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Conserved domains on  [gi|15235597|ref|NP_195468|]
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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 ...
26-328 3.61e-169

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: 472.00  E-value: 3.61e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  26 QLRRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNNNKAEKDHEENLSLagDGFDT 105
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 106 VIKAKEALDAVpnCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGgKLPHPTDDVNKLTSLFAKNGL 185
Cdd:cd00693  79 IDDIKAALEAA--CPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 186 SLNDMIALSGAHTLGFAHCTKVFNRIYTFNKTTKVDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQ 265
Cdd:cd00693 156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235597 266 QGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAF 328
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
26-328 3.61e-169

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: 472.00  E-value: 3.61e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  26 QLRRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNNNKAEKDHEENLSLagDGFDT 105
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 106 VIKAKEALDAVpnCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGgKLPHPTDDVNKLTSLFAKNGL 185
Cdd:cd00693  79 IDDIKAALEAA--CPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 186 SLNDMIALSGAHTLGFAHCTKVFNRIYTFNKTTKVDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQ 265
Cdd:cd00693 156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235597 266 QGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAF 328
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
28-329 1.71e-73

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 229.84  E-value: 1.71e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   28 RRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNnnkAEKDHEENLSLagDGFDTVI 107
Cdd:PLN03030  26 RVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPNLLL--RGYDVID 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  108 KAKEALDAvpNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVgGKLPHPTDDVNKLTSLFAKNGLSL 187
Cdd:PLN03030 101 DAKTQLEA--ACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQKFAAKGLNT 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  188 NDMIALSGAHTLGFAHCTKVFNRIYTFNKTTK-VDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQQ 266
Cdd:PLN03030 178 QDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKN 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235597  267 GKGLFTSDQVLFTDRRSKPTVDLWAN----NGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAFN 329
Cdd:PLN03030 258 GRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-293 1.84e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 222.05  E-value: 1.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597    43 VRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIastNNNKAEKDHEENLSLAgDGFDTVIKAKEALDAVpnCRNK 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLL---DGFKPEKDAPPNLGLR-KGFEVIDDIKAKLEAA--CPGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   123 VSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGFA 202
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   203 HctkvfnriytfnkttkvdptvnkdyvtelkascprnidprvainmdpttprqfdnvyyKNLQQGKGLFTSDQVLFTDRR 282
Cdd:pfam00141 155 H----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 15235597   283 SKPTVDLWANN 293
Cdd:pfam00141 177 TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
26-328 3.61e-169

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: 472.00  E-value: 3.61e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  26 QLRRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNNNKAEKDHEENLSLagDGFDT 105
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 106 VIKAKEALDAVpnCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGgKLPHPTDDVNKLTSLFAKNGL 185
Cdd:cd00693  79 IDDIKAALEAA--CPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 186 SLNDMIALSGAHTLGFAHCTKVFNRIYTFNKTTKVDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQ 265
Cdd:cd00693 156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235597 266 QGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAF 328
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
28-329 1.71e-73

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 229.84  E-value: 1.71e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   28 RRNFYAGSCPNVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNnnkAEKDHEENLSLagDGFDTVI 107
Cdd:PLN03030  26 RVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPNLLL--RGYDVID 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  108 KAKEALDAvpNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVgGKLPHPTDDVNKLTSLFAKNGLSL 187
Cdd:PLN03030 101 DAKTQLEA--ACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQKFAAKGLNT 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  188 NDMIALSGAHTLGFAHCTKVFNRIYTFNKTTK-VDPTVNKDYVTELKASCPRNIDPRVAINMDPTTPRQFDNVYYKNLQQ 266
Cdd:PLN03030 178 QDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKN 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235597  267 GKGLFTSDQVLFTDRRSKPTVDLWAN----NGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDCGAFN 329
Cdd:PLN03030 258 GRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-293 1.84e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 222.05  E-value: 1.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597    43 VRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIastNNNKAEKDHEENLSLAgDGFDTVIKAKEALDAVpnCRNK 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLL---DGFKPEKDAPPNLGLR-KGFEVIDDIKAKLEAA--CPGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   123 VSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGFA 202
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   203 HctkvfnriytfnkttkvdptvnkdyvtelkascprnidprvainmdpttprqfdnvyyKNLQQGKGLFTSDQVLFTDRR 282
Cdd:pfam00141 155 H----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 15235597   283 SKPTVDLWANN 293
Cdd:pfam00141 177 TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
41-310 3.98e-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: 96.07  E-value: 3.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  41 QIVRNAVQKKVQQTFTTIPATLRLYFHDCFV--------NGCDASVmiastnNNKAEKDHEENLslagdGFDTVIKAKEA 112
Cdd:cd00314   1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSI------RFEPELDRPENG-----GLDKALRALEP 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 113 LDAVPNCRNKVSCADILTMATRDVVNLA--GGPQYDVELGRLDGLSSTAASV--GGKLPHPTDDVNKLTSLFAKNGLSLN 188
Cdd:cd00314  70 IKSAYDGGNPVSRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGVPdpEGLLPNETSSATELRDKFKRMGLSPS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 189 DMIALS-GAHTL-GFAHCtkvfnriYTFNKTTKVDPTVnkdyvtelkascprnidprvainmdptTPRQFDNVYYKNL-- 264
Cdd:cd00314 150 ELVALSaGAHTLgGKNHG-------DLLNYEGSGLWTS---------------------------TPFTFDNAYFKNLld 195
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 265 --------------QQGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGR 310
Cdd:cd00314 196 mnwewrvgspdpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
43-314 9.44e-22

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: 92.27  E-value: 9.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  43 VRNAVQKKVQQTfTTIPATLRLYFH-----DCFVN--GCDASVmiastnNNKAEKDHEENLSLAgdgfdtviKAKEALDA 115
Cdd:cd00691  16 ARNDIAKLIDDK-NCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAGLD--------IARKLLEP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 116 VPNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSG 195
Cdd:cd00691  81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 196 AHTLGFAHCTKV-FNRIYTFNKTTkvdptvnkdyvtelkascprnidprvainmdpttprqFDNVYYKNLQQGK------ 268
Cdd:cd00691 161 AHTLGRCHKERSgYDGPWTKNPLK-------------------------------------FDNSYFKELLEEDwklptp 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15235597 269 GL--FTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGVK 314
Cdd:cd00691 204 GLlmLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGVP 251
PLN02608 PLN02608
L-ascorbate peroxidase
59-325 3.19e-14

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 71.72  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   59 PATLRLYFHDcfVNGCDASVMIASTNN---NKAEKDHEEN--LSLAGDgFDTVIKAKEAldavpncrnKVSCADILTMAT 133
Cdd:PLN02608  32 PIMLRLAWHD--AGTYDAKTKTGGPNGsirNEEEYSHGANngLKIAID-LCEPVKAKHP---------KITYADLYQLAG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  134 RDVVNLAGGPQYDVELGRLDglsSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGFAHCTKV-FNRIY 212
Cdd:PLN02608 100 VVAVEVTGGPTIDFVPGRKD---SNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAHPERSgFDGPW 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  213 TFNkttkvdptvnkdyvtelkascprnidprvainmdpttPRQFDNVYYKNLQQG--KGL--FTSDQVLFTDRRSKPTVD 288
Cdd:PLN02608 177 TKE-------------------------------------PLKFDNSYFVELLKGesEGLlkLPTDKALLEDPEFRPYVE 219
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15235597  289 LWANNGQLFNQAFINSMIKLGRVGVKTGSNGNIRRDC 325
Cdd:PLN02608 220 LYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKST 256
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
60-313 3.44e-14

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: 72.04  E-value: 3.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  60 ATLRLYFHDCFV------------NGCDASVMIASTnnnkaekdhEENLSLAGDGFDTVIkakEALDAVPNcRNKVSCAD 127
Cdd:cd00692  40 ESLRLTFHDAIGfspalaagqfggGGADGSIVLFDD---------IETAFHANIGLDEIV---EALRPFHQ-KHNVSMAD 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 128 ILTMATR-DVVNLAGGPQYDVELGRLDglsSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGfahctk 206
Cdd:cd00692 107 FIQFAGAvAVSNCPGAPRLEFYAGRKD---ATQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVA------ 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597 207 vfnriytfnKTTKVDPTVnkdyvtelkascPRniDPrvainMDpTTPRQFDNVYY-----KN-LQQGKGL---------- 270
Cdd:cd00692 178 ---------AQDFVDPSI------------AG--TP-----FD-STPGVFDTQFFietllKGtAFPGSGGnqgevesplp 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15235597 271 ----FTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGV 313
Cdd:cd00692 229 gefrLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
PLN02879 PLN02879
L-ascorbate peroxidase
35-312 4.09e-14

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 70.86  E-value: 4.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   35 SCPNVEQIVRNAVQKKVQQTFTTI------PATLRLYFHDcfVNGCDASVMIAS---TNNNKAEKDHEENlslagDGFDT 105
Cdd:PLN02879   5 SYPEVKEEYKKAVQRCKRKLRGLIaekhcaPIVLRLAWHS--AGTFDVKTKTGGpfgTIRHPQELAHDAN-----NGLDI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  106 VIKAkeaLDAVPNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAAsvgGKLPHPTDDVNKLTSLFAKNGL 185
Cdd:PLN02879  78 AVRL---LDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPE---GRLPQATKGVDHLRDVFGRMGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  186 SLNDMIALSGAHTLGFAHCTKV-FNRIYTFNkttkvdptvnkdyvtelkascprnidprvainmdpttPRQFDNVYYKNL 264
Cdd:PLN02879 152 NDKDIVALSGGHTLGRCHKERSgFEGAWTPN-------------------------------------PLIFDNSYFKEI 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15235597  265 QQG--KGLFT--SDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVG 312
Cdd:PLN02879 195 LSGekEGLLQlpTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELG 246
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
27-229 3.88e-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: 62.48  E-value: 3.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  27 LRRNFYAGSCPnveqivrnaVQKKVQQTFTTIPAT-LRLYFHDCF-------VNGCDASVMIastnnnkaEKDHEENLsl 98
Cdd:cd08201  19 SARGFVAGVTP---------CTDCAPGPGRQAAAEwLRTAFHDMAthnvddgTGGLDASIQY--------ELDRPENI-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  99 aGDGFDTVIKakealDAVPNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAASVggklPHPTDDVNKLTS 178
Cdd:cd08201  80 -GSGFNTTLN-----FFVNFYSPRSSMADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQAGV----PEPQTDLGTTTE 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235597 179 LFAKNGLSLNDMIALSG-AHTLGFAHC----------TKVFNRIYTFNKTTKVDPTVNKDYV 229
Cdd:cd08201 150 SFRRQGFSTSEMIALVAcGHTLGGVHSedfpeivppgSVPDTVLQFFDTTIQFDNKVVTEYL 211
PLN02364 PLN02364
L-ascorbate peroxidase 1
37-312 5.33e-11

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 62.02  E-value: 5.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597   37 PNVEQIVRNAVQKKVQQTFTTI------PATLRLYFHDCFVNGCDASVMIA-STNNNKAEKDHEENlslagDGFDTVIKA 109
Cdd:PLN02364   6 PTVSEDYKKAVEKCRRKLRGLIaekncaPIMVRLAWHSAGTFDCQSRTGGPfGTMRFDAEQAHGAN-----SGIHIALRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  110 keaLDAVPNCRNKVSCADILTMATRDVVNLAGGPQYDVELGRLDGLSSTAAsvgGKLPHPTDDVNKLTSLFAKN-GLSLN 188
Cdd:PLN02364  81 ---LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE---GRLPDATKGCDHLRDVFAKQmGLSDK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235597  189 DMIALSGAHTLGFAHCTKV-FNRIYTFNkttkvdptvnkdyvtelkascprnidprvainmdpttPRQFDNVYYKNLQQG 267
Cdd:PLN02364 155 DIVALSGAHTLGRCHKDRSgFEGAWTSN-------------------------------------PLIFDNSYFKELLSG 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15235597  268 --KGL--FTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVG 312
Cdd:PLN02364 198 ekEGLlqLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELG 246
 
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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