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Conserved domains on  [gi|18390426|ref|NP_563715|]
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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;
155-350 1.05e-83

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 254.51  E-value: 1.05e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426    155 DMVIQLKQ--ELIVNSFKTIDGRGANVHIAnGGCITIQFVTNVIVHGLHIHDCKPtgnamvrssetHFGWrtmaDGDAIS 232
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIK-GGGLTIKSVSNVIIRNLTIHDPKP-----------VYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426    233 IFGSSHVWIDHNSLSHCA---------DGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYMRDKAMQVTIAYNHFGvG 303
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 18390426    304 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRYAAPK 350
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
155-350 1.05e-83

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 254.51  E-value: 1.05e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426    155 DMVIQLKQ--ELIVNSFKTIDGRGANVHIAnGGCITIQFVTNVIVHGLHIHDCKPtgnamvrssetHFGWrtmaDGDAIS 232
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIK-GGGLTIKSVSNVIIRNLTIHDPKP-----------VYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426    233 IFGSSHVWIDHNSLSHCA---------DGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYMRDKAMQVTIAYNHFGvG 303
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 18390426    304 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRYAAPK 350
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
105-397 1.21e-53

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 181.73  E-value: 1.21e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 105 IGFGR---NAIGGRDGRFYVVTDPRDdnpvnprpgtLRHAVIQDRPLWIVFkrDMVIQL-KQELIVNSFKTIDGRGANVH 180
Cdd:COG3866  36 EGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGAT 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 181 IANGGcITIQFVTNVIVHGLHIHDCKPTGNAmvrssethfgwrtmaDGDAISIFGSSHVWIDHNSLSHCADGLVDAVMGS 260
Cdd:COG3866 104 ITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 261 TAITISNNHL----THHNEVMLLGHSDSYMRDKAmQVTIAYNHFGvGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGGSA 335
Cdd:COG3866 168 DNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGKL-RVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390426 336 NPTINSQGNRYAAPKNPFAKEVTKRVDTPAshwkgwNWRSEGDLLQN--GAYFTSSGAAASGSY 397
Cdd:COG3866 246 GAQVLVENNYFENVKGPLATSDGSSLLDPG------YLYARGNVFDNstGTAPAGSGTVFTPPY 303
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 161-344 7.76e-21

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: 90.34  E-value: 7.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426   161 KQELIVNSFKTIDGR-GANVHIANGGCITIQFVTNVIVHGLHIhdckptgnamvrssETHFGWrtMADGDAISIFGSSHV 239
Cdd:pfam00544  27 RSQIGVPSNTTIIGIiGTNGKFTNFGSLIIKGSSNVIVRNLYI--------------GTPDGW--NKDWDAIRIDNSPNV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426   240 WIDHNSLS----HCA---------DGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYM-RDKA-MQVTIAYNHFGvGL 304
Cdd:pfam00544  91 WVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNNsQDTGkLRVTYHHNVYN-RV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 18390426   305 IQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGN 344
Cdd:pfam00544 170 TERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
155-350 1.05e-83

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 254.51  E-value: 1.05e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426    155 DMVIQLKQ--ELIVNSFKTIDGRGANVHIAnGGCITIQFVTNVIVHGLHIHDCKPtgnamvrssetHFGWrtmaDGDAIS 232
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIK-GGGLTIKSVSNVIIRNLTIHDPKP-----------VYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426    233 IFGSSHVWIDHNSLSHCA---------DGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYMRDKAMQVTIAYNHFGvG 303
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 18390426    304 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRYAAPK 350
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
105-397 1.21e-53

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 181.73  E-value: 1.21e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 105 IGFGR---NAIGGRDGRFYVVTDPRDdnpvnprpgtLRHAVIQDRPLWIVFkrDMVIQL-KQELIVNSFKTIDGRGANVH 180
Cdd:COG3866  36 EGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGAT 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 181 IANGGcITIQFVTNVIVHGLHIHDCKPTGNAmvrssethfgwrtmaDGDAISIFGSSHVWIDHNSLSHCADGLVDAVMGS 260
Cdd:COG3866 104 ITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 261 TAITISNNHL----THHNEVMLLGHSDSYMRDKAmQVTIAYNHFGvGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGGSA 335
Cdd:COG3866 168 DNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGKL-RVTFHHNLFA-NNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390426 336 NPTINSQGNRYAAPKNPFAKEVTKRVDTPAshwkgwNWRSEGDLLQN--GAYFTSSGAAASGSY 397
Cdd:COG3866 246 GAQVLVENNYFENVKGPLATSDGSSLLDPG------YLYARGNVFDNstGTAPAGSGTVFTPPY 303
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 161-344 7.76e-21

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: 90.34  E-value: 7.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426   161 KQELIVNSFKTIDGR-GANVHIANGGCITIQFVTNVIVHGLHIhdckptgnamvrssETHFGWrtMADGDAISIFGSSHV 239
Cdd:pfam00544  27 RSQIGVPSNTTIIGIiGTNGKFTNFGSLIIKGSSNVIVRNLYI--------------GTPDGW--NKDWDAIRIDNSPNV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426   240 WIDHNSLS----HCA---------DGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYM-RDKA-MQVTIAYNHFGvGL 304
Cdd:pfam00544  91 WVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNNsQDTGkLRVTYHHNVYN-RV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 18390426   305 IQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGN 344
Cdd:pfam00544 170 TERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 187-276 5.75e-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: 37.39  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426   187 ITIQFVTNVIVHGLHIHDCKPTGNAMVRSSETHF-GWR-TMADGDAISIFGSSHVWIDHNSLSHCADGLVDAVMGSTAIT 264
Cdd:pfam13229  49 IEISGSSNNTISNNTISNNGGGGIALRGSSNNLIeNNTiSNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVT 128

                          90
                  ....*....|..
gi 18390426   265 ISNNHLTHHNEV 276
Cdd:pfam13229 129 ISNNTVTNNKGA 140
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 131-272 9.18e-03

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: 37.97  E-value: 9.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 131 VNPRPGTLRHAVIQDRPLWIVFKRDMVIQLKQE---LIVNS-------FkTIDGRGaNVHIANGGCITIQFVTNVIVHGL 200
Cdd:COG3420  37 IEVPPGTYEGNIVIDKPLTLIGEGGAVIDGGGKgtvITITAdnvtvrgL-TITGSG-DSLTDDDAGIYVRGADNAVIENN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390426 201 HIHDC------KPTGNAMVR-----SSETHFGWRtmadGDAISIFGSSHVWIDHNSLSHCADGLVdaVMGSTAITISNNH 269
Cdd:COG3420 115 RIENNlfgiylEGSDNNVIRnntisGNRDLRADR----GNGIHLWNSPGNVIEGNTISGGRDGIY--LEFSDNNVIRNNT 188


                ...
gi 18390426 270 LTH 272
Cdd:COG3420 189 IRN 191
 
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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