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Conserved domains on  [gi|15220729|ref|NP_174324|]
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Pectin lyase-like superfamily 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;
109-289 7.25e-88

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 262.98  E-value: 7.25e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729    109 DMVIVLKS--QLMINSYKTIDGRGAKVEIANGpCLRIRQVKHVIIHGISIHDCKaDPNGMDGDGIRVFQSTHVWIDHCFL 186
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPK-PVYGSDGDAISIDGSSNVWIDHVSL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729    187 SRC---------HDGLIDVIVSSTAVTISNNYFTQHDKVMLLGHDDSYMGDKDMRVTIAFNTFGpGLIERMPRVRRGYAH 257
Cdd:smart00656  79 SGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-NLRQRAPRVRFGYVH 157

                          170       180       190
                   ....*....|....*....|....*....|..
gi 15220729    258 VANNRYEKWQMYAIGGSANPIIFSEGNYFVAP 289
Cdd:smart00656 158 VYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
109-289 7.25e-88

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 262.98  E-value: 7.25e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729    109 DMVIVLKS--QLMINSYKTIDGRGAKVEIANGpCLRIRQVKHVIIHGISIHDCKaDPNGMDGDGIRVFQSTHVWIDHCFL 186
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPK-PVYGSDGDAISIDGSSNVWIDHVSL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729    187 SRC---------HDGLIDVIVSSTAVTISNNYFTQHDKVMLLGHDDSYMGDKDMRVTIAFNTFGpGLIERMPRVRRGYAH 257
Cdd:smart00656  79 SGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-NLRQRAPRVRFGYVH 157

                          170       180       190
                   ....*....|....*....|....*....|..
gi 15220729    258 VANNRYEKWQMYAIGGSANPIIFSEGNYFVAP 289
Cdd:smart00656 158 VYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
53-359 9.52e-58

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 190.58  E-value: 9.52e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729  53 QALAHCAVGYGKA---AIGGKNGPIYVVTNPSDnptrpspgtLRYAVSQPKPLWITFarDMVIVL-KSQLMINSYKTIDG 128
Cdd:COG3866  29 AAAAPAPEGFASVnggTTGGAGGTVVTVTTLAD---------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 129 RGAKVEIANGPcLRIRQVKHVIIHGISIHDCKaDPNGMDGDGIRVFQSTHVWIDHCFLSRCHDGLIDVIVSSTAVTISNN 208
Cdd:COG3866  98 QGDGATITGGG-LNIKGASNVIIRNLRFRNGD-DGGGSGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSDNVTVSWN 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 209 YFTQ----HDKVMLLGHDDSYmGDKDMRVTIAFNTFGpGLIERMPRVRRGYAHVANNRYEKW-QMYAIGGSANPIIFSEG 283
Cdd:COG3866 176 IFAEgkgdHGKGMLIGSSDSD-TTGKLRVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGGGAQVLVEN 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 284 NYF-VAPEKRSSKQVTKRMMAGpdskrwKWGTSRDVFMN--GAFFGPPGVIVRPLYkggeGFRVAHGSLVPSL-TSSAGP 359
Cdd:COG3866 254 NYFeNVKGPLATSDGSSLLDPG------YLYARGNVFDNstGTAPAGSGTVFTPPY----SYTLDPASDVKTLvLAGAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 115-286 1.65e-27

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: 107.68  E-value: 1.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729   115 KSQLMINSYKTIDGR-GAKVEIANGPCLRIRQVKHVIIHGISIHdcKADPNGMDGDGIRVFQSTHVWIDHCFLS------ 187
Cdd:pfam00544  27 RSQIGVPSNTTIIGIiGTNGKFTNFGSLIIKGSSNVIVRNLYIG--TPDGWNKDWDAIRIDNSPNVWVDHVTISdgsftd 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729   188 -------RCHDGLIDVIVSSTAVTISNNYFTQHDKVMLLGH-DDSYMGDK-DMRVTIAFNTFGpGLIERMPRVRRGYAHV 258
Cdd:pfam00544 105 dgyttkyVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHsDDNNSQDTgKLRVTYHHNVYN-RVTERAPLVRYGSIHA 183

                         170       180
                  ....*....|....*....|....*...
gi 15220729   259 ANNRYEKWQMYAIGGSANPIIFSEGNYF 286
Cdd:pfam00544 184 YNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
109-289 7.25e-88

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 262.98  E-value: 7.25e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729    109 DMVIVLKS--QLMINSYKTIDGRGAKVEIANGpCLRIRQVKHVIIHGISIHDCKaDPNGMDGDGIRVFQSTHVWIDHCFL 186
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPK-PVYGSDGDAISIDGSSNVWIDHVSL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729    187 SRC---------HDGLIDVIVSSTAVTISNNYFTQHDKVMLLGHDDSYMGDKDMRVTIAFNTFGpGLIERMPRVRRGYAH 257
Cdd:smart00656  79 SGCtvtgfgddtYDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-NLRQRAPRVRFGYVH 157

                          170       180       190
                   ....*....|....*....|....*....|..
gi 15220729    258 VANNRYEKWQMYAIGGSANPIIFSEGNYFVAP 289
Cdd:smart00656 158 VYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
53-359 9.52e-58

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 190.58  E-value: 9.52e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729  53 QALAHCAVGYGKA---AIGGKNGPIYVVTNPSDnptrpspgtLRYAVSQPKPLWITFarDMVIVL-KSQLMINSYKTIDG 128
Cdd:COG3866  29 AAAAPAPEGFASVnggTTGGAGGTVVTVTTLAD---------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 129 RGAKVEIANGPcLRIRQVKHVIIHGISIHDCKaDPNGMDGDGIRVFQSTHVWIDHCFLSRCHDGLIDVIVSSTAVTISNN 208
Cdd:COG3866  98 QGDGATITGGG-LNIKGASNVIIRNLRFRNGD-DGGGSGGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGSDNVTVSWN 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 209 YFTQ----HDKVMLLGHDDSYmGDKDMRVTIAFNTFGpGLIERMPRVRRGYAHVANNRYEKW-QMYAIGGSANPIIFSEG 283
Cdd:COG3866 176 IFAEgkgdHGKGMLIGSSDSD-TTGKLRVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGGGAQVLVEN 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 284 NYF-VAPEKRSSKQVTKRMMAGpdskrwKWGTSRDVFMN--GAFFGPPGVIVRPLYkggeGFRVAHGSLVPSL-TSSAGP 359
Cdd:COG3866 254 NYFeNVKGPLATSDGSSLLDPG------YLYARGNVFDNstGTAPAGSGTVFTPPY----SYTLDPASDVKTLvLAGAGA 323
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 115-286 1.65e-27

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: 107.68  E-value: 1.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729   115 KSQLMINSYKTIDGR-GAKVEIANGPCLRIRQVKHVIIHGISIHdcKADPNGMDGDGIRVFQSTHVWIDHCFLS------ 187
Cdd:pfam00544  27 RSQIGVPSNTTIIGIiGTNGKFTNFGSLIIKGSSNVIVRNLYIG--TPDGWNKDWDAIRIDNSPNVWVDHVTISdgsftd 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729   188 -------RCHDGLIDVIVSSTAVTISNNYFTQHDKVMLLGH-DDSYMGDK-DMRVTIAFNTFGpGLIERMPRVRRGYAHV 258
Cdd:pfam00544 105 dgyttkyVQHDGALDIKKGSDYVTISYSLFHGHKKTGLIGHsDDNNSQDTgKLRVTYHHNVYN-RVTERAPLVRYGSIHA 183

                         170       180
                  ....*....|....*....|....*...
gi 15220729   259 ANNRYEKWQMYAIGGSANPIIFSEGNYF 286
Cdd:pfam00544 184 YNNVYVNIYLYSFGVGQNGSVLSESNSF 211
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 142-211 7.74e-04

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: 41.06  E-value: 7.74e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729 142 RIRQVKHVIIHGISIHDcKADPNGMDGDGIRVFQSTHVWIDHCFLSRCHDGLidVIVSSTAVTISNNYFT 211
Cdd:COG3420 124 YLEGSDNNVIRNNTISG-NRDLRADRGNGIHLWNSPGNVIEGNTISGGRDGI--YLEFSDNNVIRNNTIR 190
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 143-240 8.21e-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: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220729   143 IRQVKHVIIHGISIHDCkadpngmDGDGIRVFQSTHVWIDHCFLSRCHDGLIDVIVSSTAVTISNNYFTQHDKV-MLLGH 221
Cdd:pfam13229  74 LRGSSNNLIENNTISNN-------GGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVTISNNTVTNNKGAgILIVG 146

                          90
                  ....*....|....*....
gi 15220729   222 DDSYmgdkdmrVTIAFNTF 240
Cdd:pfam13229 147 GSSN-------NTVENNTF 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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