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Conserved domains on  [gi|79313133|ref|NP_001030646|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

PMEI domain-containing protein( domain architecture ID 10204984)

PMEI domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 39-190 2.95e-35

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: 120.99  E-value: 2.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  39 TKELINNFCSnlEMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGkDQQLKGSYESCVAS 118
Cdd:cd15797   1 TEELIDTICK--KTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTT-DPKLKNRYESCSKN 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313133 119 YGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNEPPLVFNRVENFANMCYVTWSFGSLI 190
Cdd:cd15797  78 YNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSKPPKDPSPLAKYNRDVEDLCDIILVISDLL 149
 
Name Accession Description Interval E-value
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 39-190 2.95e-35

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: 120.99  E-value: 2.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  39 TKELINNFCSnlEMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGkDQQLKGSYESCVAS 118
Cdd:cd15797   1 TEELIDTICK--KTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTT-DPKLKNRYESCSKN 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313133 119 YGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNEPPLVFNRVENFANMCYVTWSFGSLI 190
Cdd:cd15797  78 YNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSKPPKDPSPLAKYNRDVEDLCDIILVISDLL 149
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 38-186 6.70e-23

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: 89.35  E-value: 6.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133     38 VTKELINNFCSNleMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSgKDQQLKGSYESCVA 117
Cdd:smart00856   2 PTSKLIDSICKS--TDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKT-KDPRLKAALKDCLE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133    118 SYGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEG-PSNEPPLVFNRVENFANMCYVTWSF 186
Cdd:smart00856  79 LYDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEEnDDKVKSPLTKRNDNLEKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 27-183 2.80e-14

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: 67.44  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133    27 PSSSSLSFKDIVTKELINNFCSNLEmfDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGkDQ 106
Cdd:TIGR01614  16 LVATSSSNSLNATQSLIKRICKKTE--YPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTKG-DP 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79313133   107 QLKGSYESCVASYGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNE-PPLVFNRVENFANMCYVT 183
Cdd:TIGR01614  93 RDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGIvKSPLTKRNNNVKKLSSIT 170
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 41-180 6.24e-10

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: 55.25  E-value: 6.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133    41 ELINNFCSNleMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGKDQQLKGSYESCVASYG 120
Cdd:pfam04043   1 SLIKTACKK--TPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79313133   121 QAIKELEKAQKFLSSNSFTQ--ALVAISDAFYKAGDCKDAFEGPSNEPPL--VFNRVENFANMC 180
Cdd:pfam04043  79 DAVDELNRALDALKAGDSSRddAQTWLSAALTNQDTCEDGFKEAVKGQLKssMKSPLRNLTKLT 142
 
Name Accession Description Interval E-value
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 39-190 2.95e-35

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: 120.99  E-value: 2.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  39 TKELINNFCSnlEMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGkDQQLKGSYESCVAS 118
Cdd:cd15797   1 TEELIDTICK--KTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTT-DPKLKNRYESCSKN 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79313133 119 YGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNEPPLVFNRVENFANMCYVTWSFGSLI 190
Cdd:cd15797  78 YNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSKPPKDPSPLAKYNRDVEDLCDIILVISDLL 149
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 38-186 6.70e-23

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: 89.35  E-value: 6.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133     38 VTKELINNFCSNleMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSgKDQQLKGSYESCVA 117
Cdd:smart00856   2 PTSKLIDSICKS--TDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKT-KDPRLKAALKDCLE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133    118 SYGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEG-PSNEPPLVFNRVENFANMCYVTWSF 186
Cdd:smart00856  79 LYDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEEnDDKVKSPLTKRNDNLEKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 27-183 2.80e-14

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: 67.44  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133    27 PSSSSLSFKDIVTKELINNFCSNLEmfDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGkDQ 106
Cdd:TIGR01614  16 LVATSSSNSLNATQSLIKRICKKTE--YPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTKG-DP 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79313133   107 QLKGSYESCVASYGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNE-PPLVFNRVENFANMCYVT 183
Cdd:TIGR01614  93 RDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGIvKSPLTKRNNNVKKLSSIT 170
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 41-180 6.24e-10

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: 55.25  E-value: 6.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133    41 ELINNFCSNleMFDRQFCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSSGKDQQLKGSYESCVASYG 120
Cdd:pfam04043   1 SLIKTACKK--TPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79313133   121 QAIKELEKAQKFLSSNSFTQ--ALVAISDAFYKAGDCKDAFEGPSNEPPL--VFNRVENFANMC 180
Cdd:pfam04043  79 DAVDELNRALDALKAGDSSRddAQTWLSAALTNQDTCEDGFKEAVKGQLKssMKSPLRNLTKLT 142
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 54-181 1.52e-09

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: 53.97  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  54 DRQFCAKWFNADQKTKSISVQG--FISLRVkeTREFGLQTQALMSKLAKSSgKDQQLKGSYESCVASYGQAIKELEKAQK 131
Cdd:cd14859   6 YYKLCVSSLSSDPRSSTADLKGlaNIALDA--ALANASDTQAFIAKLLKST-KDPALKKALRDCADDYDDAVDDLEDAIN 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 79313133 132 FLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNEPPLV---FNRVENFANMCY 181
Cdd:cd14859  83 ALLSGDYDDAKTHVSAALDDADTCEEAFKESSGLPSPLttrNDDLKRLCSIAL 135
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 81-168 5.32e-07

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: 275444 [Multi-domain]  Cd Length: 148  Bit Score: 46.97  E-value: 5.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  81 VKETREFGLQTQALMSKLAKSSGKDQQLKGSYESCVASYGQAIKELEKAQKFLSSNSFTQALVAISDAFYKAGDCKDAFE 160
Cdd:cd15800  40 IKALIAKTKQAKALAKKLAKSPSTSPEVKSALDVCKESYDDALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFA 119


                ....*...
gi 79313133 161 GPSNEPPL 168
Cdd:cd15800 120 ESGLVSPL 127
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 53-183 6.04e-07

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: 46.97  E-value: 6.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  53 FDRQFCAKWFNADQKTKSIS-VQGFISLRVKETREFGLQTQALMSKLAKSSGKDQQLKGSYESCVASYGQAIKELEKAQK 131
Cdd:cd15795  11 VDYDFCVSSLQSDPRSRTAAdLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSDAVDSLKSALD 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 79313133 132 FLSSNSFTQALVAISDAFYKAGDCKDAFEGPSNEPPLVFNRVENFANMCYVT 183
Cdd:cd15795  91 ALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIVVSPLTKENDELFQLALIA 142
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 57-183 1.34e-05

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: 43.09  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  57 FCAKWFNADQKTKSISVQGFISLRVKETREFGLQTQALMSKLAKSsGKDQQLKGSYESCVASYGQAIKELEKAQKFLSSN 136
Cdd:cd15801  14 LCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSELLNT-AKDPYVQQCLEDCSENYEDAVEQLNDSLAALDSK 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 79313133 137 SFTQALVAISDAFYKAGDCKDAFEGPSNEPPLVFNRVENFANMCYVT 183
Cdd:cd15801  93 AYGDVKTWVTAALADAETCEDAFKEKPGDKSPLTARNGDFSKLCSIA 139
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 56-181 5.61e-04

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: 38.50  E-value: 5.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313133  56 QFCAKWFNAD-QKTKSISVQGFISLRVKETREFGLQTQALMSKLaKSSGKDQQLKGSYESCVASYGQAIK-ELEKAQKFL 133
Cdd:cd15796  15 DLCVSILRSDpRSTTAADVKGLALIMLDAVLAKANDTLRKIGEL-LKKTTDPALKRALSSCAEEYGVIVEdDLPQAIEAL 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 79313133 134 SSNSFTQALVAISDAFYKAGDCKDAFEGPSNEPPLVFNR-VENFANMCY 181
Cdd:cd15796  94 KKGDYKAAKDSMYDAGKEADSCEEQFKGSSSSPLTDRNKaVHDLAVVAA 142
 
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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