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Conserved domains on  [gi|670441236|ref|XP_008660905|]
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peroxidase 4 [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 ...
27-322 7.29e-157

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: 440.41  E-value: 7.29e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  27 LKVGYYDKTCPDVQQIVQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDETPFFESEKDATPNaNSLHGFDVID 106
Cdd:cd00693    2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 107 EIKSYVEHACPATVSCADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEYgLPAPNSTLAELINLFKQYDLDARD 186
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 187 MAALSGAHTIGTARCHHYRDRVYGYNGEGGAD--IDPSFAELRRQTCQSAYDAP--APFDEQTPMRFDNAYYRDLVGRRG 262
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDptLDPAYAAQLRKKCPAGGDDDtlVPLDPGTPNTFDNSYYKNLLAGRG 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 263 LLTSDQALYGyGGPLDHLVKMYSTNGEAFAKDFAKAIVKMGKIPPPHGMQGEIRLSCSKI 322
Cdd:cd00693  240 LLTSDQALLS-DPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
27-322 7.29e-157

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: 440.41  E-value: 7.29e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  27 LKVGYYDKTCPDVQQIVQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDETPFFESEKDATPNaNSLHGFDVID 106
Cdd:cd00693    2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 107 EIKSYVEHACPATVSCADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEYgLPAPNSTLAELINLFKQYDLDARD 186
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 187 MAALSGAHTIGTARCHHYRDRVYGYNGEGGAD--IDPSFAELRRQTCQSAYDAP--APFDEQTPMRFDNAYYRDLVGRRG 262
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDptLDPAYAAQLRKKCPAGGDDDtlVPLDPGTPNTFDNSYYKNLLAGRG 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 263 LLTSDQALYGyGGPLDHLVKMYSTNGEAFAKDFAKAIVKMGKIPPPHGMQGEIRLSCSKI 322
Cdd:cd00693  240 LLTSDQALLS-DPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
5-323 4.01e-74

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 231.38  E-value: 4.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236   5 RTCSWLIVLSVLLVCTTANGDRLKVGYYDKTCPDVQQIVQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDETp 84
Cdd:PLN03030   3 RFIVILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGS- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  85 ffESEKDATPNAnSLHGFDVIDEIKSYVEHACPATVSCADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEyGLP 164
Cdd:PLN03030  82 --NTEKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 165 APNSTLAELINLFKQYDLDARDMAALSGAHTIGTARCHHYRDRVYGYNGEG-GAD--IDPSFAELRRQTCQSAYDAP--A 239
Cdd:PLN03030 158 GFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGnGADpsIDASFVPQLQALCPQNGDGSrrI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 240 PFDEQTPMRFDNAYYRDLVGRRGLLTSDQALYGYGGPLDHLVKMYSTNGEA---FAKDFAKAIVKMGKIPPPHGMQGEIR 316
Cdd:PLN03030 238 ALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGVRGLAglnFNVEFGRSMVKMSNIGVKTGTNGEIR 317

                 ....*..
gi 670441236 317 LSCSKIN 323
Cdd:PLN03030 318 KVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-287 3.28e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 221.28  E-value: 3.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236   43 VQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDEtpfFESEKDATPNANSLHGFDVIDEIKSYVEHACPATVSC 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  123 ADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEYGLPAPNSTLAELINLFKQYDLDARDMAALSGAHTIGTARch 202
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  203 hyrdrvygyngeggadidpsfaelrrqtcqsaydapapfdeqtpmrfdnayyRDLVGRRGLLTSDQALYGyGGPLDHLVK 282
Cdd:pfam00141 156 ----------------------------------------------------KNLLDGRGLLTSDQALLS-DPRTRALVE 182

                  ....*
gi 670441236  283 MYSTN 287
Cdd:pfam00141 183 RYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
27-322 7.29e-157

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: 440.41  E-value: 7.29e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  27 LKVGYYDKTCPDVQQIVQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDETPFFESEKDATPNaNSLHGFDVID 106
Cdd:cd00693    2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 107 EIKSYVEHACPATVSCADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEYgLPAPNSTLAELINLFKQYDLDARD 186
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 187 MAALSGAHTIGTARCHHYRDRVYGYNGEGGAD--IDPSFAELRRQTCQSAYDAP--APFDEQTPMRFDNAYYRDLVGRRG 262
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDptLDPAYAAQLRKKCPAGGDDDtlVPLDPGTPNTFDNSYYKNLLAGRG 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 263 LLTSDQALYGyGGPLDHLVKMYSTNGEAFAKDFAKAIVKMGKIPPPHGMQGEIRLSCSKI 322
Cdd:cd00693  240 LLTSDQALLS-DPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
5-323 4.01e-74

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 231.38  E-value: 4.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236   5 RTCSWLIVLSVLLVCTTANGDRLKVGYYDKTCPDVQQIVQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDETp 84
Cdd:PLN03030   3 RFIVILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGS- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  85 ffESEKDATPNAnSLHGFDVIDEIKSYVEHACPATVSCADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEyGLP 164
Cdd:PLN03030  82 --NTEKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 165 APNSTLAELINLFKQYDLDARDMAALSGAHTIGTARCHHYRDRVYGYNGEG-GAD--IDPSFAELRRQTCQSAYDAP--A 239
Cdd:PLN03030 158 GFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGnGADpsIDASFVPQLQALCPQNGDGSrrI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 240 PFDEQTPMRFDNAYYRDLVGRRGLLTSDQALYGYGGPLDHLVKMYSTNGEA---FAKDFAKAIVKMGKIPPPHGMQGEIR 316
Cdd:PLN03030 238 ALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGVRGLAglnFNVEFGRSMVKMSNIGVKTGTNGEIR 317

                 ....*..
gi 670441236 317 LSCSKIN 323
Cdd:PLN03030 318 KVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-287 3.28e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 221.28  E-value: 3.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236   43 VQSVMAFRVGRDQSVAPAVLRLFFHDCFVDGCDGSVLLDEtpfFESEKDATPNANSLHGFDVIDEIKSYVEHACPATVSC 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  123 ADILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAEYGLPAPNSTLAELINLFKQYDLDARDMAALSGAHTIGTARch 202
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  203 hyrdrvygyngeggadidpsfaelrrqtcqsaydapapfdeqtpmrfdnayyRDLVGRRGLLTSDQALYGyGGPLDHLVK 282
Cdd:pfam00141 156 ----------------------------------------------------KNLLDGRGLLTSDQALLS-DPRTRALVE 182

                  ....*
gi 670441236  283 MYSTN 287
Cdd:pfam00141 183 RYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
41-304 8.29e-30

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: 114.17  E-value: 8.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  41 QIVQSVMAFRVGRDQSVAPAVLRLFFHDCFVD--------GCDGSVLldetpfFESEKDATPNANSLHGFDVIDEIKSYV 112
Cdd:cd00314    1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIR------FEPELDRPENGGLDKALRALEPIKSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 113 EHACPatVSCADILALASRDAVALL--GGPSWKVQLGRKDSRVANRTGA--EYGLPAPNSTLAELINLFKQYDLDARDMA 188
Cdd:cd00314   75 DGGNP--VSRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGVPdpEGLLPNETSSATELRDKFKRMGLSPSELV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 189 ALS-GAHTIGtarchhyrdrvygynGEGGADIDPSFAElrrqtcqsaydapaPFDEQTPMRFDNAYYRDL---------- 257
Cdd:cd00314  153 ALSaGAHTLG---------------GKNHGDLLNYEGS--------------GLWTSTPFTFDNAYFKNLldmnwewrvg 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 670441236 258 ------VGRRGLLTSDQALyGYGGPLDHLVKMYSTNGEAFAKDFAKAIVKMGK 304
Cdd:cd00314  204 spdpdgVKGPGLLPSDYAL-LSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
53-302 1.06e-23

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: 97.66  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  53 RDQSVAPAVLRLFFHDCFV----DGCDGSvllDETPFFESEKDATPNANSLHGFDVIDEIKsyVEHAcpaTVSCADILAL 128
Cdd:cd00691   25 DDKNCAPILVRLAWHDSGTydkeTKTGGS---NGTIRFDPELNHGANAGLDIARKLLEPIK--KKYP---DISYADLWQL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 129 ASRDAVALLGGPSWKVQLGRKDSRVANRTGAEYGLPAPNSTLAELINLFKQYDLDARDMAALSGAHTIGtaRCHhyRDRv 208
Cdd:cd00691   97 AGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLG--RCH--KER- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 209 ygyngeggadidpsfaelrrqtcqSAYDAPAPFDeqtPMRFDNAYYRDLVGRR------GL--LTSDQALYgyggpLD-- 278
Cdd:cd00691  172 ------------------------SGYDGPWTKN---PLKFDNSYFKELLEEDwklptpGLlmLPTDKALL-----EDpk 219
                        250       260
                 ....*....|....*....|....*.
gi 670441236 279 --HLVKMYSTNGEAFAKDFAKAIVKM 302
Cdd:cd00691  220 frPYVELYAKDQDAFFKDYAEAHKKL 245
PLN02608 PLN02608
L-ascorbate peroxidase
55-307 1.28e-14

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 72.87  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  55 QSVAPAVLRLFFHDC-------FVDGCDGSVlldetpffESEKDATPNANSlhGF----DVIDEIKSyvEHAcpaTVSCA 123
Cdd:PLN02608  28 KNCAPIMLRLAWHDAgtydaktKTGGPNGSI--------RNEEEYSHGANN--GLkiaiDLCEPVKA--KHP---KITYA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 124 DILALASRDAVALLGGPSWKVQLGRKDSRVANRTGAeygLPAPNSTLAELINLFKQYDLDARDMAALSGAHTIGTARchh 203
Cdd:PLN02608  93 DLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGR---LPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAH--- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 204 yRDRvygyngeggadidpsfaelrrqtcqSAYDAPApfdEQTPMRFDNAYYRDLV--GRRGL--LTSDQALygyggpLD- 278
Cdd:PLN02608 167 -PER-------------------------SGFDGPW---TKEPLKFDNSYFVELLkgESEGLlkLPTDKAL------LEd 211
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 670441236 279 ----HLVKMYSTNGEAFAKDFA---KAIVKMGKIPP 307
Cdd:PLN02608 212 pefrPYVELYAKDEDAFFRDYAeshKKLSELGFTPP 247
PLN02364 PLN02364
L-ascorbate peroxidase 1
54-305 2.42e-13

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 68.57  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  54 DQSVAPAVLRLFFHDCFVDGCDGSVlldETPF----FESEKDATPNANSLHGFDVIDEIKSYVehacpATVSCADILALA 129
Cdd:PLN02364  29 EKNCAPIMVRLAWHSAGTFDCQSRT---GGPFgtmrFDAEQAHGANSGIHIALRLLDPIREQF-----PTISFADFHQLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 130 SRDAVALLGGPSWKVQLGRKDSrvaNRTGAEYGLPAPNSTLAELINLF-KQYDLDARDMAALSGAHTIGtaRCHhyRDRV 208
Cdd:PLN02364 101 GVVAVEVTGGPDIPFHPGREDK---PQPPPEGRLPDATKGCDHLRDVFaKQMGLSDKDIVALSGAHTLG--RCH--KDRS 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 209 yGYNGEGGADidpsfaelrrqtcqsaydapapfdeqtPMRFDNAYYRDLVG--RRGL--LTSDQALygyggpLDH----- 279
Cdd:PLN02364 174 -GFEGAWTSN---------------------------PLIFDNSYFKELLSgeKEGLlqLVSDKAL------LDDpvfrp 219
                        250       260
                 ....*....|....*....|....*.
gi 670441236 280 LVKMYSTNGEAFAKDFAKAIVKMGKI 305
Cdd:PLN02364 220 LVEKYAADEDAFFADYAEAHMKLSEL 245
PLN02879 PLN02879
L-ascorbate peroxidase
54-305 4.20e-12

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 65.08  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  54 DQSVAPAVLRLFFHDCfvdGCDGSVLLDETPF--FESEKDATPNANSlhGFDVIDEIKSYVEHACPaTVSCADILALASR 131
Cdd:PLN02879  30 EKHCAPIVLRLAWHSA---GTFDVKTKTGGPFgtIRHPQELAHDANN--GLDIAVRLLDPIKELFP-ILSYADFYQLAGV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 132 DAVALLGGPSWKVQLGRKDSRVANRTGAeygLPAPNSTLAELINLFKQYDLDARDMAALSGAHTIGtaRCHHYRDrvyGY 211
Cdd:PLN02879 104 VAVEITGGPEIPFHPGRLDKVEPPPEGR---LPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG--RCHKERS---GF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 212 NGEGgadidpsfaelrrqtcqsaydapapfdEQTPMRFDNAYYRDLVG--RRGLLT--SDQALygYGGPLDH-LVKMYST 286
Cdd:PLN02879 176 EGAW---------------------------TPNPLIFDNSYFKEILSgeKEGLLQlpTDKAL--LDDPLFLpFVEKYAA 226
                        250
                 ....*....|....*....
gi 670441236 287 NGEAFAKDFAKAIVKMGKI 305
Cdd:PLN02879 227 DEDAFFEDYTEAHLKLSEL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
38-323 4.20e-09

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: 57.02  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236  38 DVQQIVQSVMaFRVGRDQSVAPAVLRLFFHDCFV------------DGCDGSVLLdetpfFESEKDATPNANSLHgfDVI 105
Cdd:cd00692   19 DILDDIQGNL-FNGGECGEEAHESLRLTFHDAIGfspalaagqfggGGADGSIVL-----FDDIETAFHANIGLD--EIV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 106 DEIKSYVE-HacpaTVSCADILALASrdAVALL---GGPSWKVQLGRKDSRVANRTGAeygLPAPNSTLAELINLFKQYD 181
Cdd:cd00692   91 EALRPFHQkH----NVSMADFIQFAG--AVAVSncpGAPRLEFYAGRKDATQPAPDGL---VPEPFDSVDKILARFADAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 182 LDARDMAALSGAHTIGTARchhyrdrvygyngeggaDIDPSFAElrrqtcqsaydapAPFDeQTPMRFDNAYYRDLVGRR 261
Cdd:cd00692  162 FSPDELVALLAAHSVAAQD-----------------FVDPSIAG-------------TPFD-STPGVFDTQFFIETLLKG 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 262 GLLTSDQALYGYG-GPL--------DHLV----------KMYSTNGEAFAKDFAKAIVKMGK--------------IPPP 308
Cdd:cd00692  211 TAFPGSGGNQGEVeSPLpgefrlqsDFLLardprtacewQSFVNNQAKMNAAFAAAMLKLSLlgqdnisltdcsdvIPPP 290
                        330
                 ....*....|....*
gi 670441236 309 HGMQGEIRLSCSKIN 323
Cdd:cd00692  291 KPLSQDPTFPAGLTM 305
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
121-200 7.65e-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: 49.77  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670441236 121 SCADILALASRDAVALLGGPSWKVQLGRKDSRVAnrtgAEYGLPAPNSTLAELINLFKQYDLDARDMAALSG-AHTIGTA 199
Cdd:cd08201   99 SMADLIAMGVVTSVASCGGPVVPFRAGRIDATEA----GQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGV 174

                 .
gi 670441236 200 R 200
Cdd:cd08201  175 H 175
 
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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