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Conserved domains on  [gi|15234394|ref|NP_195361|]
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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 ...
29-329 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: 515.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  29 KLFPGYYAHSCPQVNEIVRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSGRVATEKNSNPNsKSARGFDVV 108
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 109 DQIKAELEKQCPGTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRsASLSQSNNNIPAPNNTFQTILSKFNRQGLDIT 188
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGR-VSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 189 DLVALSGSHTIGFSRCTSFRQRLYNQSGNGSPDMTLEQSFAANLRQRCPKSGGDQILSVLDIISAASFDNSYFKNLIENK 268
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234394 269 GLLNSDQVLFSSNEkSRELVKKYAEDQGEFFEQFAESMIKMGNISPLTGSSGEIRKNCRKI 329
Cdd:cd00693 239 GLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-329 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: 515.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  29 KLFPGYYAHSCPQVNEIVRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSGRVATEKNSNPNsKSARGFDVV 108
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 109 DQIKAELEKQCPGTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRsASLSQSNNNIPAPNNTFQTILSKFNRQGLDIT 188
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGR-VSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 189 DLVALSGSHTIGFSRCTSFRQRLYNQSGNGSPDMTLEQSFAANLRQRCPKSGGDQILSVLDIISAASFDNSYFKNLIENK 268
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234394 269 GLLNSDQVLFSSNEkSRELVKKYAEDQGEFFEQFAESMIKMGNISPLTGSSGEIRKNCRKI 329
Cdd:cd00693 239 GLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
33-330 2.43e-89

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 270.29  E-value: 2.43e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   33 GYYAHSCPQVNEIVRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSgrvATEKNSNPNSkSARGFDVVDQIK 112
Cdd:PLN03030  28 GFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGS---NTEKTALPNL-LLRGYDVIDDAK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  113 AELEKQCPGTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRsASLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVA 192
Cdd:PLN03030 104 TQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGR-VSLASDASNLPGFTDSIDVQKQKFAAKGLNTQDLVT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  193 LSGSHTIGFSRCTSFRQRLYN--QSGNGSpDMTLEQSFAANLRQRCPKSGGDQILSVLDIISAASFDNSYFKNLIENKGL 270
Cdd:PLN03030 183 LVGGHTIGTTACQFFRYRLYNftTTGNGA-DPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGI 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234394  271 LNSDQVLFsSNEKSRELVKKYAEDQG----EFFEQFAESMIKMGNISPLTGSSGEIRKNCRKIN 330
Cdd:PLN03030 262 LESDQKLW-TDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
46-294 1.04e-81

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 245.94  E-value: 1.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394    46 VRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSgrvATEKNSNPNSKSARGFDVVDQIKAELEKQCPGTVSC 125
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGF---KPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   126 ADVLTLAARDSSVLTGGPSWVVPLGRRDSRSASLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVALSGSHTIGFSRct 205
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   206 sfrqrlynqsgngspdmtleqsfaanlrqrcpksggdqilsvldiisaasfdnsyfKNLIENKGLLNSDQVLFSSNEkSR 285
Cdd:pfam00141 156 --------------------------------------------------------KNLLDGRGLLTSDQALLSDPR-TR 178

                  ....*....
gi 15234394   286 ELVKKYAED 294
Cdd:pfam00141 179 ALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-329 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: 515.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  29 KLFPGYYAHSCPQVNEIVRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSGRVATEKNSNPNsKSARGFDVV 108
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 109 DQIKAELEKQCPGTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRsASLSQSNNNIPAPNNTFQTILSKFNRQGLDIT 188
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGR-VSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 189 DLVALSGSHTIGFSRCTSFRQRLYNQSGNGSPDMTLEQSFAANLRQRCPKSGGDQILSVLDIISAASFDNSYFKNLIENK 268
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234394 269 GLLNSDQVLFSSNEkSRELVKKYAEDQGEFFEQFAESMIKMGNISPLTGSSGEIRKNCRKI 329
Cdd:cd00693 239 GLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
33-330 2.43e-89

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 270.29  E-value: 2.43e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   33 GYYAHSCPQVNEIVRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSgrvATEKNSNPNSkSARGFDVVDQIK 112
Cdd:PLN03030  28 GFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGS---NTEKTALPNL-LLRGYDVIDDAK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  113 AELEKQCPGTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRsASLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVA 192
Cdd:PLN03030 104 TQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGR-VSLASDASNLPGFTDSIDVQKQKFAAKGLNTQDLVT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  193 LSGSHTIGFSRCTSFRQRLYN--QSGNGSpDMTLEQSFAANLRQRCPKSGGDQILSVLDIISAASFDNSYFKNLIENKGL 270
Cdd:PLN03030 183 LVGGHTIGTTACQFFRYRLYNftTTGNGA-DPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGI 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234394  271 LNSDQVLFsSNEKSRELVKKYAEDQG----EFFEQFAESMIKMGNISPLTGSSGEIRKNCRKIN 330
Cdd:PLN03030 262 LESDQKLW-TDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
46-294 1.04e-81

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 245.94  E-value: 1.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394    46 VRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSgrvATEKNSNPNSKSARGFDVVDQIKAELEKQCPGTVSC 125
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGF---KPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   126 ADVLTLAARDSSVLTGGPSWVVPLGRRDSRSASLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVALSGSHTIGFSRct 205
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   206 sfrqrlynqsgngspdmtleqsfaanlrqrcpksggdqilsvldiisaasfdnsyfKNLIENKGLLNSDQVLFSSNEkSR 285
Cdd:pfam00141 156 --------------------------------------------------------KNLLDGRGLLTSDQALLSDPR-TR 178

                  ....*....
gi 15234394   286 ELVKKYAED 294
Cdd:pfam00141 179 ALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
44-311 1.07e-33

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: 124.57  E-value: 1.07e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  44 EIVRSVVAKAVARETRMAASLLRLHFHDCFVQ--------GCDGSLlldssgRVATEKNSNPNSKSARGFDVVDQIKAEL 115
Cdd:cd00314   1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSI------RFEPELDRPENGGLDKALRALEPIKSAY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 116 EKQCPgtVSCADVLTLAA--RDSSVLTGGPSWVVPLGRRDSRSASLS--QSNNNIPAPNNTFQTILSKFNRQGLDITDLV 191
Cdd:cd00314  75 DGGNP--VSRADLIALAGavAVESTFGGGPLIPFRFGRLDATEPDLGvpDPEGLLPNETSSATELRDKFKRMGLSPSELV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 192 ALS-GSHTI-GFSRCTSFRQRLYNQSgNGSPDmtleqsfaanlrqrcpksggdqilsvldiisaaSFDNSYFKNLIENK- 268
Cdd:cd00314 153 ALSaGAHTLgGKNHGDLLNYEGSGLW-TSTPF---------------------------------TFDNAYFKNLLDMNw 198
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234394 269 ---------------GLLNSDQVLFSSNEkSRELVKKYAEDQGEFFEQFAESMIKMGN 311
Cdd:cd00314 199 ewrvgspdpdgvkgpGLLPSDYALLSDSE-TRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
46-309 7.65e-26

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: 103.44  E-value: 7.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  46 VRSVVAKAVArETRMAASLLRLHFH-----DCFVQ--GCDGSLlldssgRVATEKNSNPNSKSARGFDVVDQIKaeleKQ 118
Cdd:cd00691  16 ARNDIAKLID-DKNCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAGLDIARKLLEPIK----KK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 119 CPGtVSCADVLTLAARDSSVLTGGPswVVP--LGRRDSRSASLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVALSGS 196
Cdd:cd00691  85 YPD-ISYADLWQLAGVVAIEEMGGP--KIPfrPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 197 HTIGfsRCtsFRQRlynqSGNGSPdmtleqsfaanlrqrcpksGGDQILSvldiisaasFDNSYFKNLIENK------GL 270
Cdd:cd00691 162 HTLG--RC--HKER----SGYDGP-------------------WTKNPLK---------FDNSYFKELLEEDwklptpGL 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15234394 271 --LNSDQVLFSsNEKSRELVKKYAEDQGEFFEQFAESMIKM 309
Cdd:cd00691 206 lmLPTDKALLE-DPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
PLN02608 PLN02608
L-ascorbate peroxidase
52-326 2.56e-14

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 72.10  E-value: 2.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   52 KAVARETRMAASLLRLHFHDCFVQ-------GCDGSLlldssgRVATEKNSNPNSKSARGFDVVDQIKAELEKqcpgtVS 124
Cdd:PLN02608  22 RALIASKNCAPIMLRLAWHDAGTYdaktktgGPNGSI------RNEEEYSHGANNGLKIAIDLCEPVKAKHPK-----IT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  125 CADVLTLAARDSSVLTGGPSWVVPLGRRDSrsaSLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVALSGSHTIGfsrc 204
Cdd:PLN02608  91 YADLYQLAGVVAVEVTGGPTIDFVPGRKDS---NACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLG---- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  205 tsfrqrlynqsgngspdmtleqsfaanlRQRCPKSGGDQILSVldiiSAASFDNSYFKNLI--ENKGLLN--SDQVLFSS 280
Cdd:PLN02608 164 ----------------------------RAHPERSGFDGPWTK----EPLKFDNSYFVELLkgESEGLLKlpTDKALLED 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15234394  281 NEkSRELVKKYAEDQGEFFEQFAESMIKMGNISPLTGSSGEIRKNC 326
Cdd:PLN02608 212 PE-FRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKST 256
PLN02364 PLN02364
L-ascorbate peroxidase 1
40-317 7.48e-13

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 67.41  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   40 PQVNEIVRSVVAK------AVARETRMAASLLRLHFHDCFVQGCD-------GSLLLDSsgrvatEKNSNPNSKSARGFD 106
Cdd:PLN02364   6 PTVSEDYKKAVEKcrrklrGLIAEKNCAPIMVRLAWHSAGTFDCQsrtggpfGTMRFDA------EQAHGANSGIHIALR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  107 VVDQIKaeleKQCPgTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRSASlsqSNNNIPAPNNTFQTILSKFNRQ-GL 185
Cdd:PLN02364  80 LLDPIR----EQFP-TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPP---PEGRLPDATKGCDHLRDVFAKQmGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  186 DITDLVALSGSHTIGfsRCTSfrqrlyNQSGngspdmtLEQSFAANlrqrcpksggdqilsvldiisAASFDNSYFKNLI 265
Cdd:PLN02364 152 SDKDIVALSGAHTLG--RCHK------DRSG-------FEGAWTSN---------------------PLIFDNSYFKELL 195
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15234394  266 --ENKGLLN--SDQVLFsSNEKSRELVKKYAEDQGEFFEQFAESMIKMGNISPLTG 317
Cdd:PLN02364 196 sgEKEGLLQlvSDKALL-DDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
PLN02879 PLN02879
L-ascorbate peroxidase
38-312 1.98e-11

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 63.16  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394   38 SCPQVNEIVRSVVAK------AVARETRMAASLLRLHFHDCfvqgcdGSLLLDSS--GRVATEKNSNPNSKSAR-GFDVV 108
Cdd:PLN02879   5 SYPEVKEEYKKAVQRckrklrGLIAEKHCAPIVLRLAWHSA------GTFDVKTKtgGPFGTIRHPQELAHDANnGLDIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  109 DQIKAELEKQCPgTVSCADVLTLAARDSSVLTGGPSWVVPLGRRDSRSASlsqSNNNIPAPNNTFQTILSKFNRQGLDIT 188
Cdd:PLN02879  79 VRLLDPIKELFP-ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPP---PEGRLPQATKGVDHLRDVFGRMGLNDK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  189 DLVALSGSHTIGfsRCTSFRqrlynqSGngspdmtLEQSFAANlrqrcpksggdqilsvldiisAASFDNSYFKNLI--E 266
Cdd:PLN02879 155 DIVALSGGHTLG--RCHKER------SG-------FEGAWTPN---------------------PLIFDNSYFKEILsgE 198
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15234394  267 NKGLLN--SDQVLFSsNEKSRELVKKYAEDQGEFFEQFAESMIKMGNI 312
Cdd:PLN02879 199 KEGLLQlpTDKALLD-DPLFLPFVEKYAADEDAFFEDYTEAHLKLSEL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
65-223 2.10e-07

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: 51.63  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  65 LRLHFHDCFV------------QGCDGSLLLDSSgrvaTEKNSNPNSksarGFD-VVDQIKAELEKQcpgTVSCADVLTL 131
Cdd:cd00692  42 LRLTFHDAIGfspalaagqfggGGADGSIVLFDD----IETAFHANI----GLDeIVEALRPFHQKH---NVSMADFIQF 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 132 AArdsSVLT----GGPSWVVPLGRRDSRSASlsqSNNNIPAPNNTFQTILSKFNRQGLDITDLVALSGSHTIGfsrctsf 207
Cdd:cd00692 111 AG---AVAVsncpGAPRLEFYAGRKDATQPA---PDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVA------- 177
                       170
                ....*....|....*..
gi 15234394 208 RQRLYNQSGNGSP-DMT 223
Cdd:cd00692 178 AQDFVDPSIAGTPfDST 194
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
52-216 3.21e-05

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: 44.77  E-value: 3.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394  52 KAVARETRMAASLLRLHFHDCFVQGCD-GSLLLDSSgrVATEKNSNPNSKSArgfdvVDQIKAELEKQCPGTVSCADVLT 130
Cdd:cd08201  33 CAPGPGRQAAAEWLRTAFHDMATHNVDdGTGGLDAS--IQYELDRPENIGSG-----FNTTLNFFVNFYSPRSSMADLIA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234394 131 LAARDSSVLTGGPswVVPL--GRRDSRSASlsqsNNNIPAPNNTFQTILSKFNRQGLDITDLVALSG-SHTIGFSRCTSF 207
Cdd:cd08201 106 MGVVTSVASCGGP--VVPFraGRIDATEAG----QAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDF 179

                ....*....
gi 15234394 208 RQRLYNQSG 216
Cdd:cd08201 180 PEIVPPGSV 188
 
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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