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Conserved domains on  [gi|1063693938|ref|NP_001320618|]
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cell wall / vacuolar inhibitor of fructosidase 1 [Arabidopsis thaliana]

Protein Classification

CIF_like domain-containing protein( domain architecture ID 10204982)

CIF_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 24-165 9.97e-48

Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are secreted apoplastic enzymes belonging to the glycoside hydrolase family 32 (EC 3.2.1.26) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. Their activity is tightly regulated by compartment-specific inhibitor proteins at transcriptional and post-transcriptional levels. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity). Interaction of invertase inhibitor Nt-CIF (Nicotiana tabacum cell-wall inhibitor of beta-fructosidase) with CWI is strictly pH-dependent, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.


:

Pssm-ID: 275440 [Multi-domain]  Cd Length: 148  Bit Score: 151.75  E-value: 9.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPR-GSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKTI 100
Cdd:cd15796     2 DLIDETCKKTPNYDLCVSILRSDPRsTTAADVKGLALIMLDAVLAKANDTLRKIGELLKKTtdPALKRALSSCAEEYGVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063693938 101 LNADVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG--SSPLTSLTKSMQKISNVTRAIVRML 165
Cdd:cd15796    82 VEDDLPQAIEALKKGDYKAAKDSMYDAGKEADSCEEQFKGssSSPLTDRNKAVHDLAVVAAAIVRQL 148
 
Name Accession Description Interval E-value
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 24-165 9.97e-48

Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are secreted apoplastic enzymes belonging to the glycoside hydrolase family 32 (EC 3.2.1.26) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. Their activity is tightly regulated by compartment-specific inhibitor proteins at transcriptional and post-transcriptional levels. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity). Interaction of invertase inhibitor Nt-CIF (Nicotiana tabacum cell-wall inhibitor of beta-fructosidase) with CWI is strictly pH-dependent, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.


Pssm-ID: 275440 [Multi-domain]  Cd Length: 148  Bit Score: 151.75  E-value: 9.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPR-GSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKTI 100
Cdd:cd15796     2 DLIDETCKKTPNYDLCVSILRSDPRsTTAADVKGLALIMLDAVLAKANDTLRKIGELLKKTtdPALKRALSSCAEEYGVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063693938 101 LNADVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG--SSPLTSLTKSMQKISNVTRAIVRML 165
Cdd:cd15796    82 VEDDLPQAIEALKKGDYKAAKDSMYDAGKEADSCEEQFKGssSSPLTDRNKAVHDLAVVAAAIVRQL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-161 4.27e-21

Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences, suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.


Pssm-ID: 214860 [Multi-domain]  Cd Length: 148  Bit Score: 83.57  E-value: 4.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938   24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKTIL 101
Cdd:smart00856   5 KLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTkdPRLKAALKDCLELYDDAV 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063693938  102 NaDVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG-----SSPLTSLTKSMQKISNVTRAI 161
Cdd:smart00856  85 D-SLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEEnddkvKSPLTKRNDNLEKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 24-166 1.45e-20

pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, characterized by four conserved Cys residues, shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this model followed immediately by a pectinesterase domain, pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family.


Pssm-ID: 273717 [Multi-domain]  Cd Length: 178  Bit Score: 83.24  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKtIL 101
Cdd:TIGR01614  30 SLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTKgdPRDKSALEDCVELYS-DA 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938 102 NADVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNGS-----SPLTSLTKSMQKISNVTRAIVRMLL 166
Cdd:TIGR01614 109 VDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELggivkSPLTKRNNNVKKLSSITLAIIKMLT 178
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-161 1.61e-12

Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences (personal obs:C Yeats), suggesting that both PMEs and their inhibitor are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.


Pssm-ID: 461143 [Multi-domain]  Cd Length: 148  Bit Score: 61.41  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKKRPEL---KRALDECSRRYKTI 100
Cdd:pfam04043   1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSakdKAALEDCLELYDDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063693938 101 LNaDVPEAIEAISKGVPKFG--EDGVIDAGVEASVCQGGFNG------SSPLTSLTKSMQKISNVTRAI 161
Cdd:pfam04043  81 VD-ELNRALDALKAGDSSRDdaQTWLSAALTNQDTCEDGFKEavkgqlKSSMKSPLRNLTKLTSNALAI 148
 
Name Accession Description Interval E-value
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 24-165 9.97e-48

Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are secreted apoplastic enzymes belonging to the glycoside hydrolase family 32 (EC 3.2.1.26) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. Their activity is tightly regulated by compartment-specific inhibitor proteins at transcriptional and post-transcriptional levels. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity). Interaction of invertase inhibitor Nt-CIF (Nicotiana tabacum cell-wall inhibitor of beta-fructosidase) with CWI is strictly pH-dependent, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.


Pssm-ID: 275440 [Multi-domain]  Cd Length: 148  Bit Score: 151.75  E-value: 9.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPR-GSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKTI 100
Cdd:cd15796     2 DLIDETCKKTPNYDLCVSILRSDPRsTTAADVKGLALIMLDAVLAKANDTLRKIGELLKKTtdPALKRALSSCAEEYGVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063693938 101 LNADVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG--SSPLTSLTKSMQKISNVTRAIVRML 165
Cdd:cd15796    82 VEDDLPQAIEALKKGDYKAAKDSMYDAGKEADSCEEQFKGssSSPLTDRNKAVHDLAVVAAAIVRQL 148
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 24-165 3.21e-26

Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context.


Pssm-ID: 275441 [Multi-domain]  Cd Length: 149  Bit Score: 97.11  E-value: 3.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKK--RPELKRALDECSRRYKTIL 101
Cdd:cd15797     3 ELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSttDPKLKNRYESCSKNYNDAI 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063693938 102 NAdVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG----SSPLTSLTKSMQKISNVTRAIVRML 165
Cdd:cd15797    83 DA-LEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSKppkdPSPLAKYNRDVEDLCDIILVISDLL 149
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 30-164 2.20e-22

pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context. CIF (cell-wall inhibitor of beta-fructosidase from tobacco) is structurally similar to PMEI and these members are also included in this model. Comparison of the CIF/INV1 structure with the complex between PMEI/PME suggests a common targeting mechanism in PMEI and CIF. However, CIF and PMEI use distinct surface areas to selectively inhibit very different enzymatic scaffolds.


Pssm-ID: 275438 [Multi-domain]  Cd Length: 140  Bit Score: 86.72  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  30 CKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYK--KRPELKRALDECSRRYKTILNaDVPE 107
Cdd:cd14859     1 CKKTSYYKLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFIAKLLKstKDPALKKALRDCADDYDDAVD-DLED 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063693938 108 AIEAISKGVPKFGEDGVIDAGVEASVCQGGFNGS----SPLTSLTKSMQKISNVTRAIVRM 164
Cdd:cd14859    80 AINALLSGDYDDAKTHVSAALDDADTCEEAFKESsglpSPLTTRNDDLKRLCSIALAIILL 140
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-161 4.27e-21

Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences, suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.


Pssm-ID: 214860 [Multi-domain]  Cd Length: 148  Bit Score: 83.57  E-value: 4.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938   24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKTIL 101
Cdd:smart00856   5 KLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTkdPRLKAALKDCLELYDDAV 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063693938  102 NaDVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG-----SSPLTSLTKSMQKISNVTRAI 161
Cdd:smart00856  85 D-SLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEEnddkvKSPLTKRNDNLEKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 24-166 1.45e-20

pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, characterized by four conserved Cys residues, shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this model followed immediately by a pectinesterase domain, pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family.


Pssm-ID: 273717 [Multi-domain]  Cd Length: 178  Bit Score: 83.24  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKKR--PELKRALDECSRRYKtIL 101
Cdd:TIGR01614  30 SLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTKgdPRDKSALEDCVELYS-DA 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938 102 NADVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNGS-----SPLTSLTKSMQKISNVTRAIVRMLL 166
Cdd:TIGR01614 109 VDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELggivkSPLTKRNNNVKKLSSITLAIIKMLT 178
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 25-165 6.60e-16

Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.


Pssm-ID: 275445 [Multi-domain]  Cd Length: 146  Bit Score: 70.05  E-value: 6.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  25 IIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYK--KRPELKRALDECSRRYKTILn 102
Cdd:cd15801     1 LIEEACKKTLDPDLCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSELLNtaKDPYVQQCLEDCSENYEDAV- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063693938 103 ADVPEAIEAISKGvpKFGE--DGVIDAGVEASVCQGGF----NGSSPLTSLTKSMQKISNVTRAIVRML 165
Cdd:cd15801    80 EQLNDSLAALDSK--AYGDvkTWVTAALADAETCEDAFkekpGDKSPLTARNGDFSKLCSIALAIIKLL 146
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 30-164 1.06e-13

Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen allergen Pla a 1 belongs to a class of allergens related to proteinaceous invertase and pectin methylesterase inhibitors. Platanus acerifolia is an important cause of pollinosis; Pla a 1 has a prevalence of about 80% among plane tree pollen-allergic patients. Recombinant Pla a 1 binds IgE in vitro, similar to its natural counterpart, rendering it suitable for specific diagnosis and structural studies. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity).


Pssm-ID: 275439 [Multi-domain]  Cd Length: 148  Bit Score: 64.69  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  30 CKETPDFNLCVSLLNSDPRGSS-ADTSGLALI----LIDKikglATKTLNEINGLYKKR---PELKRALDECSRRYKTIL 101
Cdd:cd15795     7 GDPNVDYDFCVSSLQSDPRSRTaADLKGLAVIatklAIAN----ATATKAKIEKLLKSKkypSDLKKALRDCLSLYSDAV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063693938 102 NAdVPEAIEAISKGVPKFGEDGVIDAGVEASVCQGGFNG----SSPLTSLTKSMQKISNVTRAIVRM 164
Cdd:cd15795    83 DS-LKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEakivVSPLTKENDELFQLALIALAITSM 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-161 1.61e-12

Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences (personal obs:C Yeats), suggesting that both PMEs and their inhibitor are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.


Pssm-ID: 461143 [Multi-domain]  Cd Length: 148  Bit Score: 61.41  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063693938  24 SIIEPTCKETPDFNLCVSLLNSDPRGSSADTSGLALILIDKIKGLATKTLNEINGLYKKRPEL---KRALDECSRRYKTI 100
Cdd:pfam04043   1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSakdKAALEDCLELYDDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063693938 101 LNaDVPEAIEAISKGVPKFG--EDGVIDAGVEASVCQGGFNG------SSPLTSLTKSMQKISNVTRAI 161
Cdd:pfam04043  81 VD-ELNRALDALKAGDSSRDdaQTWLSAALTNQDTCEDGFKEavkgqlKSSMKSPLRNLTKLTSNALAI 148
 
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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