NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|257697836|emb|CBC81743|]
View 

unnamed protein product [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
120-315 2.51e-81

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 247.19  E-value: 2.51e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836   120 DMVITL--ENELMVNSYKTIDGRGAKVEIAyGPCITIQDVTNVIVHGISIHDCKPGKygmvrsspthvghrkGSDGDAIA 197
Cdd:smart00656   1 DVTITLdnAGTIIINSNKTIDGRGSKVEIK-GGGLTIKSVSNVIIRNLTIHDPKPVY---------------GSDGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836   198 IFGSSNIWIDHCYLASCT---------DGLIDVIHASTGITISNNYFTQHDKVMLLGHNDDFVQDVKMKVTVAFNHFGpG 268
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 257697836   269 LVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYFIASD 315
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
120-315 2.51e-81

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 247.19  E-value: 2.51e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836   120 DMVITL--ENELMVNSYKTIDGRGAKVEIAyGPCITIQDVTNVIVHGISIHDCKPGKygmvrsspthvghrkGSDGDAIA 197
Cdd:smart00656   1 DVTITLdnAGTIIINSNKTIDGRGSKVEIK-GGGLTIKSVSNVIIRNLTIHDPKPVY---------------GSDGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836   198 IFGSSNIWIDHCYLASCT---------DGLIDVIHASTGITISNNYFTQHDKVMLLGHNDDFVQDVKMKVTVAFNHFGpG 268
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 257697836   269 LVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYFIASD 315
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
71-384 2.17e-50

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 172.10  E-value: 2.17e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836  71 VGFGS---STLGGKKGNLYVVTNPYDnaqnpqpgsLRYGVIQAKPLWITFakDMVITLEN-ELMVNSYKTIDGRGAKVEI 146
Cdd:COG3866   36 EGFASvngGTTGGAGGTVVTVTTLAD---------LRAALEASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGATI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836 147 AYGPcITIQDVTNVIVHGISIHDCKPGKygmvrsspthvghrkGSDGDAIAIFGSSNIWIDHCYLASCTDGLIDVIHAST 226
Cdd:COG3866  105 TGGG-LNIKGASNVIIRNLRFRNGDDGG---------------GSGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836 227 GITISNNYFTQ----HDKVMLLGHNDDFVQDvKMKVTVAFNHFGpGLVERMPRVRRGYAHVANNRYDKWI-MYAIGGSAD 301
Cdd:COG3866  169 NVTVSWNIFAEgkgdHGKGMLIGSSDSDTTG-KLRVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWGnNYGIGSGGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836 302 PTIFSEGNYFIASDKSNSKEVTKREVKGGwnnwRWRTSKDVFKN-GAYFVPSGYGSISLPYSsaqrFTVAPGNLVPSL-T 379
Cdd:COG3866  247 AQVLVENNYFENVKGPLATSDGSSLLDPG----YLYARGNVFDNsTGTAPAGSGTVFTPPYS----YTLDPASDVKTLvL 318

                 ....*
gi 257697836 380 ADAGP 384
Cdd:COG3866  319 AGAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
185-311 1.10e-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: 89.57  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836  185 VGHRKGS--DGDAIAIFGSSNIWIDHCYLASCT-------------DGLIDVIHASTGITISNNYFTQHDKVMLLGHNDD 249
Cdd:pfam00544  69 IGTPDGWnkDWDAIRIDNSPNVWVDHVTISDGSftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDD 148
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257697836  250 FV-QDV-KMKVTVAFNHFGpGLVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYF 311
Cdd:pfam00544 149 NNsQDTgKLRVTYHHNVYN-RVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
120-315 2.51e-81

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 247.19  E-value: 2.51e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836   120 DMVITL--ENELMVNSYKTIDGRGAKVEIAyGPCITIQDVTNVIVHGISIHDCKPGKygmvrsspthvghrkGSDGDAIA 197
Cdd:smart00656   1 DVTITLdnAGTIIINSNKTIDGRGSKVEIK-GGGLTIKSVSNVIIRNLTIHDPKPVY---------------GSDGDAIS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836   198 IFGSSNIWIDHCYLASCT---------DGLIDVIHASTGITISNNYFTQHDKVMLLGHNDDFVQDVKMKVTVAFNHFGpG 268
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 257697836   269 LVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYFIASD 315
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
71-384 2.17e-50

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 172.10  E-value: 2.17e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836  71 VGFGS---STLGGKKGNLYVVTNPYDnaqnpqpgsLRYGVIQAKPLWITFakDMVITLEN-ELMVNSYKTIDGRGAKVEI 146
Cdd:COG3866   36 EGFASvngGTTGGAGGTVVTVTTLAD---------LRAALEASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGATI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836 147 AYGPcITIQDVTNVIVHGISIHDCKPGKygmvrsspthvghrkGSDGDAIAIFGSSNIWIDHCYLASCTDGLIDVIHAST 226
Cdd:COG3866  105 TGGG-LNIKGASNVIIRNLRFRNGDDGG---------------GSGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836 227 GITISNNYFTQ----HDKVMLLGHNDDFVQDvKMKVTVAFNHFGpGLVERMPRVRRGYAHVANNRYDKWI-MYAIGGSAD 301
Cdd:COG3866  169 NVTVSWNIFAEgkgdHGKGMLIGSSDSDTTG-KLRVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWGnNYGIGSGGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836 302 PTIFSEGNYFIASDKSNSKEVTKREVKGGwnnwRWRTSKDVFKN-GAYFVPSGYGSISLPYSsaqrFTVAPGNLVPSL-T 379
Cdd:COG3866  247 AQVLVENNYFENVKGPLATSDGSSLLDPG----YLYARGNVFDNsTGTAPAGSGTVFTPPYS----YTLDPASDVKTLvL 318

                 ....*
gi 257697836 380 ADAGP 384
Cdd:COG3866  319 AGAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
185-311 1.10e-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: 89.57  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836  185 VGHRKGS--DGDAIAIFGSSNIWIDHCYLASCT-------------DGLIDVIHASTGITISNNYFTQHDKVMLLGHNDD 249
Cdd:pfam00544  69 IGTPDGWnkDWDAIRIDNSPNVWVDHVTISDGSftddgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDD 148
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257697836  250 FV-QDV-KMKVTVAFNHFGpGLVERMPRVRRGYAHVANNRYDKWIMYAIGGSADPTIFSEGNYF 311
Cdd:pfam00544 149 NNsQDTgKLRVTYHHNVYN-RVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
152-241 1.63e-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: 38.93  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257697836  152 ITIQDVTNVIVHGISIHDCKPGKYGMVRSSPTHVGHRK--GSDGDAIAIFGSSNIWIDHCYLASCTDGLIDVIHASTGIT 229
Cdd:pfam13229  49 IEISGSSNNTISNNTISNNGGGGIALRGSSNNLIENNTisNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVT 128
                          90
                  ....*....|..
gi 257697836  230 ISNNYFTQHDKV 241
Cdd:pfam13229 129 ISNNTVTNNKGA 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH