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Conserved domains on  [gi|15230142|ref|NP_189110|]
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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;
166-361 2.68e-82

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.43  E-value: 2.68e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142    166 DMVITLTQ--ELIMNSFKTIDGRGVNVAIAGGaCITIQYVTNIIIHGINVHDCrrtgnamvrssPSHYGWrtmaDGDAIS 243
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDP-----------KPVYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142    244 IFGSSHIWIDHNSLSNCA---------DGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSYTRDKLMQVTIAYNHFGeG 314
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15230142    315 LIQRMPRCRHGYFHVVNNDYTHWVMYAIGGSANPTINSQGNRFLAPG 361
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
166-361 2.68e-82

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.43  E-value: 2.68e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142    166 DMVITLTQ--ELIMNSFKTIDGRGVNVAIAGGaCITIQYVTNIIIHGINVHDCrrtgnamvrssPSHYGWrtmaDGDAIS 243
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDP-----------KPVYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142    244 IFGSSHIWIDHNSLSNCA---------DGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSYTRDKLMQVTIAYNHFGeG 314
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15230142    315 LIQRMPRCRHGYFHVVNNDYTHWVMYAIGGSANPTINSQGNRFLAPG 361
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
115-366 1.07e-50

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 174.41  E-value: 1.07e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 115 AIGFGR---NAIGGRDGRYYVVTDPSDhdavnprpgtLRHAVIQDRPLWIVFkrDMVITLTQ-ELIMNSFKTIDGRGVNV 190
Cdd:COG3866  35 PEGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 191 AIAGGAcITIQYVTNIIIHGINVHDCRRTGNAmvrsspshygwrtmaDGDAISIFGSSHIWIDHNSLSNCADGLIDAIMG 270
Cdd:COG3866 103 TITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRG 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 271 STAITISNNY----MTHHNEVMLMGHSDSYTRDKLmQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWV-MYAIGGS 345
Cdd:COG3866 167 SDNVTVSWNIfaegKGDHGKGMLIGSSDSDTTGKL-RVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWGnNYGIGSG 244

                       250       260
                ....*....|....*....|.
gi 15230142 346 ANPTINSQGNRFLAPGNPFAK 366
Cdd:COG3866 245 GGAQVLVENNYFENVKGPLAT 265
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 237-357 1.38e-19

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: 86.88  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142   237 ADGDAISIFGSSHIWIDHNSLS----NCA---------DGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSY--TRDKL 301
Cdd:pfam00544  77 KDWDAIRIDNSPNVWVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNnsQDTGK 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230142   302 MQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWVMYAIGGSANPTINSQGNRF 357
Cdd:pfam00544 157 LRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
166-361 2.68e-82

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 251.43  E-value: 2.68e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142    166 DMVITLTQ--ELIMNSFKTIDGRGVNVAIAGGaCITIQYVTNIIIHGINVHDCrrtgnamvrssPSHYGWrtmaDGDAIS 243
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDP-----------KPVYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142    244 IFGSSHIWIDHNSLSNCA---------DGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSYTRDKLMQVTIAYNHFGeG 314
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15230142    315 LIQRMPRCRHGYFHVVNNDYTHWVMYAIGGSANPTINSQGNRFLAPG 361
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAPI 190
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
115-366 1.07e-50

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 174.41  E-value: 1.07e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 115 AIGFGR---NAIGGRDGRYYVVTDPSDhdavnprpgtLRHAVIQDRPLWIVFkrDMVITLTQ-ELIMNSFKTIDGRGVNV 190
Cdd:COG3866  35 PEGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLSKsPLKVNSNKTIAGQGDGA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 191 AIAGGAcITIQYVTNIIIHGINVHDCRRTGNAmvrsspshygwrtmaDGDAISIFGSSHIWIDHNSLSNCADGLIDAIMG 270
Cdd:COG3866 103 TITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRG 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 271 STAITISNNY----MTHHNEVMLMGHSDSYTRDKLmQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWV-MYAIGGS 345
Cdd:COG3866 167 SDNVTVSWNIfaegKGDHGKGMLIGSSDSDTTGKL-RVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWGnNYGIGSG 244

                       250       260
                ....*....|....*....|.
gi 15230142 346 ANPTINSQGNRFLAPGNPFAK 366
Cdd:COG3866 245 GGAQVLVENNYFENVKGPLAT 265
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 237-357 1.38e-19

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: 86.88  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142   237 ADGDAISIFGSSHIWIDHNSLS----NCA---------DGLIDAIMGSTAITISNNYMTHHNEVMLMGHSDSY--TRDKL 301
Cdd:pfam00544  77 KDWDAIRIDNSPNVWVDHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNnsQDTGK 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230142   302 MQVTIAYNHFgEGLIQRMPRCRHGYFHVVNNDYTHWVMYAIGGSANPTINSQGNRF 357
Cdd:pfam00544 157 LRVTYHHNVY-NRVTERAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESNSF 211
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 137-283 2.96e-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: 39.51  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 137 SDHDAVNPRPGTLRHAVIQDRPLwivfkrdmvitltqELIMNSFKTIDGRGV---------NVAIAG------------- 194
Cdd:COG3420  32 PPGDTIEVPPGTYEGNIVIDKPL--------------TLIGEGGAVIDGGGKgtvititadNVTVRGltitgsgdsltdd 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142 195 GACITIQYVTNIIIHGINVHDC------RRTGNAMVR-----SSPSHYGWRtmadGDAISIFGSSHIWIDHNSLSNCADG 263
Cdd:COG3420  98 DAGIYVRGADNAVIENNRIENNlfgiylEGSDNNVIRnntisGNRDLRADR----GNGIHLWNSPGNVIEGNTISGGRDG 173

                       170       180
                ....*....|....*....|
gi 15230142 264 LIdaIMGSTAITISNNYMTH 283
Cdd:COG3420 174 IY--LEFSDNNVIRNNTIRN 191
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 198-297 3.64e-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: 38.16  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230142   198 ITIQYVTNIIIHGINVHDCRRTGNAMVRSSPSH-YGWR-TMADGDAISIFGSSHIWIDHNSLSNCADGLIDAIMGSTAIT 275
Cdd:pfam13229  49 IEISGSSNNTISNNTISNNGGGGIALRGSSNNLiENNTiSNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVT 128

                          90       100
                  ....*....|....*....|....
gi 15230142   276 ISNNYMTHHNE--VMLMGHSDSYT 297
Cdd:pfam13229 129 ISNNTVTNNKGagILIVGGSSNNT 152
 
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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