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Conserved domains on  [gi|6912618|ref|NP_036545|]
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glutaminyl-peptide cyclotransferase precursor [Homo sapiens]

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) ...
51-358 0e+00

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: 504.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   51 SALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPT 130
Cdd:cd03880   1 STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTFTNIIATLNPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  131 AKRHLVLACHYDSKYFSHWnnrVFVGATDSAVPCAMMLELARALDKKLLSLKTVSdSKPDLSLQLIFFDGEEAFLHWSPQ 210
Cdd:cd03880  81 AKRYLVLACHYDSKYFPEG---EFIGATDSAVPCAMLLYLARSLDAALTRKWPKS-KKSDLGLQLIFFDGEEAFEEWSDT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  211 DSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLE 290
Cdd:cd03880 157 DSLYGSRHLAAKWESTPYPPGSRYSGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIEKRLRKLGLLESHPSE 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6912618  291 GRYFQNYS-YGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEY 358
Cdd:cd03880 237 RKYFQPHSkYTPDIEDDHIPFLERGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 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) ...
51-358 0e+00

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: 504.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   51 SALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPT 130
Cdd:cd03880   1 STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTFTNIIATLNPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  131 AKRHLVLACHYDSKYFSHWnnrVFVGATDSAVPCAMMLELARALDKKLLSLKTVSdSKPDLSLQLIFFDGEEAFLHWSPQ 210
Cdd:cd03880  81 AKRYLVLACHYDSKYFPEG---EFIGATDSAVPCAMLLYLARSLDAALTRKWPKS-KKSDLGLQLIFFDGEEAFEEWSDT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  211 DSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLE 290
Cdd:cd03880 157 DSLYGSRHLAAKWESTPYPPGSRYSGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIEKRLRKLGLLESHPSE 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6912618  291 GRYFQNYS-YGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEY 358
Cdd:cd03880 237 RKYFQPHSkYTPDIEDDHIPFLERGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
Peptidase_M28 pfam04389
Peptidase family M28;
122-355 1.15e-49

Peptidase family M28;


Pssm-ID: 398200 [Multi-domain]  Cd Length: 192  Bit Score: 165.14  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618    122 NIISTLNPTA-KRHLVLACHYDSKYFShwnnrvfVGATDSAVPCAMMLELARALDKKllslktvsdSKPDLSLQLIFFDG 200
Cdd:pfam04389   1 NVIAKLPGKApDEVVLLSAHYDSVGTG-------PGATDNASGVAALLELARVLAAG---------QRPKRSVRFLFFDA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618    201 EEAflhwspqdSLYGSRHLAAKmastpHPPGARgtsqlhgMDLLVLLDLIGAPNPTFpnffpNSARWFERLQAIEHELHE 280
Cdd:pfam04389  65 EEA--------GLLGSHHFAKS-----HPPLKK-------IRAVINLDMIGSGGPAF-----LFQSGPGGSSLLEKYLKA 119
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6912618    281 LGLLKDHSLEGRYFQNYsyGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFV 355
Cdd:pfam04389 120 AAKPYGRTLAEDPFQER--GGPGRSDHAPFIKAGIPGLDLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
135-361 3.55e-12

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 225143 [Multi-domain]  Cd Length: 435  Bit Score: 67.24  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  135 LVLACHYDSKYFShwnnrvfVGATDSAVPCAMMLELARALdkkllslktvSDSKPDLSLQLIFFDGEEAFLHwspqdsly 214
Cdd:COG2234 211 GLLGAHIDSVPTG-------PGADDNASGVAALLELARVL----------KGNPPKRTVRFVAFGAEESGLL-------- 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  215 GSRHLAAKMAStphppgargtSQLHGMDLLVLLDLIGAPNPT---------FPNFFPNSARwFERLQAIEHelhelgllk 285
Cdd:COG2234 266 GSEAYVKRLSK----------DLDKKIALVINLDMLGSPNPTptlilygngLERVPPGLRA-VAALIGRPV--------- 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  286 DHSLEGRYFqNYSyggviqdDHIPFLRRGVPVLHLIPSPFPEVW-----HTMDDNEEnlDESTIDNLNKIL-QVFVLEYL 359
Cdd:COG2234 326 DPSTVQDFD-PRS-------DHYPFTEAGIPSLFLFSGAPGGVEavawgHTAADTDK--DLSTLDQHGDAVaATLVLDVA 395

                ..
gi 6912618  360 HL 361
Cdd:COG2234 396 AE 397
 
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) ...
51-358 0e+00

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: 504.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   51 SALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPT 130
Cdd:cd03880   1 STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNFIIDFLKSLLAGWTVELDNFTEKTPIGEVTFTNIIATLNPP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  131 AKRHLVLACHYDSKYFSHWnnrVFVGATDSAVPCAMMLELARALDKKLLSLKTVSdSKPDLSLQLIFFDGEEAFLHWSPQ 210
Cdd:cd03880  81 AKRYLVLACHYDSKYFPEG---EFIGATDSAVPCAMLLYLARSLDAALTRKWPKS-KKSDLGLQLIFFDGEEAFEEWSDT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  211 DSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLE 290
Cdd:cd03880 157 DSLYGSRHLAAKWESTPYPPGSRYSGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIEKRLRKLGLLESHPSE 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6912618  291 GRYFQNYS-YGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEY 358
Cdd:cd03880 237 RKYFQPHSkYTPDIEDDHIPFLERGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
120-358 1.01e-51

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: 170.60  E-value: 1.01e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  120 FSNIISTLNPT--AKRHLVLACHYDSKYFShwnnrvfVGATDSAVPCAMMLELARALDKKLLslktvsdsKPDLSLQLIF 197
Cdd:cd02690   1 GYNVIATIKGSdkPDEVILIGAHYDSVPLS-------PGANDNASGVAVLLELARVLSKLQL--------KPKRSIRFAF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  198 FDGEEAFLHwspqdslyGSRHLAAKMASTphppgargtsqLHGMDLLVLLDLIGAPNPT-FPNFFP-NSARWFERLQAIE 275
Cdd:cd02690  66 WDAEELGLL--------GSKYYAEQLLSS-----------LKNIRAALNLDMIGGAGPDlYLQTAPgNDALVEKLLRALA 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  276 HELHELGLlkdhslegrYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSP--FPEVWHTMDDNEENLDESTIDNLNKILQV 353
Cdd:cd02690 127 HELENVVY---------TVVYKEDGGTGGSDHRPFLARGIPAASLIQSEsyNFPYYHTTQDTLENIDKDTLKRAGDILAS 197

                ....*
gi 6912618  354 FVLEY 358
Cdd:cd02690 198 FLYRL 202
Peptidase_M28 pfam04389
Peptidase family M28;
122-355 1.15e-49

Peptidase family M28;


Pssm-ID: 398200 [Multi-domain]  Cd Length: 192  Bit Score: 165.14  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618    122 NIISTLNPTA-KRHLVLACHYDSKYFShwnnrvfVGATDSAVPCAMMLELARALDKKllslktvsdSKPDLSLQLIFFDG 200
Cdd:pfam04389   1 NVIAKLPGKApDEVVLLSAHYDSVGTG-------PGATDNASGVAALLELARVLAAG---------QRPKRSVRFLFFDA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618    201 EEAflhwspqdSLYGSRHLAAKmastpHPPGARgtsqlhgMDLLVLLDLIGAPNPTFpnffpNSARWFERLQAIEHELHE 280
Cdd:pfam04389  65 EEA--------GLLGSHHFAKS-----HPPLKK-------IRAVINLDMIGSGGPAF-----LFQSGPGGSSLLEKYLKA 119
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6912618    281 LGLLKDHSLEGRYFQNYsyGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFV 355
Cdd:pfam04389 120 AAKPYGRTLAEDPFQER--GGPGRSDHAPFIKAGIPGLDLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
M28_like cd08656
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
67-360 2.72e-22

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: 94.90  E-value: 2.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   67 QNDLQPllieRYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSfSNIISTLNPTAKRHLVLACHYDSKYF 146
Cdd:cd08656  11 QVDFGP----RVPNTAAHKACGEYLAGKLEAFGAKVYNQYADLIAYDGTILKA-RNIIGAYNPESKKRVLLCAHWDSRPY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  147 SHWNNR------VFVGATDSAVPCAMMLELARALDKKllslktvsdsKPDLSLQLIFFDGEE----AFLHWSPQDSLY-- 214
Cdd:cd08656  86 ADNDADpkkhhtPILGANDGASGVGALLEIARQIQQQ----------APAIGIDIIFFDAEDygtpEFYEGKYKSDTWcl 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  215 GSRHLAakmaSTPHPPGARGTSQlhgmdllVLLDLIGAPNPTFpNFFPNSARWFERL-QAIEHELHELGLlkdhsleGRY 293
Cdd:cd08656 156 GSQYWA----RNPHVQGYNARYG-------ILLD*VGGKNATF-LKEQYSLRTARDIvKKIWKTAKRLGY-------GKY 216
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6912618  294 FQNYSyGGVIQDDHIPFLR-RGVPVLHLI------PSPFPEVWHTMDDNEENLDESTidnLNKILQVfVLEYLH 360
Cdd:cd08656 217 FVPEA-GGTITDDHLYVNQlARIPTIDIInydperPTGFPSYWHTIQDN*ENIDKET---LKAVGQT-VLEVIY 285
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
72-356 5.85e-13

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: 68.25  E-value: 5.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   72 PLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTL---NPTAKRHLVLACHYD------ 142
Cdd:cd05663   7 DELEGRLTGTKGEKLAADYIAQRFEELGLEPGLDNGTYFQPFEFTTGTGRNVIGVLpgkGDVADETVVVGAHYDhlgygg 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  143 --SKYFSHwNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDskpdlsLQLIFFDGEEAflhwspqdSLYGSRHLA 220
Cdd:cd05663  87 egSLARGD-ESLIHNGADDNASGVAAMLELAAKLVDSDTSLALSRN------LVFIAFSGEEL--------GLLGSKHFV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  221 AKMastPHPPGArgTSQLHGMDLLVLLDligapNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSlegryfqnysyg 300
Cdd:cd05663 152 KNP---PFPIKN--TVYMINMDMVGRLR-----DNKLIVQGTGTSPGWEQLVQARNKATGFKLILDPT------------ 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6912618  301 GVIQDDHIPFLRRGVPVLHLIPSPFPEvWHTMDDNEENLDestIDNLNKILQVFVL 356
Cdd:cd05663 210 GYGPSDHTSFYLDDVPVLHFFTGAHSD-YHRPSDDSDKLN---YDGMADIADFAVR 261
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
135-361 3.55e-12

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 225143 [Multi-domain]  Cd Length: 435  Bit Score: 67.24  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  135 LVLACHYDSKYFShwnnrvfVGATDSAVPCAMMLELARALdkkllslktvSDSKPDLSLQLIFFDGEEAFLHwspqdsly 214
Cdd:COG2234 211 GLLGAHIDSVPTG-------PGADDNASGVAALLELARVL----------KGNPPKRTVRFVAFGAEESGLL-------- 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  215 GSRHLAAKMAStphppgargtSQLHGMDLLVLLDLIGAPNPT---------FPNFFPNSARwFERLQAIEHelhelgllk 285
Cdd:COG2234 266 GSEAYVKRLSK----------DLDKKIALVINLDMLGSPNPTptlilygngLERVPPGLRA-VAALIGRPV--------- 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  286 DHSLEGRYFqNYSyggviqdDHIPFLRRGVPVLHLIPSPFPEVW-----HTMDDNEEnlDESTIDNLNKIL-QVFVLEYL 359
Cdd:COG2234 326 DPSTVQDFD-PRS-------DHYPFTEAGIPSLFLFSGAPGGVEavawgHTAADTDK--DLSTLDQHGDAVaATLVLDVA 395

                ..
gi 6912618  360 HL 361
Cdd:COG2234 396 AE 397
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
67-211 2.07e-11

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: 64.15  E-value: 2.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   67 QNDLQpLLIERYP---GSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYG--------------YRSFSNIISTLNP 129
Cdd:cd03875  10 WEDLQ-VLISIGPhpyGSHNNDKVRDYLLARVEEIKERANANGLEVEVQDDTGsgsfnflssgmtlvYFEVTNIVVRISG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  130 T---AKRHLVLACHYDSKYFSHwnnrvfvGATDSAVPCAMMLELARALdkkllslkTVSDSKPDLSLQLIFFDGEEAFL- 205
Cdd:cd03875  89 KnsnSLPALLLNAHFDSVPTSP-------GATDDGMGVAVMLEVLRYL--------SKSGHQPKRDIIFLFNGAEENGLl 153
                       170
                ....*....|....
gi 6912618  206 --------HWSPQD 211
Cdd:cd03875 154 gahafitqHPWAKN 167
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
77-318 2.22e-11

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: 63.53  E-value: 2.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   77 RYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLS----QTPYGYRSFSNIISTLnPTAKR---HLVLACHYD--SKYFS 147
Cdd:cd05660  12 RAPGSEGEKKTVDYLAEQFKELGLKPAGSDGSYLQavplVSKIEYSTSHNVVAIL-PGSKLpdeYIVLSAHWDhlGIGPP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  148 HWNNRVFVGATDSAVPCAMMLELARALDKkllslktvSDSKPDLSLQLIFFDGEEAFLHwspqdslyGSRHLAAkmastp 227
Cdd:cd05660  91 IGGDEIYNGAVDNASGVAAVLELARVFAA--------QDQRPKRSIVFLAVTAEEKGLL--------GSRYYAA------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  228 HPPGArgtsqlhgMDLLVL---LDLIGAPNPTfpnffpnsaRWFERLQAIEHELHELglLKDHSleGRYFQNYSY----- 299
Cdd:cd05660 149 NPIFP--------LDKIVAnlnIDMIGRIGPT---------KDVLLIGSGSSELENI--LKEAA--KAVGRVVDYdpnpe 207
                       250       260
                ....*....|....*....|
gi 6912618  300 -GGVIQDDHIPFLRRGVPVL 318
Cdd:cd05660 208 nGSFYRSDHYNFAKKGVPVL 227
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
77-354 3.37e-10

M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain.


Pssm-ID: 349912 [Multi-domain]  Cd Length: 268  Bit Score: 59.79  E-value: 3.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   77 RYPGSPGSYAARQHIMQRIQRLQ-ADWVleiDTFlsQTPYGYRSF------SNIISTL---NPTAKrHLVLACHYDskYF 146
Cdd:cd05662  17 RKTGTKGAAKTRAYIIERFKQIGlLPWG---DRF--EHPFSYTKRfstrqgVNVLAVIkgsEPPTK-WRVVSAHYD--HL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  147 SHWNNRVFVGATDSAVPCAMMLELARALDKKllslktvsdsKPDLSLQLIFFDGEEAflhwspqdSLYGSRHLAAKMast 226
Cdd:cd05662  89 GIRGGKIYNGADDNASGVAALLALAEYFKKH----------PPKHNVIFAATDAEEP--------GLRGSYAFVEAL--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  227 phppgargTSQLHGMDLLVLLDLIGapNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLE-GRYFQNYSYggVIQD 305
Cdd:cd05662 148 --------KVPRAQIELNINLDMIS--RPERNELYVEGASQFPQLTSILENVKGTCIKALHPKDtDGSIGSIDW--TRAS 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6912618  306 DHIPFLRRGVPVLHLIPSPFPEvWHTMDDNEENLDESTIDNLNK-ILQVF 354
Cdd:cd05662 216 DHYPFHKAKIPWLYFGVEDHPD-YHKPTDDFETIDQEFFAAVVEsAVQLF 264
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
121-355 7.20e-10

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: 58.02  E-value: 7.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  121 SNIISTL--NPTAKRHLVLACHYDskyfsH-------WNNRVFVGATDSAVPCAMMLELARALDKKLlslktvsdsKPDL 191
Cdd:cd03877   2 HNVVGVLegSDLPDETIVIGAHYD-----HlgigggdSGDKIYNGADDNASGVAAVLELARYFAKQK---------TPKR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  192 SLQLIFFDGEEAflhwspqdSLYGSRHLAAK---------------MASTPHPPGArgtsqlhgmdllvlLDLIGAPNPT 256
Cdd:cd03877  68 SIVFAAFTAEEK--------GLLGSKYFAENpkfpldkivamlnldMIGRLGRSKD--------------VYLIGSGSSE 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  257 FPNFFPNSARWFERlqaiehelhelGLLKDHSLEGRYFQNysyggviqdDHIPFLRRGVPVLHLIPSPFPEvWHTMDDNE 336
Cdd:cd03877 126 LENLLKKANKAAGR-----------VLSKDPLPEWGFFRS---------DHYPFAKAGVPALYFFTGLHDD-YHKPSDDY 184
                       250       260
                ....*....|....*....|
gi 6912618  337 ENLD-ESTIDNLNKILQVFV 355
Cdd:cd03877 185 EKIDyEGMARVVNLIYQLLR 204
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
77-357 1.44e-09

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: 57.97  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   77 RYPGSPGSYAARQHIMQRIQRLQADwvLEIDTFLSQtpygyrsfsNIISTLNPTAKRH----LVLACHYDSKYFSHwnnr 152
Cdd:cd05661  28 GVAGTPEELKAARYIEQQLKSLGYE--VEVQPFTSH---------NVIATKKPDNNKNnndiIIVTSHYDSVVKAP---- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  153 vfvGATDSAVPCAMMLELARALdkkllslktvSDSKPDLSLQLIFFDGEEAflhwspqdSLYGSRHLAAKMAStphppga 232
Cdd:cd05661  93 ---GANDNASGTAVTLELARVF----------KKVKTDKELRFIAFGAEEN--------GLLGSKYYVASLSE------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  233 rgtSQLHGMDLLVLLDLIGAPNPTFPNFFPNSarwferLQAIEHELHELGLLKDHSLEGryfqNYSYGGVIQDDHIPFLR 312
Cdd:cd05661 145 ---DEIKRTIGVFNLDMVGTSDAKAGDLYAYT------IDGKPNLVTDSGAAASKRLSG----VLPLVQQGSSDHVPFHE 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6912618  313 RGVPV---LHLIPSPFP--EVWHTMDDNEENLDESTIDNLNKILQVFVLE 357
Cdd:cd05661 212 AGIPAalfIHMDPETEPvePWYHTPNDTVENISKERLDNALDIVGTAVYQ 261
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
78-353 1.25e-04

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: 43.21  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618   78 YPGSPGSYAARQHIMQriqrlqaDWVLEIDTFLSQTPYGYRS-FSNIISTLNPTAKRH--LVLACHYDSKYFSHwnnrvf 154
Cdd:cd05640  16 HDPSAFLAAAAEYIAQ-------ELVGSGYNVTSHFFSHQEGvYANLIADLPGSYSQDklILIGAHYDTVPGSP------ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  155 vGATDSAVPCAMMLELARALdkkllslktvSDSKPDLSLQLIFFDGEEAFLHWSpqdSLYGSRHLAAKMastphppgARG 234
Cdd:cd05640  83 -GADDNASGVAALLELARLL----------ATLDPNHTLRFVAFDLEEYPFFAR---GLMGSHAYAEDL--------LRP 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912618  235 TSQLHGMdllVLLDLIGAPNPtfpnfFPNSARWFERLQAIEHE-----LHELGLLKDHSLEGRYFQNYSYG--------- 300
Cdd:cd05640 141 LTPIVGM---LSLEMIGYYDP-----FPHSQAYPAGFELHFYPhmgdfIAVVGRLRSRKLVRAFKRAFRMLsdfpvesln 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6912618  301 ---------GVIQDDHIPFLRRGVPVLHLIPSPFPEV--WHTMDDNEENLdestidNLNKILQV 353
Cdd:cd05640 213 lpfngpgvpPFRRSDHSSFWDHGYPAIMVTDTAFYRNpqYHLPCDTPDTL------NYKFLTRV 270
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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