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Conserved domains on  [gi|15228090|ref|NP_181250|]
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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 ...
29-326 5.10e-142

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: 403.05  E-value: 5.10e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  29 ELEMNYYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLETARGVESEQKSKRSFGMRNFKYVK 108
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 109 IIKDALEKECPSTVSCADIVALSARDGIVMLKGPKIEmIKTGRRDSRGSYLGDVETLiPNHNDSLSSVISTFNSIGIDVE 188
Cdd:cd00693  81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYE-VPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 189 ATVALLGAHSVGRVHCVNLVHRLYPT-----IDPTLDPSYALYLKKRCPSPTPDPNAVlysRNDRETPMVVDNMYYKNIM 263
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFsgtgdPDPTLDPAYAAQLRKKCPAGGDDDTLV---PLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228090 264 AHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYV 326
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-326 5.10e-142

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: 403.05  E-value: 5.10e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  29 ELEMNYYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLETARGVESEQKSKRSFGMRNFKYVK 108
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 109 IIKDALEKECPSTVSCADIVALSARDGIVMLKGPKIEmIKTGRRDSRGSYLGDVETLiPNHNDSLSSVISTFNSIGIDVE 188
Cdd:cd00693  81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYE-VPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 189 ATVALLGAHSVGRVHCVNLVHRLYPT-----IDPTLDPSYALYLKKRCPSPTPDPNAVlysRNDRETPMVVDNMYYKNIM 263
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFsgtgdPDPTLDPAYAAQLRKKCPAGGDDDTLV---PLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228090 264 AHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYV 326
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
46-291 1.08e-59

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 189.70  E-value: 1.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090    46 IRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLEtarGVESEQKSKRSFGMRN-FKYVKIIKDALEKECPSTVSC 124
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRKgFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090   125 ADIVALSARDGIVMLKGPKIEMiKTGRRDSRGSYLGDVETLIPNHNDSLSSVISTFNSIGIDVEATVALLGAHSVGRVHc 204
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPV-PLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090   205 vnlvhrlyptidptldpsyalylkkrcpsptpdpnavlysrndretpmvvdnmyyKNIMAHKGLLVIDDELATDPRTAPF 284
Cdd:pfam00141 156 -------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRAL 180

                  ....*..
gi 15228090   285 VAKMAAD 291
Cdd:pfam00141 181 VERYAAD 187
PLN03030 PLN03030
cationic peroxidase; Provisional
34-327 1.05e-52

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 176.30  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090   34 YYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLEtarGVESEQKSKRSFGMRNFKYVKIIKDA 113
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID---GSNTEKTALPNLLLRGYDVIDDAKTQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  114 LEKECPSTVSCADIVALSARDGIVMLKGPKIEmIKTGRRDSRGSYLGDVETLiPNHNDSLSSVISTFNSIGIDVEATVAL 193
Cdd:PLN03030 106 LEAACPGVVSCADILALAARDSVVLTNGLTWP-VPTGRRDGRVSLASDASNL-PGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  194 LGAHSVGRVHCVNLVHRLYPTI------DPTLDPSYALYLKKRCPSPTPDPNAVLYSRNDRETpmvVDNMYYKNIMAHKG 267
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNFTttgngaDPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNR---FDASFFSNLKNGRG 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228090  268 LLVIDDELATDPRTAPFVAK------MAADNnyFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYVN 327
Cdd:PLN03030 261 ILESDQKLWTDASTRTFVQRflgvrgLAGLN--FNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-326 5.10e-142

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: 403.05  E-value: 5.10e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  29 ELEMNYYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLETARGVESEQKSKRSFGMRNFKYVK 108
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 109 IIKDALEKECPSTVSCADIVALSARDGIVMLKGPKIEmIKTGRRDSRGSYLGDVETLiPNHNDSLSSVISTFNSIGIDVE 188
Cdd:cd00693  81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYE-VPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 189 ATVALLGAHSVGRVHCVNLVHRLYPT-----IDPTLDPSYALYLKKRCPSPTPDPNAVlysRNDRETPMVVDNMYYKNIM 263
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFsgtgdPDPTLDPAYAAQLRKKCPAGGDDDTLV---PLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228090 264 AHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYV 326
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
peroxidase pfam00141
Peroxidase;
46-291 1.08e-59

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 189.70  E-value: 1.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090    46 IRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLEtarGVESEQKSKRSFGMRN-FKYVKIIKDALEKECPSTVSC 124
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRKgFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090   125 ADIVALSARDGIVMLKGPKIEMiKTGRRDSRGSYLGDVETLIPNHNDSLSSVISTFNSIGIDVEATVALLGAHSVGRVHc 204
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPV-PLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090   205 vnlvhrlyptidptldpsyalylkkrcpsptpdpnavlysrndretpmvvdnmyyKNIMAHKGLLVIDDELATDPRTAPF 284
Cdd:pfam00141 156 -------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRAL 180

                  ....*..
gi 15228090   285 VAKMAAD 291
Cdd:pfam00141 181 VERYAAD 187
PLN03030 PLN03030
cationic peroxidase; Provisional
34-327 1.05e-52

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 176.30  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090   34 YYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLEtarGVESEQKSKRSFGMRNFKYVKIIKDA 113
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID---GSNTEKTALPNLLLRGYDVIDDAKTQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  114 LEKECPSTVSCADIVALSARDGIVMLKGPKIEmIKTGRRDSRGSYLGDVETLiPNHNDSLSSVISTFNSIGIDVEATVAL 193
Cdd:PLN03030 106 LEAACPGVVSCADILALAARDSVVLTNGLTWP-VPTGRRDGRVSLASDASNL-PGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  194 LGAHSVGRVHCVNLVHRLYPTI------DPTLDPSYALYLKKRCPSPTPDPNAVLYSRNDRETpmvVDNMYYKNIMAHKG 267
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNFTttgngaDPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNR---FDASFFSNLKNGRG 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228090  268 LLVIDDELATDPRTAPFVAK------MAADNnyFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYVN 327
Cdd:PLN03030 261 ILESDQKLWTDASTRTFVQRflgvrgLAGLN--FNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
44-301 2.95e-15

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: 74.11  E-value: 2.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  44 EIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKS--------CDASLLLETargveseQKSKRSFGM--RNFKYVKIIKDA 113
Cdd:cd00314   1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYDiadgkgggADGSIRFEP-------ELDRPENGGldKALRALEPIKSA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 114 LEKECPstVSCADIVALSARDGIVMLKGPKIEM-IKTGRRDSRGSYLG--DVETLIPNHNDSLSSVISTFNSIGIDVEAT 190
Cdd:cd00314  74 YDGGNP--VSRADLIALAGAVAVESTFGGGPLIpFRFGRLDATEPDLGvpDPEGLLPNETSSATELRDKFKRMGLSPSEL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 191 VALL-GAHSV-GRVHCVNLVHRLYPTIDPtldpsyalylkkrcpsptpdpnavlysrndreTPMVVDNMYYKNI------ 262
Cdd:cd00314 152 VALSaGAHTLgGKNHGDLLNYEGSGLWTS--------------------------------TPFTFDNAYFKNLldmnwe 199
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15228090 263 ----------MAHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSR 301
Cdd:cd00314 200 wrvgspdpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAK 248
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
108-308 1.30e-11

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: 63.76  E-value: 1.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 108 KIIKDALE--KECPSTVSCADIVALSardGIVMLK---GPKIEMiKTGRRDSRGSYLGDVETLIPNHNDSLSSVISTFNS 182
Cdd:cd00691  72 DIARKLLEpiKKKYPDISYADLWQLA---GVVAIEemgGPKIPF-RPGRVDASDPEECPPEGRLPDASKGADHLRDVFYR 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 183 IGIDVEATVALLGAHSVGRVHcvnlvhrlyptidptldpsyalylKKRCPSPTPdpnavlYSRNdretPMVVDNMYYKNI 262
Cdd:cd00691 148 MGFNDQEIVALSGAHTLGRCH------------------------KERSGYDGP------WTKN----PLKFDNSYFKEL 193
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15228090 263 M------AHKGLLVI--DDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSE 308
Cdd:cd00691 194 LeedwklPTPGLLMLptDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSE 247
PLN02879 PLN02879
L-ascorbate peroxidase
116-308 3.81e-07

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 50.44  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  116 KECPSTVSCADIVALSARDGIVMLKGPKIEMiKTGRRDSRGSylgDVETLIPNHNDSLSSVISTFNSIGIDVEATVALLG 195
Cdd:PLN02879  86 KELFPILSYADFYQLAGVVAVEITGGPEIPF-HPGRLDKVEP---PPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSG 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  196 AHSVGRVHcvnlvhrlyptidptldpsyalylKKRCPsptpdpnavlYSRNDRETPMVVDNMYYKNIMA--HKGLLVI-- 271
Cdd:PLN02879 162 GHTLGRCH------------------------KERSG----------FEGAWTPNPLIFDNSYFKEILSgeKEGLLQLpt 207
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15228090  272 DDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSE 308
Cdd:PLN02879 208 DKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSE 244
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
122-206 3.83e-05

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: 44.69  E-value: 3.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090 122 VSCADIVALSARDGIVMLKG-PKIEMIkTGRRD-SRGSylgdVETLIPNHNDSLSSVISTFNSIGIDVEATVALLGAHSV 199
Cdd:cd00692 102 VSMADFIQFAGAVAVSNCPGaPRLEFY-AGRKDaTQPA----PDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSV 176

                ....*..
gi 15228090 200 GRVHCVN 206
Cdd:cd00692 177 AAQDFVD 183
PLN02364 PLN02364
L-ascorbate peroxidase 1
112-314 4.09e-05

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 44.30  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  112 DALEKECPsTVSCADIVALSARDGIVMLKGPKIEMiKTGRRDSRGSylgDVETLIPNHNDSLSSVISTF-NSIGIDVEAT 190
Cdd:PLN02364  82 DPIREQFP-TISFADFHQLAGVVAVEVTGGPDIPF-HPGREDKPQP---PPEGRLPDATKGCDHLRDVFaKQMGLSDKDI 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  191 VALLGAHSVGRVHcvnlvhrlyptidptldpsyalylKKRCPsptpdpnavlYSRNDRETPMVVDNMYYKNIMA--HKGL 268
Cdd:PLN02364 157 VALSGAHTLGRCH------------------------KDRSG----------FEGAWTSNPLIFDNSYFKELLSgeKEGL 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15228090  269 L--VIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTG 314
Cdd:PLN02364 203 LqlVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
PLN02608 PLN02608
L-ascorbate peroxidase
107-308 6.37e-03

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 37.82  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  107 VKIIKDALE--KECPSTVSCADIVALSARDGIVMLKGPKIEMIKtGRRDSRGSylgDVETLIPNHNDSLSSVISTFNSIG 184
Cdd:PLN02608  72 LKIAIDLCEpvKAKHPKITYADLYQLAGVVAVEVTGGPTIDFVP-GRKDSNAC---PEEGRLPDAKKGAKHLRDVFYRMG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228090  185 IDVEATVALLGAHSVGRVHcvnlvhrlyptidptldpsyalylKKRCPSPTPdpnavlYSRNdretPMVVDNMYYKNIMA 264
Cdd:PLN02608 148 LSDKDIVALSGGHTLGRAH------------------------PERSGFDGP------WTKE----PLKFDNSYFVELLK 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15228090  265 --HKGLLVI--DDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSE 308
Cdd:PLN02608 194 geSEGLLKLptDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSE 241
 
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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