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Conserved domains on  [gi|564326527|ref|XP_006228464|]
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glutaminyl-peptide cyclotransferase-like protein isoform X1 [Rattus norvegicus]

Protein Classification

glutaminyl-peptide cyclotransferase family protein( domain architecture ID 10133850)

glutaminyl-peptide cyclotransferase (QPCT) family protein such as QPCT that is responsible for the biosynthesis of pyroglutamyl peptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_QC_like cd03880
M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) ...
 82-341 1.45e-134

M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) subfamily. QC is involved in N-terminal glutamine cyclization of many endocrine peptides and is typically abundant in brain tissue. N-terminal glutamine residue cyclization is an important post-translational event in the processing of numerous bioactive proteins, including neuropeptides, hormones, and cytokines during their maturation in the secretory pathway. The N-terminal pGlu protects them from exopeptidase degradation and/or enables them to have proper conformation for binding to their receptors. QCs are highly conserved from yeast to human. In humans, several genetic diseases, such as osteoporosis, appear to result from mutations of the QC gene. N-terminal glutamate cyclization into pyroglutamate (pGlu) is a reaction that may be related to the formation of several plaque-forming peptides, such as amyloid-(A) peptides and collagen-like Alzheimer amyloid plaque component, which play a pivotal role in Alzheimer's disease.


:

Pssm-ID: 349876 [Multi-domain]  Cd Length: 305  Bit Score: 385.05  E-value: 1.45e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  82 LRLVVGQLDPQRLWGTFLRPLLIVRPPGSPGNLQVRKFLEATLQSLSAGWHVELDPFTASTPLGPLDFGNVVATLDPGAA 161
Cdd:cd03880    3 LRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTFTNIIATLNPPAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 162 RHLTLACHYDSKFFPPGlpPFVGATDSAVPCALLLELVQALDVMLSR--IKQQAAPVTLQLLFLDGEEALKEWGPKDSLY 239
Cdd:cd03880   83 RYLVLACHYDSKYFPEG--EFIGATDSAVPCAMLLYLARSLDAALTRkwPKSKKSDLGLQLIFFDGEEAFEEWSDTDSLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 240 GSRHLAQIMESIPHSPG---PTRIQAIELFVLLDLLGAPSPIFFSHFPRTARWFQRLRSI-------------------- 296
Cdd:cd03880  161 GSRHLAAKWESTPYPPGsrySGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIekrlrklglleshpserkyf 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564326527 297 --------------------GVPVLHLIAMPFPAVWHTPADTEANLHPPTVHNLSRILAVFLAEY 341
Cdd:cd03880  241 qphskytpdieddhipflerGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
 
Name Accession Description Interval E-value
M28_QC_like cd03880
M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) ...
 82-341 1.45e-134

M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) subfamily. QC is involved in N-terminal glutamine cyclization of many endocrine peptides and is typically abundant in brain tissue. N-terminal glutamine residue cyclization is an important post-translational event in the processing of numerous bioactive proteins, including neuropeptides, hormones, and cytokines during their maturation in the secretory pathway. The N-terminal pGlu protects them from exopeptidase degradation and/or enables them to have proper conformation for binding to their receptors. QCs are highly conserved from yeast to human. In humans, several genetic diseases, such as osteoporosis, appear to result from mutations of the QC gene. N-terminal glutamate cyclization into pyroglutamate (pGlu) is a reaction that may be related to the formation of several plaque-forming peptides, such as amyloid-(A) peptides and collagen-like Alzheimer amyloid plaque component, which play a pivotal role in Alzheimer's disease.


Pssm-ID: 349876 [Multi-domain]  Cd Length: 305  Bit Score: 385.05  E-value: 1.45e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  82 LRLVVGQLDPQRLWGTFLRPLLIVRPPGSPGNLQVRKFLEATLQSLSAGWHVELDPFTASTPLGPLDFGNVVATLDPGAA 161
Cdd:cd03880    3 LRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTFTNIIATLNPPAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 162 RHLTLACHYDSKFFPPGlpPFVGATDSAVPCALLLELVQALDVMLSR--IKQQAAPVTLQLLFLDGEEALKEWGPKDSLY 239
Cdd:cd03880   83 RYLVLACHYDSKYFPEG--EFIGATDSAVPCAMLLYLARSLDAALTRkwPKSKKSDLGLQLIFFDGEEAFEEWSDTDSLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 240 GSRHLAQIMESIPHSPG---PTRIQAIELFVLLDLLGAPSPIFFSHFPRTARWFQRLRSI-------------------- 296
Cdd:cd03880  161 GSRHLAAKWESTPYPPGsrySGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIekrlrklglleshpserkyf 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564326527 297 --------------------GVPVLHLIAMPFPAVWHTPADTEANLHPPTVHNLSRILAVFLAEY 341
Cdd:cd03880  241 qphskytpdieddhipflerGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
Peptidase_M28 pfam04389
Peptidase family M28;
151-338 5.41e-33

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 121.24  E-value: 5.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  151 NVVATLDPGA-ARHLTLACHYDSKFFPPGlppfvgATDSAVPCALLLELVQALdvmlsrIKQQAAPVTLQLLFLDGEEAl 229
Cdd:pfam04389   1 NVIAKLPGKApDEVVLLSAHYDSVGTGPG------ADDNASGVAALLELARVL------AAGQRPKRSVRFLFFDAEEA- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  230 kewgpkdSLYGSRHLAQimesiPHSPGptriQAIELFVLLDLLGAPSPIFFSHFPRTARW-------------------- 289
Cdd:pfam04389  68 -------GLLGSHHFAK-----SHPPL----KKIRAVINLDMIGSGGPALLFQSGPKGSSllekylkaaakpygvtlaed 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564326527  290 -----FQRLRS-------IGVPVLHLIAMPFPAVWHTPADTEANLHPPTVHNLSRILAVFL 338
Cdd:pfam04389 132 pfqerGGPGRSdhapfikAGIPGLDLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 107-341 1.62e-12

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: 66.69  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 107 PPGSPGNLQVRKFLEATLQSLSAGWHVELDPFTASTPLGPLDFGNVVATLdPG---AARHLTLACHYDSkfFPPGLPpfv 183
Cdd:COG2234    4 AAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEI-PGtdpPDEVVVLGAHYDS--VGSIGP--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 184 GATDSAVPCALLLELVQALdvmlsriKQQAAP--VTLQLLFLDGEealkEWGpkdsLYGSRHLAQimesipHSPGPtrIQ 261
Cdd:COG2234   78 GADDNASGVAALLELARAL-------AALGPKpkRTIRFVAFGAE----EQG----LLGSRYYAE------NLKAP--LE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 262 AIELFVLLDLLGAPSP---IFFS-------------------------HFPRTARWFQR-----LRSIGVPVLHLI--AM 306
Cdd:COG2234  135 KIVAVLNLDMIGRGGPrnyLYVDgdggspeladlleaaakaylpglgvDPPEETGGYGRsdhapFAKAGIPALFLFtgAE 214

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564326527 307 PFPAVWHTPADTEANLHPPTVHNLSRILAVFLAEY 341
Cdd:COG2234  215 DYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYEL 249
 
Name Accession Description Interval E-value
M28_QC_like cd03880
M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) ...
 82-341 1.45e-134

M28 Zn-peptidase glutaminyl cyclase; Peptidase M28 family, glutaminyl cyclase (QC; EC 2.3.2.5) subfamily. QC is involved in N-terminal glutamine cyclization of many endocrine peptides and is typically abundant in brain tissue. N-terminal glutamine residue cyclization is an important post-translational event in the processing of numerous bioactive proteins, including neuropeptides, hormones, and cytokines during their maturation in the secretory pathway. The N-terminal pGlu protects them from exopeptidase degradation and/or enables them to have proper conformation for binding to their receptors. QCs are highly conserved from yeast to human. In humans, several genetic diseases, such as osteoporosis, appear to result from mutations of the QC gene. N-terminal glutamate cyclization into pyroglutamate (pGlu) is a reaction that may be related to the formation of several plaque-forming peptides, such as amyloid-(A) peptides and collagen-like Alzheimer amyloid plaque component, which play a pivotal role in Alzheimer's disease.


Pssm-ID: 349876 [Multi-domain]  Cd Length: 305  Bit Score: 385.05  E-value: 1.45e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  82 LRLVVGQLDPQRLWGTFLRPLLIVRPPGSPGNLQVRKFLEATLQSLSAGWHVELDPFTASTPLGPLDFGNVVATLDPGAA 161
Cdd:cd03880    3 LRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTFTNIIATLNPPAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 162 RHLTLACHYDSKFFPPGlpPFVGATDSAVPCALLLELVQALDVMLSR--IKQQAAPVTLQLLFLDGEEALKEWGPKDSLY 239
Cdd:cd03880   83 RYLVLACHYDSKYFPEG--EFIGATDSAVPCAMLLYLARSLDAALTRkwPKSKKSDLGLQLIFFDGEEAFEEWSDTDSLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 240 GSRHLAQIMESIPHSPG---PTRIQAIELFVLLDLLGAPSPIFFSHFPRTARWFQRLRSI-------------------- 296
Cdd:cd03880  161 GSRHLAAKWESTPYPPGsrySGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIekrlrklglleshpserkyf 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564326527 297 --------------------GVPVLHLIAMPFPAVWHTPADTEANLHPPTVHNLSRILAVFLAEY 341
Cdd:cd03880  241 qphskytpdieddhipflerGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
Peptidase_M28 pfam04389
Peptidase family M28;
151-338 5.41e-33

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 121.24  E-value: 5.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  151 NVVATLDPGA-ARHLTLACHYDSKFFPPGlppfvgATDSAVPCALLLELVQALdvmlsrIKQQAAPVTLQLLFLDGEEAl 229
Cdd:pfam04389   1 NVIAKLPGKApDEVVLLSAHYDSVGTGPG------ADDNASGVAALLELARVL------AAGQRPKRSVRFLFFDAEEA- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527  230 kewgpkdSLYGSRHLAQimesiPHSPGptriQAIELFVLLDLLGAPSPIFFSHFPRTARW-------------------- 289
Cdd:pfam04389  68 -------GLLGSHHFAK-----SHPPL----KKIRAVINLDMIGSGGPALLFQSGPKGSSllekylkaaakpygvtlaed 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564326527  290 -----FQRLRS-------IGVPVLHLIAMPFPAVWHTPADTEANLHPPTVHNLSRILAVFL 338
Cdd:pfam04389 132 pfqerGGPGRSdhapfikAGIPGLDLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 151-338 7.74e-23

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: 94.33  E-value: 7.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 151 NVVATLDPGAA--RHLTLACHYDSKffppglPPFVGATDSAVPCALLLELVQaldvMLSRIKQQaAPVTLQLLFLDGEea 228
Cdd:cd02690    3 NVIATIKGSDKpdEVILIGAHYDSV------PLSPGANDNASGVAVLLELAR----VLSKLQLK-PKRSIRFAFWDAE-- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 229 lkEWGpkdsLYGSRHLAQIMESiphspgptRIQAIELFVLLDLLGAPSPIFFSHF--PRTARWFQRLR------------ 294
Cdd:cd02690   70 --ELG----LLGSKYYAEQLLS--------SLKNIRAALNLDMIGGAGPDLYLQTapGNDALVEKLLRalahelenvvyt 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564326527 295 ------------------SIGVPVLHLI--AMPFPAVWHTPADTEANLHPPTVHNLSRILAVFL 338
Cdd:cd02690  136 vvykedggtggsdhrpflARGIPAASLIqsESYNFPYYHTTQDTLENIDKDTLKRAGDILASFL 199
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 107-341 1.62e-12

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: 66.69  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 107 PPGSPGNLQVRKFLEATLQSLSAGWHVELDPFTASTPLGPLDFGNVVATLdPG---AARHLTLACHYDSkfFPPGLPpfv 183
Cdd:COG2234    4 AAGGGGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEI-PGtdpPDEVVVLGAHYDS--VGSIGP--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 184 GATDSAVPCALLLELVQALdvmlsriKQQAAP--VTLQLLFLDGEealkEWGpkdsLYGSRHLAQimesipHSPGPtrIQ 261
Cdd:COG2234   78 GADDNASGVAALLELARAL-------AALGPKpkRTIRFVAFGAE----EQG----LLGSRYYAE------NLKAP--LE 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 262 AIELFVLLDLLGAPSP---IFFS-------------------------HFPRTARWFQR-----LRSIGVPVLHLI--AM 306
Cdd:COG2234  135 KIVAVLNLDMIGRGGPrnyLYVDgdggspeladlleaaakaylpglgvDPPEETGGYGRsdhapFAKAGIPALFLFtgAE 214

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564326527 307 PFPAVWHTPADTEANLHPPTVHNLSRILAVFLAEY 341
Cdd:COG2234  215 DYHPDYHTPSDTLDKIDLDALAKVAQLLAALVYEL 249
M28_like cd08656
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 106-288 4.41e-09

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: 349943 [Multi-domain]  Cd Length: 287  Bit Score: 56.76  E-value: 4.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 106 RPPGSPGNLQVRKFLEATLQSLSA---GWHVELDPFTASTplgpLDFGNVVATLDPGAARHLTLACHYDSKFFPPGLP-- 180
Cdd:cd08656   17 RVPNTAAHKACGEYLAGKLEAFGAkvyNQYADLIAYDGTI----LKARNIIGAYNPESKKRVLLCAHWDSRPYADNDAdp 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 181 -----PFVGATDSAVPCALLLELVQaldvmlsRIKQQAAPVTLQLLFLDGEE------ALKEWGPKDSLYGSRHLAQime 249
Cdd:cd08656   93 kkhhtPILGANDGASGVGALLEIAR-------QIQQQAPAIGIDIIFFDAEDygtpefYEGKYKSDTWCLGSQYWAR--- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564326527 250 sIPHSPGPTriqaIELFVLLDLLGAPSPIFF--SHFPRTAR 288
Cdd:cd08656  163 -NPHVQGYN----ARYGILLD*VGGKNATFLkeQYSLRTAR 198
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 106-242 1.30e-08

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: 55.29  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 106 RPPGSPGNLQVRKFLEATLQSL-----SAGWHVELDPFTASTPLGPLDFG---------NVVATLDPGAARHLT---LAC 168
Cdd:cd03875   22 HPYGSHNNDKVRDYLLARVEEIkeranANGLEVEVQDDTGSGSFNFLSSGmtlvyfevtNIVVRISGKNSNSLPallLNA 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564326527 169 HYDSKffppglPPFVGATDSAVPCALLLELVQALdvmlsrIKQQAAP-VTLQLLFLDGEEalkewgpkDSLYGSR 242
Cdd:cd03875  102 HFDSV------PTSPGATDDGMGVAVMLEVLRYL------SKSGHQPkRDIIFLFNGAEE--------NGLLGAH 156
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 105-202 3.21e-05

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: 44.87  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 105 VRPPGSPGNLQVRKFLEATLQSLsaGWHVELDPFTAStplgpldfgNVVATLDP----GAARHLTLACHYDSKFFPPglp 180
Cdd:cd05661   27 IGVAGTPEELKAARYIEQQLKSL--GYEVEVQPFTSH---------NVIATKKPdnnkNNNDIIIVTSHYDSVVKAP--- 92

                         90       100
                 ....*....|....*....|..
gi 564326527 181 pfvGATDSAVPCALLLELVQAL 202
Cdd:cd05661   93 ---GANDNASGTAVTLELARVF 111
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 100-334 4.46e-05

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: 44.37  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 100 RPLLIVRPPGSPGNLQVRKFLEATLQSL-------SAGWhveLDPFTASTPLGPldfgNVVATLDPG---AARHLTLACH 169
Cdd:cd05663    6 SDELEGRLTGTKGEKLAADYIAQRFEELglepgldNGTY---FQPFEFTTGTGR----NVIGVLPGKgdvADETVVVGAH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 170 YDSKFF--PPGLPP------FVGATDSAVPCALLLELVQALdvmLSRIKQQAAPVTLQLLFLDGEEAlkewgpkdSLYGS 241
Cdd:cd05663   79 YDHLGYggEGSLARgdesliHNGADDNASGVAAMLELAAKL---VDSDTSLALSRNLVFIAFSGEEL--------GLLGS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 242 RHLAQIMeSIPhspgptrIQAIELFVLLDLLG------------APSPIFFSHFPRTAR--------------------W 289
Cdd:cd05663  148 KHFVKNP-PFP-------IKNTVYMINMDMVGrlrdnklivqgtGTSPGWEQLVQARNKatgfklildptgygpsdhtsF 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564326527 290 FQRlrsiGVPVLHLiampFPAV---WHTPADTEANLHPPTVHNLSRIL 334
Cdd:cd05663  220 YLD----DVPVLHF----FTGAhsdYHRPSDDSDKLNYDGMADIADFA 259
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 151-323 6.78e-04

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: 40.30  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 151 NVVATLDPG--AARHLTLACHYD----------SKFFPpglppfvGATDSAVPCALLLELVQALdvmlsrIKQQAAPVTL 218
Cdd:cd03877    3 NVVGVLEGSdlPDETIVIGAHYDhlgigggdsgDKIYN-------GADDNASGVAAVLELARYF------AKQKTPKRSI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 219 QLLFLDGEEAlkewgpkdSLYGSRHLA--------QI-----MESIPHSPGPTRIQAI-----ELFVLLDLLGAPSPIFF 280
Cdd:cd03877   70 VFAAFTAEEK--------GLLGSKYFAenpkfpldKIvamlnLDMIGRLGRSKDVYLIgsgssELENLLKKANKAAGRVL 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564326527 281 SHFPRTARWFQR-----LRSIGVPVLHLIAMPFPAvWHTPADTEANLH 323
Cdd:cd03877  142 SKDPLPEWGFFRsdhypFAKAGVPALYFFTGLHDD-YHKPSDDYEKID 188
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 106-246 7.82e-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: 40.81  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 106 RPPGSPGNLQVRKFLEATLQSLSAGWHVELDPFTASTPL----GPLDFGNVVATLdPGAAR---HLTLACHYDSkfFPPG 178
Cdd:cd05660   12 RAPGSEGEKKTVDYLAEQFKELGLKPAGSDGSYLQAVPLvskiEYSTSHNVVAIL-PGSKLpdeYIVLSAHWDH--LGIG 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564326527 179 LPP-----FVGATDSAVPCALLLELVQALdvmlsRIKQQAAPVTLQLLFLDGEEAlkewgpkdSLYGSRHLAQ 246
Cdd:cd05660   89 PPIggdeiYNGAVDNASGVAAVLELARVF-----AAQDQRPKRSIVFLAVTAEEK--------GLLGSRYYAA 148
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 103-246 9.61e-04

Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.


Pssm-ID: 349944 [Multi-domain]  Cd Length: 361  Bit Score: 40.75  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 103 LIVRPPGSPGNLQVRKFLEATLQSLsaGWHVELDPFTAStplgpldfGNVVATLDPGAARHLTLACHYDSkfFPPG---- 178
Cdd:cd08659    6 LVQIPSVNPPEAEVAEYLAELLAKR--GYGIESTIVEGR--------GNLVATVGGGDGPVLLLNGHIDT--VPPGdgdk 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564326527 179 --LPPFV-----------GATD--SAVPCallleLVQALDVMLSRIKQQAAPVTlqLLFLDGEEALKEwgpkdslyGSRH 243
Cdd:cd08659   74 wsFPPFSgrirdgrlygrGACDmkGGLAA-----MVAALIELKEAGALLGGRVA--LLATVDEEVGSD--------GARA 138


                 ...
gi 564326527 244 LAQ 246
Cdd:cd08659  139 LLE 141
 
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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