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Conserved domains on  [gi|297803016|ref|XP_002869392|]
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peroxidase 45 [Arabidopsis lyrata subsp. lyrata]

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 ...
26-323 4.85e-165

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: 461.21  E-value: 4.85e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  26 QLRTGFYQNSCPNVEGIVRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMIAS----PSERDHPDDMSLagDGFDT 101
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDStannTSEKDAPPNLSL--RGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 102 VVKAKQAVDSNpnCRNKVSCADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNqLPQPGFNLNQLNGMFSRHGL 181
Cdd:cd00693   79 IDDIKAALEAA--CPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 182 SQTDMIALSGAHTIGFAHCGKFTKRIYNFSPSRRIDPTINSGYVIQLKQMCPIGVDVRIAINMDPTSPRTFDNAYFKNLQ 261
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297803016 262 QGKGLFSSDQILFTDQRSRSTVNTFANSEGAFRQAFITAITKLGRVGVLTGNAGEIRRDCSR 323
Cdd:cd00693  236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
26-323 4.85e-165

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: 461.21  E-value: 4.85e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  26 QLRTGFYQNSCPNVEGIVRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMIAS----PSERDHPDDMSLagDGFDT 101
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDStannTSEKDAPPNLSL--RGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 102 VVKAKQAVDSNpnCRNKVSCADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNqLPQPGFNLNQLNGMFSRHGL 181
Cdd:cd00693   79 IDDIKAALEAA--CPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 182 SQTDMIALSGAHTIGFAHCGKFTKRIYNFSPSRRIDPTINSGYVIQLKQMCPIGVDVRIAINMDPTSPRTFDNAYFKNLQ 261
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297803016 262 QGKGLFSSDQILFTDQRSRSTVNTFANSEGAFRQAFITAITKLGRVGVLTGNAGEIRRDCSR 323
Cdd:cd00693  236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
PLN03030 PLN03030
cationic peroxidase; Provisional
28-325 4.46e-76

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 236.39  E-value: 4.46e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  28 RTGFYQNSCPNVEGIVRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMI-ASPSERDHPDDMSLagDGFDTVVKAK 106
Cdd:PLN03030  26 RVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIdGSNTEKTALPNLLL--RGYDVIDDAK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 107 QAVDSnpNCRNKVSCADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNqLPQPGFNLNQLNGMFSRHGLSQTDM 186
Cdd:PLN03030 104 TQLEA--ACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSIDVQKQKFAAKGLNTQDL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 187 IALSGAHTIGFAHCGKFTKRIYNFSPSRR-IDPTINSGYVIQLKQMCPIGVDVRIAINMDPTSPRTFDNAYFKNLQQGKG 265
Cdd:PLN03030 181 VTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRG 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297803016 266 LFSSDQILFTDQRSRSTVNTFANSEG----AFRQAFITAITKLGRVGVLTGNAGEIRRDCSRAN 325
Cdd:PLN03030 261 ILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-289 1.30e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 222.44  E-value: 1.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016   43 VRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMIASP-SERDHPDDMSLAgDGFDTVVKAKQAVDSNpnCRNKVSC 121
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFkPEKDAPPNLGLR-KGFEVIDDIKAKLEAA--CPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  122 ADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNQLPQPGFNLNQLNGMFSRHGLSQTDMIALSGAHTIGFAHcg 201
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  202 kftkriynfspsrridptinsgyviqlkqmcpigvdvriainmdptsprtfdnayfKNLQQGKGLFSSDQILFTDQRSRS 281
Cdd:pfam00141 156 --------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRA 179

                  ....*...
gi 297803016  282 TVNTFANS 289
Cdd:pfam00141 180 LVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
26-323 4.85e-165

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: 461.21  E-value: 4.85e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  26 QLRTGFYQNSCPNVEGIVRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMIAS----PSERDHPDDMSLagDGFDT 101
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDStannTSEKDAPPNLSL--RGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 102 VVKAKQAVDSNpnCRNKVSCADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNqLPQPGFNLNQLNGMFSRHGL 181
Cdd:cd00693   79 IDDIKAALEAA--CPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 182 SQTDMIALSGAHTIGFAHCGKFTKRIYNFSPSRRIDPTINSGYVIQLKQMCPIGVDVRIAINMDPTSPRTFDNAYFKNLQ 261
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297803016 262 QGKGLFSSDQILFTDQRSRSTVNTFANSEGAFRQAFITAITKLGRVGVLTGNAGEIRRDCSR 323
Cdd:cd00693  236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
PLN03030 PLN03030
cationic peroxidase; Provisional
28-325 4.46e-76

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 236.39  E-value: 4.46e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  28 RTGFYQNSCPNVEGIVRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMI-ASPSERDHPDDMSLagDGFDTVVKAK 106
Cdd:PLN03030  26 RVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIdGSNTEKTALPNLLL--RGYDVIDDAK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 107 QAVDSnpNCRNKVSCADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNqLPQPGFNLNQLNGMFSRHGLSQTDM 186
Cdd:PLN03030 104 TQLEA--ACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSIDVQKQKFAAKGLNTQDL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 187 IALSGAHTIGFAHCGKFTKRIYNFSPSRR-IDPTINSGYVIQLKQMCPIGVDVRIAINMDPTSPRTFDNAYFKNLQQGKG 265
Cdd:PLN03030 181 VTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRG 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297803016 266 LFSSDQILFTDQRSRSTVNTFANSEG----AFRQAFITAITKLGRVGVLTGNAGEIRRDCSRAN 325
Cdd:PLN03030 261 ILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-289 1.30e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 222.44  E-value: 1.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016   43 VRNAVRQKFQQTFVTAPATLRLFFHDCFVRGCDASIMIASP-SERDHPDDMSLAgDGFDTVVKAKQAVDSNpnCRNKVSC 121
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFkPEKDAPPNLGLR-KGFEVIDDIKAKLEAA--CPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  122 ADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNQLPQPGFNLNQLNGMFSRHGLSQTDMIALSGAHTIGFAHcg 201
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  202 kftkriynfspsrridptinsgyviqlkqmcpigvdvriainmdptsprtfdnayfKNLQQGKGLFSSDQILFTDQRSRS 281
Cdd:pfam00141 156 --------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRA 179

                  ....*...
gi 297803016  282 TVNTFANS 289
Cdd:pfam00141 180 LVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
58-306 1.72e-24

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: 99.92  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  58 APATLRLFFHDCFVR--------GCDASimIASPSERDHPDDMslagdGFDTVVKAKQAVDSNPNCRNKVSCADILALAT 129
Cdd:cd00314   18 AGSLLRLAFHDAGTYdiadgkggGADGS--IRFEPELDRPENG-----GLDKALRALEPIKSAYDGGNPVSRADLIALAG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 130 REVVVLTGGPSypVELGRRDGRISTQSSvQNQLPQPGFNLNQLNGM-------FSRHGLSQTDMIALS-GAHTI-GFAHC 200
Cdd:cd00314   91 AVAVESTFGGG--PLIPFRFGRLDATEP-DLGVPDPEGLLPNETSSatelrdkFKRMGLSPSELVALSaGAHTLgGKNHG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 201 GKFTKRIYNFSPSRridptinsgyviqlkqmcpigvdvriainmdptsPRTFDNAYFKNL----------------QQGK 264
Cdd:cd00314  168 DLLNYEGSGLWTST----------------------------------PFTFDNAYFKNLldmnwewrvgspdpdgVKGP 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 297803016 265 GLFSSDQILFTDQRSRSTVNTFANSEGAFRQAFITAITKLGR 306
Cdd:cd00314  214 GLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
43-309 1.80e-21

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: 91.50  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  43 VRNAVRQKFQQTFVtAPATLRLFFH-----DCFVR--GCDASIMIASpsERDHPddmslAGDGFDTVVKAKQAV-DSNPN 114
Cdd:cd00691   16 ARNDIAKLIDDKNC-APILVRLAWHdsgtyDKETKtgGSNGTIRFDP--ELNHG-----ANAGLDIARKLLEPIkKKYPD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 115 crnkVSCADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVQNQLPQPGFNLNQLNGMFSRHGLSQTDMIALSGAHT 194
Cdd:cd00691   88 ----ISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 195 IGFAHcgkftkriynfsPSRridptinSGYviqlkqmcpigvdvriainmD-P--TSPRTFDNAYFKNLQQGK------G 265
Cdd:cd00691  164 LGRCH------------KER-------SGY--------------------DgPwtKNPLKFDNSYFKELLEEDwklptpG 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 297803016 266 L--FSSDQILFTDQRSRSTVNTFANSEGAFRQAFITAITKLGRVGV 309
Cdd:cd00691  205 LlmLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGV 250
PLN02879 PLN02879
L-ascorbate peroxidase
58-308 3.88e-16

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 76.64  E-value: 3.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  58 APATLRLFFHDCFVrgCDASIMIASP-SERDHPDDMSL-AGDGFDTVVKAKQAVDSnpnCRNKVSCADILALATREVVVL 135
Cdd:PLN02879  34 APIVLRLAWHSAGT--FDVKTKTGGPfGTIRHPQELAHdANNGLDIAVRLLDPIKE---LFPILSYADFYQLAGVVAVEI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 136 TGGPSYPVELGRRDgriSTQSSVQNQLPQPGFNLNQLNGMFSRHGLSQTDMIALSGAHTIGFAHCGKftkriynfspsrr 215
Cdd:PLN02879 109 TGGPEIPFHPGRLD---KVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKER------------- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 216 idptinSGYVIQLKQmcpigvdvriainmdptSPRTFDNAYFKNLQQG--KGLFS--SDQILFTDQRSRSTVNTFANSEG 291
Cdd:PLN02879 173 ------SGFEGAWTP-----------------NPLIFDNSYFKEILSGekEGLLQlpTDKALLDDPLFLPFVEKYAADED 229
                        250
                 ....*....|....*..
gi 297803016 292 AFRQAFITAITKLGRVG 308
Cdd:PLN02879 230 AFFEDYTEAHLKLSELG 246
PLN02608 PLN02608
L-ascorbate peroxidase
58-322 1.17e-15

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 75.96  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  58 APATLRLFFHDCFVR-------GCDASIMiaSPSERDHPDDMSL--AGDgFDTVVKAKqavdsNPncrnKVSCADILALA 128
Cdd:PLN02608  31 APIMLRLAWHDAGTYdaktktgGPNGSIR--NEEEYSHGANNGLkiAID-LCEPVKAK-----HP----KITYADLYQLA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 129 TREVVVLTGGPSYPVELGRRDGRISTQssvQNQLPQPGFNLNQLNGMFSRHGLSQTDMIALSGAHTIGFAHcgkftkriy 208
Cdd:PLN02608  99 GVVAVEVTGGPTIDFVPGRKDSNACPE---EGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAH--------- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 209 nfsPSRridptinSGYVIQLKQmcpigvdvriainmdptSPRTFDNAYFKNLQQG--KGL--FSSDQILFTDQRSRSTVN 284
Cdd:PLN02608 167 ---PER-------SGFDGPWTK-----------------EPLKFDNSYFVELLKGesEGLlkLPTDKALLEDPEFRPYVE 219
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 297803016 285 TFANSEGAFRQAFITAITKLGRVGVLTGNAGEIRRDCS 322
Cdd:PLN02608 220 LYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKSTS 257
PLN02364 PLN02364
L-ascorbate peroxidase 1
119-312 8.22e-14

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 70.11  E-value: 8.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 119 VSCADILALATREVVVLTGGPSYPVELGRRDgriSTQSSVQNQLPQPGFNLNQLNGMFSRH-GLSQTDMIALSGAHTIGF 197
Cdd:PLN02364  91 ISFADFHQLAGVVAVEVTGGPDIPFHPGRED---KPQPPPEGRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLGR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 198 AHcgkftKRIYNFSPSRRIDPTInsgyviqlkqmcpigvdvriainmdptsprtFDNAYFKNLQQG--KGLFS--SDQIL 273
Cdd:PLN02364 168 CH-----KDRSGFEGAWTSNPLI-------------------------------FDNSYFKELLSGekEGLLQlvSDKAL 211
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 297803016 274 FTDQRSRSTVNTFANSEGAFRQAFITAITKLGRVGVLTG 312
Cdd:PLN02364 212 LDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
58-309 1.15e-10

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: 61.64  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  58 APATLRLFFHDC--FVR----------GCDASIMIASPSERDHPddmslAGDGFDTVVKAKQAVDSNpncrNKVSCADIL 125
Cdd:cd00692   38 AHESLRLTFHDAigFSPalaagqfgggGADGSIVLFDDIETAFH-----ANIGLDEIVEALRPFHQK----HNVSMADFI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 126 ALATREVVV-LTGGPSYPVELGRRDgriSTQSSVQNQLPQPGFNLNQLNGMFSRHGLSQTDMIALSGAHTIgfahcgkft 204
Cdd:cd00692  109 QFAGAVAVSnCPGAPRLEFYAGRKD---ATQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSV--------- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 205 kriynfSPSRRIDPTInSGYviqlkqmcPigvdvriainMDPTsPRTFDNAYF-----KN-LQQGKGL------------ 266
Cdd:cd00692  177 ------AAQDFVDPSI-AGT--------P----------FDST-PGVFDTQFFietllKGtAFPGSGGnqgevesplpge 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 297803016 267 --FSSDQILFTDQRSRSTVNTFANSEGAFRQAFITAITKLGRVGV 309
Cdd:cd00692  231 frLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
49-203 2.26e-09

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: 57.09  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016  49 QKFQQTFVTAPAT-LRLFFHDCF-------VRGCDASIMIaspsERDHPDDMslaGDGFDTVVKakqavDSNPNCRNKVS 120
Cdd:cd08201   32 DCAPGPGRQAAAEwLRTAFHDMAthnvddgTGGLDASIQY----ELDRPENI---GSGFNTTLN-----FFVNFYSPRSS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297803016 121 CADILALATREVVVLTGGPSYPVELGRRDGRISTQSSVqnqlPQPGFNLNQLNGMFSRHGLSQTDMIALSG-AHTIGFAH 199
Cdd:cd08201  100 MADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQAGV----PEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVH 175

                 ....
gi 297803016 200 CGKF 203
Cdd:cd08201  176 SEDF 179
 
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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