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Conserved domains on  [gi|15242580|ref|NP_198831|]
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Peroxidase superfamily protein [Arabidopsis thaliana]

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

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 ...
31-327 5.28e-162

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: 453.51  E-value: 5.28e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  31 HLTVDFYSKSCPKFLDIIRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSSTAFNTAERDSSINLSLpgDGFDV 110
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 111 VIRAKTALELACPNTVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDLlPLPSMQISKLIDQFSSRGFSV 190
Cdd:cd00693  79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 191 QEMVALSGAHTIGFSHCKEFTNRVNPNNSTG-----YNPRFAVALKKACSNSkNDPTISVFNDVMTPNKFDNMYFQNIPK 265
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGdpdptLDPAYAAQLRKKCPAG-GDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242580 266 GLGLLESDHGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLSLHGVLTGRRGEIRRRCDAI 327
Cdd:cd00693 237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
31-327 5.28e-162

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: 453.51  E-value: 5.28e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  31 HLTVDFYSKSCPKFLDIIRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSSTAFNTAERDSSINLSLpgDGFDV 110
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 111 VIRAKTALELACPNTVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDLlPLPSMQISKLIDQFSSRGFSV 190
Cdd:cd00693  79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 191 QEMVALSGAHTIGFSHCKEFTNRVNPNNSTG-----YNPRFAVALKKACSNSkNDPTISVFNDVMTPNKFDNMYFQNIPK 265
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGdpdptLDPAYAAQLRKKCPAG-GDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242580 266 GLGLLESDHGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLSLHGVLTGRRGEIRRRCDAI 327
Cdd:cd00693 237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
48-292 3.21e-70

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 216.66  E-value: 3.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580    48 IRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSStafNTAERDSSINLSLpGDGFDVVIRAKTALELACPNTVS 127
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGL-RKGFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580   128 CSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDLLPLPSMQISKLIDQFSSRGFSVQEMVALSGAHTIGFSHc 207
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580   208 keftnrvnpnnstgynprfavalkkacsnskndptisvfndvmtpnkfdnmyfQNIPKGLGLLESDHGLFSDPRTRPFVE 287
Cdd:pfam00141 156 -----------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVE 182

                  ....*
gi 15242580   288 LYARD 292
Cdd:pfam00141 183 RYAAD 187
PLN03030 PLN03030
cationic peroxidase; Provisional
34-328 4.54e-66

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 210.58  E-value: 4.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580   34 VDFYSKSCPKFLDIIRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSSTafnTAERDSSINLSLpgDGFDVVIR 113
Cdd:PLN03030  27 VGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGS---NTEKTALPNLLL--RGYDVIDD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  114 AKTALELACPNTVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDlLPLPSMQISKLIDQFSSRGFSVQEM 193
Cdd:PLN03030 102 AKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSIDVQKQKFAAKGLNTQDL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  194 VALSGAHTIGFSHCKEFTNRVNPNNSTG------YNPRFAVALKKACSnSKNDPTISVFNDVMTPNKFDNMYFQNIPKGL 267
Cdd:PLN03030 181 VTLVGGHTIGTTACQFFRYRLYNFTTTGngadpsIDASFVPQLQALCP-QNGDGSRRIALDTGSSNRFDASFFSNLKNGR 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242580  268 GLLESDHGLFSDPRTRPFVELYARDQS----RFFNDFAGAMQKLSLHGVLTGRRGEIRRRCDAIN 328
Cdd:PLN03030 260 GILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
31-327 5.28e-162

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: 453.51  E-value: 5.28e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  31 HLTVDFYSKSCPKFLDIIRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSSTAFNTAERDSSINLSLpgDGFDV 110
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 111 VIRAKTALELACPNTVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDLlPLPSMQISKLIDQFSSRGFSV 190
Cdd:cd00693  79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 191 QEMVALSGAHTIGFSHCKEFTNRVNPNNSTG-----YNPRFAVALKKACSNSkNDPTISVFNDVMTPNKFDNMYFQNIPK 265
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGdpdptLDPAYAAQLRKKCPAG-GDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242580 266 GLGLLESDHGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLSLHGVLTGRRGEIRRRCDAI 327
Cdd:cd00693 237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
48-292 3.21e-70

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 216.66  E-value: 3.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580    48 IRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSStafNTAERDSSINLSLpGDGFDVVIRAKTALELACPNTVS 127
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGL-RKGFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580   128 CSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDLLPLPSMQISKLIDQFSSRGFSVQEMVALSGAHTIGFSHc 207
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580   208 keftnrvnpnnstgynprfavalkkacsnskndptisvfndvmtpnkfdnmyfQNIPKGLGLLESDHGLFSDPRTRPFVE 287
Cdd:pfam00141 156 -----------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVE 182

                  ....*
gi 15242580   288 LYARD 292
Cdd:pfam00141 183 RYAAD 187
PLN03030 PLN03030
cationic peroxidase; Provisional
34-328 4.54e-66

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 210.58  E-value: 4.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580   34 VDFYSKSCPKFLDIIRETITNKQISTPTTAAAALRLFFHDCFPNGCDASVLVSSTafnTAERDSSINLSLpgDGFDVVIR 113
Cdd:PLN03030  27 VGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGS---NTEKTALPNLLL--RGYDVIDD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  114 AKTALELACPNTVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVSDlLPLPSMQISKLIDQFSSRGFSVQEM 193
Cdd:PLN03030 102 AKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSIDVQKQKFAAKGLNTQDL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  194 VALSGAHTIGFSHCKEFTNRVNPNNSTG------YNPRFAVALKKACSnSKNDPTISVFNDVMTPNKFDNMYFQNIPKGL 267
Cdd:PLN03030 181 VTLVGGHTIGTTACQFFRYRLYNFTTTGngadpsIDASFVPQLQALCP-QNGDGSRRIALDTGSSNRFDASFFSNLKNGR 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242580  268 GLLESDHGLFSDPRTRPFVELYARDQS----RFFNDFAGAMQKLSLHGVLTGRRGEIRRRCDAIN 328
Cdd:PLN03030 260 GILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
126-312 3.70e-28

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: 109.60  E-value: 3.70e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 126 VSCSDII----AVAVRdllVTvGGPYYEISLGRRDSRTSKSSLVSDLLPLPSMQISKLIDQFSSRGFSVQEMVALSGAHT 201
Cdd:cd00691  88 ISYADLWqlagVVAIE---EM-GGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHT 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 202 IGfshckeftnRVNPNNStGYNPRFavalkkacsnSKNdptisvfndvmtPNKFDNMYFQNIP--------KGLGLLESD 273
Cdd:cd00691 164 LG---------RCHKERS-GYDGPW----------TKN------------PLKFDNSYFKELLeedwklptPGLLMLPTD 211
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15242580 274 HGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLSLHGV 312
Cdd:cd00691 212 KALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGV 250
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
46-308 3.24e-27

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: 107.24  E-value: 3.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  46 DIIRETITNKQISTPTTAAAALRLFFHDCFPngcdasvlVSSTAFNTAERDSSIN----LSLPGDGfdVVIRAKTALE-- 119
Cdd:cd00314   1 DAIKAILEDLITQAGALAGSLLRLAFHDAGT--------YDIADGKGGGADGSIRfepeLDRPENG--GLDKALRALEpi 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 120 ---LACPNTVSCSDIIA----VAVRdlLVTVGGPYYEISLGRRDSRTSKSSLVS--DLLPLPSMQISKLIDQFSSRGFSV 190
Cdd:cd00314  71 ksaYDGGNPVSRADLIAlagaVAVE--STFGGGPLIPFRFGRLDATEPDLGVPDpeGLLPNETSSATELRDKFKRMGLSP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 191 QEMVALS-GAHTI-GFSHCK---EFTNRVNPNNSTGYNPRFAVALKKacsnskndptisvfndvMTPNKFDNMYFQNIPK 265
Cdd:cd00314 149 SELVALSaGAHTLgGKNHGDllnYEGSGLWTSTPFTFDNAYFKNLLD-----------------MNWEWRVGSPDPDGVK 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15242580 266 GLGLLESDHGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLS 308
Cdd:cd00314 212 GPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMV 254
PLN02608 PLN02608
L-ascorbate peroxidase
134-308 7.57e-20

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 87.90  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  134 VAVRdllVTvGGPYYEISLGRRDSRTSKSSlvsDLLPLPSMQISKLIDQFSSRGFSVQEMVALSGAHTIGFSHckeftnr 213
Cdd:PLN02608 101 VAVE---VT-GGPTIDFVPGRKDSNACPEE---GRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAH------- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  214 vnpnnstgynprfavalkkacsnskndPTISVFNDVMTPN--KFDNMYFQNIPK----GLGLLESDHGLFSDPRTRPFVE 287
Cdd:PLN02608 167 ---------------------------PERSGFDGPWTKEplKFDNSYFVELLKgeseGLLKLPTDKALLEDPEFRPYVE 219
                        170       180
                 ....*....|....*....|.
gi 15242580  288 LYARDQSRFFNDFAGAMQKLS 308
Cdd:PLN02608 220 LYAKDEDAFFRDYAESHKKLS 240
PLN02879 PLN02879
L-ascorbate peroxidase
106-308 9.66e-15

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 72.79  E-value: 9.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  106 DGFDVVIRAKTALELACPnTVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSlvsDLLPLPSMQISKLIDQFSS 185
Cdd:PLN02879  73 NGLDIAVRLLDPIKELFP-ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPE---GRLPQATKGVDHLRDVFGR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  186 RGFSVQEMVALSGAHTIGFSHckeftnrvnpNNSTGYNPRFAvalkkacsnskNDPTIsvfndvmtpnkFDNMYFQNI-- 263
Cdd:PLN02879 149 MGLNDKDIVALSGGHTLGRCH----------KERSGFEGAWT-----------PNPLI-----------FDNSYFKEIls 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15242580  264 --PKGLGLLESDHGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLS 308
Cdd:PLN02879 197 geKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLS 243
PLN02364 PLN02364
L-ascorbate peroxidase 1
125-315 7.95e-13

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 67.41  E-value: 7.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  125 TVSCSDIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSlvsDLLPLPSMQISKLIDQFSSR-GFSVQEMVALSGAHTIG 203
Cdd:PLN02364  90 TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE---GRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  204 FSHckeftnrvnpNNSTGYNPRFAvalkkacsnskNDPTIsvfndvmtpnkFDNMYFQNI----PKGLGLLESDHGLFSD 279
Cdd:PLN02364 167 RCH----------KDRSGFEGAWT-----------SNPLI-----------FDNSYFKELlsgeKEGLLQLVSDKALLDD 214
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15242580  280 PRTRPFVELYARDQSRFFNDFAGAMQKLSLHGVLTG 315
Cdd:PLN02364 215 PVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
63-312 1.44e-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: 67.42  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  63 AAAALRLFFHDCFP------------NGCDASVLvsstAFNTAERDSSinlslPGDGFDVVIRAKTALELAcpNTVSCSD 130
Cdd:cd00692  38 AHESLRLTFHDAIGfspalaagqfggGGADGSIV----LFDDIETAFH-----ANIGLDEIVEALRPFHQK--HNVSMAD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 131 IIAVAVRDLLVTV-GGPYYEISLGRRDSRTSKsslVSDLLPLPSMQISKLIDQFSSRGFSVQEMVALSGAHTIGFShcke 209
Cdd:cd00692 107 FIQFAGAVAVSNCpGAPRLEFYAGRKDATQPA---PDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQ---- 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 210 ftNRVNPnnstgynprfAVAlkkacsnskNDPTISvfndvmTPNKFDNMYF--------------QNIPKGLGL------ 269
Cdd:cd00692 180 --DFVDP----------SIA---------GTPFDS------TPGVFDTQFFietllkgtafpgsgGNQGEVESPlpgefr 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15242580 270 LESDHGLFSDPRTRPFVELYARDQSRFFNDFAGAMQKLSLHGV 312
Cdd:cd00692 233 LQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
53-226 6.66e-11

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: 61.71  E-value: 6.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580  53 TNKQISTPTTAAAA-LRLFFHDCFPNGCDASV--LVSSTAFntaERDSSINLslpGDGFDVVIRAktaLELACPNTVSCS 129
Cdd:cd08201  31 TDCAPGPGRQAAAEwLRTAFHDMATHNVDDGTggLDASIQY---ELDRPENI---GSGFNTTLNF---FVNFYSPRSSMA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242580 130 DIIAVAVRDLLVTVGGPYYEISLGRRDSRTSKSSLVsdllPLPSMQISKLIDQFSSRGFSVQEMVALSG-AHTIGFSHCK 208
Cdd:cd08201 102 DLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQAGV----PEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSE 177
                       170
                ....*....|....*...
gi 15242580 209 EFTNRVNPNNSTGYNPRF 226
Cdd:cd08201 178 DFPEIVPPGSVPDTVLQF 195
 
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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