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Conserved domains on  [gi|659120165|ref|XP_008460048|]
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putative invertase inhibitor [Cucumis melo]

Protein Classification

PMEI-Pla_a_1_like domain-containing protein( domain architecture ID 10204980)

PMEI-Pla_a_1_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 39-183 3.16e-39

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: 130.95  E-value: 3.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  39 CKKISREDPNISFNFCLTSLKLATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKLDPFVKSCLDDCLELYSD 118
Cdd:cd15795    1 CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165 119 AIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVASPLKKRDENAFELGAIVLSI 183
Cdd:cd15795   81 AVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIVVSPLTKENDELFQLALIALAI 145
 
Name Accession Description Interval E-value
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 39-183 3.16e-39

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: 130.95  E-value: 3.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  39 CKKISREDPNISFNFCLTSLKLATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKLDPFVKSCLDDCLELYSD 118
Cdd:cd15795    1 CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165 119 AIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVASPLKKRDENAFELGAIVLSI 183
Cdd:cd15795   81 AVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIVVSPLTKENDELFQLALIALAI 145
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 9-183 4.93e-28

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: 103.27  E-value: 4.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165    9 VFILSIFFFSNFLII----QSSKTIKTADLIYKTCKKIsrEDPNisfnFCLTSLKLATNhSRCTDVRHLGLLSIGLLYRN 84
Cdd:TIGR01614   2 ASSLSLLLFLLLLSLvatsSSNSLNATQSLIKRICKKT--EYPN----FCISTLKSDPS-SAKADLQGLANISVSAALSN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165   85 VTSTCHHITKLvKNKKLDPFVKSCLDDCLELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVA- 163
Cdd:TIGR01614  75 ASDTLDHISKL-LLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGIVk 153

                         170       180
                  ....*....|....*....|
gi 659120165  164 SPLKKRDENAFELGAIVLSI 183
Cdd:TIGR01614 154 SPLTKRNNNVKKLSSITLAI 173
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 30-183 3.55e-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: 89.74  E-value: 3.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165    30 KTADLIYKTCKKisredpNISFNFCLTSLKlATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKlDPFVKSCL 109
Cdd:smart00856   2 PTSKLIDSICKS------TDYPDFCVSSLS-SDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTK-DPRLKAAL 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165   110 DDCLELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKG-VASPLKKRDENAFELGAIVLSI 183
Cdd:smart00856  74 KDCLELYDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEENDDkVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 33-183 2.15e-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 (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: 85.29  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165   33 DLIYKTCKKIsrEDPNisfnFCLTSLKlATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKLDPFVKSCLDDC 112
Cdd:pfam04043   1 SLIKTACKKT--PYPD----LCVSSLS-SDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDC 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165  113 LELYSDAIPTVKQAMKDYKSKRY--DDVNVAIGSVMDAATTCEDGFKE--RKGVASPLKKRDENAFELGAIVLSI 183
Cdd:pfam04043  74 LELYDDAVDELNRALDALKAGDSsrDDAQTWLSAALTNQDTCEDGFKEavKGQLKSSMKSPLRNLTKLTSNALAI 148
PLN02933 PLN02933
Probable pectinesterase/pectinesterase inhibitor
 109-156 5.65e-04

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178521 [Multi-domain]  Cd Length: 530  Bit Score: 39.61  E-value: 5.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 659120165 109 LDDCLELYSDAIPTVKQAMKDYKSK--RYDDVNVAIGSVMDAATTCEDGF 156
Cdd:PLN02933  92 FEDCLGLLDDTISDLTTAISKLRSSspEFNDVSMLLSNAMTNQDTCLDGF 141
 
Name Accession Description Interval E-value
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 39-183 3.16e-39

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: 130.95  E-value: 3.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  39 CKKISREDPNISFNFCLTSLKLATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKLDPFVKSCLDDCLELYSD 118
Cdd:cd15795    1 CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165 119 AIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVASPLKKRDENAFELGAIVLSI 183
Cdd:cd15795   81 AVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIVVSPLTKENDELFQLALIALAI 145
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 9-183 4.93e-28

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: 103.27  E-value: 4.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165    9 VFILSIFFFSNFLII----QSSKTIKTADLIYKTCKKIsrEDPNisfnFCLTSLKLATNhSRCTDVRHLGLLSIGLLYRN 84
Cdd:TIGR01614   2 ASSLSLLLFLLLLSLvatsSSNSLNATQSLIKRICKKT--EYPN----FCISTLKSDPS-SAKADLQGLANISVSAALSN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165   85 VTSTCHHITKLvKNKKLDPFVKSCLDDCLELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVA- 163
Cdd:TIGR01614  75 ASDTLDHISKL-LLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGIVk 153

                         170       180
                  ....*....|....*....|
gi 659120165  164 SPLKKRDENAFELGAIVLSI 183
Cdd:TIGR01614 154 SPLTKRNNNVKKLSSITLAI 173
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 34-186 4.14e-24

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: 92.01  E-value: 4.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  34 LIYKTCKKISREDpnisfnFCLTSLKLATNhSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKlDPFVKSCLDDCL 113
Cdd:cd15801    1 LIEEACKKTLDPD------LCVSALSSDPE-SKKADLRGLAELALKAAAENATATASYVSELLNTAK-DPYVQQCLEDCS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 659120165 114 ELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVASPLKKRDENAFELGAIVLSIMSL 186
Cdd:cd15801   73 ENYEDAVEQLNDSLAALDSKAYGDVKTWVTAALADAETCEDAFKEKPGDKSPLTARNGDFSKLCSIALAIIKL 145
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 30-183 3.55e-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: 89.74  E-value: 3.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165    30 KTADLIYKTCKKisredpNISFNFCLTSLKlATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKlDPFVKSCL 109
Cdd:smart00856   2 PTSKLIDSICKS------TDYPDFCVSSLS-SDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTK-DPRLKAAL 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165   110 DDCLELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKG-VASPLKKRDENAFELGAIVLSI 183
Cdd:smart00856  74 KDCLELYDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEENDDkVKSPLTKRNDNLEKLTSNALAI 148
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 31-183 4.40e-23

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: 89.79  E-value: 4.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  31 TADLIYKTCKKisredpNISFNFCLTSLKlATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKlDPFVKSCLD 110
Cdd:cd15797    1 TEELIDTICKK------TENPSFCLQILN-SDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTT-DPKLKNRYE 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 659120165 111 DCLELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVASPLKKRDENAFELGAIVLSI 183
Cdd:cd15797   73 SCSKNYNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSKPPKDPSPLAKYNRDVEDLCDIILVI 145
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 39-186 4.07e-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: 4.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  39 CKKISredpniSFNFCLTSLKLATNhSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKlDPFVKSCLDDCLELYSD 118
Cdd:cd14859    1 CKKTS------YYKLCVSSLSSDPR-SSTADLKGLANIALDAALANASDTQAFIAKLLKSTK-DPALKKALRDCADDYDD 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659120165 119 AIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVASPLKKRDENAFELGAIVLSIMSL 186
Cdd:cd14859   73 AVDDLEDAINALLSGDYDDAKTHVSAALDDADTCEEAFKESSGLPSPLTTRNDDLKRLCSIALAIILL 140
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 33-183 2.15e-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 (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: 85.29  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165   33 DLIYKTCKKIsrEDPNisfnFCLTSLKlATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKLDPFVKSCLDDC 112
Cdd:pfam04043   1 SLIKTACKKT--PYPD----LCVSSLS-SDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDC 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659120165  113 LELYSDAIPTVKQAMKDYKSKRY--DDVNVAIGSVMDAATTCEDGFKE--RKGVASPLKKRDENAFELGAIVLSI 183
Cdd:pfam04043  74 LELYDDAVDELNRALDALKAGDSsrDDAQTWLSAALTNQDTCEDGFKEavKGQLKSSMKSPLRNLTKLTSNALAI 148
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 92-187 7.58e-19

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: 78.56  E-value: 7.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  92 ITKLVKNKKLDPFVKSCLDDCLELYSDAIPTVKQAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERkGVASPLKKRDE 171
Cdd:cd15800   54 AKKLAKSPSTSPEVKSALDVCKESYDDALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAES-GLVSPLAKIND 132

                         90
                 ....*....|....*.
gi 659120165 172 NAFELGAIVLSIMSLV 187
Cdd:cd15800  133 LLKKLASNCLAIATLL 148
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 32-186 7.23e-16

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: 70.86  E-value: 7.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  32 ADLIYKTCKKIsredPNISFnfCLTSLKLATNHSRCTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKlDPFVKSCLDD 111
Cdd:cd15796    1 ADLIDETCKKT----PNYDL--CVSILRSDPRSTTAADVKGLALIMLDAVLAKANDTLRKIGELLKKTT-DPALKRALSS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165 112 CLELY----SDAIPTVKQAM--KDYKSKRYDDVNVAIgsvmdAATTCEDGFKerKGVASPLKKRDENAFELGAIVLSIMS 185
Cdd:cd15796   74 CAEEYgvivEDDLPQAIEALkkGDYKAAKDSMYDAGK-----EADSCEEQFK--GSSSSPLTDRNKAVHDLAVVAAAIVR 146


                 .
gi 659120165 186 L 186
Cdd:cd15796  147 Q 147
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 53-185 1.38e-07

Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; 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. The proteinaceous PME inhibitor (PMEI) 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: 275442 [Multi-domain]  Cd Length: 154  Bit Score: 48.59  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  53 FCLTSLKLATNHSRcTDVRHLGLLSIGLLYRNVTSTCHHITKLVKNKKLDPFVKSCLDDCLELYSDAIPTVKQAMKDYKS 132
Cdd:cd15798   11 LCKSSLSSYASSSS-TDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDLNRSLSELNS 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659120165 133 -------KRYDDVNVAIGSVMDAATTCEDGFKERKG-VASPLKKRDENAFELGAIVLSIMS 185
Cdd:cd15798   90 lskdkfsERVDDVQTWLSAALTNQDTCLDGFEETGStVKKELRASLKNVSKLTSNALALVN 150
PLN02933 PLN02933
Probable pectinesterase/pectinesterase inhibitor
 109-156 5.65e-04

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178521 [Multi-domain]  Cd Length: 530  Bit Score: 39.61  E-value: 5.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 659120165 109 LDDCLELYSDAIPTVKQAMKDYKSK--RYDDVNVAIGSVMDAATTCEDGF 156
Cdd:PLN02933  92 FEDCLGLLDDTISDLTTAISKLRSSspEFNDVSMLLSNAMTNQDTCLDGF 141
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 80-185 7.31e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 39.51  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  80 LLYRNVTSTCHHITKL------VKNKKLDPFVKSCLDDCLELYSDAIPTVKQAMKDYKS----KRYDDVNVAIGSVMDAA 149
Cdd:PLN02484 107 LIHISFNMTLQHFSKAlylsstISYVQMPPRVRSAYDSCLELLDDSVDALSRALSSVVPssggGSPQDVVTWLSAALTNH 186

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 659120165 150 TTCEDGFK--ERKGVASPLKKRDENAFELGAIVLSIMS 185
Cdd:PLN02484 187 DTCTEGFDgvNGGEVKDQMTGALKDLSELVSNCLAIFS 224
PMEI-like_4 cd15799
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ...
 102-164 8.12e-04

plant invertase/pectin methylesterase inhibitor domain-containing protein; 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: 275443 [Multi-domain]  Cd Length: 151  Bit Score: 38.16  E-value: 8.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659120165 102 DPFVKSCLDDCLELYSDAIP----TVKqAMKDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKGVAS 164
Cdd:cd15799   62 DPRLSNALSDCLELLDFSADrlswSLS-ALQNPKGDSGSDARTWLSAALTNHDTCLDGLEETGVVKS 127
PLN02313 PLN02313
Pectinesterase/pectinesterase inhibitor
 77-156 9.30e-04

Pectinesterase/pectinesterase inhibitor


Pssm-ID: 177947 [Multi-domain]  Cd Length: 587  Bit Score: 39.30  E-value: 9.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  77 SIGLLYRNVTSTCHHITKLVKNKK-LDPFVKSCLDDCLELYSDAIPTVKQAMKD---YKSKRY-----DDVNVAIGSVMD 147
Cdd:PLN02313  97 SLNLTTKAVKHNYFAVKKLIAKRKgLTPREVTALHDCLETIDETLDELHVAVEDlhqYPKQKSlrkhaDDLKTLISSAIT 176


                 ....*....
gi 659120165 148 AATTCEDGF 156
Cdd:PLN02313 177 NQGTCLDGF 185
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 94-185 1.89e-03

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 38.30  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  94 KLVKNKKLDPFVKSCLDDCLELYSDAIPTVKQAMKDYK------SKRYDDVNVAIGSVMDAATTCEDGFKERKgVASPLK 167
Cdd:PLN02745 133 KVLSFKFENPDEKDAIEDCKLLVEDAKEELKASISRINdevnklAKNVPDLNNWLSAVMSYQETCIDGFPEGK-LKSEME 211

                         90
                 ....*....|....*...
gi 659120165 168 KRDENAFELGAIVLSIMS 185
Cdd:PLN02745 212 KTFKSSQELTSNSLAMVS 229
PLN02314 PLN02314
pectinesterase
 54-161 3.16e-03

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 37.50  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659120165  54 CLTSL-KLATNHSrcTDVRHLGLLSIGLLYRNVTSTCHHITKLVkNKKLDPFVKSCLDDCLELYSDAIPTVKQAM----- 127
Cdd:PLN02314  86 CISSIsSLPTSNT--TDPETLFKLSLKVAIDELSKLSDLPQKLI-NETNDERLKSALRVCETLFDDAIDRLNDSIssmqv 162

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 659120165 128 ----KDYKSKRYDDVNVAIGSVMDAATTCEDGFKERKG 161
Cdd:PLN02314 163 gegeKILSSSKIDDLKTWLSATITDQETCIDALQELSQ 200
 
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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