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Conserved domains on  [gi|242053005|ref|XP_002455648|]
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peroxidase 2 [Sorghum bicolor]

Protein Classification

peroxidase( domain architecture ID 10091046)

peroxidase catalyzes removal of H(2)O(2), and is involved in the oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress

EC:  1.11.1.7
Gene Ontology:  GO:0004601|GO:0006979|GO:0020037
PubMed:  11054546
SCOP:  4001128|3000844

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
24-322 2.37e-151

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: 426.54  E-value: 2.37e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  24 GLQVGYYKKTCPSAEVLVRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDPTqENPQPEKLGRPNNpSLRGYEV 103
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDST-ANNTSEKDAPPNL-SLRGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 104 IDAAKSAVEKACPGTVSCADIVAFAGRDASYLLSNskVSFHMPAGRLDGRKSLASETGvFLPGPSSNLSSLVSAFAGKGL 183
Cdd:cd00693   79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGG--PSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 184 SAEDMVVLSGAHSIGRSHCTSFVqTRL-------SAPSDIAASLATLLRKQCPANptTANDAVVSQDVVSPDVLDNQFYK 256
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFS-DRLynfsgtgDPDPTLDPAYAAQLRKKCPAG--GDDDTLVPLDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242053005 257 NVLAHNVLFTSDAVLLSAPNTARMVRANARFAGSWEKKFAKAMVKMAAIGVKTGRDGEIRKNCRLV 322
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
24-322 2.37e-151

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: 426.54  E-value: 2.37e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  24 GLQVGYYKKTCPSAEVLVRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDPTqENPQPEKLGRPNNpSLRGYEV 103
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDST-ANNTSEKDAPPNL-SLRGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 104 IDAAKSAVEKACPGTVSCADIVAFAGRDASYLLSNskVSFHMPAGRLDGRKSLASETGvFLPGPSSNLSSLVSAFAGKGL 183
Cdd:cd00693   79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGG--PSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 184 SAEDMVVLSGAHSIGRSHCTSFVqTRL-------SAPSDIAASLATLLRKQCPANptTANDAVVSQDVVSPDVLDNQFYK 256
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFS-DRLynfsgtgDPDPTLDPAYAAQLRKKCPAG--GDDDTLVPLDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242053005 257 NVLAHNVLFTSDAVLLSAPNTARMVRANARFAGSWEKKFAKAMVKMAAIGVKTGRDGEIRKNCRLV 322
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
7-323 9.71e-76

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 235.24  E-value: 9.71e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005   7 TFGVILSCALLLATAT---HGLQVGYYKKTCPSAEVLVRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDPTQE 83
Cdd:PLN03030   4 FIVILFFLLAMMATTLvqgQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  84 npqpEKLGRPNNpSLRGYEVIDAAKSAVEKACPGTVSCADIVAFAGRDaSYLLSNSkVSFHMPAGRLDGRKSLASETGVf 163
Cdd:PLN03030  84 ----EKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARD-SVVLTNG-LTWPVPTGRRDGRVSLASDASN- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 164 LPGPSSNLSSLVSAFAGKGLSAEDMVVLSGAHSIGRSHCT-------SFVQTRLSAPSDIAASLATLLRKQCPANPTTAN 236
Cdd:PLN03030 156 LPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQffryrlyNFTTTGNGADPSIDASFVPQLQALCPQNGDGSR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 237 DavVSQDVVSPDVLDNQFYKNVLAHNVLFTSDAVLLSAPNTARMVRanaRFAG-------SWEKKFAKAMVKMAAIGVKT 309
Cdd:PLN03030 236 R--IALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQ---RFLGvrglaglNFNVEFGRSMVKMSNIGVKT 310
                        330
                 ....*....|....
gi 242053005 310 GRDGEIRKNCRLVN 323
Cdd:PLN03030 311 GTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
41-290 8.62e-68

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 210.11  E-value: 8.62e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005   41 VRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDptqeNPQPEKLGRPNNpSLR-GYEVIDAAKSAVEKACPGTV 119
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD----GFKPEKDAPPNL-GLRkGFEVIDDIKAKLEAACPGVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  120 SCADIVAFAGRDASYLLSNskVSFHMPAGRLDGRKSLASETGVFLPGPSSNLSSLVSAFAGKGLSAEDMVVLSGAHSIGR 199
Cdd:pfam00141  76 SCADILALAARDAVELAGG--PSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  200 SHctsfvqtrlsapsdiaaslatllrkqcpanpttandavvsqdvvspdvldnqfyKNVLAHNVLFTSDAVLLSAPNTAR 279
Cdd:pfam00141 154 AH------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRA 179
                         250
                  ....*....|.
gi 242053005  280 MVRanaRFAGS 290
Cdd:pfam00141 180 LVE---RYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
24-322 2.37e-151

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: 426.54  E-value: 2.37e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  24 GLQVGYYKKTCPSAEVLVRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDPTqENPQPEKLGRPNNpSLRGYEV 103
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDST-ANNTSEKDAPPNL-SLRGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 104 IDAAKSAVEKACPGTVSCADIVAFAGRDASYLLSNskVSFHMPAGRLDGRKSLASETGvFLPGPSSNLSSLVSAFAGKGL 183
Cdd:cd00693   79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGG--PSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 184 SAEDMVVLSGAHSIGRSHCTSFVqTRL-------SAPSDIAASLATLLRKQCPANptTANDAVVSQDVVSPDVLDNQFYK 256
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFS-DRLynfsgtgDPDPTLDPAYAAQLRKKCPAG--GDDDTLVPLDPGTPNTFDNSYYK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242053005 257 NVLAHNVLFTSDAVLLSAPNTARMVRANARFAGSWEKKFAKAMVKMAAIGVKTGRDGEIRKNCRLV 322
Cdd:cd00693  233 NLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
7-323 9.71e-76

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 235.24  E-value: 9.71e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005   7 TFGVILSCALLLATAT---HGLQVGYYKKTCPSAEVLVRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDPTQE 83
Cdd:PLN03030   4 FIVILFFLLAMMATTLvqgQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  84 npqpEKLGRPNNpSLRGYEVIDAAKSAVEKACPGTVSCADIVAFAGRDaSYLLSNSkVSFHMPAGRLDGRKSLASETGVf 163
Cdd:PLN03030  84 ----EKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARD-SVVLTNG-LTWPVPTGRRDGRVSLASDASN- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 164 LPGPSSNLSSLVSAFAGKGLSAEDMVVLSGAHSIGRSHCT-------SFVQTRLSAPSDIAASLATLLRKQCPANPTTAN 236
Cdd:PLN03030 156 LPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQffryrlyNFTTTGNGADPSIDASFVPQLQALCPQNGDGSR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 237 DavVSQDVVSPDVLDNQFYKNVLAHNVLFTSDAVLLSAPNTARMVRanaRFAG-------SWEKKFAKAMVKMAAIGVKT 309
Cdd:PLN03030 236 R--IALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQ---RFLGvrglaglNFNVEFGRSMVKMSNIGVKT 310
                        330
                 ....*....|....
gi 242053005 310 GRDGEIRKNCRLVN 323
Cdd:PLN03030 311 GTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
41-290 8.62e-68

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 210.11  E-value: 8.62e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005   41 VRAAVKKALLANPGVGAGLIRMLFHDCFVEGCDASVLLDptqeNPQPEKLGRPNNpSLR-GYEVIDAAKSAVEKACPGTV 119
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD----GFKPEKDAPPNL-GLRkGFEVIDDIKAKLEAACPGVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  120 SCADIVAFAGRDASYLLSNskVSFHMPAGRLDGRKSLASETGVFLPGPSSNLSSLVSAFAGKGLSAEDMVVLSGAHSIGR 199
Cdd:pfam00141  76 SCADILALAARDAVELAGG--PSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  200 SHctsfvqtrlsapsdiaaslatllrkqcpanpttandavvsqdvvspdvldnqfyKNVLAHNVLFTSDAVLLSAPNTAR 279
Cdd:pfam00141 154 AH------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRA 179
                         250
                  ....*....|.
gi 242053005  280 MVRanaRFAGS 290
Cdd:pfam00141 180 LVE---RYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
41-302 5.27e-25

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: 101.08  E-value: 5.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  41 VRAAVKKALLANPGVGAGLIRMLFHDCFV--------EGCDASVLLDPTQENPqpeklgrPNNPSLRGYEVIDAAKSAVE 112
Cdd:cd00314    3 IKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRFEPELDRP-------ENGGLDKALRALEPIKSAYD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 113 KACPgtVSCADIVAFAGRDASYLLSNSKVSFHMPAGRLDgrkslASETGVFLPGP-------SSNLSSLVSAFAGKGLSA 185
Cdd:cd00314   76 GGNP--VSRADLIALAGAVAVESTFGGGPLIPFRFGRLD-----ATEPDLGVPDPegllpneTSSATELRDKFKRMGLSP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 186 EDMVVLS-GAHSI-GRSHCtsfvqtrlsapsdiaaslATLLRKQCPANPTTandavvsqdvvsPDVLDNQFYKNVLAHN- 262
Cdd:cd00314  149 SELVALSaGAHTLgGKNHG------------------DLLNYEGSGLWTST------------PFTFDNAYFKNLLDMNw 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 242053005 263 ---------------VLFTSDAVLLSAPNTARMVRanaRFAGSWEK---KFAKAMVKM 302
Cdd:cd00314  199 ewrvgspdpdgvkgpGLLPSDYALLSDSETRALVE---RYASDQEKffeDFAKAWIKM 253
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
60-307 5.19e-08

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: 53.55  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  60 IRMLFHDCFV------------EGCDASVLLDPTQENPQPeklgrpNNPSLRgyEVIDAAKSAVEKAcpgTVSCADIVAF 127
Cdd:cd00692   42 LRLTFHDAIGfspalaagqfggGGADGSIVLFDDIETAFH------ANIGLD--EIVEALRPFHQKH---NVSMADFIQF 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 128 AGRDAsylLSNSkvsfhmPAG-RLD---GRK--SLASETGVfLPGPSSNLSSLVSAFAGKGLSAEDMVVLSGAHSIGRSh 201
Cdd:cd00692  111 AGAVA---VSNC------PGApRLEfyaGRKdaTQPAPDGL-VPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQ- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 202 ctSFV-QTRLSAPSDiaaslatllrkqcpanpTTandavvsqdvvsPDVLDNQFYKNVLAHNVLFTSDA-----VLLSAP 275
Cdd:cd00692  180 --DFVdPSIAGTPFD-----------------ST------------PGVFDTQFFIETLLKGTAFPGSGgnqgeVESPLP 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 242053005 276 NTARM-----VRANARFAGSWEK----------KFAKAMVKMAAIGV 307
Cdd:cd00692  229 GEFRLqsdflLARDPRTACEWQSfvnnqakmnaAFAAAMLKLSLLGQ 275
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
41-308 2.36e-05

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: 44.89  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  41 VRAAVKKaLLANPGVGAGLIRMLFH-----DCFVE--GCDASVLLDPTQENPqpeklgrPNNpslrGyevIDAAKSAVE- 112
Cdd:cd00691   16 ARNDIAK-LIDDKNCAPILVRLAWHdsgtyDKETKtgGSNGTIRFDPELNHG-------ANA----G---LDIARKLLEp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 113 -KACPGTVSCADIVAFAGRDASYLLSNSKVSFHMpaGRLD----------GRkslasetgvfLPGPSSNLSSLVSAFAGK 181
Cdd:cd00691   81 iKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRP--GRVDasdpeecppeGR----------LPDASKGADHLRDVFYRM 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 182 GLSAEDMVVLSGAHSIGRSHctsfvQTRlsapSDIAAslatllrkqcpanPTTANdavvsqdvvsPDVLDNQFYKNVLAH 261
Cdd:cd00691  149 GFNDQEIVALSGAHTLGRCH-----KER----SGYDG-------------PWTKN----------PLKFDNSYFKELLEE 196
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 242053005 262 N--------VLFTSDAVLLSAPNTARMVRANARFAGSWEKKFAKAMVKMAAIGVK 308
Cdd:cd00691  197 DwklptpglLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGVP 251
PLN02879 PLN02879
L-ascorbate peroxidase
119-306 2.28e-04

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 41.97  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 119 VSCADIVAFAGRDASYLLSNSKVSFHmpAGRLDgrKSLASETGVfLPGPSSNLSSLVSAFAGKGLSAEDMVVLSGAHSIG 198
Cdd:PLN02879  92 LSYADFYQLAGVVAVEITGGPEIPFH--PGRLD--KVEPPPEGR-LPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 199 RSHctsfvqtrlsapsdiaaslatllrkqcpaNPTTANDAVVSQDvvsPDVLDNQFYKNVLAHN----VLFTSDAVLLSA 274
Cdd:PLN02879 167 RCH-----------------------------KERSGFEGAWTPN---PLIFDNSYFKEILSGEkeglLQLPTDKALLDD 214
                        170       180       190
                 ....*....|....*....|....*....|..
gi 242053005 275 PNTARMVRANARFAGSWEKKFAKAMVKMAAIG 306
Cdd:PLN02879 215 PLFLPFVEKYAADEDAFFEDYTEAHLKLSELG 246
PLN02364 PLN02364
L-ascorbate peroxidase 1
118-306 3.11e-04

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 41.60  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 118 TVSCADIVAFAGRDASYLLSNSKVSFHmpAGRLDgrKSLASETGVfLPGPSSNLSSLVSAFAGK-GLSAEDMVVLSGAHS 196
Cdd:PLN02364  90 TISFADFHQLAGVVAVEVTGGPDIPFH--PGRED--KPQPPPEGR-LPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 197 IGRSHctsfvqtrlsapsdiaaslatllrkqcpANPTTANDAVVSqdvvSPDVLDNQFYKNVLAHN----VLFTSDAVLL 272
Cdd:PLN02364 165 LGRCH----------------------------KDRSGFEGAWTS----NPLIFDNSYFKELLSGEkeglLQLVSDKALL 212
                        170       180       190
                 ....*....|....*....|....*....|....
gi 242053005 273 SAPNTARMVRANARFAGSWEKKFAKAMVKMAAIG 306
Cdd:PLN02364 213 DDPVFRPLVEKYAADEDAFFADYAEAHMKLSELG 246
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
55-207 3.50e-04

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: 41.68  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005  55 VGAGLIRMLFHDCF-------VEGCDASVLLdptqENPQPEKLGRPNNPSLRGYEVIDAAKSavekacpgtvSCADIVAF 127
Cdd:cd08201   41 AAAEWLRTAFHDMAthnvddgTGGLDASIQY----ELDRPENIGSGFNTTLNFFVNFYSPRS----------SMADLIAM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242053005 128 AGRDASYLLSNSKVSFHmpAGRLDGRKslASETGVflPGPSSNLSSLVSAFAGKGLSAEDMVVLSG-AHSIGRSHCTSFV 206
Cdd:cd08201  107 GVVTSVASCGGPVVPFR--AGRIDATE--AGQAGV--PEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDFP 180

                 .
gi 242053005 207 Q 207
Cdd:cd08201  181 E 181
 
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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