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Conserved domains on  [gi|42565152|ref|NP_189065|]
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Pectate lyase family protein [Arabidopsis thaliana]

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;
178-373 4.90e-82

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.04  E-value: 4.90e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152    178 DMVIKLKQ--ELIMNSFKTIDARGANVHIANGaCITIQNITNVIVHGLHIHDCKrtgnvtvrsspsqagFRGTADGDAIN 255
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPK---------------PVYGSDGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152    256 IFGSSHIWIDHNSLSNCT---------DGLVDVVNGSTAITISNNHFTHHDEVMLLGHNDSYTRDKMMQVTVAYNHFGeG 326
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 42565152    327 LIQRMPRCRHGYFHVVNNDYTHWKMYAIGGSANPTINSQGNRFAAPK 373
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
178-373 4.90e-82

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.04  E-value: 4.90e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152    178 DMVIKLKQ--ELIMNSFKTIDARGANVHIANGaCITIQNITNVIVHGLHIHDCKrtgnvtvrsspsqagFRGTADGDAIN 255
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPK---------------PVYGSDGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152    256 IFGSSHIWIDHNSLSNCT---------DGLVDVVNGSTAITISNNHFTHHDEVMLLGHNDSYTRDKMMQVTVAYNHFGeG 326
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 42565152    327 LIQRMPRCRHGYFHVVNNDYTHWKMYAIGGSANPTINSQGNRFAAPK 373
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
129-442 1.74e-52

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 179.41  E-value: 1.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 129 GFGS---KAFGGRNGSYYVVTDHSDddvvnpkpgtLRHAVIQVEPLWIIFkrDMVIKL-KQELIMNSFKTIDARGANVHI 204
Cdd:COG3866  37 GFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGATI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 205 ANGAcITIQNITNVIVHGLHIHDCKRTGNvtvrsspsqagfrgtADGDAINIFGSSHIWIDHNSLSNCTDGLVDVVNGST 284
Cdd:COG3866 105 TGGG-LNIKGASNVIIRNLRFRNGDDGGG---------------SGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 285 AITISNNHF----THHDEVMLLGHNDSYTRDKmMQVTVAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-KMYAIGGSAN 359
Cdd:COG3866 169 NVTVSWNIFaegkGDHGKGMLIGSSDSDTTGK-LRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGGG 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 360 PTINSQGNRFAAPKNHSAKEVTKRLDTKGnewmewNWRSEKDLLVNGAFFTPSGEGASGdSQTLSLPAKPASMV-DAITA 438
Cdd:COG3866 247 AQVLVENNYFENVKGPLATSDGSSLLDPG------YLYARGNVFDNSTGTAPAGSGTVF-TPPYSYTLDPASDVkTLVLA 319

                ....
gi 42565152 439 SAGA 442
Cdd:COG3866 320 GAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
194-369 2.66e-22

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: 94.58  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152   194 TIDARGANVHIANGACITIQNITNVIVHglhihdckrtgNVTVRSSPSqagfrGTADGDAINIFGSSHIWIDHNSLSNCT 273
Cdd:pfam00544  38 IIGIIGTNGKFTNFGSLIIKGSSNVIVR-----------NLYIGTPDG-----WNKDWDAIRIDNSPNVWVDHVTISDGS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152   274 -------------DGLVDVVNGSTAITISNNHFTHHDEVMLLGHNDSY--TRDKMMQVTVAYNHFgEGLIQRMPRCRHGY 338
Cdd:pfam00544 102 ftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNnsQDTGKLRVTYHHNVY-NRVTERAPLVRYGS 180
                         170       180       190
                  ....*....|....*....|....*....|.
gi 42565152   339 FHVVNNDYTHWKMYAIGGSANPTINSQGNRF 369
Cdd:pfam00544 181 IHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
178-373 4.90e-82

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.04  E-value: 4.90e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152    178 DMVIKLKQ--ELIMNSFKTIDARGANVHIANGaCITIQNITNVIVHGLHIHDCKrtgnvtvrsspsqagFRGTADGDAIN 255
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPK---------------PVYGSDGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152    256 IFGSSHIWIDHNSLSNCT---------DGLVDVVNGSTAITISNNHFTHHDEVMLLGHNDSYTRDKMMQVTVAYNHFGeG 326
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 42565152    327 LIQRMPRCRHGYFHVVNNDYTHWKMYAIGGSANPTINSQGNRFAAPK 373
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
129-442 1.74e-52

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 179.41  E-value: 1.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 129 GFGS---KAFGGRNGSYYVVTDHSDddvvnpkpgtLRHAVIQVEPLWIIFkrDMVIKL-KQELIMNSFKTIDARGANVHI 204
Cdd:COG3866  37 GFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGATI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 205 ANGAcITIQNITNVIVHGLHIHDCKRTGNvtvrsspsqagfrgtADGDAINIFGSSHIWIDHNSLSNCTDGLVDVVNGST 284
Cdd:COG3866 105 TGGG-LNIKGASNVIIRNLRFRNGDDGGG---------------SGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 285 AITISNNHF----THHDEVMLLGHNDSYTRDKmMQVTVAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-KMYAIGGSAN 359
Cdd:COG3866 169 NVTVSWNIFaegkGDHGKGMLIGSSDSDTTGK-LRVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGGG 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 360 PTINSQGNRFAAPKNHSAKEVTKRLDTKGnewmewNWRSEKDLLVNGAFFTPSGEGASGdSQTLSLPAKPASMV-DAITA 438
Cdd:COG3866 247 AQVLVENNYFENVKGPLATSDGSSLLDPG------YLYARGNVFDNSTGTAPAGSGTVF-TPPYSYTLDPASDVkTLVLA 319

                ....
gi 42565152 439 SAGA 442
Cdd:COG3866 320 GAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
194-369 2.66e-22

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: 94.58  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152   194 TIDARGANVHIANGACITIQNITNVIVHglhihdckrtgNVTVRSSPSqagfrGTADGDAINIFGSSHIWIDHNSLSNCT 273
Cdd:pfam00544  38 IIGIIGTNGKFTNFGSLIIKGSSNVIVR-----------NLYIGTPDG-----WNKDWDAIRIDNSPNVWVDHVTISDGS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152   274 -------------DGLVDVVNGSTAITISNNHFTHHDEVMLLGHNDSY--TRDKMMQVTVAYNHFgEGLIQRMPRCRHGY 338
Cdd:pfam00544 102 ftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNnsQDTGKLRVTYHHNVY-NRVTERAPLVRYGS 180
                         170       180       190
                  ....*....|....*....|....*....|.
gi 42565152   339 FHVVNNDYTHWKMYAIGGSANPTINSQGNRF 369
Cdd:pfam00544 181 IHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
203-295 9.10e-05

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 44.52  E-value: 9.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152 203 HIANGACITIQNITNVIVHGLHIHDC------KRTGNVTVR-----SSPSQAGFRGtadgDAINIFGSSHIWIDHNSLSN 271
Cdd:COG3420  94 LTDDDAGIYVRGADNAVIENNRIENNlfgiylEGSDNNVIRnntisGNRDLRADRG----NGIHLWNSPGNVIEGNTISG 169
                        90       100
                ....*....|....*....|....
gi 42565152 272 CTDGLvdVVNGSTAITISNNHFTH 295
Cdd:COG3420 170 GRDGI--YLEFSDNNVIRNNTIRN 191
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
210-299 4.18e-03

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: 37.77  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152   210 ITIQNITNVIVHGLHIHDCKRTGnVTVRSSpSQAGFRGT----ADGDAINIFGSSHIWIDHNSLSNCTDGLVDVVNGSTA 285
Cdd:pfam13229  49 IEISGSSNNTISNNTISNNGGGG-IALRGS-SNNLIENNtisnNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNN 126
                          90
                  ....*....|....
gi 42565152   286 ITISNNHFTHHDEV 299
Cdd:pfam13229 127 VTISNNTVTNNKGA 140
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
208-299 7.93e-03

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: 37.00  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565152   208 ACITIQNITNVIVHGLHIHDCKRTGnVTVRSSpSQAGFRGT----ADGDAINIFGSSHIWIDHNSLSNCTDGLVDVVNGS 283
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYG-IYLRGS-SNATIENNtitnNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSS 78
                          90
                  ....*....|....*.
gi 42565152   284 TaITISNNHFTHHDEV 299
Cdd:pfam13229  79 N-NLIENNTISNNGGA 93
 
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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