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Conserved domains on  [gi|15221078|ref|NP_175244|]
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Pectin lyase-like superfamily protein [Arabidopsis thaliana]

Protein Classification

polysaccharide lyase domain-containing protein( domain architecture ID 139546)

polysaccharide lyase domain-containing protein may function as a hydrolase

Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PL-6 super family cl19188
Polysaccharide Lyase Family 6; Polysaccharide Lyase Family 6 is a family of beta-helical ...
 79-471 3.28e-118

Polysaccharide Lyase Family 6; Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate.


The actual alignment was detected with superfamily member PLN02793:

Pssm-ID: 450265 [Multi-domain]  Cd Length: 443  Bit Score: 353.80  E-value: 3.28e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   79 VFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGV-VLAPEGGVFKITSTIFSGPCKPGLVFQLDGVLMPPDGPEEWpEK 157
Cdd:PLN02793  52 VLHVGDFGAKGDGVTDDTQAFKEAWKMACSSKVKTrIVIPAGYTFLVRPIDLGGPCKAKLTLQISGTIIAPKDPDVW-KG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  158 DNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDLPCKphrgpdgSSSSGPC-ASPTMIRFFMSNNIEVKGLRIQNSPQFHM 236
Cdd:PLN02793 131 LNPRKWLYFHGVNHLTVEGGGTVNGMGHEWWAQSCK-------INHTNPCrHAPTAITFHKCKDLRVENLNVIDSQQMHI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  237 KFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSLGVHN 316
Cdd:PLN02793 204 AFTNCRRVTISGLKVIAPATSPNTDGIHISASRGVVIKDSIVRTGDDCISIVGNSSRIKIRNIACGPGHGISIGSLGKSN 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  317 SQACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNCIIVDQYYCQS-KDCRNETSAVKVFDVEYRN 395
Cdd:PLN02793 284 SWSEVRDITVDGAFLSNTDNGVRIKTWQGGSGNASKITFQNIFMENVSNPIIIDQYYCDSrKPCANQTSAVKVENISFVH 363

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221078  396 IKGTyDVRSPPIHFACSDTVACTNITMSEVELLPEEGELVDDpFCWNAYGKQETLTIPPiDCLLDGSPVVEEAYDS 471
Cdd:PLN02793 364 IKGT-SATEEAIKFACSDSSPCEGLYLEDVQLLSSTGDFTES-FCWEAYGSSSGQVYPP-PCFSDSTSFIKQKVQS 436
 
Name Accession Description Interval E-value
PLN02793 PLN02793
Probable polygalacturonase
 79-471 3.28e-118

Probable polygalacturonase


Pssm-ID: 215426 [Multi-domain]  Cd Length: 443  Bit Score: 353.80  E-value: 3.28e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   79 VFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGV-VLAPEGGVFKITSTIFSGPCKPGLVFQLDGVLMPPDGPEEWpEK 157
Cdd:PLN02793  52 VLHVGDFGAKGDGVTDDTQAFKEAWKMACSSKVKTrIVIPAGYTFLVRPIDLGGPCKAKLTLQISGTIIAPKDPDVW-KG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  158 DNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDLPCKphrgpdgSSSSGPC-ASPTMIRFFMSNNIEVKGLRIQNSPQFHM 236
Cdd:PLN02793 131 LNPRKWLYFHGVNHLTVEGGGTVNGMGHEWWAQSCK-------INHTNPCrHAPTAITFHKCKDLRVENLNVIDSQQMHI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  237 KFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSLGVHN 316
Cdd:PLN02793 204 AFTNCRRVTISGLKVIAPATSPNTDGIHISASRGVVIKDSIVRTGDDCISIVGNSSRIKIRNIACGPGHGISIGSLGKSN 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  317 SQACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNCIIVDQYYCQS-KDCRNETSAVKVFDVEYRN 395
Cdd:PLN02793 284 SWSEVRDITVDGAFLSNTDNGVRIKTWQGGSGNASKITFQNIFMENVSNPIIIDQYYCDSrKPCANQTSAVKVENISFVH 363

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221078  396 IKGTyDVRSPPIHFACSDTVACTNITMSEVELLPEEGELVDDpFCWNAYGKQETLTIPPiDCLLDGSPVVEEAYDS 471
Cdd:PLN02793 364 IKGT-SATEEAIKFACSDSSPCEGLYLEDVQLLSSTGDFTES-FCWEAYGSSSGQVYPP-PCFSDSTSFIKQKVQS 436
Glyco_hydro_28 pfam00295
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2. ...
 156-427 6.69e-72

Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism.


Pssm-ID: 425588 [Multi-domain]  Cd Length: 319  Bit Score: 230.35  E-value: 6.69e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   156 EKDNKNQWLVFYRLDGFTFSGkGTVEGNGQKWWDLPCKphrgpdgSSSSGPCAsPTMIRFFMSNNIEVKGLRIQNSPQFH 235
Cdd:pfam00295  38 EWNGKLIWISGSSITVTGASG-GTIDGQGQRWWDGKGT-------KKNGGKKK-PKFIYIHKVKNSKITGLNIKNSPVFH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   236 MKFDGCQGVLINEIQISSP---KLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGcSDVDIQGVTCGPSHGISIGSL 312
Cdd:pfam00295 109 FSVQSGTDLTISDITIDNSagdSNGHNTDGFDVGSSSGVTISNTNIYNQDDCIAINSG-SNISITNVTCGGGHGISIGSV 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   313 GVHNSQAcVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENV-LNCIIVDQYYCQSKDCRNETSAVKVFDV 391
Cdd:pfam00295 188 GGRSDNT-VKNVTVKDSTVVNSDNGVRIKTISGATGTVSNITYENIVLSNIsKYGIVIDQDYENGEPTGKPTSGVKISDI 266

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15221078   392 EYRNIKGTYDVRSPPIHFACSDTVaCTNITMSEVEL 427
Cdd:pfam00295 267 TFKNVTGTVASSATAVYLLCGDGS-CSGWTWSGVNI 301
Pgu1 COG5434
Polygalacturonase [Carbohydrate transport and metabolism];
79-399 5.50e-63

Polygalacturonase [Carbohydrate transport and metabolism];


Pssm-ID: 444185 [Multi-domain]  Cd Length: 373  Bit Score: 208.91  E-value: 5.50e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  79 VFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGVVLAPEGgVFKiTSTIFsgpCKPGLVFQLD--GVLMPPDGPEEWP- 155
Cdd:COG5434   9 TFNITDFGAKGDGKTLNTAAIQKAIDACAAAGGGTVLVPAG-TYL-TGPIF---LKSNVTLHLEkgATLLGSTDPADYPl 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 156 --------EKDNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDLPCKPHRGPDGSSSSGPCASPTMIRFFMSNNIEVKGLR 227
Cdd:COG5434  84 vetrweggELKGYSALIYAENAENIAITGEGTIDGNGDAWWPWKKEARQSGWVPVGAYDYLRPRLIQLKNCKNVLLEGVT 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 228 IQNSPQFHMKFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTG----------CSDVDIQ 297
Cdd:COG5434 164 LRNSPFWTIHPLGCENVTVDGVTIDNPADAPNTDGIDPDSCRNVLIENCYIDTGDDAIAIKSGrdadgrrnrpTENIVIR 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 298 GVTCGPSHG-ISIGSlgvhNSQACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNC-IIVDQYYcq 375
Cdd:COG5434 244 NCTFRSGHGgIVIGS----ETSGGVRNVTVENCTFDGTDRGLRIKSRRGRGGVVENITIRNITMRNVKGTpIFINLFY-- 317

                       330       340
                ....*....|....*....|....
gi 15221078 376 SKDCRNETSAVKvfDVEYRNIKGT 399
Cdd:COG5434 318 EGDRGGPTPTFR--NITISNVTAT 339
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
 73-129 3.03e-04

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 43.27  E-value: 3.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15221078  73 DSDSGCVFDVTSFGAVGDGSCDDTAAFQDAWKAacAVESGVVLAPEgGVFKITSTIF 129
Cdd:cd23668 297 DYPASQFVNVKDYGAKGDGVTDDTAALQAILNT--AAGGKIVYFPA-GTYIVTDTLF 350
 
Name Accession Description Interval E-value
PLN02793 PLN02793
Probable polygalacturonase
 79-471 3.28e-118

Probable polygalacturonase


Pssm-ID: 215426 [Multi-domain]  Cd Length: 443  Bit Score: 353.80  E-value: 3.28e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   79 VFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGV-VLAPEGGVFKITSTIFSGPCKPGLVFQLDGVLMPPDGPEEWpEK 157
Cdd:PLN02793  52 VLHVGDFGAKGDGVTDDTQAFKEAWKMACSSKVKTrIVIPAGYTFLVRPIDLGGPCKAKLTLQISGTIIAPKDPDVW-KG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  158 DNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDLPCKphrgpdgSSSSGPC-ASPTMIRFFMSNNIEVKGLRIQNSPQFHM 236
Cdd:PLN02793 131 LNPRKWLYFHGVNHLTVEGGGTVNGMGHEWWAQSCK-------INHTNPCrHAPTAITFHKCKDLRVENLNVIDSQQMHI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  237 KFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSLGVHN 316
Cdd:PLN02793 204 AFTNCRRVTISGLKVIAPATSPNTDGIHISASRGVVIKDSIVRTGDDCISIVGNSSRIKIRNIACGPGHGISIGSLGKSN 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  317 SQACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNCIIVDQYYCQS-KDCRNETSAVKVFDVEYRN 395
Cdd:PLN02793 284 SWSEVRDITVDGAFLSNTDNGVRIKTWQGGSGNASKITFQNIFMENVSNPIIIDQYYCDSrKPCANQTSAVKVENISFVH 363

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221078  396 IKGTyDVRSPPIHFACSDTVACTNITMSEVELLPEEGELVDDpFCWNAYGKQETLTIPPiDCLLDGSPVVEEAYDS 471
Cdd:PLN02793 364 IKGT-SATEEAIKFACSDSSPCEGLYLEDVQLLSSTGDFTES-FCWEAYGSSSGQVYPP-PCFSDSTSFIKQKVQS 436
PLN02218 PLN02218
polygalacturonase ADPG
 82-427 2.22e-98

polygalacturonase ADPG


Pssm-ID: 177865 [Multi-domain]  Cd Length: 431  Bit Score: 302.33  E-value: 2.22e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   82 VTSFGAVGDGSCDDTAAFQDAWKAACAVESGV-VLAPEGGVFKITSTIFSGPCKPGLVFQLDGVLmppDGPEEWPEKDNK 160
Cdd:PLN02218  70 VSDFGAKGDGKTDDTQAFVNAWKKACSSNGAVnLLVPKGNTYLLKSIQLTGPCKSIRTVQIFGTL---SASQKRSDYKDI 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  161 NQWLVFYRLDGFTFSGKGT--VEGNGQKWWDLPCKPHRgpdgsssSGPCA-SPTMIRFFMSNNIEVKGLRIQNSPQFHMK 237
Cdd:PLN02218 147 SKWIMFDGVNNLSVDGGSTgvVDGNGETWWQNSCKRNK-------AKPCTkAPTALTFYNSKSLIVKNLRVRNAQQIQIS 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  238 FDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSLGVHNS 317
Cdd:PLN02218 220 IEKCSNVQVSNVVVTAPADSPNTDGIHITNTQNIRVSNSIIGTGDDCISIESGSQNVQINDITCGPGHGISIGSLGDDNS 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  318 QACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNCIIVDQYYCQSKDCRNETSAVKVFDVEYRNIK 397
Cdd:PLN02218 300 KAFVSGVTVDGAKLSGTDNGVRIKTYQGGSGTASNIIFQNIQMENVKNPIIIDQDYCDKSKCTSQQSAVQVKNVVYRNIS 379

                        330       340       350
                 ....*....|....*....|....*....|
gi 15221078  398 GTyDVRSPPIHFACSDTVACTNITMSEVEL 427
Cdd:PLN02218 380 GT-SASDVAITFNCSKNYPCQGIVLDNVNI 408
PLN02188 PLN02188
polygalacturonase/glycoside hydrolase family protein
 73-454 1.80e-82

polygalacturonase/glycoside hydrolase family protein


Pssm-ID: 215120 [Multi-domain]  Cd Length: 404  Bit Score: 260.55  E-value: 1.80e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   73 DSDSGCVFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGVVLAPEGGVFKITSTIFSGPCKPglVFQLDGVLmppDGPE 152
Cdd:PLN02188  30 KGSSTFLFDVRSFGARANGHTDDSKAFMAAWKAACASTGAVTLLIPPGTYYIGPVQFHGPCTN--VSSLTFTL---KAAT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  153 EWPEKDNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDLPCKPHRGPdgssssgpCAS-PTMIRFFMSNNIEVKGLRIQNS 231
Cdd:PLN02188 105 DLSRYGSGNDWIEFGWVNGLTLTGGGTFDGQGAAAWPFNKCPIRKD--------CKLlPTSVKFVNMNNTVVRGITSVNS 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  232 PQFHMKFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGS 311
Cdd:PLN02188 177 KFFHIALVECRNFKGSGLKISAPSDSPNTDGIHIERSSGVYISDSRIGTGDDCISIGQGNSQVTITRIRCGPGHGISVGS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  312 LGVHNSQACVSNITVRNTVIRDSDNGLRVKTWQG--GTGSVSNLLFENIQMENVLNCIIVDQYYCQSKDC-RNETSAVKV 388
Cdd:PLN02188 257 LGRYPNEGDVTGLVVRDCTFTGTTNGIRIKTWANspGKSAATNMTFENIVMNNVTNPIIIDQKYCPFYSCeSKYPSGVTL 336

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221078  389 FDVEYRNIKGTyDVRSPPIHFACSDTVACTNITMSEVELLPEEGELVDDPFCWNAYGKQETLTIPP 454
Cdd:PLN02188 337 SDIYFKNIRGT-SSSQVAVLLKCSRGVPCQGVYLQDVHLDLSSGEGGTSSSCENVRAKYIGTQIPP 401
PLN03010 PLN03010
polygalacturonase
 77-433 1.50e-75

polygalacturonase


Pssm-ID: 215540 [Multi-domain]  Cd Length: 409  Bit Score: 242.98  E-value: 1.50e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   77 GCVFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGV--VLAPEGGVFKITSTIFSGPCKPGLV-FQLDGVLMPPDGPEE 153
Cdd:PLN03010  44 GQNYNVLKFGAKGDGQTDDSNAFLQAWNATCGGEGNIntLLIPSGKTYLLQPIEFKGPCKSTSIkVQLDGIIVAPSNIVA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  154 WpeKDNKNQ-WLVFYRLDGFTFSGKGTVEGNGQKWWDlpckphrgpdgssssgpcasptMIRFFMSNNIEVKGLRIQNSP 232
Cdd:PLN03010 124 W--SNPKSQmWISFSTVSGLMIDGSGTIDGRGSSFWE----------------------ALHISKCDNLTINGITSIDSP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  233 QFHMKFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSL 312
Cdd:PLN03010 180 KNHISIKTCNYVAISKINILAPETSPNTDGIDISYSTNINIFDSTIQTGDDCIAINSGSSNINITQINCGPGHGISVGSL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  313 GVHNSQACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNCIIVDQYYC-QSKDCRNETSAVKVFDV 391
Cdd:PLN03010 260 GADGANAKVSDVHVTHCTFNQTTNGARIKTWQGGQGYARNISFENITLINTKNPIIIDQQYIdKGKLDATKDSAVAISNV 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 15221078  392 EYRNIKGTyDVRSPPIHFACSDTVACTNITMSEVELLPEEGE 433
Cdd:PLN03010 340 KYVGFRGT-TSNENAITLKCSAITHCKDVVMDDIDVTMENGE 380
PLN03003 PLN03003
Probable polygalacturonase At3g15720
 80-458 2.19e-75

Probable polygalacturonase At3g15720


Pssm-ID: 178580 [Multi-domain]  Cd Length: 456  Bit Score: 243.82  E-value: 2.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   80 FDVTSFGAVGDGSCDDTAAFQDAWKAACA-VESGVVLAPEGGVFKITSTIFSGPCKPGLVF-QLDGVLMPPDgPEEWpeK 157
Cdd:PLN03003  24 LDVTQFGAVGDGVTDDSQAFLKAWEAVCSgTGDGQFVVPAGMTFMLQPLKFQGSCKSTPVFvQMLGKLVAPS-KGNW--K 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  158 DNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDlpckpHRGpdgssssgpcASPTMIRFFMSNNIEVKGLRIQNSPQFHMK 237
Cdd:PLN03003 101 GDKDQWILFTDIEGLVIEGDGEINGQGSSWWE-----HKG----------SRPTALKFRSCNNLRLSGLTHLDSPMAHIH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  238 FDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSLGVHNS 317
Cdd:PLN03003 166 ISECNYVTISSLRINAPESSPNTDGIDVGASSNVVIQDCIIATGDDCIAINSGTSNIHISGIDCGPGHGISIGSLGKDGE 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  318 QACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNCIIVDQYYC-----QSKDcrNETSAVKVFDVE 392
Cdd:PLN03003 246 TATVENVCVQNCNFRGTMNGARIKTWQGGSGYARMITFNGITLDNVENPIIIDQFYNggdsdNAKD--RKSSAVEVSKVV 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221078  393 YRNIKGTYDVRSpPIHFACSDTVACTNITMSEV--ELLPEEGELVDDPFCWNAYGKQeTLTIPPIDCL 458
Cdd:PLN03003 324 FSNFIGTSKSEY-GVDFRCSERVPCTEIFLRDMkiETASSGSGQVAQGQCLNVRGAS-TIAVPGLECL 389
Glyco_hydro_28 pfam00295
Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2. ...
 156-427 6.69e-72

Glycosyl hydrolases family 28; Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism.


Pssm-ID: 425588 [Multi-domain]  Cd Length: 319  Bit Score: 230.35  E-value: 6.69e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   156 EKDNKNQWLVFYRLDGFTFSGkGTVEGNGQKWWDLPCKphrgpdgSSSSGPCAsPTMIRFFMSNNIEVKGLRIQNSPQFH 235
Cdd:pfam00295  38 EWNGKLIWISGSSITVTGASG-GTIDGQGQRWWDGKGT-------KKNGGKKK-PKFIYIHKVKNSKITGLNIKNSPVFH 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   236 MKFDGCQGVLINEIQISSP---KLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGcSDVDIQGVTCGPSHGISIGSL 312
Cdd:pfam00295 109 FSVQSGTDLTISDITIDNSagdSNGHNTDGFDVGSSSGVTISNTNIYNQDDCIAINSG-SNISITNVTCGGGHGISIGSV 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   313 GVHNSQAcVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENV-LNCIIVDQYYCQSKDCRNETSAVKVFDV 391
Cdd:pfam00295 188 GGRSDNT-VKNVTVKDSTVVNSDNGVRIKTISGATGTVSNITYENIVLSNIsKYGIVIDQDYENGEPTGKPTSGVKISDI 266

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 15221078   392 EYRNIKGTYDVRSPPIHFACSDTVaCTNITMSEVEL 427
Cdd:pfam00295 267 TFKNVTGTVASSATAVYLLCGDGS-CSGWTWSGVNI 301
PLN02155 PLN02155
polygalacturonase
 74-458 2.27e-71

polygalacturonase


Pssm-ID: 165802 [Multi-domain]  Cd Length: 394  Bit Score: 231.50  E-value: 2.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078   74 SDSGCVFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGVVLAPEGGVFKITSTIFSGPCKPGLVFQLDGVLMppdGPEE 153
Cdd:PLN02155  22 SSASNVFNVVSFGAKPDGVTDSTAAFLKAWQGACGSASSATVVVPTGTFLLKVITFGGPCKSKITFQVAGTVV---APED 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  154 WPEKDNKNQWLVFYRLDGFTFSGkGTVEGNGQKWWDLPCKPHRGPDGSSSsgpcasptmIRFFMSNNIEVKGLRIQNSPQ 233
Cdd:PLN02155  99 YRTFGNSGYWILFNKVNRFSLVG-GTFDARANGFWSCRKSGQNCPPGVRS---------ISFNSAKDVIISGVKSMNSQV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  234 FHMKFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTGCSDVDIQGVTCGPSHGISIGSLG 313
Cdd:PLN02155 169 SHMTLNGCTNVVVRNVKLVAPGNSPNTDGFHVQFSTGVTFTGSTVQTGDDCVAIGPGTRNFLITKLACGPGHGVSIGSLA 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  314 VHNSQACVSNITVRNTVIRDSDNGLRVKTW-QGGTGSVSNLLFENIQMENVLNCIIVDQYYCQSKD-CRNETSAVKVFDV 391
Cdd:PLN02155 249 KELNEDGVENVTVSSSVFTGSQNGVRIKSWaRPSTGFVRNVFFQDLVMKNVENPIIIDQNYCPTHEgCPNEYSGVKISQV 328

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221078  392 EYRNIKGTYDVRSpPIHFACSDTVACTNITMSEVELLPEEGELVDDpFCWNAYGKQETLtIPPIDCL 458
Cdd:PLN02155 329 TYKNIQGTSATQE-AMKLVCSKSSPCTGITLQDIKLTYNKGTPATS-FCFNAVGKSLGV-IQPTSCL 392
Pgu1 COG5434
Polygalacturonase [Carbohydrate transport and metabolism];
79-399 5.50e-63

Polygalacturonase [Carbohydrate transport and metabolism];


Pssm-ID: 444185 [Multi-domain]  Cd Length: 373  Bit Score: 208.91  E-value: 5.50e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078  79 VFDVTSFGAVGDGSCDDTAAFQDAWKAACAVESGVVLAPEGgVFKiTSTIFsgpCKPGLVFQLD--GVLMPPDGPEEWP- 155
Cdd:COG5434   9 TFNITDFGAKGDGKTLNTAAIQKAIDACAAAGGGTVLVPAG-TYL-TGPIF---LKSNVTLHLEkgATLLGSTDPADYPl 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 156 --------EKDNKNQWLVFYRLDGFTFSGKGTVEGNGQKWWDLPCKPHRGPDGSSSSGPCASPTMIRFFMSNNIEVKGLR 227
Cdd:COG5434  84 vetrweggELKGYSALIYAENAENIAITGEGTIDGNGDAWWPWKKEARQSGWVPVGAYDYLRPRLIQLKNCKNVLLEGVT 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 228 IQNSPQFHMKFDGCQGVLINEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIGTG----------CSDVDIQ 297
Cdd:COG5434 164 LRNSPFWTIHPLGCENVTVDGVTIDNPADAPNTDGIDPDSCRNVLIENCYIDTGDDAIAIKSGrdadgrrnrpTENIVIR 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 298 GVTCGPSHG-ISIGSlgvhNSQACVSNITVRNTVIRDSDNGLRVKTWQGGTGSVSNLLFENIQMENVLNC-IIVDQYYcq 375
Cdd:COG5434 244 NCTFRSGHGgIVIGS----ETSGGVRNVTVENCTFDGTDRGLRIKSRRGRGGVVENITIRNITMRNVKGTpIFINLFY-- 317

                       330       340
                ....*....|....*....|....
gi 15221078 376 SKDCRNETSAVKvfDVEYRNIKGT 399
Cdd:COG5434 318 EGDRGGPTPTFR--NITISNVTAT 339
Pectate_lyase_3 pfam12708
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure ...
 80-128 6.06e-05

Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.


Pssm-ID: 403800 [Multi-domain]  Cd Length: 213  Bit Score: 44.23  E-value: 6.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15221078    80 FDVTSFGAVGDGSCDDTAAFQDAWKAACAVESG-VVLAPeGGVFKITSTI 128
Cdd:pfam12708   2 RNVKDYGAKGDGVTDDTAAIQKAIDDGGATTTPaVVYFP-PGTYLVSSPI 50
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
 73-129 3.03e-04

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 43.27  E-value: 3.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15221078  73 DSDSGCVFDVTSFGAVGDGSCDDTAAFQDAWKAacAVESGVVLAPEgGVFKITSTIF 129
Cdd:cd23668 297 DYPASQFVNVKDYGAKGDGVTDDTAALQAILNT--AAGGKIVYFPA-GTYIVTDTLF 350
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 218-338 1.86e-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: 40.29  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 218 SNNIEVKGLRIQNsPQFHMKFDGCQGVLI--NEIQISSPKLSPNTDGIHLGNTRSVGIYNSVVSNGDDCISIgTGCSDVD 295
Cdd:COG3420 106 ADNAVIENNRIEN-NLFGIYLEGSDNNVIrnNTISGNRDLRADRGNGIHLWNSPGNVIEGNTISGGRDGIYL-EFSDNNV 183

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15221078 296 IQGVTcgpshgISIGSLGVHNSQAcvSNITVRNTVIRDSDNGL 338
Cdd:COG3420 184 IRNNT------IRNLRYGIHYMYS--NDNLVEGNTFRDNGAGI 218
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 218-338 2.49e-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: 39.90  E-value: 2.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221078 218 SNNIEVKGLRIQNSPQFHMKFDGcqGVLI---NEIQISSPKLSPNTDGIHLGNTRSVGIY-NSVVSNGDDCISIGTG--- 290
Cdd:COG3420  77 ADNVTVRGLTITGSGDSLTDDDA--GIYVrgaDNAVIENNRIENNLFGIYLEGSDNNVIRnNTISGNRDLRADRGNGihl 154

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15221078 291 --CSDVDIQGVT-CGPSHGISIgslgvHNSqacvSNITVRNTVIRDSDNGL 338
Cdd:COG3420 155 wnSPGNVIEGNTiSGGRDGIYL-----EFS----DNNVIRNNTIRNLRYGI 196
GH55_beta13glucanase-like cd23668
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
 70-102 4.66e-03

fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.


Pssm-ID: 467840 [Multi-domain]  Cd Length: 623  Bit Score: 39.42  E-value: 4.66e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15221078  70 APGDSDSG-CVF-DVTSFGAVGDGSCDDTAAFQDA 102
Cdd:cd23668  12 SPFNPNSSyKVFrNVKDYGAKGDGVTDDTAAINAA 46
 
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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