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Conserved domains on  [gi|670445259|ref|XP_008662930|]
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peroxidase 5 [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 ...
29-334 0e+00

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: 510.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  29 KLEVGFYEHSCAQAEDIVRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINSTPGNLAEKDSVANNpSMRGFDVI 108
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 109 DDAKAVLEAHCPRTVSCADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVldNNVPAPTDEVDELIESFKRKGLNA 188
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV--GNLPSPFFSVSQLISLFASKGLTV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 189 DDMVTLSGAHTIGRSHCSSFTQRLYNFSGQlGQTDPSLDPAYAGHLKARCPWPSSDDqmdpTVVPLDPVTPATFDNQYYK 268
Cdd:cd00693  158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGT-GDPDPTLDPAYAAQLRKKCPAGGDDD----TLVPLDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670445259 269 NVLAHKVLFISDNTLLDNPWTAGMVHFNAAVEKAWQVKFAKAMVKMGKVQVLTGDEGEIREKCFAV 334
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-334 0e+00

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: 510.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  29 KLEVGFYEHSCAQAEDIVRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINSTPGNLAEKDSVANNpSMRGFDVI 108
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 109 DDAKAVLEAHCPRTVSCADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVldNNVPAPTDEVDELIESFKRKGLNA 188
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV--GNLPSPFFSVSQLISLFASKGLTV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 189 DDMVTLSGAHTIGRSHCSSFTQRLYNFSGQlGQTDPSLDPAYAGHLKARCPWPSSDDqmdpTVVPLDPVTPATFDNQYYK 268
Cdd:cd00693  158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGT-GDPDPTLDPAYAAQLRKKCPAGGDDD----TLVPLDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670445259 269 NVLAHKVLFISDNTLLDNPWTAGMVHFNAAVEKAWQVKFAKAMVKMGKVQVLTGDEGEIREKCFAV 334
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
32-335 1.02e-93

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 281.85  E-value: 1.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  32 VGFYEHSCAQAEDIVRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINstpGNLAEKDSVANNpSMRGFDVIDDA 111
Cdd:PLN03030  27 VGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID---GSNTEKTALPNL-LLRGYDVIDDA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 112 KAVLEAHCPRTVSCADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVldNNVPAPTDEVDELIESFKRKGLNADDM 191
Cdd:PLN03030 103 KTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA--SNLPGFTDSIDVQKQKFAAKGLNTQDL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 192 VTLSGAHTIGRSHCSSFTQRLYNFSGQLGQTDPSLDPAYAGHLKARCPWPSSDDQMdptvVPLDPVTPATFDNQYYKNVL 271
Cdd:PLN03030 181 VTLVGGHTIGTTACQFFRYRLYNFTTTGNGADPSIDASFVPQLQALCPQNGDGSRR----IALDTGSSNRFDASFFSNLK 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670445259 272 AHKVLFISDNTLLDNPWTAGMVHFNAAVEK----AWQVKFAKAMVKMGKVQVLTGDEGEIREKCFAVN 335
Cdd:PLN03030 257 NGRGILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
46-204 2.62e-74

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 227.45  E-value: 2.62e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259   46 VRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINstpGNLAEKDSVANNpSMR-GFDVIDDAKAVLEAHCPRTVS 124
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNL-GLRkGFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  125 CADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVlDNNVPAPTDEVDELIESFKRKGLNADDMVTLSGAHTIGRSH 204
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEA-NSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH 155
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-334 0e+00

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: 510.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  29 KLEVGFYEHSCAQAEDIVRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINSTPGNLAEKDSVANNpSMRGFDVI 108
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 109 DDAKAVLEAHCPRTVSCADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVldNNVPAPTDEVDELIESFKRKGLNA 188
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV--GNLPSPFFSVSQLISLFASKGLTV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 189 DDMVTLSGAHTIGRSHCSSFTQRLYNFSGQlGQTDPSLDPAYAGHLKARCPWPSSDDqmdpTVVPLDPVTPATFDNQYYK 268
Cdd:cd00693  158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGT-GDPDPTLDPAYAAQLRKKCPAGGDDD----TLVPLDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670445259 269 NVLAHKVLFISDNTLLDNPWTAGMVHFNAAVEKAWQVKFAKAMVKMGKVQVLTGDEGEIREKCFAV 334
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
32-335 1.02e-93

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 281.85  E-value: 1.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  32 VGFYEHSCAQAEDIVRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINstpGNLAEKDSVANNpSMRGFDVIDDA 111
Cdd:PLN03030  27 VGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID---GSNTEKTALPNL-LLRGYDVIDDA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 112 KAVLEAHCPRTVSCADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVldNNVPAPTDEVDELIESFKRKGLNADDM 191
Cdd:PLN03030 103 KTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA--SNLPGFTDSIDVQKQKFAAKGLNTQDL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 192 VTLSGAHTIGRSHCSSFTQRLYNFSGQLGQTDPSLDPAYAGHLKARCPWPSSDDQMdptvVPLDPVTPATFDNQYYKNVL 271
Cdd:PLN03030 181 VTLVGGHTIGTTACQFFRYRLYNFTTTGNGADPSIDASFVPQLQALCPQNGDGSRR----IALDTGSSNRFDASFFSNLK 256
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670445259 272 AHKVLFISDNTLLDNPWTAGMVHFNAAVEK----AWQVKFAKAMVKMGKVQVLTGDEGEIREKCFAVN 335
Cdd:PLN03030 257 NGRGILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
46-204 2.62e-74

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 227.45  E-value: 2.62e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259   46 VRNAVRRGIAREPGVGAGLIRMHFHDCFVRGCDGSILINstpGNLAEKDSVANNpSMR-GFDVIDDAKAVLEAHCPRTVS 124
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNL-GLRkGFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  125 CADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVlDNNVPAPTDEVDELIESFKRKGLNADDMVTLSGAHTIGRSH 204
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEA-NSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH 155
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
44-316 3.46e-29

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: 112.63  E-value: 3.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  44 DIVRNAVRRGIAREPGVGAGLIRMHFHDCFVR--------GCDGSILinstpgNLAEKDSVANNPSMRGFDVIDDAKAVL 115
Cdd:cd00314    1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIR------FEPELDRPENGGLDKALRALEPIKSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 116 EAHCPrtVSCADIVAFAARDSTYLAGGLDYKVPsgRRDGRVSKEEEVLD-----NNVPAPTDEVDELIESFKRKGLNADD 190
Cdd:cd00314   75 DGGNP--VSRADLIALAGAVAVESTFGGGPLIP--FRFGRLDATEPDLGvpdpeGLLPNETSSATELRDKFKRMGLSPSE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 191 MVTLS-GAHTI-GRSHCSSFTQRLYnfsgqlgqtdpsldpayaghlkarcpwpssddqmdptvvPLDPVTPATFDNQYYK 268
Cdd:cd00314  151 LVALSaGAHTLgGKNHGDLLNYEGS---------------------------------------GLWTSTPFTFDNAYFK 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670445259 269 NVLAHKVLFISDNTLLDNPWTAGM----------------VHFNAAVEKAWQVKFAKAMVKMGK 316
Cdd:cd00314  192 NLLDMNWEWRVGSPDPDGVKGPGLlpsdyallsdsetralVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
46-314 5.68e-13

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: 67.61  E-value: 5.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  46 VRNAVRRGIArEPGVGAGLIRMHFH-----DCFVrGCDGSiliNSTPGNLAEKDSVANNpsmrGfdvIDDAKAVLE---A 117
Cdd:cd00691   16 ARNDIAKLID-DKNCAPILVRLAWHdsgtyDKET-KTGGS---NGTIRFDPELNHGANA----G---LDIARKLLEpikK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 118 HCPRtVSCADIVAFAARDSTYLAGGLDYKVPSGRRDgRVSKEEEVLDNNVPAPTDEVDELIESFKRKGLNADDMVTLSGA 197
Cdd:cd00691   84 KYPD-ISYADLWQLAGVVAIEEMGGPKIPFRPGRVD-ASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 198 HTIGRSHcssftqrlYNFSGqlgqtdpsldpaYAGhlkarcPWPSSddqmdptvvpldpvtPATFDNQYYKNVLAHK--- 274
Cdd:cd00691  162 HTLGRCH--------KERSG------------YDG------PWTKN---------------PLKFDNSYFKELLEEDwkl 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 670445259 275 -----VLFISDNTLLDNPWTAGMVHFNAAVEKAWQVKFAKAMVKM 314
Cdd:cd00691  201 ptpglLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
65-315 8.28e-11

Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173826 [Multi-domain]  Cd Length: 328  Bit Score: 62.03  E-value: 8.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  65 IRMHFHDC--FVR----------GCDGSILINSTpgnlAEKDSVANNpsmrGFDVIDDA-KAVLEAHcprTVSCADIVAF 131
Cdd:cd00692   42 LRLTFHDAigFSPalaagqfgggGADGSIVLFDD----IETAFHANI----GLDEIVEAlRPFHQKH---NVSMADFIQF 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 132 AARDSTY-LAGGLDYKVPSGRRDgrvsKEEEVLDNNVPAPTDEVDELIESFKRKGLNADDMVTLSGAHTIGRSHcssftq 210
Cdd:cd00692  111 AGAVAVSnCPGAPRLEFYAGRKD----ATQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQD------ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 211 rlynfsgqlgqtdpSLDPAYAGhlkarcpwpssddqmdptvVPLDPvTPATFDNQYYKNVLAHKVLFI------------ 278
Cdd:cd00692  181 --------------FVDPSIAG-------------------TPFDS-TPGVFDTQFFIETLLKGTAFPgsggnqgevesp 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 670445259 279 --------SDNTLLDNPWTA----GMVHFNAavekAWQVKFAKAMVKMG 315
Cdd:cd00692  227 lpgefrlqSDFLLARDPRTAcewqSFVNNQA----KMNAAFAAAMLKLS 271
PLN02364 PLN02364
L-ascorbate peroxidase 1
122-322 1.38e-10

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 60.86  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 122 TVSCADIVAFAARDSTYLAGGLDYKVPSGRRDgrvsKEEEVLDNNVPAPTDEVDELIESF-KRKGLNADDMVTLSGAHTI 200
Cdd:PLN02364  90 TISFADFHQLAGVVAVEVTGGPDIPFHPGRED----KPQPPPEGRLPDATKGCDHLRDVFaKQMGLSDKDIVALSGAHTL 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 201 GRSHcssftQRLYNFSGqlgqtdpsldpayaghlkarcPWPSSddqmdptvvpldpvtPATFDNQYYKNVLAHK----VL 276
Cdd:PLN02364 166 GRCH-----KDRSGFEG---------------------AWTSN---------------PLIFDNSYFKELLSGEkeglLQ 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 670445259 277 FISDNTLLDNPWTAGMVHFNAAVEKAWQVKFAKAMVKMGKVQVLTG 322
Cdd:PLN02364 205 LVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
PLN02879 PLN02879
L-ascorbate peroxidase
123-317 1.53e-10

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 60.84  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 123 VSCADIVAFAARDSTYLAGGLDYKVPSGRRDgrvsKEEEVLDNNVPAPTDEVDELIESFKRKGLNADDMVTLSGAHTIGR 202
Cdd:PLN02879  92 LSYADFYQLAGVVAVEITGGPEIPFHPGRLD----KVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 203 SHcssftQRLYNFSGQLGQtdpsldpayaghlkarcpwpssddqmdptvvpldpvTPATFDNQYYKNVLAHK----VLFI 278
Cdd:PLN02879 168 CH-----KERSGFEGAWTP------------------------------------NPLIFDNSYFKEILSGEkeglLQLP 206
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 670445259 279 SDNTLLDNPWTAGMVHFNAAVEKAWQVKFAKAMVKMGKV 317
Cdd:PLN02879 207 TDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSEL 245
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
60-227 1.12e-07

Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.


Pssm-ID: 173829  Cd Length: 264  Bit Score: 52.08  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259  60 VGAGLIRMHFHDCF-------VRGCDGSILINstpGNLAEKDSVANNPSMRGFDVIddakavleaHCPRTvSCADIVAFA 132
Cdd:cd08201   41 AAAEWLRTAFHDMAthnvddgTGGLDASIQYE---LDRPENIGSGFNTTLNFFVNF---------YSPRS-SMADLIAMG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 133 ARDSTYLAGGLDYKVPSGRRDGRVSKEEevldnNVPAPTDEVDELIESFKRKGLNADDMVTLSG-AHTIGRSHCSSFTQR 211
Cdd:cd08201  108 VVTSVASCGGPVVPFRAGRIDATEAGQA-----GVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDFPEI 182
                        170       180
                 ....*....|....*....|.
gi 670445259 212 LYNFSG-----QLGQTDPSLD 227
Cdd:cd08201  183 VPPGSVpdtvlQFFDTTIQFD 203
PLN02608 PLN02608
L-ascorbate peroxidase
108-204 6.36e-06

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 47.07  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670445259 108 IDDAKAVLEAHcPRtVSCADIVAFAARDSTYLAGGLDYKVPSGRRDGRVSKEEEVLdnnvPAPTDEVDELIESFKRKGLN 187
Cdd:PLN02608  76 IDLCEPVKAKH-PK-ITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRL----PDAKKGAKHLRDVFYRMGLS 149
                         90
                 ....*....|....*..
gi 670445259 188 ADDMVTLSGAHTIGRSH 204
Cdd:PLN02608 150 DKDIVALSGGHTLGRAH 166
 
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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