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Conserved domains on  [gi|1002279097|ref|XP_015643865|]
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peroxidase P7 [Oryza sativa Japonica Group]

Protein Classification

peroxidase( domain architecture ID 10091046)

peroxidase catalyzes removal of H(2)O(2), and is involved in the oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress

EC:  1.11.1.7
Gene Ontology:  GO:0004601|GO:0006979|GO:0020037
PubMed:  11054546
SCOP:  4001128|3000844

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
25-317 1.01e-165

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


:

Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 462.75  E-value: 1.01e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  25 QLSTRYYDGKCPNVQSIVRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDDTANFTGEKNAGPNaNSVRGYEVI 104
Cdd:cd00693     1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 105 DAIKTQVEASCNATVSCADILALAARDAVNLLGGPTWTVQLGRRDALTaSQSAANGNLPGPGSDLATLVTMFGNKGLSPR 184
Cdd:cd00693    80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV-SSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 185 DMTALSGAHTLGQARCATFRSRIFG-------DGNVDAAFAALRQQACPQSGGDTTLAPIDVQTPDAFDNAYYANLVKKQ 257
Cdd:cd00693   159 DLVALSGAHTIGRAHCSSFSDRLYNfsgtgdpDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 258 GLFHSDQELFNGGSQDALVRKYAGNAGMFAADFAKAMVRMGALLPAAGTPTEVRLNCRKV 317
Cdd:cd00693   239 GLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
25-317 1.01e-165

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 462.75  E-value: 1.01e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  25 QLSTRYYDGKCPNVQSIVRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDDTANFTGEKNAGPNaNSVRGYEVI 104
Cdd:cd00693     1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 105 DAIKTQVEASCNATVSCADILALAARDAVNLLGGPTWTVQLGRRDALTaSQSAANGNLPGPGSDLATLVTMFGNKGLSPR 184
Cdd:cd00693    80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV-SSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 185 DMTALSGAHTLGQARCATFRSRIFG-------DGNVDAAFAALRQQACPQSGGDTTLAPIDVQTPDAFDNAYYANLVKKQ 257
Cdd:cd00693   159 DLVALSGAHTIGRAHCSSFSDRLYNfsgtgdpDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 258 GLFHSDQELFNGGSQDALVRKYAGNAGMFAADFAKAMVRMGALLPAAGTPTEVRLNCRKV 317
Cdd:cd00693   239 GLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
42-282 1.25e-79

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 240.16  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  42 VRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDdtaNFTGEKNAGPNANSVRGYEVIDAIKTQVEASCNATVSC 121
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 122 ADILALAARDAVNLLGGPTWTVQLGRRDALTASQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGQARca 201
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 202 tfrsrifgdgnvdaafaalrqqacpqsggdttlapidvqtpdafdnayyANLVKKQGLFHSDQELFNGGSQDALVRKYAG 281
Cdd:pfam00141 156 -------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVERYAA 186

                  .
gi 1002279097 282 N 282
Cdd:pfam00141 187 D 187
PLN03030 PLN03030
cationic peroxidase; Provisional
30-318 4.86e-74

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 230.61  E-value: 4.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  30 YYDGKCPNVQSIVRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDDTANftgEKNAGPNAnSVRGYEVIDAIKT 109
Cdd:PLN03030   29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT---EKTALPNL-LLRGYDVIDDAKT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 110 QVEASCNATVSCADILALAARDAVNLLGGPTWTVQLGRRDALTASQSAANgNLPGPGSDLATLVTMFGNKGLSPRDMTAL 189
Cdd:PLN03030  105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 190 SGAHTLGQARCATFRSRIF--------GDGNVDAAFAALRQQACPQSGGDTTLAPIDVQTPDAFDNAYYANLVKKQGLFH 261
Cdd:PLN03030  184 VGGHTIGTTACQFFRYRLYnftttgngADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILE 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002279097 262 SDQELFNGGSQDALVRKYAGNAGM----FAADFAKAMVRMGALLPAAGTPTEVRLNCRKVN 318
Cdd:PLN03030  264 SDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
25-317 1.01e-165

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 462.75  E-value: 1.01e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  25 QLSTRYYDGKCPNVQSIVRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDDTANFTGEKNAGPNaNSVRGYEVI 104
Cdd:cd00693     1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 105 DAIKTQVEASCNATVSCADILALAARDAVNLLGGPTWTVQLGRRDALTaSQSAANGNLPGPGSDLATLVTMFGNKGLSPR 184
Cdd:cd00693    80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV-SSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 185 DMTALSGAHTLGQARCATFRSRIFG-------DGNVDAAFAALRQQACPQSGGDTTLAPIDVQTPDAFDNAYYANLVKKQ 257
Cdd:cd00693   159 DLVALSGAHTIGRAHCSSFSDRLYNfsgtgdpDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 258 GLFHSDQELFNGGSQDALVRKYAGNAGMFAADFAKAMVRMGALLPAAGTPTEVRLNCRKV 317
Cdd:cd00693   239 GLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
42-282 1.25e-79

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 240.16  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  42 VRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDdtaNFTGEKNAGPNANSVRGYEVIDAIKTQVEASCNATVSC 121
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 122 ADILALAARDAVNLLGGPTWTVQLGRRDALTASQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGQARca 201
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 202 tfrsrifgdgnvdaafaalrqqacpqsggdttlapidvqtpdafdnayyANLVKKQGLFHSDQELFNGGSQDALVRKYAG 281
Cdd:pfam00141 156 -------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVERYAA 186

                  .
gi 1002279097 282 N 282
Cdd:pfam00141 187 D 187
PLN03030 PLN03030
cationic peroxidase; Provisional
30-318 4.86e-74

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 230.61  E-value: 4.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  30 YYDGKCPNVQSIVRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDDTANftgEKNAGPNAnSVRGYEVIDAIKT 109
Cdd:PLN03030   29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT---EKTALPNL-LLRGYDVIDDAKT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 110 QVEASCNATVSCADILALAARDAVNLLGGPTWTVQLGRRDALTASQSAANgNLPGPGSDLATLVTMFGNKGLSPRDMTAL 189
Cdd:PLN03030  105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 190 SGAHTLGQARCATFRSRIF--------GDGNVDAAFAALRQQACPQSGGDTTLAPIDVQTPDAFDNAYYANLVKKQGLFH 261
Cdd:PLN03030  184 VGGHTIGTTACQFFRYRLYnftttgngADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILE 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002279097 262 SDQELFNGGSQDALVRKYAGNAGM----FAADFAKAMVRMGALLPAAGTPTEVRLNCRKVN 318
Cdd:PLN03030  264 SDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
40-298 9.46e-35

Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.


Pssm-ID: 173823 [Multi-domain]  Cd Length: 255  Bit Score: 126.88  E-value: 9.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  40 SIVRAGMAQAVAAEPRMGASILRMFFHDCFV--------NGCDASIllddtaNFTGEKNAGPNANSVRGYEVIDAIKTQV 111
Cdd:cd00314     1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSI------RFEPELDRPENGGLDKALRALEPIKSAY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 112 EASCnaTVSCADILALAARDAVNLL--GGPTWTVQLGRRDALTASQSAAN--GNLPGPGSDLATLVTMFGNKGLSPRDMT 187
Cdd:cd00314    75 DGGN--PVSRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGVPDpeGLLPNETSSATELRDKFKRMGLSPSELV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 188 ALS-GAHTL-GQARCATFRSRifgdgnvdaafaalrqqacpqsggdttLAPIDVQTPDAFDNAYYANL------------ 253
Cdd:cd00314   153 ALSaGAHTLgGKNHGDLLNYE---------------------------GSGLWTSTPFTFDNAYFKNLldmnwewrvgsp 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279097 254 ----VKKQGLFHSDQELFNGGSQDALVRKYAGNAGMFAADFAKAMVRMG 298
Cdd:cd00314   206 dpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMV 254
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
52-297 3.80e-21

Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.


Pssm-ID: 173825 [Multi-domain]  Cd Length: 253  Bit Score: 90.34  E-value: 3.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  52 AEPRMGASILRMFFH-----DCFVN--GCDASIllddtaNFTGEKNAGPNANSVRGYEVIDAIKTQveascNATVSCADI 124
Cdd:cd00691    25 DDKNCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAGLDIARKLLEPIKKK-----YPDISYADL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 125 LALAARDAVNLLGGPTWTVQLGRRDALTASQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGqaRCATFR 204
Cdd:cd00691    94 WQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLG--RCHKER 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 205 SrifgdgNVDAAFAalrqqacpqsggdttlapidvQTPDAFDNAYYANLV------KKQGL--FHSDQELFNGGSQDALV 276
Cdd:cd00691   172 S------GYDGPWT---------------------KNPLKFDNSYFKELLeedwklPTPGLlmLPTDKALLEDPKFRPYV 224
                         250       260
                  ....*....|....*....|.
gi 1002279097 277 RKYAGNAGMFAADFAKAMVRM 297
Cdd:cd00691   225 ELYAKDQDAFFKDYAEAHKKL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
82-300 5.84e-16

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 75.89  E-value: 5.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  82 TANFTGEKNAGPNANSVRGYEVIDAIKTQVeascnATVSCADILALAARDAVNLLGGPTWTVQLGRRDAltaSQSAANGN 161
Cdd:PLN02364   59 TMRFDAEQAHGANSGIHIALRLLDPIREQF-----PTISFADFHQLAGVVAVEVTGGPDIPFHPGREDK---PQPPPEGR 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 162 LPGPGSDLATLVTMFGNK-GLSPRDMTALSGAHTLGqaRCATFRSrifgdgNVDAAFAAlrqqacpqsggdttlapidvq 240
Cdd:PLN02364  131 LPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLG--RCHKDRS------GFEGAWTS--------------------- 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279097 241 TPDAFDNAYYANLV--KKQGLFH--SDQELFNGGSQDALVRKYAGNAGMFAADFAKAMVRMGAL 300
Cdd:PLN02364  182 NPLIFDNSYFKELLsgEKEGLLQlvSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSEL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
60-300 8.22e-12

Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173826 [Multi-domain]  Cd Length: 328  Bit Score: 65.11  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  60 ILRMFFHDCFV------------NGCDASILLDDTANFTGEKNAGPNansvrgyEVIDAIKTQVEascNATVSCADILAL 127
Cdd:cd00692    41 SLRLTFHDAIGfspalaagqfggGGADGSIVLFDDIETAFHANIGLD-------EIVEALRPFHQ---KHNVSMADFIQF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 128 AARDAV-NLLGGPTWTVQLGRRDAltaSQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGQARcatfrsr 206
Cdd:cd00692   111 AGAVAVsNCPGAPRLEFYAGRKDA---TQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQD------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 207 ifgdgNVDAAFAALRQQACP-----QSGGDTTLApiDVQTPDAFDN-AYYANLVKKQGLFHSDQELfnggSQDALVR--- 277
Cdd:cd00692   181 -----FVDPSIAGTPFDSTPgvfdtQFFIETLLK--GTAFPGSGGNqGEVESPLPGEFRLQSDFLL----ARDPRTAcew 249
                         250       260
                  ....*....|....*....|....
gi 1002279097 278 -KYAGNAGMFAADFAKAMVRMGAL 300
Cdd:cd00692   250 qSFVNNQAKMNAAFAAAMLKLSLL 273
PLN02879 PLN02879
L-ascorbate peroxidase
119-300 9.42e-12

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 63.93  E-value: 9.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 119 VSCADILALAARDAVNLLGGPTWTVQLGRRDALtasQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGqa 198
Cdd:PLN02879   92 LSYADFYQLAGVVAVEITGGPEIPFHPGRLDKV---EPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG-- 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 199 RCATFRSRIFGDGnvdaafaalrqqacpqsggdttlapidVQTPDAFDNAYYANLV--KKQGLFH--SDQELFNGGSQDA 274
Cdd:PLN02879  167 RCHKERSGFEGAW---------------------------TPNPLIFDNSYFKEILsgEKEGLLQlpTDKALLDDPLFLP 219
                         170       180
                  ....*....|....*....|....*.
gi 1002279097 275 LVRKYAGNAGMFAADFAKAMVRMGAL 300
Cdd:PLN02879  220 FVEKYAADEDAFFEDYTEAHLKLSEL 245
PLN02608 PLN02608
L-ascorbate peroxidase
118-300 2.41e-09

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 57.47  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 118 TVSCADILALAARDAVNLLGGPTWTVQLGRRDAltaSQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGQ 197
Cdd:PLN02608   88 KITYADLYQLAGVVAVEVTGGPTIDFVPGRKDS---NACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGR 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097 198 ARcatfRSRIFGDGnvdaafaalrqqacPQSggdttlapidvQTPDAFDNAYYANLVKKQ--GLFH--SDQELFNGGSQD 273
Cdd:PLN02608  165 AH----PERSGFDG--------------PWT-----------KEPLKFDNSYFVELLKGEseGLLKlpTDKALLEDPEFR 215
                         170       180
                  ....*....|....*....|....*..
gi 1002279097 274 ALVRKYAGNAGMFAADFAKAMVRMGAL 300
Cdd:PLN02608  216 PYVELYAKDEDAFFRDYAESHKKLSEL 242
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
58-203 2.97e-07

Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.


Pssm-ID: 173829  Cd Length: 264  Bit Score: 50.93  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279097  58 ASILRMFFHDCF-------VNGCDASILLDdtanFTGEKNAGPNANSVRGYevidaiktqVEASCNATVSCADILALAAR 130
Cdd:cd08201    43 AEWLRTAFHDMAthnvddgTGGLDASIQYE----LDRPENIGSGFNTTLNF---------FVNFYSPRSSMADLIAMGVV 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279097 131 DAVNLLGGPTWTVQLGRRDALTASQSAangnLPGPGSDLATLVTMFGNKGLSPRDMTALSG-AHTLGQARCATF 203
Cdd:cd08201   110 TSVASCGGPVVPFRAGRIDATEAGQAG----VPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDF 179
 
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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