSLLINCHFDSVVDS 181
Cdd:cd03879   41 VESAEWLLDQVQAIIASSGRSGA---TVEQFTHSFP--------------QPsIIATIPGSEKSDEIVVIGAHQDSINGS 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 642928504 182 -------PGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEE 221
Cdd:cd03879  104 npsngraPGADDDGSGTVTILEALRVLLESGFQPKNTIEFHWYAAEE 150
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
153-221 2.06e-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: 44.27  E-value: 2.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 642928504 153 QNVVVKVSSKIKSPHSLLINCHFD--SVVDSPGGS-------DDGAGCAVMLEILRVLSKSPKILRHNIIFLFNGGEE 221
Cdd:cd05660   60 HNVVAILPGSKLPDEYIVLSAHWDhlGIGPPIGGDeiyngavDNASGVAAVLELARVFAAQDQRPKRSIVFLAVTAEE 137
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
147-221 2.38e-04

Di- or tripeptidase [Amino acid transport and metabolism];


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 44.27  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 147 NVYRD-VQNVVVKVSSKI--KSPhSLLINCHFDSVVDSPG--------------------GSDDGAGCAVMLEILRVLsK 203
Cdd:COG2195   39 EVEEDeAGNVIATLPATPgyNVP-TIGLQAHMDTVPQFPGdgikpqidgglitadgtttlGADDKAGVAAILAALEYL-K 116
                         90
                 ....*....|....*...
gi 642928504 204 SPKILRHNIIFLFNGGEE 221
Cdd:COG2195  117 EPEIPHGPIEVLFTPDEE 134
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
154-257 7.09e-04

M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.


Pssm-ID: 349881 [Multi-domain]  Cd Length: 362  Bit Score: 42.96  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 154 NVVVKVSSKIKsPHSLLInCHFDSV------------VDS-----PGGSDDGAGCAVMLEILRVLSKSPKILRHNIIFLF 216
Cdd:cd03885   50 HLIATFKGTGG-KRVLLI-GHMDTVfpegtlafrpftVDGdraygPGVADMKGGLVVILHALKALKAAGGRDYLPITVLL 127
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 642928504 217 NGGEENFMPASHGFITQHkwASEVRTFINLEACGAGGREVL 257
Cdd:cd03885  128 NSDEEIGSPGSRELIEEE--AKGADYVLVFEPARADGNLVT 166
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
103-222 2.39e-03

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: 40.74  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 103 VTAVQLLKGA--VQEIIDNAHENHVIELDVQKASGDFNLEFLDGM----------TNVYRDVQNVVVKvsSKIKSPHS-L 169
Cdd:cd03876    2 ITVDNLMAHLqqLQDIADANGGNRAFGSPGYNASVDYVKNELKAAgyydvtlqpfTSLYRTTYNVIAE--TKGGDPNNvV 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 642928504 170 LINCHFDSVVDSPGGSDDGAGCAVMLEILRVLSKsPKILRHnIIFLFNGGEEN 222
Cdd:cd03876   80 MLGAHLDSVSAGPGINDNGSGSAALLEVALALAK-FKVKNA-VRFAWWTAEEF 130
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
182-221 3.42e-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: 39.92  E-value: 3.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 642928504 182 PGGSDDGAGCAVMLEILRVLSKSPKiLRHNIIFLFNGGEE 221
Cdd:cd03877   40 NGADDNASGVAAVLELARYFAKQKT-PKRSIVFAAFTAEE 78
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
152-221 3.99e-03

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: 40.55  E-value: 3.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 642928504 152 VQNVVVKVSSKIKSPHSLLINCHFDSVV--------DSPGGSDDGAGCAVMLEILRVLSK-SPKIlrhNIIFLFNGGEE 221
Cdd:cd05642   88 ISNVVATLKGSEDPDRVYVVSGHYDSRVsdvmdyesDAPGANDDASGVAVSMELARIFAKhRPKA---TIVFTAVAGEE 163
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
154-221 5.19e-03

M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.


Pssm-ID: 349932 [Multi-domain]  Cd Length: 368  Bit Score: 40.13  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642928504 154 NVVVKVSSKIKSPHSLLINCHFDSVVdsPG---------------------GSDDGAGCAVMLEILRVLsKSPKILRHNI 212
Cdd:cd05683   55 NLICTLKADKEEVPKILFTSHMDTVT--PGinvkppqiadgyiysdgttilGADDKAGIAAILEAIRVI-KEKNIPHGQI 131

                 ....*....
gi 642928504 213 IFLFNGGEE 221
Cdd:cd05683  132 QFVITVGEE 140
 
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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