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Conserved domains on  [gi|293334319|ref|NP_001167809|]
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Peroxidase 4-like precursor [Zea mays]

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 ...
32-322 4.53e-169

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: 471.23  E-value: 4.53e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  32 STSFYSKKCPDVQSIVRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDDTATFTGEKNAGPNaNSVRGYEVIDA 111
Cdd:cd00693    3 SVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVIDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 112 IKARVEASCNATVSCADILALAARDAVNLLGGPSWTVYLGRRDARTaSQSDANANLPGPGSSLATLVTMFGNKGLSARDM 191
Cdd:cd00693   82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV-SSANDVGNLPSPFFSVSQLISLFASKGLTVTDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 192 TALSGAHTVGQARCATFRNRIYN-------DGNINATFASLRQQTCPLAGGDAALAPIDVQTPEAFDNAYYKNLMARQGL 264
Cdd:cd00693  161 VALSGAHTIGRAHCSSFSDRLYNfsgtgdpDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 293334319 265 FHSDQELFNGGSQDALVKKYSGNAAMFTADFAKAMVRMGAISPLTATQGEVRLDCRKV 322
Cdd:cd00693  241 LTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
32-322 4.53e-169

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: 471.23  E-value: 4.53e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  32 STSFYSKKCPDVQSIVRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDDTATFTGEKNAGPNaNSVRGYEVIDA 111
Cdd:cd00693    3 SVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVIDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 112 IKARVEASCNATVSCADILALAARDAVNLLGGPSWTVYLGRRDARTaSQSDANANLPGPGSSLATLVTMFGNKGLSARDM 191
Cdd:cd00693   82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV-SSANDVGNLPSPFFSVSQLISLFASKGLTVTDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 192 TALSGAHTVGQARCATFRNRIYN-------DGNINATFASLRQQTCPLAGGDAALAPIDVQTPEAFDNAYYKNLMARQGL 264
Cdd:cd00693  161 VALSGAHTIGRAHCSSFSDRLYNfsgtgdpDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 293334319 265 FHSDQELFNGGSQDALVKKYSGNAAMFTADFAKAMVRMGAISPLTATQGEVRLDCRKV 322
Cdd:cd00693  241 LTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
47-287 1.86e-80

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 242.47  E-value: 1.86e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319   47 VRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDdtaTFTGEKNAGPNANSVRGYEVIDAIKARVEASCNATVSC 126
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  127 ADILALAARDAVNLLGGPSWTVYLGRRDARTASQSDANANLPGPGSSLATLVTMFGNKGLSARDMTALSGAHTVGQARca 206
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  207 tfrnriyndgninatfaslrqqtcplaggdaalapidvqtpeafdnayyKNLMARQGLFHSDQELFNGGSQDALVKKYSG 286
Cdd:pfam00141 156 -------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVERYAA 186

                  .
gi 293334319  287 N 287
Cdd:pfam00141 187 D 187
PLN03030 PLN03030
cationic peroxidase; Provisional
35-323 6.27e-80

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 246.02  E-value: 6.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  35 FYSKKCPDVQSIVRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDDTATftgEKNAGPNAnSVRGYEVIDAIKA 114
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT---EKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 115 RVEASCNATVSCADILALAARDAVNLLGGPSWTVYLGRRDARTASQSDANaNLPGPGSSLATLVTMFGNKGLSARDMTAL 194
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 195 SGAHTVGQARCATFRNRIYN--------DGNINATFASLRQQTCPLAGGDAALAPIDVQTPEAFDNAYYKNLMARQGLFH 266
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNftttgngaDPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILE 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 293334319 267 SDQELFNGGSQDALVKKYSGNAAM----FTADFAKAMVRMGAISPLTATQGEVRLDCRKVN 323
Cdd:PLN03030 264 SDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
32-322 4.53e-169

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: 471.23  E-value: 4.53e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  32 STSFYSKKCPDVQSIVRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDDTATFTGEKNAGPNaNSVRGYEVIDA 111
Cdd:cd00693    3 SVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVIDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 112 IKARVEASCNATVSCADILALAARDAVNLLGGPSWTVYLGRRDARTaSQSDANANLPGPGSSLATLVTMFGNKGLSARDM 191
Cdd:cd00693   82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV-SSANDVGNLPSPFFSVSQLISLFASKGLTVTDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 192 TALSGAHTVGQARCATFRNRIYN-------DGNINATFASLRQQTCPLAGGDAALAPIDVQTPEAFDNAYYKNLMARQGL 264
Cdd:cd00693  161 VALSGAHTIGRAHCSSFSDRLYNfsgtgdpDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 293334319 265 FHSDQELFNGGSQDALVKKYSGNAAMFTADFAKAMVRMGAISPLTATQGEVRLDCRKV 322
Cdd:cd00693  241 LTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
47-287 1.86e-80

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 242.47  E-value: 1.86e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319   47 VRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDdtaTFTGEKNAGPNANSVRGYEVIDAIKARVEASCNATVSC 126
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  127 ADILALAARDAVNLLGGPSWTVYLGRRDARTASQSDANANLPGPGSSLATLVTMFGNKGLSARDMTALSGAHTVGQARca 206
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  207 tfrnriyndgninatfaslrqqtcplaggdaalapidvqtpeafdnayyKNLMARQGLFHSDQELFNGGSQDALVKKYSG 286
Cdd:pfam00141 156 -------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVERYAA 186

                  .
gi 293334319  287 N 287
Cdd:pfam00141 187 D 187
PLN03030 PLN03030
cationic peroxidase; Provisional
35-323 6.27e-80

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 246.02  E-value: 6.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  35 FYSKKCPDVQSIVRAGVASAVAAEKRMGASILRMFFHDCFVNGCDASILLDDTATftgEKNAGPNAnSVRGYEVIDAIKA 114
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT---EKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 115 RVEASCNATVSCADILALAARDAVNLLGGPSWTVYLGRRDARTASQSDANaNLPGPGSSLATLVTMFGNKGLSARDMTAL 194
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 195 SGAHTVGQARCATFRNRIYN--------DGNINATFASLRQQTCPLAGGDAALAPIDVQTPEAFDNAYYKNLMARQGLFH 266
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNftttgngaDPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILE 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 293334319 267 SDQELFNGGSQDALVKKYSGNAAM----FTADFAKAMVRMGAISPLTATQGEVRLDCRKVN 323
Cdd:PLN03030 264 SDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
45-303 1.15e-31

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: 118.80  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  45 SIVRAGVASAVAAEKRMGASILRMFFHDCFV--------NGCDASILLDDtatftgEKNAGPNANSVRGYEVIDAIKARV 116
Cdd:cd00314    1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRFEP------ELDRPENGGLDKALRALEPIKSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 117 EASCnaTVSCADILALAARDAVNLL--GGPSWTVYLGRRDARTASQS--DANANLPGPGSSLATLVTMFGNKGLSARDMT 192
Cdd:cd00314   75 DGGN--PVSRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGvpDPEGLLPNETSSATELRDKFKRMGLSPSELV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 193 ALS-GAHTV-GQARCATFrnriyndgninatfaslrqqtcplaggDAALAPIDVQTPEAFDNAYYKNL------------ 258
Cdd:cd00314  153 ALSaGAHTLgGKNHGDLL---------------------------NYEGSGLWTSTPFTFDNAYFKNLldmnwewrvgsp 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 293334319 259 ----MARQGLFHSDQELFNGGSQDALVKKYSGNAAMFTADFAKAMVRMG 303
Cdd:cd00314  206 dpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMV 254
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
47-302 1.05e-19

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: 86.49  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  47 VRAGVASAVAaEKRMGASILRMFFH-----DCFVN--GCDASIllddtaTFTGEKNAGPNANSVRGYEVIDAIKARveas 119
Cdd:cd00691   16 ARNDIAKLID-DKNCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAGLDIARKLLEPIKKK---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 120 cNATVSCADILALAARDAVNLLGGPSWTVYLGRRDARTASQSDANANLPGPGSSLATLVTMFGNKGLSARDMTALSGAHT 199
Cdd:cd00691   85 -YPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 200 VGqaRCatFRNRiyndgninatfaslrqqtcplAGGDAALAPidvqTPEAFDNAYYKNLM------ARQGL--FHSDQEL 271
Cdd:cd00691  164 LG--RC--HKER---------------------SGYDGPWTK----NPLKFDNSYFKELLeedwklPTPGLlmLPTDKAL 214
                        250       260       270
                 ....*....|....*....|....*....|.
gi 293334319 272 FNGGSQDALVKKYSGNAAMFTADFAKAMVRM 302
Cdd:cd00691  215 LEDPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
57-310 8.23e-16

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 75.89  E-value: 8.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  57 AEKRMGASILRMFFHDCFVNGCDASILLD-DTATFTGEKNAGPNANSVRGYEVIDAIKARVeascnATVSCADILALAAR 135
Cdd:PLN02364  28 AEKNCAPIMVRLAWHSAGTFDCQSRTGGPfGTMRFDAEQAHGANSGIHIALRLLDPIREQF-----PTISFADFHQLAGV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 136 DAVNLLGGPSWTVYLGRRDArtaSQSDANANLPGPGSSLATLVTMFGNK-GLSARDMTALSGAHTVGqaRCATFRnriyn 214
Cdd:PLN02364 103 VAVEVTGGPDIPFHPGREDK---PQPPPEGRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLG--RCHKDR----- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 215 dgninatfaslrqqtcplAGGDAALapidVQTPEAFDNAYYKNLMA--RQGLFH--SDQELFNGGSQDALVKKYSGNAAM 290
Cdd:PLN02364 173 ------------------SGFEGAW----TSNPLIFDNSYFKELLSgeKEGLLQlvSDKALLDDPVFRPLVEKYAADEDA 230
                        250       260
                 ....*....|....*....|
gi 293334319 291 FTADFAKAMVRMGAISPLTA 310
Cdd:PLN02364 231 FFADYAEAHMKLSELGFADA 250
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
65-322 3.56e-11

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: 63.18  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  65 ILRMFFHDCFV------------NGCDASILLDDTATFTGEKNAGPNansvrgyEVIDAIKARVEascNATVSCADILAL 132
Cdd:cd00692   41 SLRLTFHDAIGfspalaagqfggGGADGSIVLFDDIETAFHANIGLD-------EIVEALRPFHQ---KHNVSMADFIQF 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 133 AARDAV-NLLGGPSWTVYLGRRDARTASqsdANANLPGPGSSLATLVTMFGNKGLSARDMTALSGAHTVGQARcatfrnr 211
Cdd:cd00692  111 AGAVAVsNCPGAPRLEFYAGRKDATQPA---PDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQD------- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 212 iyndgNINATFASlrqqtcplaggdaalAPIDvQTPEAFDNAYYKNLMAR----------QGL----------FHSDQEL 271
Cdd:cd00692  181 -----FVDPSIAG---------------TPFD-STPGVFDTQFFIETLLKgtafpgsggnQGEvesplpgefrLQSDFLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 293334319 272 fnggSQDALV----KKYSGNAAMFTADFAKAMVRMGAI----SPLTatqgevrlDCRKV 322
Cdd:cd00692  240 ----ARDPRTacewQSFVNNQAKMNAAFAAAMLKLSLLgqdnISLT--------DCSDV 286
PLN02879 PLN02879
L-ascorbate peroxidase
124-305 3.05e-10

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 59.69  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 124 VSCADILALAARDAVNLLGGPSWTVYLGRRDArtaSQSDANANLPGPGSSLATLVTMFGNKGLSARDMTALSGAHTVGqa 203
Cdd:PLN02879  92 LSYADFYQLAGVVAVEITGGPEIPFHPGRLDK---VEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG-- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 204 RCATFRnriyndgninatfaslrqqtcplAGGDAALapidVQTPEAFDNAYYKNLMA--RQGLFH--SDQELFNGGSQDA 279
Cdd:PLN02879 167 RCHKER-----------------------SGFEGAW----TPNPLIFDNSYFKEILSgeKEGLLQlpTDKALLDDPLFLP 219
                        170       180
                 ....*....|....*....|....*.
gi 293334319 280 LVKKYSGNAAMFTADFAKAMVRMGAI 305
Cdd:PLN02879 220 FVEKYAADEDAFFEDYTEAHLKLSEL 245
PLN02608 PLN02608
L-ascorbate peroxidase
54-204 4.84e-08

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 53.61  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  54 AVAAEKRMGASILRMFFHDCFVNgcdasilldDTATFTGeknaGPNAnSVRGYE------------VID---AIKARvea 118
Cdd:PLN02608  23 ALIASKNCAPIMLRLAWHDAGTY---------DAKTKTG----GPNG-SIRNEEeyshgannglkiAIDlcePVKAK--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 119 scNATVSCADILALAARDAVNLLGGPSWTVYLGRRDArtaSQSDANANLPGPGSSLATLVTMFGNKGLSARDMTALSGAH 198
Cdd:PLN02608  86 --HPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDS---NACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGH 160

                 ....*.
gi 293334319 199 TVGQAR 204
Cdd:PLN02608 161 TLGRAH 166
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
53-208 3.12e-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: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319  53 SAVAAEKRMGASILRMFFHDCF-------VNGCDASILLDdtatFTGEKNAGPNANSVRGYevidaikarVEASCNATVS 125
Cdd:cd08201   33 CAPGPGRQAAAEWLRTAFHDMAthnvddgTGGLDASIQYE----LDRPENIGSGFNTTLNF---------FVNFYSPRSS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 293334319 126 CADILALAARDAVNLLGGPSWTVYLGRRDARTASQsdanANLPGPGSSLATLVTMFGNKGLSARDMTALSG-AHTVGQAR 204
Cdd:cd08201  100 MADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQ----AGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVH 175

                 ....
gi 293334319 205 CATF 208
Cdd:cd08201  176 SEDF 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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