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Conserved domains on  [gi|254281335|ref|NP_001156849|]
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glutaminyl-peptide cyclotransferase-like protein isoform 2 [Homo sapiens]

Protein Classification

zinc-binding metallopeptidase family protein( domain architecture ID 56613)

zinc-binding metallopeptidase family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zinc_peptidase_like super family cl14876
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 79-285 1.20e-100

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).


The actual alignment was detected with superfamily member cd03880:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 305  Bit Score: 296.84  E-value: 1.20e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  79 ARLRRVVGQLDPQRLWSTYLRPLLVVRTPGSPGNLQVRK----------------------------------------- 117
Cdd:cd03880    1 STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNfiidflksllagwtveldnftektpigevtftniiatlnpp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 118 ---------------------------AAP--------------------------VTLQLLFLDGEEALKEWGPKDSLY 144
Cdd:cd03880   81 akrylvlachydskyfpegefigatdsAVPcamllylarsldaaltrkwpkskksdLGLQLIFFDGEEAFEEWSDTDSLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 145 GSRHLAQLMESIPHSPG---PTRIQAIELFMLLDLLGAPNPTFYSHFPRTVRWFHRLRSIEKRLHRLNLLQSHPQEVMYF 221
Cdd:cd03880  161 GSRHLAAKWESTPYPPGsrySGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIEKRLRKLGLLESHPSERKYF 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254281335 222 QPGEPFG-SVEDDHIPFLRRGVPVLHLISTPFPAVWHTPADTEVNLHPPTVHNLCRILAVFLAEY 285
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) ...
 79-285 1.20e-100

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: 296.84  E-value: 1.20e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  79 ARLRRVVGQLDPQRLWSTYLRPLLVVRTPGSPGNLQVRK----------------------------------------- 117
Cdd:cd03880    1 STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNfiidflksllagwtveldnftektpigevtftniiatlnpp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 118 ---------------------------AAP--------------------------VTLQLLFLDGEEALKEWGPKDSLY 144
Cdd:cd03880   81 akrylvlachydskyfpegefigatdsAVPcamllylarsldaaltrkwpkskksdLGLQLIFFDGEEAFEEWSDTDSLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 145 GSRHLAQLMESIPHSPG---PTRIQAIELFMLLDLLGAPNPTFYSHFPRTVRWFHRLRSIEKRLHRLNLLQSHPQEVMYF 221
Cdd:cd03880  161 GSRHLAAKWESTPYPPGsrySGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIEKRLRKLGLLESHPSERKYF 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254281335 222 QPGEPFG-SVEDDHIPFLRRGVPVLHLISTPFPAVWHTPADTEVNLHPPTVHNLCRILAVFLAEY 285
Cdd:cd03880  241 QPHSKYTpDIEDDHIPFLERGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
Peptidase_M28 pfam04389
Peptidase family M28;
120-282 6.63e-30

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 111.61  E-value: 6.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  120 PVTLQLLFLDGEEAlkewgpkdSLYGSRHLAQLmesipHSPGptriQAIELFMLLDLLGAPNPTFYSHFPRTVRWfhrlr 199
Cdd:pfam04389  54 KRSVRFLFFDAEEA--------GLLGSHHFAKS-----HPPL----KKIRAVINLDMIGSGGPALLFQSGPKGSS----- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  200 SIEKRLHRLNLLQSHPQEVMYFQPGEPFGsvEDDHIPFLRRGVPVLHLISTPFPAVWHTPADTEVNLHPPTVHNLCRILA 279
Cdd:pfam04389 112 LLEKYLKAAAKPYGVTLAEDPFQERGGPG--RSDHAPFIKAGIPGLDLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVL 189


                  ...
gi 254281335  280 VFL 282
Cdd:pfam04389 190 ALV 192
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 122-285 1.37e-11

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: 63.23  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 122 TLQLLFLDGEEalkeWGpkdsLYGSRHLAQLMesiphspgPTRIQAIELFMLLDLLGAPNPTFYSHFPrTVRWFHRLRsi 201
Cdd:COG2234  106 TIRFVAFGAEE----QG----LLGSRYYAENL--------KAPLEKIVAVLNLDMIGRGGPRNYLYVD-GDGGSPELA-- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 202 eKRLHRLNLLQSHPQEVMYFQPGEPFGSveDDHIPFLRRGVPVLHLISTPFP--AVWHTPADTEVNLHPPTVHNLCRILA 279
Cdd:COG2234  167 -DLLEAAAKAYLPGLGVDPPEETGGYGR--SDHAPFAKAGIPALFLFTGAEDyhPDYHTPSDTLDKIDLDALAKVAQLLA 243


                 ....*.
gi 254281335 280 VFLAEY 285
Cdd:COG2234  244 ALVYEL 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) ...
 79-285 1.20e-100

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: 296.84  E-value: 1.20e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  79 ARLRRVVGQLDPQRLWSTYLRPLLVVRTPGSPGNLQVRK----------------------------------------- 117
Cdd:cd03880    1 STLRHLPELSDDNEHFNNLLAPILIPRVPGSPGHREVRNfiidflksllagwtveldnftektpigevtftniiatlnpp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 118 ---------------------------AAP--------------------------VTLQLLFLDGEEALKEWGPKDSLY 144
Cdd:cd03880   81 akrylvlachydskyfpegefigatdsAVPcamllylarsldaaltrkwpkskksdLGLQLIFFDGEEAFEEWSDTDSLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 145 GSRHLAQLMESIPHSPG---PTRIQAIELFMLLDLLGAPNPTFYSHFPRTVRWFHRLRSIEKRLHRLNLLQSHPQEVMYF 221
Cdd:cd03880  161 GSRHLAAKWESTPYPPGsrySGRLDRIDLLVLLDLLGAPNPTFPSYFPNTHGWYKRLADIEKRLRKLGLLESHPSERKYF 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254281335 222 QPGEPFG-SVEDDHIPFLRRGVPVLHLISTPFPAVWHTPADTEVNLHPPTVHNLCRILAVFLAEY 285
Cdd:cd03880  241 QPHSKYTpDIEDDHIPFLERGVPVLHLIPSPFPSVWHTLDDDEENLDYPTIRNWNKILRVFVAEY 305
Peptidase_M28 pfam04389
Peptidase family M28;
120-282 6.63e-30

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 111.61  E-value: 6.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  120 PVTLQLLFLDGEEAlkewgpkdSLYGSRHLAQLmesipHSPGptriQAIELFMLLDLLGAPNPTFYSHFPRTVRWfhrlr 199
Cdd:pfam04389  54 KRSVRFLFFDAEEA--------GLLGSHHFAKS-----HPPL----KKIRAVINLDMIGSGGPALLFQSGPKGSS----- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335  200 SIEKRLHRLNLLQSHPQEVMYFQPGEPFGsvEDDHIPFLRRGVPVLHLISTPFPAVWHTPADTEVNLHPPTVHNLCRILA 279
Cdd:pfam04389 112 LLEKYLKAAAKPYGVTLAEDPFQERGGPG--RSDHAPFIKAGIPGLDLAFTDFGYRYHTPADTIDNIDPGTLQRIGDLVL 189


                  ...
gi 254281335  280 VFL 282
Cdd:pfam04389 190 ALV 192
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 122-282 2.79e-17

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: 78.15  E-value: 2.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 122 TLQLLFLDGEEalkeWGpkdsLYGSRHLAQLMESiphspgptRIQAIELFMLLDLLGAPNPTFYSHFPRTVRWfhrlrSI 201
Cdd:cd02690   60 SIRFAFWDAEE----LG----LLGSKYYAEQLLS--------SLKNIRAALNLDMIGGAGPDLYLQTAPGNDA-----LV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 202 EKRLHRLNLLQSHPqeVMYFQPGEPFGSVEDDHIPFLRRGVPVLHLISTP--FPAVWHTPADTEVNLHPPTVHNLCRILA 279
Cdd:cd02690  119 EKLLRALAHELENV--VYTVVYKEDGGTGGSDHRPFLARGIPAASLIQSEsyNFPYYHTTQDTLENIDKDTLKRAGDILA 196


                 ...
gi 254281335 280 VFL 282
Cdd:cd02690  197 SFL 199
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 122-285 1.37e-11

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: 63.23  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 122 TLQLLFLDGEEalkeWGpkdsLYGSRHLAQLMesiphspgPTRIQAIELFMLLDLLGAPNPTFYSHFPrTVRWFHRLRsi 201
Cdd:COG2234  106 TIRFVAFGAEE----QG----LLGSRYYAENL--------KAPLEKIVAVLNLDMIGRGGPRNYLYVD-GDGGSPELA-- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 202 eKRLHRLNLLQSHPQEVMYFQPGEPFGSveDDHIPFLRRGVPVLHLISTPFP--AVWHTPADTEVNLHPPTVHNLCRILA 279
Cdd:COG2234  167 -DLLEAAAKAYLPGLGVDPPEETGGYGR--SDHAPFAKAGIPALFLFTGAEDyhPDYHTPSDTLDKIDLDALAKVAQLLA 243


                 ....*.
gi 254281335 280 VFLAEY 285
Cdd:COG2234  244 ALVYEL 249
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 125-267 3.86e-05

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: 43.77  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 125 LLFLDGEEAlkewgpkdSLYGSRHLAQLMesiphspgPTRIQAIELFMLLDLLGAPNP--TFYSHFPRTVRWFHRLRSIE 202
Cdd:cd03877   71 FAAFTAEEK--------GLLGSKYFAENP--------KFPLDKIVAMLNLDMIGRLGRskDVYLIGSGSSELENLLKKAN 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254281335 203 KRLHRLNLLQSHPQEVMYfqpgepfgsvEDDHIPFLRRGVPVLHLiSTPFPAVWHTPADTEVNLH 267
Cdd:cd03877  135 KAAGRVLSKDPLPEWGFF----------RSDHYPFAKAGVPALYF-FTGLHDDYHKPSDDYEKID 188
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 132-268 1.32e-04

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


Pssm-ID: 349912 [Multi-domain]  Cd Length: 268  Bit Score: 42.45  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 132 EALKEWGPKDS------------LYGSRHLAQLMesiphspgPTRIQAIELFMLLDLLGAPN-PTFY----SHFPRtvrw 194
Cdd:cd05662  114 EYFKKHPPKHNvifaatdaeepgLRGSYAFVEAL--------KVPRAQIELNINLDMISRPErNELYvegaSQFPQ---- 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254281335 195 fhrLRSIEKRLHRLNLLQSHPQEVmyfqpGEPFGSVE----DDHIPFLRRGVPVLHLISTPFPAvWHTPADTEVNLHP 268
Cdd:cd05662  182 ---LTSILENVKGTCIKALHPKDT-----DGSIGSIDwtraSDHYPFHKAKIPWLYFGVEDHPD-YHKPTDDFETIDQ 250
M28_like cd08656
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 114-266 2.71e-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: 349943 [Multi-domain]  Cd Length: 287  Bit Score: 41.74  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 114 QVRKAAP-VTLQLLFLDGEE-ALKEWGPKDSLYGSRHL-AQLMESIPHSPGPTRIQAIelfmLLDLLGAPNPTFY--SHF 188
Cdd:cd08656  118 QIQQQAPaIGIDIIFFDAEDyGTPEFYEGKYKSDTWCLgSQYWARNPHVQGYNARYGI----LLD*VGGKNATFLkeQYS 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281335 189 PRTVRwfHRLRSIEKRLHRLNLLQshpqevmYFQPgEPFGSVEDDHIPFLR-RGVPVLHLIS------TPFPAVWHTPAD 261
Cdd:cd08656  194 LRTAR--DIVKKIWKTAKRLGYGK-------YFVP-EAGGTITDDHLYVNQlARIPTIDIINydperpTGFPSYWHTIQD 263


                 ....*
gi 254281335 262 TEVNL 266
Cdd:cd08656  264 N*ENI 268
 
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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