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Conserved domains on  [gi|670379539|ref|XP_008670598|]
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peroxidase 2-like [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 ...
72-367 2.28e-136

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: 390.72  E-value: 2.28e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  72 GLTVGYYKN-CPGAEGIVREAVEKAMDNgNRGIGAGLVRIFFHDCFVRGCDASVLLRNTSGssNQTEMFGLPNInSLRGF 150
Cdd:cd00693    1 QLSVGFYSKsCPNAESIVRSVVRAAVKA-DPRLAAALLRLHFHDCFVRGCDASVLLDSTAN--NTSEKDAPPNL-SLRGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 151 QVIDDAKAELEKACPRTVSCADIVAFAARDATRnLSyGAIDFQMPAGRLDGRVSLKEEAEkNLPGPFDSLDDLQKSFAAQ 230
Cdd:cd00693   77 DVIDDIKAALEAACPGVVSCADILALAARDAVV-LA-GGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 231 GLGFNDMVTLSGAHSIGVARCRFFTNRL-------PPNPSdMDRDLARSLKATCDQNGLDSKVVQ-DPVTPVALDNQYYK 302
Cdd:cd00693  154 GLTVTDLVALSGAHTIGRAHCSSFSDRLynfsgtgDPDPT-LDPAYAAQLRKKCPAGGDDDTLVPlDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 670379539 303 NVHNGKVLFTSDAALNSTDDARKVVDGFANNAVDWYRAFADAMVKMGNIRDRTINrpKPEIREKC 367
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGS--QGEIRKNC 295
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
72-367 2.28e-136

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: 390.72  E-value: 2.28e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  72 GLTVGYYKN-CPGAEGIVREAVEKAMDNgNRGIGAGLVRIFFHDCFVRGCDASVLLRNTSGssNQTEMFGLPNInSLRGF 150
Cdd:cd00693    1 QLSVGFYSKsCPNAESIVRSVVRAAVKA-DPRLAAALLRLHFHDCFVRGCDASVLLDSTAN--NTSEKDAPPNL-SLRGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 151 QVIDDAKAELEKACPRTVSCADIVAFAARDATRnLSyGAIDFQMPAGRLDGRVSLKEEAEkNLPGPFDSLDDLQKSFAAQ 230
Cdd:cd00693   77 DVIDDIKAALEAACPGVVSCADILALAARDAVV-LA-GGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 231 GLGFNDMVTLSGAHSIGVARCRFFTNRL-------PPNPSdMDRDLARSLKATCDQNGLDSKVVQ-DPVTPVALDNQYYK 302
Cdd:cd00693  154 GLTVTDLVALSGAHTIGRAHCSSFSDRLynfsgtgDPDPT-LDPAYAAQLRKKCPAGGDDDTLVPlDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 670379539 303 NVHNGKVLFTSDAALNSTDDARKVVDGFANNAVDWYRAFADAMVKMGNIRDRTINrpKPEIREKC 367
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGS--QGEIRKNC 295
PLN03030 PLN03030
cationic peroxidase; Provisional
70-371 1.22e-66

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 213.67  E-value: 1.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  70 GAGLTVGYY-KNCPGAEGIVREAVEKAMdNGNRGIGAGLVRIFFHDCFVRGCDASVLLRNTSgssnqTEMFGLPNInSLR 148
Cdd:PLN03030  22 GQGTRVGFYsTTCPQAESIVRKTVQSHF-QSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN-----TEKTALPNL-LLR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 149 GFQVIDDAKAELEKACPRTVSCADIVAFAARDA---TRNLSYgaidfQMPAGRLDGRVSLKEEAeKNLPGPFDSLDDLQK 225
Cdd:PLN03030  95 GYDVIDDAKTQLEAACPGVVSCADILALAARDSvvlTNGLTW-----PVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 226 SFAAQGLGFNDMVTLSGAHSIGVARCRFFTNRL-----PPNPSD--MDRDLARSLKATCDQNGLDSK-VVQDPVTPVALD 297
Cdd:PLN03030 169 KFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLynfttTGNGADpsIDASFVPQLQALCPQNGDGSRrIALDTGSSNRFD 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670379539 298 NQYYKNVHNGKVLFTSDAALNSTDDARKVVDGFAN----NAVDWYRAFADAMVKMGNIRDRTinRPKPEIREKCFIYN 371
Cdd:PLN03030 249 ASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKT--GTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
88-333 2.03e-63

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 200.48  E-value: 2.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539   88 VREAVEKAMDNgNRGIGAGLVRIFFHDCFVRGCDASVLLRNtsgssNQTEMFGLPNiNSLR-GFQVIDDAKAELEKACPR 166
Cdd:pfam00141   1 VRSVVRAAFKA-DPTMGPSLLRLHFHDCFVGGCDGSVLLDG-----FKPEKDAPPN-LGLRkGFEVIDDIKAKLEAACPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  167 TVSCADIVAFAARDATRNLsyGAIDFQMPAGRLDGRVSLKEEAEKNLPGPFDSLDDLQKSFAAQGLGFNDMVTLSGAHSI 246
Cdd:pfam00141  74 VVSCADILALAARDAVELA--GGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  247 GVARcrfftnrlppnpsdmdrdlarslkatcdqngldskvvqdpvtpvaldnqyyKNVHNGKVLFTSDAALNSTDDARKV 326
Cdd:pfam00141 152 GRAH---------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRAL 180

                  ....*..
gi 670379539  327 VDGFANN 333
Cdd:pfam00141 181 VERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
72-367 2.28e-136

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: 390.72  E-value: 2.28e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  72 GLTVGYYKN-CPGAEGIVREAVEKAMDNgNRGIGAGLVRIFFHDCFVRGCDASVLLRNTSGssNQTEMFGLPNInSLRGF 150
Cdd:cd00693    1 QLSVGFYSKsCPNAESIVRSVVRAAVKA-DPRLAAALLRLHFHDCFVRGCDASVLLDSTAN--NTSEKDAPPNL-SLRGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 151 QVIDDAKAELEKACPRTVSCADIVAFAARDATRnLSyGAIDFQMPAGRLDGRVSLKEEAEkNLPGPFDSLDDLQKSFAAQ 230
Cdd:cd00693   77 DVIDDIKAALEAACPGVVSCADILALAARDAVV-LA-GGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 231 GLGFNDMVTLSGAHSIGVARCRFFTNRL-------PPNPSdMDRDLARSLKATCDQNGLDSKVVQ-DPVTPVALDNQYYK 302
Cdd:cd00693  154 GLTVTDLVALSGAHTIGRAHCSSFSDRLynfsgtgDPDPT-LDPAYAAQLRKKCPAGGDDDTLVPlDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 670379539 303 NVHNGKVLFTSDAALNSTDDARKVVDGFANNAVDWYRAFADAMVKMGNIRDRTINrpKPEIREKC 367
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGS--QGEIRKNC 295
PLN03030 PLN03030
cationic peroxidase; Provisional
70-371 1.22e-66

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 213.67  E-value: 1.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  70 GAGLTVGYY-KNCPGAEGIVREAVEKAMdNGNRGIGAGLVRIFFHDCFVRGCDASVLLRNTSgssnqTEMFGLPNInSLR 148
Cdd:PLN03030  22 GQGTRVGFYsTTCPQAESIVRKTVQSHF-QSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN-----TEKTALPNL-LLR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 149 GFQVIDDAKAELEKACPRTVSCADIVAFAARDA---TRNLSYgaidfQMPAGRLDGRVSLKEEAeKNLPGPFDSLDDLQK 225
Cdd:PLN03030  95 GYDVIDDAKTQLEAACPGVVSCADILALAARDSvvlTNGLTW-----PVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 226 SFAAQGLGFNDMVTLSGAHSIGVARCRFFTNRL-----PPNPSD--MDRDLARSLKATCDQNGLDSK-VVQDPVTPVALD 297
Cdd:PLN03030 169 KFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLynfttTGNGADpsIDASFVPQLQALCPQNGDGSRrIALDTGSSNRFD 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670379539 298 NQYYKNVHNGKVLFTSDAALNSTDDARKVVDGFAN----NAVDWYRAFADAMVKMGNIRDRTinRPKPEIREKCFIYN 371
Cdd:PLN03030 249 ASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKT--GTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
88-333 2.03e-63

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 200.48  E-value: 2.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539   88 VREAVEKAMDNgNRGIGAGLVRIFFHDCFVRGCDASVLLRNtsgssNQTEMFGLPNiNSLR-GFQVIDDAKAELEKACPR 166
Cdd:pfam00141   1 VRSVVRAAFKA-DPTMGPSLLRLHFHDCFVGGCDGSVLLDG-----FKPEKDAPPN-LGLRkGFEVIDDIKAKLEAACPG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  167 TVSCADIVAFAARDATRNLsyGAIDFQMPAGRLDGRVSLKEEAEKNLPGPFDSLDDLQKSFAAQGLGFNDMVTLSGAHSI 246
Cdd:pfam00141  74 VVSCADILALAARDAVELA--GGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  247 GVARcrfftnrlppnpsdmdrdlarslkatcdqngldskvvqdpvtpvaldnqyyKNVHNGKVLFTSDAALNSTDDARKV 326
Cdd:pfam00141 152 GRAH---------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRAL 180

                  ....*..
gi 670379539  327 VDGFANN 333
Cdd:pfam00141 181 VERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
88-350 2.32e-23

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: 97.61  E-value: 2.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  88 VREAVEKAMDNGNRgIGAGLVRIFFHDCFVR--------GCDASVLLrntsgssnQTEMFGLPNINSLRGFQVIDDAKAE 159
Cdd:cd00314    3 IKAILEDLITQAGA-LAGSLLRLAFHDAGTYdiadgkggGADGSIRF--------EPELDRPENGGLDKALRALEPIKSA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 160 LEKACPrtVSCADIVAFAARDATRNLSYGAIDFQMPAGRLDGRVSLKEEA--EKNLPGPFDSLDDLQKSFAAQGLGFNDM 237
Cdd:cd00314   74 YDGGNP--VSRADLIALAGAVAVESTFGGGPLIPFRFGRLDATEPDLGVPdpEGLLPNETSSATELRDKFKRMGLSPSEL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 238 VTLS-GAHSI-GVARCRFFTNRLPPnpsdmdrdlarslkatcdqngldskvvQDPVTPVALDNQYYKNV----------- 304
Cdd:cd00314  152 VALSaGAHTLgGKNHGDLLNYEGSG---------------------------LWTSTPFTFDNAYFKNLldmnwewrvgs 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 670379539 305 -----HNGKVLFTSDAALNSTDDARKVVDGFANNAVDWYRAFADAMVKMGN 350
Cdd:cd00314  205 pdpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
88-348 7.26e-08

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: 52.98  E-value: 7.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539  88 VREAVEKAMDNGNRG-IgagLVRIFFHDCfvrGC-DASVllrNTsGSSNQTEMFGlPNINslrgfqviDDAKAELEKAC- 164
Cdd:cd00691   16 ARNDIAKLIDDKNCApI---LVRLAWHDS---GTyDKET---KT-GGSNGTIRFD-PELN--------HGANAGLDIARk 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 165 ---------PRtVSCADIVAFAARDATRNLSYGAIDFQMpaGRLDGRVSLKEEAEKNLPGPFDSLDDLQKSFAAqgLGFN 235
Cdd:cd00691   77 llepikkkyPD-ISYADLWQLAGVVAIEEMGGPKIPFRP--GRVDASDPEECPPEGRLPDASKGADHLRDVFYR--MGFN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 236 D--MVTLSGAHSIGvaRCRfftnrlppnpsdmdRDlaRSlkatcdqnGLDSKVVQDPVTpvaLDNQYYKNVHNGK----- 308
Cdd:cd00691  152 DqeIVALSGAHTLG--RCH--------------KE--RS--------GYDGPWTKNPLK---FDNSYFKELLEEDwklpt 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 670379539 309 ---VLFTSDAALNSTDDARKVVDGFANNAVDWYRAFADAMVKM 348
Cdd:cd00691  203 pglLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
168-349 1.53e-06

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: 49.32  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 168 VSCADIVAFAARDATRNLSYGA-IDFqmpagrLDGRVSLKEEAEKNL-PGPFDSLDDLQKSFAAQGLGFNDMVTLSGAHS 245
Cdd:cd00692  102 VSMADFIQFAGAVAVSNCPGAPrLEF------YAGRKDATQPAPDGLvPEPFDSVDKILARFADAGFSPDELVALLAAHS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 246 IGVarcrfftnrlppnpsdmdrdlarslkatcdQNGLDSKVVQDPV--TPVALDNQYY-----KNV-------HNGKVL- 310
Cdd:cd00692  176 VAA------------------------------QDFVDPSIAGTPFdsTPGVFDTQFFietllKGTafpgsggNQGEVEs 225
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 670379539 311 -------FTSDAALnsTDDARKVVD--GFANNAVDWYRAFADAMVKMG 349
Cdd:cd00692  226 plpgefrLQSDFLL--ARDPRTACEwqSFVNNQAKMNAAFAAAMLKLS 271
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
101-314 4.67e-06

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: 47.46  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 101 RGIGAGLVRIFFHDCF-------VRGCDASVLLRNTSGssnqtEMFGLPNINSLRGFQVIDDakaelekacPRTvSCADI 173
Cdd:cd08201   39 RQAAAEWLRTAFHDMAthnvddgTGGLDASIQYELDRP-----ENIGSGFNTTLNFFVNFYS---------PRS-SMADL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 174 VAFAARDATRNLSYGAIDFQmpAGRLDGrvslKEEAEKNLPGPFDSLDDLQKSFAAQGLGFNDMVTLSG-AHSIGVARCR 252
Cdd:cd08201  104 IAMGVVTSVASCGGPVVPFR--AGRIDA----TEAGQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSE 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670379539 253 FFTNRLPPNPS-DMDRDLARSlkatcdQNGLDSKVVQD---PVTPVALDNQYYKNVHNGKVLFTSD 314
Cdd:cd08201  178 DFPEIVPPGSVpDTVLQFFDT------TIQFDNKVVTEylsGTTNNPLVVGPNNTTNSDLRIFSSD 237
PLN02879 PLN02879
L-ascorbate peroxidase
188-351 5.59e-05

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 44.28  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 188 GAIDFQMPAGRLDgrvSLKEEAEKNLPGPFDSLDDLQKSFAAQGLGFNDMVTLSGAHSIGvaRCRfftnrlppnpsdmdr 267
Cdd:PLN02879 110 GGPEIPFHPGRLD---KVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG--RCH--------------- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 268 dlarslkatCDQNGLDSKVVQDPVTpvaLDNQYYKNVHNGK----VLFTSDAALNSTDDARKVVDGFANNAVDWYRAFAD 343
Cdd:PLN02879 170 ---------KERSGFEGAWTPNPLI---FDNSYFKEILSGEkeglLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTE 237

                 ....*...
gi 670379539 344 AMVKMGNI 351
Cdd:PLN02879 238 AHLKLSEL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
167-351 9.98e-05

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 43.53  E-value: 9.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 167 TVSCADIVAFAARDATRnlSYGAIDFQMPAGRLDgrvSLKEEAEKNLPGPFDSLDDLQKSFAAQ-GLGFNDMVTLSGAHS 245
Cdd:PLN02364  90 TISFADFHQLAGVVAVE--VTGGPDIPFHPGRED---KPQPPPEGRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670379539 246 IGvaRCRfftnrlppnpsdmdrdlarslkatCDQNGLDSKVVQDPVTpvaLDNQYYKNVHNGK----VLFTSDAALNSTD 321
Cdd:PLN02364 165 LG--RCH------------------------KDRSGFEGAWTSNPLI---FDNSYFKELLSGEkeglLQLVSDKALLDDP 215
                        170       180       190
                 ....*....|....*....|....*....|
gi 670379539 322 DARKVVDGFANNAVDWYRAFADAMVKMGNI 351
Cdd:PLN02364 216 VFRPLVEKYAADEDAFFADYAEAHMKLSEL 245
 
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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