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Conserved domains on  [gi|22330888|ref|NP_683536|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

PMEI-like_2 domain-containing protein( domain architecture ID 10205026)

PMEI-like_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 127-263 2.65e-45

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: 149.05  E-value: 2.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 127 SPEIKTICGKTDNPPLCESSVSPLLTpQLKPNTSSVLILAIQASITATKAAMAIVEKVDAS------------DCQELYD 194
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPFLT-KGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSpstspevksaldVCKESYD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330888 195 DAVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGEPNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:cd15800  80 DALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PLN02217 super family cl33436
probable pectinesterase/pectinesterase inhibitor
 27-120 1.42e-05

probable pectinesterase/pectinesterase inhibitor


The actual alignment was detected with superfamily member PLN02217:

Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 45.85  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   27 SRSDSPFSTPAPAPEVmkpiaSPANSPAEIYTDSPvasPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSA 106
Cdd:PLN02217 578 ASSNTTFSSDSPSTVV-----APSTSPPAGHLGSP---PATPSKIVSPSTSPPASHLGSPSTTPSSPESSIKVASTETAS 649

                         90
                 ....*....|....
gi 22330888  107 APSGIKVSSSPKSL 120
Cdd:PLN02217 650 PESSIKVASTESSV 663
 
Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 127-263 2.65e-45

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: 149.05  E-value: 2.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 127 SPEIKTICGKTDNPPLCESSVSPLLTpQLKPNTSSVLILAIQASITATKAAMAIVEKVDAS------------DCQELYD 194
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPFLT-KGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSpstspevksaldVCKESYD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330888 195 DAVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGEPNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:cd15800  80 DALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 130-259 1.84e-31

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: 113.62  E-value: 1.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    130 IKTICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASITATKAAMAIV-----------EKVDASDCQELYDDAVV 198
Cdd:smart00856   7 IDSICKSTDYPDFCVSSLSSDPSSS-ATDPKDLAKIAIKVALSQATKTLSFIskllkktkdprLKAALKDCLELYDDAVD 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330888    199 NLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEE--SGEPNPLAYVADKLTKMVSNCLAI 259
Cdd:smart00856  86 SLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEEndDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 130-259 8.28e-27

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: 101.47  E-value: 8.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   130 IKTICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASITATKAAMAIVEKVDAS------------DCQELYDDAV 197
Cdd:pfam04043   3 IKTACKKTPYPDLCVSSLSSDPASA-ASPPKGLAKAAVNVALSNATSALSFISKLLKKskksakdkaaleDCLELYDDAV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330888   198 VNLEDAVNAVKSSD--IATVNTNLSAAMTDYSTCNDGFEESGEP---NPLAYVADKLTKMVSNCLAI 259
Cdd:pfam04043  82 DELNRALDALKAGDssRDDAQTWLSAALTNQDTCEDGFKEAVKGqlkSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 130-263 3.69e-20

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


Pssm-ID: 273717 [Multi-domain]  Cd Length: 178  Bit Score: 84.78  E-value: 3.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   130 IKTICGKTDNPPLCESSvsplLTPQLKPNTSSVLILA-IQASITATKAAMAI-------------VEKVDASDCQELYDD 195
Cdd:TIGR01614  32 IKRICKKTEYPNFCIST----LKSDPSSAKADLQGLAnISVSAALSNASDTLdhiskllltkgdpRDKSALEDCVELYSD 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   196 AVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGE--PNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:TIGR01614 108 AVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGivKSPLTKRNNNVKKLSSITLAIIKML 177
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 112-259 1.90e-10

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 60.69  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  112 KVSSSPKSLLNPPllSPEIKTICGKTDNPPLCESSVspLLTPQLKPNTSSVLI------------LAIQASITATKAAMA 179
Cdd:PLN02484  60 SGQTSPKSLHRKP--TQAISKTCSKTRFPNLCVDSL--LDFPGSLTASESDLIhisfnmtlqhfsKALYLSSTISYVQMP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  180 IVEKVDASDCQELYDDAVVNLEDAVNAVKSS----DIATVNTNLSAAMTDYSTCNDGFEE---SGEPNPLAYVADKLTKM 252
Cdd:PLN02484 136 PRVRSAYDSCLELLDDSVDALSRALSSVVPSsgggSPQDVVTWLSAALTNHDTCTEGFDGvngGEVKDQMTGALKDLSEL 215


                 ....*..
gi 22330888  253 VSNCLAI 259
Cdd:PLN02484 216 VSNCLAI 222
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 27-120 1.42e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 45.85  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   27 SRSDSPFSTPAPAPEVmkpiaSPANSPAEIYTDSPvasPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSA 106
Cdd:PLN02217 578 ASSNTTFSSDSPSTVV-----APSTSPPAGHLGSP---PATPSKIVSPSTSPPASHLGSPSTTPSSPESSIKVASTETAS 649

                         90
                 ....*....|....
gi 22330888  107 APSGIKVSSSPKSL 120
Cdd:PLN02217 650 PESSIKVASTESSV 663
 
Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 127-263 2.65e-45

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: 149.05  E-value: 2.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 127 SPEIKTICGKTDNPPLCESSVSPLLTpQLKPNTSSVLILAIQASITATKAAMAIVEKVDAS------------DCQELYD 194
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPFLT-KGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSpstspevksaldVCKESYD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330888 195 DAVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGEPNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:cd15800  80 DALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 130-259 1.84e-31

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: 113.62  E-value: 1.84e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    130 IKTICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASITATKAAMAIV-----------EKVDASDCQELYDDAVV 198
Cdd:smart00856   7 IDSICKSTDYPDFCVSSLSSDPSSS-ATDPKDLAKIAIKVALSQATKTLSFIskllkktkdprLKAALKDCLELYDDAVD 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22330888    199 NLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEE--SGEPNPLAYVADKLTKMVSNCLAI 259
Cdd:smart00856  86 SLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEEndDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 130-259 8.28e-27

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: 101.47  E-value: 8.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   130 IKTICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASITATKAAMAIVEKVDAS------------DCQELYDDAV 197
Cdd:pfam04043   3 IKTACKKTPYPDLCVSSLSSDPASA-ASPPKGLAKAAVNVALSNATSALSFISKLLKKskksakdkaaleDCLELYDDAV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22330888   198 VNLEDAVNAVKSSD--IATVNTNLSAAMTDYSTCNDGFEESGEP---NPLAYVADKLTKMVSNCLAI 259
Cdd:pfam04043  82 DELNRALDALKAGDssRDDAQTWLSAALTNQDTCEDGFKEAVKGqlkSSMKSPLRNLTKLTSNALAI 148
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 132-259 9.99e-21

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: 85.57  E-value: 9.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 132 TICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASITATKAAMAIV------------EKVDASDCQELYDDAVVN 199
Cdd:cd15798   1 AICSSTPYPDLCKSSLSSYASSS-STDPKELAKAALNAALDEAKKALALLssllkssgsnprEKAALEDCLELLDDAVDD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330888 200 LEDAVNAVKSSD-------IATVNTNLSAAMTDYSTCNDGFEESGEPNPLAYVA--DKLTKMVSNCLAI 259
Cdd:cd15798  80 LNRSLSELNSLSkdkfserVDDVQTWLSAALTNQDTCLDGFEETGSTVKKELRAslKNVSKLTSNALAL 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 130-263 3.69e-20

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


Pssm-ID: 273717 [Multi-domain]  Cd Length: 178  Bit Score: 84.78  E-value: 3.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   130 IKTICGKTDNPPLCESSvsplLTPQLKPNTSSVLILA-IQASITATKAAMAI-------------VEKVDASDCQELYDD 195
Cdd:TIGR01614  32 IKRICKKTEYPNFCIST----LKSDPSSAKADLQGLAnISVSAALSNASDTLdhiskllltkgdpRDKSALEDCVELYSD 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   196 AVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGE--PNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:TIGR01614 108 AVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGivKSPLTKRNNNVKKLSSITLAIIKML 177
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 130-263 2.18e-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: 71.21  E-value: 2.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 130 IKTICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASIT-ATKAAMAIVEKVDA----------SDCQELYDDAVV 198
Cdd:cd15801   2 IEEACKKTLDPDLCVSALSSDPESK-KADLRGLAELALKAAAEnATATASYVSELLNTakdpyvqqclEDCSENYEDAVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330888 199 NLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEE-SGEPNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:cd15801  81 QLNDSLAALDSKAYGDVKTWVTAALADAETCEDAFKEkPGDKSPLTARNGDFSKLCSIALAIIKLL 146
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 134-262 3.71e-15

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: 70.54  E-value: 3.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 134 CGKTDNPPLCESSVSPlltpqlKPNTS----------SVLILAIQASITATKAAMAIVEKVDA------SDCQELYDDAV 197
Cdd:cd14859   1 CKKTSYYKLCVSSLSS------DPRSStadlkglaniALDAALANASDTQAFIAKLLKSTKDPalkkalRDCADDYDDAV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22330888 198 VNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGE-PNPLAYVADKLTKMVSNCLAISTL 262
Cdd:cd14859  75 DDLEDAINALLSGDYDDAKTHVSAALDDADTCEEAFKESSGlPSPLTTRNDDLKRLCSIALAIILL 140
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 129-263 1.87e-12

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: 63.21  E-value: 1.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 129 EIKTICGKTDNPPLCESsvspLLTPQLKPNTSSVLILA--------IQASITATKAAMAIVEKVDA------SDCQELYD 194
Cdd:cd15797   4 LIDTICKKTENPSFCLQ----ILNSDPRSASADLVGLAqiaidlaqSNATNTLKLIQSLIKSTTDPklknryESCSKNYN 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 195 DAVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFE-ESGEPNPLAYVADKLTKMVSNCLAISTLI 263
Cdd:cd15797  80 DAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSkPPKDPSPLAKYNRDVEDLCDIILVISDLL 149
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 158-259 4.21e-11

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: 59.69  E-value: 4.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 158 NTSSVLILAIQASITATKAAMAIVEKVDAS------------DCQELYDDAVVNLEDAVNAVKSSDIATVNTNLSAAMTD 225
Cdd:cd15795  31 DLKGLAVIATKLAIANATATKAKIEKLLKSkkypsdlkkalrDCLSLYSDAVDSLKSALDALKSGDYGDANYDLSAATDA 110

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22330888 226 YSTCNDGFEESG-EPNPLAYVADKLTKMVSNCLAI 259
Cdd:cd15795 111 PVTCEDAFKEAKiVVSPLTKENDELFQLALIALAI 145
PMEI-like_4 cd15799
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ...
 142-259 1.42e-10

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: 58.19  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888 142 LCESSVSPLLTPQLKPNTSSVLILAIQASITATKAAMAIV-----------EKVDASDCQELYD---DAVVNLEDAVNAV 207
Cdd:cd15799  14 PSVSSSANALSAQCLKVPLDVFLAALKTTVDRIQSALSMVsklrngsddprLSNALSDCLELLDfsaDRLSWSLSALQNP 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 22330888 208 KSSDIATVNTNLSAAMTDYSTCNDGFEESGEPNPL-AYVADKLTKMVSNCLAI 259
Cdd:cd15799  94 KGDSGSDARTWLSAALTNHDTCLDGLEETGVVKSLvAAALSNLTSLLREALAM 146
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 112-259 1.90e-10

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 60.69  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  112 KVSSSPKSLLNPPllSPEIKTICGKTDNPPLCESSVspLLTPQLKPNTSSVLI------------LAIQASITATKAAMA 179
Cdd:PLN02484  60 SGQTSPKSLHRKP--TQAISKTCSKTRFPNLCVDSL--LDFPGSLTASESDLIhisfnmtlqhfsKALYLSSTISYVQMP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  180 IVEKVDASDCQELYDDAVVNLEDAVNAVKSS----DIATVNTNLSAAMTDYSTCNDGFEE---SGEPNPLAYVADKLTKM 252
Cdd:PLN02484 136 PRVRSAYDSCLELLDDSVDALSRALSSVVPSsgggSPQDVVTWLSAALTNHDTCTEGFDGvngGEVKDQMTGALKDLSEL 215


                 ....*..
gi 22330888  253 VSNCLAI 259
Cdd:PLN02484 216 VSNCLAI 222
PLN02314 PLN02314
pectinesterase
 123-263 2.10e-09

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 57.53  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  123 PPLLSP--EIKTICGKTDNPPLCESSVSPLLTPQlKPNTSSVLILAIQASITATKAAMAIVEKVDAS-----------DC 189
Cdd:PLN02314  64 PPELTPatSLKAVCSVTRYPESCISSISSLPTSN-TTDPETLFKLSLKVAIDELSKLSDLPQKLINEtnderlksalrVC 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  190 QELYDDAVVNLEDAVNAVK---------SSDIATVNTNLSAAMTDYSTCNDGFEESGEP--------NPLAYVADKLTKM 252
Cdd:PLN02314 143 ETLFDDAIDRLNDSISSMQvgegekilsSSKIDDLKTWLSATITDQETCIDALQELSQNkyanstltNEVKTAMSNSTEF 222

                        170
                 ....*....|.
gi 22330888  253 VSNCLAISTLI 263
Cdd:PLN02314 223 TSNSLAIVSKI 233
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 102-262 2.54e-09

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 57.17  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  102 ESSSAAPSGIKVSSSPKSLLNPPLLSPEIKTICGKTDNPPLCESSVSPLL---TPQLKPntSSVLILAIQASITATKAAM 178
Cdd:PLN02745  54 QNQSGNGNNSSKDSPVKSESPVSQVDKIIQTVCNATLYKQTCENTLKKGTekdPSLAQP--KDLLKSAIKAVNDDLDKVL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  179 AIV---------EKVDASDCQELYDDAVVNLEDAVNAVK------SSDIATVNTNLSAAMTDYSTCNDGFEESGEPNPLA 243
Cdd:PLN02745 132 KKVlsfkfenpdEKDAIEDCKLLVEDAKEELKASISRINdevnklAKNVPDLNNWLSAVMSYQETCIDGFPEGKLKSEME 211

                        170       180
                 ....*....|....*....|
gi 22330888  244 YVADKLTKMVSNCLA-ISTL 262
Cdd:PLN02745 212 KTFKSSQELTSNSLAmVSSL 231
PLN02506 PLN02506
putative pectinesterase/pectinesterase inhibitor
 113-261 1.27e-07

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 215280 [Multi-domain]  Cd Length: 537  Bit Score: 52.24  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  113 VSSSPKSLLNPPLLspeIKTICGKTDNPPLCESSVSPLLTPQLKPNTSSVLILAIQASITATKAAMAIVEKVDA------ 186
Cdd:PLN02506  23 TSSSPYQELNFQAL---IAQACQFVENHSSCVSNIQAELKKSGPRTPHSVLSAALKATLDEARLAIDMITKFNAlsisyr 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  187 -----SDCQELYDDAVVNLEDAV---NAVKSSDIAT-----VNTNLSAAMTDYSTCNDGFE--ESGEPNPLAYVADKLTK 251
Cdd:PLN02506 100 eqvaiEDCKELLDFSVSELAWSLlemNKIRAGHDNVayegnLKAWLSAALSNQDTCLEGFEgtDRHLENFIKGSLKQVTQ 179

                        170
                 ....*....|
gi 22330888  252 MVSNCLAIST 261
Cdd:PLN02506 180 LISNVLAMYT 189
PLN02468 PLN02468
putative pectinesterase/pectinesterase inhibitor
 126-263 1.92e-07

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178087 [Multi-domain]  Cd Length: 565  Bit Score: 51.42  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  126 LSPEIKTICGKTDNPPLCESSVSPLLTP-QLKPntSSVLILAIQASIT---------------------ATKAAMaivek 183
Cdd:PLN02468  63 ISTSVKAVCDVTLYKDSCYETLAPAPKAsQLQP--EELFKYAVKVAINelskasqafsnsegflgvkdnMTNAAL----- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  184 vdaSDCQELYDDAVVNLEDAVNAVKSSDIATV----NTNLSAAMTDYSTCNDGFEesgEPNPLAYVADKL---TKMVSNC 256
Cdd:PLN02468 136 ---NACQELLDLAIDNLNNSLTSSGGVSVLDNvddlRTWLSSAGTYQETCIDGLA---EPNLKSFGENHLknsTELTSNS 209


                 ....*..
gi 22330888  257 LAISTLI 263
Cdd:PLN02468 210 LAIITWI 216
PLN02416 PLN02416
probable pectinesterase/pectinesterase inhibitor
 114-259 4.14e-07

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178037 [Multi-domain]  Cd Length: 541  Bit Score: 50.70  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  114 SSSPKSLLNPPLLSpeIKTICGKTDNPPLCESSVSPLLTPQLKPNTSSVLILAIQASIT-ATK---------AAMAIVEK 183
Cdd:PLN02416  27 NASYTTSLDPHLSS--LTSFCKSTPYPDACFDSLKLSISINISPNILNFLLQTLQTAISeAGKltnllsgagQSSNIIEK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  184 VDAS--DCQELYDDAVVNLEDAVNAVKSSD---IATVNTNLSAAMTDYSTCNDGFEESGEPNPLAYVADKLT--KMVSNC 256
Cdd:PLN02416 105 QRGTiqDCKELHQITVSSLKRSVSRIQAGDsrkLADARAYLSAALTNKNTCLEGLDSASGPLKPKLVNSFTStyKHVSNS 184


                 ...
gi 22330888  257 LAI 259
Cdd:PLN02416 185 LSM 187
PLN02933 PLN02933
Probable pectinesterase/pectinesterase inhibitor
 188-240 2.73e-06

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178521 [Multi-domain]  Cd Length: 530  Bit Score: 48.08  E-value: 2.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22330888  188 DCQELYDDAVVNLEDAVNAVKSS--DIATVNTNLSAAMTDYSTCNDGFEESGEPN 240
Cdd:PLN02933  94 DCLGLLDDTISDLTTAISKLRSSspEFNDVSMLLSNAMTNQDTCLDGFSTSDNEN 148
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 27-120 1.42e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 45.85  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   27 SRSDSPFSTPAPAPEVmkpiaSPANSPAEIYTDSPvasPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSA 106
Cdd:PLN02217 578 ASSNTTFSSDSPSTVV-----APSTSPPAGHLGSP---PATPSKIVSPSTSPPASHLGSPSTTPSSPESSIKVASTETAS 649

                         90
                 ....*....|....
gi 22330888  107 APSGIKVSSSPKSL 120
Cdd:PLN02217 650 PESSIKVASTESSV 663
PHA03247 PHA03247
large tegument protein UL36; Provisional
 27-153 5.15e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    27 SRSDSPFSTPAPAPEVMK--------PIASPANSPAEIYTDSPVASPEAPADSFSPKNPPVEIDIYSPAASpeAPVASPE 98
Cdd:PHA03247 2699 ADPPPPPPTPEPAPHALVsatplppgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP--APPAAPA 2776

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 22330888    99 APAESSSAAPSGIKVSSSPKSLLNPPLLSPEIKTICGKTDNPPLCESSVSPLLTP 153
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 25-110 7.07e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   25 VESRSDSPFSTPAPAPEVMKPIASPANSPAEIYTDSPVASPEAPADSfSPKNPPVEIDIYSPAASPEAPVASPEAPAESS 104
Cdd:PRK07764 420 AAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP-APAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498


                 ....*.
gi 22330888  105 SAAPSG 110
Cdd:PRK07764 499 APAAPA 504
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 35-117 7.41e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   35 TPAPAPeVMKPIASPANSPAEIYTDSPVASPEAPADSfSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSAAPSGIKVS 114
Cdd:PRK14951 388 APAAAP-VAQAAAAPAPAAAPAAAASAPAAPPAAAPP-APVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVR 465


                 ...
gi 22330888  115 SSP 117
Cdd:PRK14951 466 VAP 468
PLN02916 PLN02916
pectinesterase family protein
 187-259 7.87e-04

pectinesterase family protein


Pssm-ID: 178504 [Multi-domain]  Cd Length: 502  Bit Score: 40.33  E-value: 7.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22330888  187 SDCQELYDDAVVNLEDAVNAVKSSDIATVNTNLSAAMTDYSTCNDGFEESGEPN-PLAYvadKLTKMVSNCLAI 259
Cdd:PLN02916  66 SDCEKLYDESEARLSKLLVSHENFTVEDARTWLSGVLANHHTCLDGLEQKGQGHkPMAH---NVTFVLSEALAL 136
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-157 8.14e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    25 VESRSDSPFSTPAPAPEVMKPIASPANSPAEIYTDSPvASPEAPADSFSPKNPPVEIDIYSPAASPE------------- 91
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP-AGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvapggdvrrrp 2866

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330888    92 ---APVASPEAPAESSSAAPSGIKVSSSPKSLLNPPLLSPEIKTICGKTDNPPLCESSVSPLLTPQLKP 157
Cdd:PHA03247 2867 psrSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
PHA03247 PHA03247
large tegument protein UL36; Provisional
 14-161 1.21e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    14 TVSILVTISTHVESRSDSPFSTPAPAPEvmkpiaSPANSPAEIYTDSPVASPEAPADSFSPKNPPVEIDIYSPAAS-PEA 92
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPAAPAPP------AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrPAV 2788

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22330888    93 PVASPEAPAESSSAAPSGIKVSSSPKSLLNPPLLSPeikticGKTDNPPLCESSVSPLLTPQLKPNTSS 161
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP------AGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
PHA03247 PHA03247
large tegument protein UL36; Provisional
 32-129 1.62e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    32 PFSTPAPAPEVMKPIASPANSPAEIYTDSPVASPEAPADSFSPKNPpveIDIYSPAASPEAPVASPEAPAESSSAAPSGI 111
Cdd:PHA03247 2556 PPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAP---VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS 2632

                          90
                  ....*....|....*...
gi 22330888   112 KVSSSPKSLLNPPLLSPE 129
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPE 2650
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 44-149 2.07e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.29  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   44 KPIASPANSPAEIYTDSpvASPEAPADSFSPKNPPVEIDIYSPAaSPEAPVASPEAPAESSSAAPSGIKVSSSPKSLLNP 123
Cdd:PTZ00449 560 KPGPAKEHKPSKIPTLS--KKPEFPKDPKHPKDPEEPKKPKRPR-SAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRP 636

                         90       100
                 ....*....|....*....|....*.
gi 22330888  124 PllSPEIKTICGKTDNPPLCESSVSP 149
Cdd:PTZ00449 637 P--PPQRPSSPERPEGPKIIKSPKPP 660
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 34-130 2.56e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   34 STPAPAPEvmkpiASPANSPAEIYTDSPVASPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSAAPSGIKV 113
Cdd:PRK14951 379 KTPARPEA-----AAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPA 453

                         90
                 ....*....|....*..
gi 22330888  114 SSSPKSLLNPPLLSPEI 130
Cdd:PRK14951 454 QAAPETVAIPVRVAPEP 470
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 31-110 3.82e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 38.72  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    31 SPFSTPAPAPEVMKPIASPANSPAEIYTDSPVASPEAPADSFSPKNPPveidiySPAASPEAPVASPEAPAESSSAAPSG 110
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPP------KPAAAAAAAAAPAAPPAAAAAAAPAA 110
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 28-117 4.00e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 38.33  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    28 RSDSPFSTPAPAPEVMKPIASPANSPAEIYTDSPVASPEAPADSFSPKNPpveidiySPAASPEAPVASPEAPAESSSAA 107
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKP-------AAAAAAAAAPAAPPAAAAAAAPA 109

                          90
                  ....*....|
gi 22330888   108 PSGIKVSSSP 117
Cdd:PRK12270  110 AAAVEDEVTP 119
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
25-109 4.27e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 38.32  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   25 VESRSDSPFSTPAPAPEVMKPIASPANSPAEIytdSPVASPEAPADSFSPKNP-----PVEIDIYSPAASPEAPVASPEA 99
Cdd:PRK12323 395 AAPAPAAPPAAPAAAPAAAAAARAVAAAPARR---SPAPEALAAARQASARGPggapaPAPAPAAAPAAAARPAAAGPRP 471

                         90
                 ....*....|
gi 22330888  100 PAESSSAAPS 109
Cdd:PRK12323 472 VAAAAAAAPA 481
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
25-109 5.71e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 37.91  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   25 VESRSDSPFSTPAPAPEVMKPIASPANSPAEiytdspvASPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESS 104
Cdd:PRK07003 459 ADSRCDERDAQPPADSGSASAPASDAPPDAA-------FEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPE 531


                 ....*
gi 22330888  105 SAAPS 109
Cdd:PRK07003 532 ARPPT 536
PLN02995 PLN02995
Probable pectinesterase/pectinesterase inhibitor
 127-260 7.51e-03

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178574 [Multi-domain]  Cd Length: 539  Bit Score: 37.35  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888  127 SPEIKTICGKTDNPPLCESSVSPLLTPQLKPNTSSVLILAIQASITATKAAMA-----------IVEKVDASDCQELYDD 195
Cdd:PLN02995  34 STDIDGWCDKTPYPDPCKCYFKNHNGFRQPTQISEFRVMLVEAAMDRAISARDeltnsgknctdFKKQAVLADCIDLYGD 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22330888  196 AVVNLEDAVNAVKSSDIAT-------VNTNLSAAMTDYSTCNDG---FEESGEPNPLAyVADKLTKMVSNCLAIS 260
Cdd:PLN02995 114 TIMQLNRTLQGVSPKAGAAkrctdfdAQTWLSTALTNTETCRRGssdLNVSDFITPIV-SNTKISHLISNCLAVN 187
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 29-109 7.53e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 37.66  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888   29 SDSPFSTPAPAPEVMKPIASPANSPAEIYTDSPVASPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSAAP 108
Cdd:PRK07764 405 APAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAP 484


                 .
gi 22330888  109 S 109
Cdd:PRK07764 485 P 485
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 35-124 9.19e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 37.46  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330888    35 TPAPAPEVMKPIASPANSPAEIY-TDSPVASPEAPADSFSPKNPPVEIDIYSPAASPEAPVASPEAPAESSSAAPSGIKV 113
Cdd:PHA03307   96 APASPAREGSPTPPGPSSPDPPPpTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP 175

                          90
                  ....*....|.
gi 22330888   114 SSSPKSLLNPP 124
Cdd:PHA03307  176 LSSPEETARAP 186
 
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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