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Conserved domains on  [gi|118197955|gb|ABK78766|]
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major allergen Cup a 1, partial [Hesperocyparis arizonica]

Protein Classification

polysaccharide lyase family 1 protein( domain architecture ID 10652760)

polysaccharide lyase family 1 protein such as pectate lyase that catalyzes the eliminative cleavage of pectate to yield oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at the non-reducing ends, and pectin lyase that catalyzes the eliminative cleavage of the methyl ester pectin

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
76-273 4.33e-72

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 222.15  E-value: 4.33e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955    76 NMNIKLQM--PLYVNGYKTIDGRGADVHLGNGGpcLFMRKASHVILHGLHIHGCNtsvlgdvlvsesigvePVHAQDGDA 153
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGGG--LTIKSVSNVIIRNLTIHDPK----------------PVYGSDGDA 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955   154 ITMRNVTNAWIDHNSLSDC---------SDGLIDVTLGSTGITISNNHFFNHHKVMLLGHDDTYDDDKSMKVTVAFNQFG 224
Cdd:smart00656  63 ISIDGSSNVWIDHVSLSGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 118197955   225 pNAGQRMPRARYGLVHVANNNYDQWNIYAIGGSSNPTILSEGNSFTAPN 273
Cdd:smart00656 143 -NLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
76-273 4.33e-72

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 222.15  E-value: 4.33e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955    76 NMNIKLQM--PLYVNGYKTIDGRGADVHLGNGGpcLFMRKASHVILHGLHIHGCNtsvlgdvlvsesigvePVHAQDGDA 153
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGGG--LTIKSVSNVIIRNLTIHDPK----------------PVYGSDGDA 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955   154 ITMRNVTNAWIDHNSLSDC---------SDGLIDVTLGSTGITISNNHFFNHHKVMLLGHDDTYDDDKSMKVTVAFNQFG 224
Cdd:smart00656  63 ISIDGSSNVWIDHVSLSGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 118197955   225 pNAGQRMPRARYGLVHVANNNYDQWNIYAIGGSSNPTILSEGNSFTAPN 273
Cdd:smart00656 143 -NLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
27-270 1.03e-48

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 166.32  E-value: 1.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955  27 VGFGS---STMGGKGGEIYTVTSSEDnpvnptpgtLRYGATREKALWIIFSQNMNIKlQMPLYVNGYKTIDGRGADVHLG 103
Cdd:COG3866   36 EGFASvngGTTGGAGGTVVTVTTLAD---------LRAALEASGPRIIVVSGTIDLS-KSPLKVNSNKTIAGQGDGATIT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955 104 NGGpcLFMRKASHVILHGLHIHGCNTSVlgdvlvsesigvepvhAQDGDAITMRNVTNAWIDHNSLSDCSDGLIDVTLGS 183
Cdd:COG3866  106 GGG--LNIKGASNVIIRNLRFRNGDDGG----------------GSGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955 184 TGITISNNHFF----NHHKVMLLGHDDTYDDDKSmKVTVAFNQFGpNAGQRMPRARYGLVHVANNNYDQW-NIYAIGGSS 258
Cdd:COG3866  168 DNVTVSWNIFAegkgDHGKGMLIGSSDSDTTGKL-RVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                        250
                 ....*....|..
gi 118197955 259 NPTILSEGNSFT 270
Cdd:COG3866  246 GAQVLVENNYFE 257
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 141-269 2.36e-23

Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.


Pssm-ID: 366158  Cd Length: 211  Bit Score: 96.12  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955  141 IGVEPVHAQDGDAITMRNVTNAWIDHNSLSDCS-------------DGLIDVTLGSTGITISNNHFFNHHKVMLLGHDDT 207
Cdd:pfam00544  69 IGTPDGWNKDWDAIRIDNSPNVWVDHVTISDGSftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDD 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118197955  208 YD--DDKSMKVTVAFNQFGpNAGQRMPRARYGLVHVANNNYDQWNIYAIGGSSNPTILSEGNSF 269
Cdd:pfam00544 149 NNsqDTGKLRVTYHHNVYN-RVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
76-273 4.33e-72

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 222.15  E-value: 4.33e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955    76 NMNIKLQM--PLYVNGYKTIDGRGADVHLGNGGpcLFMRKASHVILHGLHIHGCNtsvlgdvlvsesigvePVHAQDGDA 153
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGGG--LTIKSVSNVIIRNLTIHDPK----------------PVYGSDGDA 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955   154 ITMRNVTNAWIDHNSLSDC---------SDGLIDVTLGSTGITISNNHFFNHHKVMLLGHDDTYDDDKSMKVTVAFNQFG 224
Cdd:smart00656  63 ISIDGSSNVWIDHVSLSGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG 142

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 118197955   225 pNAGQRMPRARYGLVHVANNNYDQWNIYAIGGSSNPTILSEGNSFTAPN 273
Cdd:smart00656 143 -NLRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
27-270 1.03e-48

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 166.32  E-value: 1.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955  27 VGFGS---STMGGKGGEIYTVTSSEDnpvnptpgtLRYGATREKALWIIFSQNMNIKlQMPLYVNGYKTIDGRGADVHLG 103
Cdd:COG3866   36 EGFASvngGTTGGAGGTVVTVTTLAD---------LRAALEASGPRIIVVSGTIDLS-KSPLKVNSNKTIAGQGDGATIT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955 104 NGGpcLFMRKASHVILHGLHIHGCNTSVlgdvlvsesigvepvhAQDGDAITMRNVTNAWIDHNSLSDCSDGLIDVTLGS 183
Cdd:COG3866  106 GGG--LNIKGASNVIIRNLRFRNGDDGG----------------GSGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955 184 TGITISNNHFF----NHHKVMLLGHDDTYDDDKSmKVTVAFNQFGpNAGQRMPRARYGLVHVANNNYDQW-NIYAIGGSS 258
Cdd:COG3866  168 DNVTVSWNIFAegkgDHGKGMLIGSSDSDTTGKL-RVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                        250
                 ....*....|..
gi 118197955 259 NPTILSEGNSFT 270
Cdd:COG3866  246 GAQVLVENNYFE 257
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 141-269 2.36e-23

Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.


Pssm-ID: 366158  Cd Length: 211  Bit Score: 96.12  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118197955  141 IGVEPVHAQDGDAITMRNVTNAWIDHNSLSDCS-------------DGLIDVTLGSTGITISNNHFFNHHKVMLLGHDDT 207
Cdd:pfam00544  69 IGTPDGWNKDWDAIRIDNSPNVWVDHVTISDGSftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDD 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118197955  208 YD--DDKSMKVTVAFNQFGpNAGQRMPRARYGLVHVANNNYDQWNIYAIGGSSNPTILSEGNSF 269
Cdd:pfam00544 149 NNsqDTGKLRVTYHHNVYN-RVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
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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