|
Name |
Accession |
Description |
Interval |
E-value |
| PME_inhib |
TIGR01614 |
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ... |
5-197 |
2.13e-42 |
|
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: 140.63 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 5 VVLSLTLMVFINSSNFPKTAATPPgtYQNHTTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNA 84
Cdd:TIGR01614 1 MASSLSLLLFLLLLSLVATSSSNS--LNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 85 TLVVSNLLQkaKAAKSHEVSILKDCVDEMKDTIDELKQAVAEMKyvrgggkttEEHLKNVKTWVSSALTDEGTCTDGFEE 164
Cdd:TIGR01614 79 LDHISKLLL--TKGDPRDKSALEDCVELYSDAVDALDKALASLK---------SKDYSDAETWLSSALTDPSTCEDGFEE 147
|
170 180 190
....*....|....*....|....*....|...
gi 15234980 165 GrvNVETKKKVKKAISELSKTTSNTLALLTHYL 197
Cdd:TIGR01614 148 L--GGIVKSPLTKRNNNVKKLSSITLAIIKMLT 178
|
|
| PMEI-like_3 |
cd15798 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ... |
40-196 |
2.26e-38 |
|
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: 129.48 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 40 TACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKaKAAKSHEVSILKDCVDEMKDTIDE 119
Cdd:cd15798 1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKS-SGSNPREKAALEDCLELLDDAVDD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234980 120 LKQAVAEMKyvRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEEgrVNVETKKKVKKAISELSKTTSNTLALLTHY 196
Cdd:cd15798 80 LNRSLSELN--SLSKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNAL 152
|
|
| PMEI |
smart00856 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
32-192 |
1.61e-37 |
|
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: 127.10 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 32 QNHTTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKaaKSHEVSILKDCVD 111
Cdd:smart00856 1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTK--DPRLKAALKDCLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 112 EMKDTIDELKQAVAEMKyvrgggkttEEHLKNVKTWVSSALTDEGTCTDGFEEgrVNVETKKKVKKAISELSKTTSNTLA 191
Cdd:smart00856 79 LYDDAVDSLEKALEELK---------SGDYDDVATWLSAALTDQDTCLDGFEE--NDDKVKSPLTKRNDNLEKLTSNALA 147
|
.
gi 15234980 192 L 192
Cdd:smart00856 148 I 148
|
|
| PMEI |
pfam04043 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
36-192 |
9.25e-33 |
|
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: 114.95 E-value: 9.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 36 TYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEvSILKDCVDEMKD 115
Cdd:pfam04043 1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDK-AALEDCLELYDD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234980 116 TIDELKQAVAEMkyvrgggKTTEEHLKNVKTWVSSALTDEGTCTDGFEEgRVNVETKKKVKKAISELSKTTSNTLAL 192
Cdd:pfam04043 80 AVDELNRALDAL-------KAGDSSRDDAQTWLSAALTNQDTCEDGFKE-AVKGQLKSSMKSPLRNLTKLTSNALAI 148
|
|
| PLN02313 |
PLN02313 |
Pectinesterase/pectinesterase inhibitor |
38-193 |
4.34e-22 |
|
Pectinesterase/pectinesterase inhibitor
Pssm-ID: 177947 [Multi-domain] Cd Length: 587 Bit Score: 92.84 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 38 VKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEVSILKDCVDEMKDTI 117
Cdd:PLN02313 62 LKSVCSSTLYPELCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKLIAKRKGLTPREVTALHDCLETIDETL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234980 118 DELKQAVAEMkYVRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEEGRVNVETKKKVKKAISELSKTTSNTLALL 193
Cdd:PLN02313 142 DELHVAVEDL-HQYPKQKSLRKHADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEHMCSNALAMI 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PME_inhib |
TIGR01614 |
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ... |
5-197 |
2.13e-42 |
|
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: 140.63 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 5 VVLSLTLMVFINSSNFPKTAATPPgtYQNHTTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNA 84
Cdd:TIGR01614 1 MASSLSLLLFLLLLSLVATSSSNS--LNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 85 TLVVSNLLQkaKAAKSHEVSILKDCVDEMKDTIDELKQAVAEMKyvrgggkttEEHLKNVKTWVSSALTDEGTCTDGFEE 164
Cdd:TIGR01614 79 LDHISKLLL--TKGDPRDKSALEDCVELYSDAVDALDKALASLK---------SKDYSDAETWLSSALTDPSTCEDGFEE 147
|
170 180 190
....*....|....*....|....*....|...
gi 15234980 165 GrvNVETKKKVKKAISELSKTTSNTLALLTHYL 197
Cdd:TIGR01614 148 L--GGIVKSPLTKRNNNVKKLSSITLAIIKMLT 178
|
|
| PMEI-like_3 |
cd15798 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ... |
40-196 |
2.26e-38 |
|
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: 129.48 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 40 TACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKaKAAKSHEVSILKDCVDEMKDTIDE 119
Cdd:cd15798 1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKS-SGSNPREKAALEDCLELLDDAVDD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234980 120 LKQAVAEMKyvRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEEgrVNVETKKKVKKAISELSKTTSNTLALLTHY 196
Cdd:cd15798 80 LNRSLSELN--SLSKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNAL 152
|
|
| PMEI |
smart00856 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
32-192 |
1.61e-37 |
|
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: 127.10 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 32 QNHTTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKaaKSHEVSILKDCVD 111
Cdd:smart00856 1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTK--DPRLKAALKDCLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 112 EMKDTIDELKQAVAEMKyvrgggkttEEHLKNVKTWVSSALTDEGTCTDGFEEgrVNVETKKKVKKAISELSKTTSNTLA 191
Cdd:smart00856 79 LYDDAVDSLEKALEELK---------SGDYDDVATWLSAALTDQDTCLDGFEE--NDDKVKSPLTKRNDNLEKLTSNALA 147
|
.
gi 15234980 192 L 192
Cdd:smart00856 148 I 148
|
|
| PMEI |
pfam04043 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
36-192 |
9.25e-33 |
|
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: 114.95 E-value: 9.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 36 TYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEvSILKDCVDEMKD 115
Cdd:pfam04043 1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDK-AALEDCLELYDD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234980 116 TIDELKQAVAEMkyvrgggKTTEEHLKNVKTWVSSALTDEGTCTDGFEEgRVNVETKKKVKKAISELSKTTSNTLAL 192
Cdd:pfam04043 80 AVDELNRALDAL-------KAGDSSRDDAQTWLSAALTNQDTCEDGFKE-AVKGQLKSSMKSPLRNLTKLTSNALAI 148
|
|
| PLN02313 |
PLN02313 |
Pectinesterase/pectinesterase inhibitor |
38-193 |
4.34e-22 |
|
Pectinesterase/pectinesterase inhibitor
Pssm-ID: 177947 [Multi-domain] Cd Length: 587 Bit Score: 92.84 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 38 VKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEVSILKDCVDEMKDTI 117
Cdd:PLN02313 62 LKSVCSSTLYPELCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKLIAKRKGLTPREVTALHDCLETIDETL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234980 118 DELKQAVAEMkYVRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEEGRVNVETKKKVKKAISELSKTTSNTLALL 193
Cdd:PLN02313 142 DELHVAVEDL-HQYPKQKSLRKHADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEHMCSNALAMI 216
|
|
| PLN02484 |
PLN02484 |
probable pectinesterase/pectinesterase inhibitor |
5-194 |
1.28e-18 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178102 [Multi-domain] Cd Length: 587 Bit Score: 83.04 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 5 VVLSLTLMVFINSSNFPKTAATPPGTYQNHTTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNA 84
Cdd:PLN02484 43 IVSAVAAAIFAGVRAKASGQTSPKSLHRKPTQAISKTCSKTRFPNLCVDSLLDFPGSLTASESDLIHISFNMTLQHFSKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 85 TLVVSNLlqKAKAAKSHEVSILKDCVDEMKDTIDELKQAVAEMKYVRGGGKTteehlKNVKTWVSSALTDEGTCTDGFEE 164
Cdd:PLN02484 123 LYLSSTI--SYVQMPPRVRSAYDSCLELLDDSVDALSRALSSVVPSSGGGSP-----QDVVTWLSAALTNHDTCTEGFDG 195
|
170 180 190
....*....|....*....|....*....|.
gi 15234980 165 grVNV-ETKKKVKKAISELSKTTSNTLALLT 194
Cdd:PLN02484 196 --VNGgEVKDQMTGALKDLSELVSNCLAIFS 224
|
|
| PLN02314 |
PLN02314 |
pectinesterase |
5-198 |
1.90e-18 |
|
pectinesterase
Pssm-ID: 215179 [Multi-domain] Cd Length: 586 Bit Score: 82.57 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 5 VVLSLTLMVFINSSNFPKTAATPPGTYQNhtTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLnlnvKSAKNA 84
Cdd:PLN02314 42 IIIGAVVGTVVHKRKNESNPSPPPELTPA--TSLKAVCSVTRYPESCISSISSLPTSNTTDPETLFKLSL----KVAIDE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 85 TLVVSNLLQKAKAAKSHEV--SILKDCVDEMKDTIDELKQAVAEMKyVRGGGKT-TEEHLKNVKTWVSSALTDEGTCTDG 161
Cdd:PLN02314 116 LSKLSDLPQKLINETNDERlkSALRVCETLFDDAIDRLNDSISSMQ-VGEGEKIlSSSKIDDLKTWLSATITDQETCIDA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15234980 162 FEE----GRVNVETKKKVKKAISELSKTTSNTLALLTHYLS 198
Cdd:PLN02314 195 LQElsqnKYANSTLTNEVKTAMSNSTEFTSNSLAIVSKILG 235
|
|
| PMEI-like_2 |
cd15800 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ... |
38-192 |
6.14e-15 |
|
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: 68.54 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 38 VKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKShEVSILKDCVDEMKDTI 117
Cdd:cd15800 4 VKDICKKTDYPALCLSTVKPFLTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTSPE-VKSALDVCKESYDDAL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234980 118 DELKQAvaeMKYVRGGGKTTeehlknVKTWVSSALTDEGTCTDGFEE-GRVNVetkkkVKKAISELSKTTSNTLAL 192
Cdd:cd15800 83 DNLKKA---LKAIKSRDIGT------LNSMLSAAITDYSTCDDAFAEsGLVSP-----LAKINDLLKKLASNCLAI 144
|
|
| PMEI-like_1 |
cd15801 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ... |
37-194 |
6.72e-15 |
|
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: 68.51 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 37 YVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEVsiLKDCVDEMKDT 116
Cdd:cd15801 1 LIEEACKKTLDPDLCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSELLNTAKDPYVQQC--LEDCSENYEDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 117 IDELKQAVAEMkyvrgggktTEEHLKNVKTWVSSALTDEGTCTDGFEE--GRVNVETKKKvkkaiSELSKTTSNTLALLT 194
Cdd:cd15801 79 VEQLNDSLAAL---------DSKAYGDVKTWVTAALADAETCEDAFKEkpGDKSPLTARN-----GDFSKLCSIALAIIK 144
|
|
| PLN02990 |
PLN02990 |
Probable pectinesterase/pectinesterase inhibitor |
4-195 |
1.39e-13 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215535 [Multi-domain] Cd Length: 572 Bit Score: 68.51 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 4 FVVLSLTLMVFINSSNFPKTA-ATPPGTYQNHTTYVKTACNSTTYPTMCYNCLSSySSTIKSDPIKLCTTSLNLNVKSAK 82
Cdd:PLN02990 21 LLVIMVVAVAIVTSRNTSHNSeKIVPVQIKTTTKAVEAVCAPTDYKETCVNSLMK-ASPDSTQPLDLIKLGFNVTIRSIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 83 NATLVVSNLLqKAKAAKSHEVS-ILKDCVDEMKDTIDELKQAvaeMKYVRGGGKTT-EEHLKNVKTWVSSALTDEGTCTD 160
Cdd:PLN02990 100 DSIKKASGEL-KAKAANDPETKgALELCEKLMNDATDDLKKC---LDNFDGFSIDQiEDFVEDLRVWLSGSIAYQQTCMD 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 15234980 161 GFEEGRVNV-ETKKKVKKAISELsktTSNTLALLTH 195
Cdd:PLN02990 176 TFEEIKSNLsQDMLKIFKTSREL---TSNGLAMITN 208
|
|
| PLN02745 |
PLN02745 |
Putative pectinesterase/pectinesterase inhibitor |
21-198 |
4.26e-13 |
|
Putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 178346 [Multi-domain] Cd Length: 596 Bit Score: 66.80 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 21 PKTAATPPGtyqNHTTYVKTACNSTTYPTMCYNCLSSYSstiKSDPIKLCTTSLnlnVKSA-KNATLVVSNLLQKAKAAK 99
Cdd:PLN02745 68 PVKSESPVS---QVDKIIQTVCNATLYKQTCENTLKKGT---EKDPSLAQPKDL---LKSAiKAVNDDLDKVLKKVLSFK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 100 S---HEVSILKDCVDEMKDTIDELKqavAEMKYVRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEEGRVNVETKKKVK 176
Cdd:PLN02745 139 FenpDEKDAIEDCKLLVEDAKEELK---ASISRINDEVNKLAKNVPDLNNWLSAVMSYQETCIDGFPEGKLKSEMEKTFK 215
|
170 180
....*....|....*....|....*
gi 15234980 177 KAiSELsktTSNTLAL---LTHYLS 198
Cdd:PLN02745 216 SS-QEL---TSNSLAMvssLTSFLS 236
|
|
| PLN03043 |
PLN03043 |
Probable pectinesterase/pectinesterase inhibitor; Provisional |
41-198 |
4.63e-12 |
|
Probable pectinesterase/pectinesterase inhibitor; Provisional
Pssm-ID: 178606 [Multi-domain] Cd Length: 538 Bit Score: 63.73 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 41 ACNSTTYPTMCYNCLSSYSSTiKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAK---AAKSHEVSILKDCVDEMKDTI 117
Cdd:PLN03043 5 ACKSTLYPKLCRSILSTVKSS-PSDPYEYGKFSVKQCLKQARRLSKVINYYLTHENqpgKMTHEEIGALADCGELSELNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 118 DELKQAVAEMKYVRgggKTTEEHLKNVKTWVSSALTDEGTCTDGFeegrvnVETKKKVKKAI----SELSKTTSNTLALL 193
Cdd:PLN03043 84 DYLETISSELKSAE---LMTDALVERVTSLLSGVVTNQQTCYDGL------VDSKSSFAAALgaplGNLTRLYSVSLGLV 154
|
....*
gi 15234980 194 THYLS 198
Cdd:PLN03043 155 SHALN 159
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
3-199 |
1.47e-11 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 62.41 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 3 RFVVLSLTLMVFIN-------SSNFPKTAATPPGTYQNHTTYVKTACNSTTYPTMCYNCLSSYSSTiKSDPIKLCTTSLN 75
Cdd:PLN02217 14 RYVIISISSVLLISmvvavtiGVSVNKSDNEGKGEITTSVKAIKDVCAPTDYKETCEDTLRKDAKN-TSDPLELVKTAFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 76 LNVKSAKNATLVVSNLLQKAKAAKSHEVsiLKDCVDEMKDTIDELKQAVAEMkyvrggGK----TTEEHLKNVKTWVSSA 151
Cdd:PLN02217 93 ATMKQISDVAKKSQTMIELQKDPRTKMA--LDQCKELMDYAIGELSKSFEEL------GKfefhKVDEALIKLRIWLSAT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15234980 152 LTDEGTCTDGFEEGRVNV-ETKKKVKKAISELsktTSNTLALLTHYLSY 199
Cdd:PLN02217 165 ISHEQTCLDGFQGTQGNAgETIKKALKTAVQL---THNGLAMVSEMSNY 210
|
|
| PMEI-like_4 |
cd15799 |
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ... |
54-193 |
1.89e-11 |
|
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: 59.35 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 54 CLSSYSSTI-KSDPIKLCTTSLNLNVKSAKNATLVVsnlLQKAK--AAKSHEVSI-------LKDCVDEMKDTIDELKQA 123
Cdd:cd15799 10 CLAIPSVSSsANALSAQCLKVPLDVFLAALKTTVDR---IQSALsmVSKLRNGSDdprlsnaLSDCLELLDFSADRLSWS 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 124 VAEMKyvrgggKTTEEHLKNVKTWVSSALTDEGTCTDGFEEGRVNvetKKKVKKAISELSKTTSNTLALL 193
Cdd:cd15799 87 LSALQ------NPKGDSGSDARTWLSAALTNHDTCLDGLEETGVV---KSLVAAALSNLTSLLREALAMV 147
|
|
| PLN02468 |
PLN02468 |
putative pectinesterase/pectinesterase inhibitor |
35-194 |
4.53e-11 |
|
putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 178087 [Multi-domain] Cd Length: 565 Bit Score: 61.05 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 35 TTYVKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEVSILKDCVDEMK 114
Cdd:PLN02468 64 STSVKAVCDVTLYKDSCYETLAPAPKASQLQPEELFKYAVKVAINELSKASQAFSNSEGFLGVKDNMTNAALNACQELLD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 115 DTIDELKQAVAEmkyvrGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEEGRVNVETKKKVKKAiSELsktTSNTLALLT 194
Cdd:PLN02468 144 LAIDNLNNSLTS-----SGGVSVLDNVDDLRTWLSSAGTYQETCIDGLAEPNLKSFGENHLKNS-TEL---TSNSLAIIT 214
|
|
| PLN02506 |
PLN02506 |
putative pectinesterase/pectinesterase inhibitor |
7-195 |
8.66e-11 |
|
putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 215280 [Multi-domain] Cd Length: 537 Bit Score: 60.33 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 7 LSLTLMVFINSSNFPKTAATPPGTyQNHTTYVKTACNSTTYPTMCyncLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATL 86
Cdd:PLN02506 7 LLILMLLPVHLESLETTSSSPYQE-LNFQALIAQACQFVENHSSC---VSNIQAELKKSGPRTPHSVLSAALKATLDEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 87 VVSNLLQK--AKAAKSHEVSILKDCVDEMKDTIDELKQAVAEMKYVRGGGKTTEEHlKNVKTWVSSALTDEGTCTDGFEE 164
Cdd:PLN02506 83 LAIDMITKfnALSISYREQVAIEDCKELLDFSVSELAWSLLEMNKIRAGHDNVAYE-GNLKAWLSAALSNQDTCLEGFEG 161
|
170 180 190
....*....|....*....|....*....|.
gi 15234980 165 GRVNVEtkKKVKKAISELSKTTSNTLALLTH 195
Cdd:PLN02506 162 TDRHLE--NFIKGSLKQVTQLISNVLAMYTQ 190
|
|
| PMEI_like |
cd14859 |
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ... |
42-193 |
1.83e-10 |
|
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: 56.67 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 42 CNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSHEVsiLKDCVDEMKDTIDELK 121
Cdd:cd14859 1 CKKTSYYKLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFIAKLLKSTKDPALKKA--LRDCADDYDDAVDDLE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234980 122 QAVAEMKyvrgggkttEEHLKNVKTWVSSALTDEGTCTDGFEEGRVNVETKKKVKKAISELsktTSNTLALL 193
Cdd:cd14859 79 DAINALL---------SGDYDDAKTHVSAALDDADTCEEAFKESSGLPSPLTTRNDDLKRL---CSIALAII 138
|
|
| PLN02933 |
PLN02933 |
Probable pectinesterase/pectinesterase inhibitor |
68-193 |
2.75e-10 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178521 [Multi-domain] Cd Length: 530 Bit Score: 58.87 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 68 KLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKSH-EVSILKDCVDEMKDTIDELKQAVAEMKyvrgggkTTEEHLKNVKT 146
Cdd:PLN02933 53 ELIIADLNLTILKVNLASSNFSDLQTRLGPNLTHrERCAFEDCLGLLDDTISDLTTAISKLR-------SSSPEFNDVSM 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15234980 147 WVSSALTDEGTCTDGF------EEGRVNVETKKKVKKAISELSKTTSNTLALL 193
Cdd:PLN02933 126 LLSNAMTNQDTCLDGFstsdneNNNDMTYELPENLKESILDISNHLSNSLAML 178
|
|
| PLN02416 |
PLN02416 |
probable pectinesterase/pectinesterase inhibitor |
4-193 |
6.05e-10 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178037 [Multi-domain] Cd Length: 541 Bit Score: 57.63 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 4 FVVLSLTLMVFINSSNFPKTAATPPGTYQN----HTTYVKTACNSTTYPTMCYNCLS-SYSSTIKSDPIKLCTTSLNLNV 78
Cdd:PLN02416 3 FSSLNLLLFLLFFSPFFFSSAWYSNASYTTsldpHLSSLTSFCKSTPYPDACFDSLKlSISINISPNILNFLLQTLQTAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 79 KSAKNATLVVS------NLLQKAKAAkshevsiLKDCVDEMKDTIDELKQAVAEmkyVRGGgktTEEHLKNVKTWVSSAL 152
Cdd:PLN02416 83 SEAGKLTNLLSgagqssNIIEKQRGT-------IQDCKELHQITVSSLKRSVSR---IQAG---DSRKLADARAYLSAAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15234980 153 TDEGTCTDGFEEGrvNVETKKKVKKAISELSKTTSNTLALL 193
Cdd:PLN02416 150 TNKNTCLEGLDSA--SGPLKPKLVNSFTSTYKHVSNSLSML 188
|
|
| PLN02713 |
PLN02713 |
Probable pectinesterase/pectinesterase inhibitor |
3-195 |
2.14e-08 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215383 [Multi-domain] Cd Length: 566 Bit Score: 53.26 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 3 RFVVLSLTLMVFINSSNFPKTAATPPGTYQNHTTyvktACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTT-SLNlnvKSA 81
Cdd:PLN02713 4 KLILLTTLALLLLLFFSSSSASDPPPSTPVSPST----ICNTTPDPSFCKSVLPHNQPGNVYDYGRFSVRkSLS---QSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 82 KNATLVVSNLLQKAKAAKSHEVSILKDCVDEMKDTIDELKQAVAEMKyvrgGGKTTEEHLK--NVKTWVSSALTDEGTCT 159
Cdd:PLN02713 77 KFLSLVDRYLKRNSTLLSKSAIRALEDCQFLAGLNIDFLLSSFETVN----SSSKTLSDPQadDVQTLLSAILTNQQTCL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 15234980 160 DGFEEGRVNVETKKKVKKAISELSKTTSNTLALLTH 195
Cdd:PLN02713 153 DGLQAASSAWSVRNGLAVPLSNDTKLYSVSLALFTK 188
|
|
| PLN02170 |
PLN02170 |
probable pectinesterase/pectinesterase inhibitor |
56-196 |
1.12e-07 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215114 [Multi-domain] Cd Length: 529 Bit Score: 51.13 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 56 SSYSSTIKSDPIKLCTTSLNLNVKSAKNATL----VVSNLLQKAKAAKSHEVSILKDCVDEMKDTIDELKQAVaemkyVR 131
Cdd:PLN02170 48 PNSDSSSRSSPSSSSKQGFLSSVQESMNHALfarsLAFNLTLSHRTVQTHTFDPVNDCLELLDDTLDMLSRIV-----VI 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234980 132 GGGKTTEEhlkNVKTWVSSALTDEGTCTDGFEEGRVNVETKKKVKKAISELSKTTSNTLAL-LTHY 196
Cdd:PLN02170 123 KHADHDEE---DVHTWLSAALTNQETCEQSLQEKSSSYKHGLAMDFVARNLTGLLTNSLDLfVSVK 185
|
|
| PLN02201 |
PLN02201 |
probable pectinesterase/pectinesterase inhibitor |
36-194 |
1.72e-07 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 177852 [Multi-domain] Cd Length: 520 Bit Score: 50.65 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 36 TYVKTACNSTTYPTMCYNCLSSYSSTIKSdpiklcttSLNLNVKSAKNATLVVSNLLQKAkaAKSHEVSILKDCVDEMKD 115
Cdd:PLN02201 15 LCVSSKEAFSSTDLLQMECLKVPPSEFVS--------SLKTTVDVIRKVVSIVSQFDKVF--GDSRLSNAISDCLDLLDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 116 TIDELKQAVAEMKYVRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEegrvnvETKKKVKKAISE-LSKTTSNTLALLT 194
Cdd:PLN02201 85 AAEELSWSISASQNPNGKDNSTGDVGSDLRTWLSAALSNQDTCIEGFD------GTNGIVKKLVAGsLSQVGSTVRELLT 158
|
|
| PLN02698 |
PLN02698 |
Probable pectinesterase/pectinesterase inhibitor |
1-193 |
4.69e-07 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178301 [Multi-domain] Cd Length: 497 Bit Score: 49.17 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 1 MLRFVVLSLtlmvfINSSnfpktAATPPGTYQNHttyVKTACNSTTYPTMCYNCLSSYsstiKSDPIKLCTTSLNlnvKS 80
Cdd:PLN02698 1 MIDMVIFWV-----LGAS-----SRNMPFAYQNE---VQRECSFTKYPSLCVQTLRGL----RHDGVDIVSVLVN---KT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 81 AKNATLVVSNLLQKAKAAKSHEV----SILKDCVDEMKDTIDELKQAVAEMKyvrgggKTTEEHLKNVKTWVSSALTDEG 156
Cdd:PLN02698 61 ISETNLPLSSSMGSSYQLSLEEAtytpSVSDSCERLMKMSLKRLRQSLLALK------GSSRKNKHDIQTWLSAALTFQQ 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 15234980 157 TCTDGFEEGRVNVETK--KKVKKAISELSKTTSNTLALL 193
Cdd:PLN02698 135 ACKDSIVDSTGYSGTSaiSQISQKMDHLSRLVSNSLALV 173
|
|
| PLN02301 |
PLN02301 |
pectinesterase/pectinesterase inhibitor |
33-193 |
1.03e-06 |
|
pectinesterase/pectinesterase inhibitor
Pssm-ID: 215170 [Multi-domain] Cd Length: 548 Bit Score: 48.34 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 33 NHTTYVKTACNSTTYPTMCYNCLSSYS--STIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKAAKshEVSILKDCV 110
Cdd:PLN02301 48 SPPSLLQTLCDRAHDQDSCQAMVSEIAtnTVMKLNRVDLLQVLLKESTPHLQNTIEMASEIRIRINDPR--DKAALADCV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 111 DEMKDTIDELKQAVAEMkyvrgGGKTTEEHlKNVKTWVSSALTDEGTCTDGfeegrVNVETKKKVKKAISELSKTTSNTL 190
Cdd:PLN02301 126 ELMDLSKDRIKDSVEAL-----GNVTSKSH-ADAHTWLSSVLTNHVTCLDG-----INGPSRQSMKPGLKDLISRARTSL 194
|
...
gi 15234980 191 ALL 193
Cdd:PLN02301 195 AIL 197
|
|
| PMEI-Pla_a_1_like |
cd15795 |
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ... |
40-167 |
9.33e-06 |
|
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: 43.89 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 40 TACNSTTYPTMCYNCLSSYSSTIK-SDPIKLCTTSLNLNVKSAKNATLVVSNLLqKAKAAKSHEVSILKDCVDEMKDTID 118
Cdd:cd15795 5 AAGDPNVDYDFCVSSLQSDPRSRTaADLKGLAVIATKLAIANATATKAKIEKLL-KSKKYPSDLKKALRDCLSLYSDAVD 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15234980 119 ELKQAVAEMKyvrgggkttEEHLKNVKTWVSSALTDEGTCTDGFEEGRV 167
Cdd:cd15795 84 SLKSALDALK---------SGDYGDANYDLSAATDAPVTCEDAFKEAKI 123
|
|
| PMEI |
cd15797 |
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ... |
38-192 |
1.55e-05 |
|
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: 43.18 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 38 VKTACNSTTYPTMCYNCLSSYSSTIKSDPIKLCTTSLNLNVKSAKNATLVVSNLLQKAKaaKSHEVSILKDCVDEMKDTI 117
Cdd:cd15797 5 IDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTT--DPKLKNRYESCSKNYNDAI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234980 118 DELKQAVAEMKyvRGGGKTTEEHlknvktwVSSALTDEGTCTDGFEEgrvNVETKKKVKKAISELSKTTSNTLAL 192
Cdd:cd15797 83 DALEEAKKSLS--SGDYDGLNKA-------ASAALDAVSTCEDELSK---PPKDPSPLAKYNRDVEDLCDIILVI 145
|
|
| PLN02995 |
PLN02995 |
Probable pectinesterase/pectinesterase inhibitor |
1-192 |
6.98e-05 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178574 [Multi-domain] Cd Length: 539 Bit Score: 42.74 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 1 MLRFVVLSLTLMVFINSSNFPKTAATppgtyQNHTTYVKTACNSTTYPTMCYNCLSSYSSTikSDPIKLCTTSLNLNVKS 80
Cdd:PLN02995 5 MQKISFLSLHLLLLLLLCVHPLTTVA-----DGNSTDIDGWCDKTPYPDPCKCYFKNHNGF--RQPTQISEFRVMLVEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 81 AKNATLVVSNLLQKAK-AAKSHEVSILKDCVDEMKDTIDELKQAVAEMKYVRGGGKTTEEHlkNVKTWVSSALTDEGTCT 159
Cdd:PLN02995 78 MDRAISARDELTNSGKnCTDFKKQAVLADCIDLYGDTIMQLNRTLQGVSPKAGAAKRCTDF--DAQTWLSTALTNTETCR 155
|
170 180 190
....*....|....*....|....*....|...
gi 15234980 160 DGFEEGRVNVETKKKVKKaiSELSKTTSNTLAL 192
Cdd:PLN02995 156 RGSSDLNVSDFITPIVSN--TKISHLISNCLAV 186
|
|
| PLN02708 |
PLN02708 |
Probable pectinesterase/pectinesterase inhibitor |
21-199 |
1.43e-03 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215379 [Multi-domain] Cd Length: 553 Bit Score: 38.66 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 21 PKTAATPPGTYQnhttyvktACNSTTYPTMCYNCLSSySSTIKSD--PIKLCTTSLNLNVKSAKNATLVVSNLLQkAKAA 98
Cdd:PLN02708 38 PSSPSTPPQILL--------ACNATRFPDTCVSSLSN-AGRVPPDpkPIQIIQSAISVSRENLKTAQSMVKSILD-SSAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234980 99 KSHEVSILKDCVDEMkdtidelkqAVAEMKYVRGGGKTTEEHLKNVKTWVSSALTDEGTCTDGFEegrvNVETKKKVKKA 178
Cdd:PLN02708 108 NVNRTTAATNCLEVL---------SNSEHRISSTDIALPRGKIKDARAWMSAALLYQYDCWSALK----YVNDTSQVNDT 174
|
170 180
....*....|....*....|....
gi 15234980 179 ISELSKT---TSNTLALLTHYLSY 199
Cdd:PLN02708 175 MSFLDSLiglTSNALSMMASYDIF 198
|
|
| |
