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Conserved domains on  [gi|1280990763|ref|XP_022978930|]
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probable pectate lyase 12 [Cucurbita maxima]

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

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List of domain hits

 Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
149-343 1.48e-75

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 235.25  E-value: 1.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  149 NMLIKLKQ--ELIFNSYKTLDGRGANVHIVGGGcITLQYISNVIIHNIHIHHCYPSGntmvrsspthygyrtKSDGDGIS 226
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGGG-LTIKSVSNVIIRNLTIHDPKPVY---------------GSDGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  227 IFGSKDVWIDHCSLSHCK---------DGLIDAVMGSTGITISNNYFSHHDEVMLLGHSDSYLPDSGMQVTIAFNHFGeK 297
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1280990763  298 LVQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGSPTINSQGNRYTAP 343
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
149-343 1.48e-75

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 235.25  E-value: 1.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  149 NMLIKLKQ--ELIFNSYKTLDGRGANVHIVGGGcITLQYISNVIIHNIHIHHCYPSGntmvrsspthygyrtKSDGDGIS 226
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGGG-LTIKSVSNVIIRNLTIHDPKPVY---------------GSDGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  227 IFGSKDVWIDHCSLSHCK---------DGLIDAVMGSTGITISNNYFSHHDEVMLLGHSDSYLPDSGMQVTIAFNHFGeK 297
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1280990763  298 LVQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGSPTINSQGNRYTAP 343
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
98-414 6.77e-47

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 165.16  E-value: 6.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  98 AIGFGQY---ALGGKNGEFYIVTDDSDddavnpkpgtLRYAVIQPQPLWIVFpaNMLIKL-KQELIFNSYKTLDGRGANV 173
Cdd:COG3866    35 PEGFASVnggTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 174 HIVGGGcITLQYISNViihnihihhcypsgntMVRSSPTHYGYRTKSDG-DGISIFGSKDVWIDHCSLSHCKDGLIDAVM 252
Cdd:COG3866   103 TITGGG-LNIKGASNV----------------IIRNLRFRNGDDGGGSGgDAIGIEGAHNVWIDHCTFSWGYDGLLDIKR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 253 GSTGITISNNYFS----HHDEVMLLGHSDSYlPDSGMQVTIAFNHFgEKLVQRMPRCRRGYIHVVNNDFTQW-EMYAIGG 327
Cdd:COG3866   166 GSDNVTVSWNIFAegkgDHGKGMLIGSSDSD-TTGKLRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 328 SGSPTINSQGNRYtapydRNAKEVTKRVETSESEWRGwNWRSDGDILVN--GAFFVTSGQGLEVKYEkaYSVEPKSvALI 405
Cdd:COG3866   244 GGGAQVLVENNYF-----ENVKGPLATSDGSSLLDPG-YLYARGNVFDNstGTAPAGSGTVFTPPYS--YTLDPAS-DVK 314


                  ....*....
gi 1280990763 406 DQLTWHAGP 414
Cdd:COG3866   315 TLVLAGAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 202-338 5.77e-20

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: 88.03  E-value: 5.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 202 SGNTMVRSSPTHYGYRTKSDGDGISIFGSKDVWIDHCSLSHCK-------------DGLIDAVMGSTGITISNNYFSHHD 268
Cdd:pfam00544  59 SSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWVDHVTISDGSftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHK 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280990763 269 EVMLLGHSDSYLP-DSG-MQVTIAFNHFgEKLVQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGSPTINSQGN 338
Cdd:pfam00544 139 KTGLIGHSDDNNSqDTGkLRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
149-343 1.48e-75

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 235.25  E-value: 1.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  149 NMLIKLKQ--ELIFNSYKTLDGRGANVHIVGGGcITLQYISNVIIHNIHIHHCYPSGntmvrsspthygyrtKSDGDGIS 226
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGGG-LTIKSVSNVIIRNLTIHDPKPVY---------------GSDGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  227 IFGSKDVWIDHCSLSHCK---------DGLIDAVMGSTGITISNNYFSHHDEVMLLGHSDSYLPDSGMQVTIAFNHFGeK 297
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1280990763  298 LVQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGSPTINSQGNRYTAP 343
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
98-414 6.77e-47

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 165.16  E-value: 6.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763  98 AIGFGQY---ALGGKNGEFYIVTDDSDddavnpkpgtLRYAVIQPQPLWIVFpaNMLIKL-KQELIFNSYKTLDGRGANV 173
Cdd:COG3866    35 PEGFASVnggTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 174 HIVGGGcITLQYISNViihnihihhcypsgntMVRSSPTHYGYRTKSDG-DGISIFGSKDVWIDHCSLSHCKDGLIDAVM 252
Cdd:COG3866   103 TITGGG-LNIKGASNV----------------IIRNLRFRNGDDGGGSGgDAIGIEGAHNVWIDHCTFSWGYDGLLDIKR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 253 GSTGITISNNYFS----HHDEVMLLGHSDSYlPDSGMQVTIAFNHFgEKLVQRMPRCRRGYIHVVNNDFTQW-EMYAIGG 327
Cdd:COG3866   166 GSDNVTVSWNIFAegkgDHGKGMLIGSSDSD-TTGKLRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 328 SGSPTINSQGNRYtapydRNAKEVTKRVETSESEWRGwNWRSDGDILVN--GAFFVTSGQGLEVKYEkaYSVEPKSvALI 405
Cdd:COG3866   244 GGGAQVLVENNYF-----ENVKGPLATSDGSSLLDPG-YLYARGNVFDNstGTAPAGSGTVFTPPYS--YTLDPAS-DVK 314


                  ....*....
gi 1280990763 406 DQLTWHAGP 414
Cdd:COG3866   315 TLVLAGAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 202-338 5.77e-20

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: 88.03  E-value: 5.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 202 SGNTMVRSSPTHYGYRTKSDGDGISIFGSKDVWIDHCSLSHCK-------------DGLIDAVMGSTGITISNNYFSHHD 268
Cdd:pfam00544  59 SSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWVDHVTISDGSftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHK 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280990763 269 EVMLLGHSDSYLP-DSG-MQVTIAFNHFgEKLVQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGSPTINSQGN 338
Cdd:pfam00544 139 KTGLIGHSDDNNSqDTGkLRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 218-317 9.06e-04

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 39.70  E-value: 9.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280990763 218 TKSDGDGISIFGSKDVWIDHCSLSHCKDGLIdAVMGSTGITISNNYFSHHDE--VMLLGHSDS---------------YL 280
Cdd:pfam13229  42 TNNGGDGIEISGSSNNTISNNTISNNGGGGI-ALRGSSNNLIENNTISNNGGagIYLSDSSNNtienniihnnggsgiVI 120

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1280990763 281 PDSGMQVTIAFNHF-GEKLVQRMPRCRRGYIHVVNNDF 317
Cdd:pfam13229 121 EDSSNNVTISNNTVtNNKGAGILIVGGSSNNTVENNTF 158
 
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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