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Conserved domains on  [gi|30690396|ref|NP_850652|]
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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 ...
30-333 4.73e-178

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: 495.50  E-value: 4.73e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  30 QLTPTFYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAAPNaNSARGFPVI 109
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 110 DRMKAAVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFfALANTNLPAPFFTLPQLKASFQNVGLDrP 189
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSS-ANDVGNLPSPFFSVSQLISLFASKGLT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 190 SDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKEL 269
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690396 270 KGLIQTDQELFSSPnatDTIPLVREYADGTQKFFNAFVEAMNRMGNITPLTGTQGQIRQNCRVV 333
Cdd:cd00693 238 RGLLTSDQALLSDP---RTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
30-333 4.73e-178

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: 495.50  E-value: 4.73e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  30 QLTPTFYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAAPNaNSARGFPVI 109
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 110 DRMKAAVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFfALANTNLPAPFFTLPQLKASFQNVGLDrP 189
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSS-ANDVGNLPSPFFSVSQLISLFASKGLT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 190 SDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKEL 269
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690396 270 KGLIQTDQELFSSPnatDTIPLVREYADGTQKFFNAFVEAMNRMGNITPLTGTQGQIRQNCRVV 333
Cdd:cd00693 238 RGLLTSDQALLSDP---RTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
35-334 1.34e-78

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 243.71  E-value: 1.34e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   35 FYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTsfrTEKDAAPNAnSARGFPVIDRMKA 114
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  115 AVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANtNLPAPFFTLPQLKASFQNVGLDrPSDLVA 194
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLN-TQDLVT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  195 LSGGHTFGKNQCQFIMDRLYNFSNTGL-PDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKELKGLI 273
Cdd:PLN03030 183 LVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGIL 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690396  274 QTDQELFSSpnaTDTIPLVREYAdGTQKF----FNA-FVEAMNRMGNITPLTGTQGQIRQNCRVVN 334
Cdd:PLN03030 263 ESDQKLWTD---ASTRTFVQRFL-GVRGLaglnFNVeFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
47-297 3.27e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 232.45  E-value: 3.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396    47 VRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNttsFRTEKDAAPNANSARGFPVIDRMKAAVETACPRTVSC 126
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   127 ADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANTNLPAPFFTLPQLKASFQNVGLDrPSDLVALSGGHTFGKNQc 206
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLT-AEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   207 qfimdrlynfsntglpdptlnttylqtlrgqcprngnqtvlvdfdlrtptvfdnkyyVNLKELKGLIQTDQELFSSPnat 286
Cdd:pfam00141 156 ---------------------------------------------------------KNLLDGRGLLTSDQALLSDP--- 175
                         250
                  ....*....|.
gi 30690396   287 DTIPLVREYAD 297
Cdd:pfam00141 176 RTRALVERYAA 186
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
30-333 4.73e-178

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: 495.50  E-value: 4.73e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  30 QLTPTFYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAAPNaNSARGFPVI 109
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 110 DRMKAAVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFfALANTNLPAPFFTLPQLKASFQNVGLDrP 189
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSS-ANDVGNLPSPFFSVSQLISLFASKGLT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 190 SDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKEL 269
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690396 270 KGLIQTDQELFSSPnatDTIPLVREYADGTQKFFNAFVEAMNRMGNITPLTGTQGQIRQNCRVV 333
Cdd:cd00693 238 RGLLTSDQALLSDP---RTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
35-334 1.34e-78

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 243.71  E-value: 1.34e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   35 FYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTsfrTEKDAAPNAnSARGFPVIDRMKA 114
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  115 AVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANtNLPAPFFTLPQLKASFQNVGLDrPSDLVA 194
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLN-TQDLVT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  195 LSGGHTFGKNQCQFIMDRLYNFSNTGL-PDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKELKGLI 273
Cdd:PLN03030 183 LVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGIL 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690396  274 QTDQELFSSpnaTDTIPLVREYAdGTQKF----FNA-FVEAMNRMGNITPLTGTQGQIRQNCRVVN 334
Cdd:PLN03030 263 ESDQKLWTD---ASTRTFVQRFL-GVRGLaglnFNVeFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
47-297 3.27e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 232.45  E-value: 3.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396    47 VRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNttsFRTEKDAAPNANSARGFPVIDRMKAAVETACPRTVSC 126
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   127 ADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANTNLPAPFFTLPQLKASFQNVGLDrPSDLVALSGGHTFGKNQc 206
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLT-AEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   207 qfimdrlynfsntglpdptlnttylqtlrgqcprngnqtvlvdfdlrtptvfdnkyyVNLKELKGLIQTDQELFSSPnat 286
Cdd:pfam00141 156 ---------------------------------------------------------KNLLDGRGLLTSDQALLSDP--- 175
                         250
                  ....*....|.
gi 30690396   287 DTIPLVREYAD 297
Cdd:pfam00141 176 RTRALVERYAA 186
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
47-315 2.00e-38

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: 137.67  E-value: 2.00e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  47 VRDTIVNELRSDPRIAASILRLHFHDCFV--------NGCDASILLDNttsfrtEKDAAPNANSARGFPVIDRMKAAVET 118
Cdd:cd00314   3 IKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRFEP------ELDRPENGGLDKALRALEPIKSAYDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 119 ACPrtVSCADILTIAAQQAVNLA--GGPSWRVPLGRRDSLQAFFALANT--NLPAPFFTLPQLKASFQNVGLDrPSDLVA 194
Cdd:cd00314  77 GNP--VSRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGVPDPegLLPNETSSATELRDKFKRMGLS-PSELVA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 195 LSGGhtfgknqcqfimdrlynfsntglpdptlnttyLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKELK---- 270
Cdd:cd00314 154 LSAG--------------------------------AHTLGGKNHGDLLNYEGSGLWTSTPFTFDNAYFKNLLDMNwewr 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30690396 271 ------------GLIQTDQELFSSPnatDTIPLVREYADGTQKFFNAFVEAMNRMGN 315
Cdd:cd00314 202 vgspdpdgvkgpGLLPSDYALLSDS---ETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
53-309 8.08e-17

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: 78.78  E-value: 8.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  53 NELRS---DPRIAASILRLHFH-----DCFVN--GCDASIlldnttSFRTEKDAAPNA--NSARGF--PVIDRMkaavet 118
Cdd:cd00691  18 NDIAKlidDKNCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAglDIARKLlePIKKKY------ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 119 acPRtVSCADILTIAAQQAVNLAGGPS--WRvpLGRRDSLQAFFALANTNLPAPFFTLPQLKASFQNVGL-DRpsDLVAL 195
Cdd:cd00691  86 --PD-ISYADLWQLAGVVAIEEMGGPKipFR--PGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFnDQ--EIVAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 196 SGGHTFGknqcqfimdRLY-NFSNTGLPdptlNTtylqtlrgqcprngnqtvlvdfdlRTPTVFDNKYYVNLKELK---- 270
Cdd:cd00691 159 SGAHTLG---------RCHkERSGYDGP----WT------------------------KNPLKFDNSYFKELLEEDwklp 201
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 30690396 271 --GLIQ--TDQELFSSPnatDTIPLVREYADGTQKFFNAFVEA 309
Cdd:cd00691 202 tpGLLMlpTDKALLEDP---KFRPYVELYAKDQDAFFKDYAEA 241
PLN02608 PLN02608
L-ascorbate peroxidase
62-313 5.74e-09

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 56.31  E-value: 5.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   62 AASILRLHFHDC-------FVNGCDASIlldnttsfRTEKDAAPNANSarGFPVIDRMKAAVETACPRtVSCADILTIAA 134
Cdd:PLN02608  31 APIMLRLAWHDAgtydaktKTGGPNGSI--------RNEEEYSHGANN--GLKIAIDLCEPVKAKHPK-ITYADLYQLAG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  135 QQAVNLAGGPSWRVPLGRRDSLQAffaLANTNLPAPFFTLPQLKASFQNVGL-DRpsDLVALSGGHTFGknqcqfimdrl 213
Cdd:PLN02608 100 VVAVEVTGGPTIDFVPGRKDSNAC---PEEGRLPDAKKGAKHLRDVFYRMGLsDK--DIVALSGGHTLG----------- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  214 ynfsntglpdptlnttylqtlRGQCPRNGnqtvlvdFD---LRTPTVFDNKYYVNL--KELKGLIQ--TDQELFSSPnat 286
Cdd:PLN02608 164 ---------------------RAHPERSG-------FDgpwTKEPLKFDNSYFVELlkGESEGLLKlpTDKALLEDP--- 212
                        250       260
                 ....*....|....*....|....*..
gi 30690396  287 DTIPLVREYADGTQKFFNAFVEAMNRM 313
Cdd:PLN02608 213 EFRPYVELYAKDEDAFFRDYAESHKKL 239
PLN02879 PLN02879
L-ascorbate peroxidase
89-316 3.02e-08

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 53.91  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   89 SFRTEKDAAPNANSarGFPVIDRMKAAVETACPrTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQaffalantnlP 168
Cdd:PLN02879  60 TIRHPQELAHDANN--GLDIAVRLLDPIKELFP-ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVE----------P 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  169 APFFTLPQ-------LKASFQNVGLDrPSDLVALSGGHTFGknqcqfimdrlynfsntglpdptlnttylqtlRGQCPRN 241
Cdd:PLN02879 127 PPEGRLPQatkgvdhLRDVFGRMGLN-DKDIVALSGGHTLG--------------------------------RCHKERS 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690396  242 GNQTVLVdfdlRTPTVFDNKYYVNL--KELKGLIQ--TDQELFSSPNATdtiPLVREYADGTQKFFNAFVEAMNRMGNI 316
Cdd:PLN02879 174 GFEGAWT----PNPLIFDNSYFKEIlsGEKEGLLQlpTDKALLDDPLFL---PFVEKYAADEDAFFEDYTEAHLKLSEL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
89-321 1.25e-07

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 52.01  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396   89 SFRTEKDAAPNANSarGFPVIDRMKAAVETACPrTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQaffalantnlP 168
Cdd:PLN02364  59 TMRFDAEQAHGANS--GIHIALRLLDPIREQFP-TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQ----------P 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  169 APFFTLP-------QLKASF-QNVGLDrPSDLVALSGGHTFGKnqCQfiMDRlynfsntglpdptlnttylQTLRGQCPR 240
Cdd:PLN02364 126 PPEGRLPdatkgcdHLRDVFaKQMGLS-DKDIVALSGAHTLGR--CH--KDR-------------------SGFEGAWTS 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  241 NgnqtvlvdfdlrtPTVFDNKYYVNL--KELKGLIQ--TDQELFSSPNATdtiPLVREYADGTQKFFNAFVEAMNRMGNI 316
Cdd:PLN02364 182 N-------------PLIFDNSYFKELlsGEKEGLLQlvSDKALLDDPVFR---PLVEKYAADEDAFFADYAEAHMKLSEL 245

                 ....*
gi 30690396  317 TPLTG 321
Cdd:PLN02364 246 GFADA 250
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
62-264 6.90e-05

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


Pssm-ID: 173826 [Multi-domain]  Cd Length: 328  Bit Score: 44.31  E-value: 6.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  62 AASILRLHFHDCFV------------NGCDASILLdnttsFRTEKDAaPNANSARGFpVIDRMKAAVETacpRTVSCADI 129
Cdd:cd00692  38 AHESLRLTFHDAIGfspalaagqfggGGADGSIVL-----FDDIETA-FHANIGLDE-IVEALRPFHQK---HNVSMADF 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396 130 LTIAAQQAV-NLAGGPSWRVPLGRRDSLQAffalANTNL-PAPFFTLPQLKASFQNVGLDrPSDLVALSGGHTFGKNqcq 207
Cdd:cd00692 108 IQFAGAVAVsNCPGAPRLEFYAGRKDATQP----APDGLvPEPFDSVDKILARFADAGFS-PDELVALLAAHSVAAQ--- 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30690396 208 fimdrlyNFSNTGLP-DPtlnttylqtlrgqcprngnqtvlvdFDlRTPTVFDNKYYV 264
Cdd:cd00692 180 -------DFVDPSIAgTP-------------------------FD-STPGVFDTQFFI 204
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
61-202 5.39e-03

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: 38.22  E-value: 5.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690396  61 IAASILRLHFHDCF-------VNGCDASIlldnttsfRTEKDAAPNANSArgfpvidrMKAAVET----ACPRTvSCADI 129
Cdd:cd08201  41 AAAEWLRTAFHDMAthnvddgTGGLDASI--------QYELDRPENIGSG--------FNTTLNFfvnfYSPRS-SMADL 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690396 130 LTIAAQQAVNLAGGPSWRVPLGRRDSLQAffalANTNLPAPFFTLPQLKASFQNVGLDRPsDLVALSG-GHTFG 202
Cdd:cd08201 104 IAMGVVTSVASCGGPVVPFRAGRIDATEA----GQAGVPEPQTDLGTTTESFRRQGFSTS-EMIALVAcGHTLG 172
 
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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