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Conserved domains on  [gi|1162490558|ref|XP_020396977|]
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peroxidase 2 [Zea mays]

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 ...
52-348 4.24e-148

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: 419.61  E-value: 4.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  52 LSVGYYKDKCAEAETIVQEAVRAA---DAGTKAGLLRLFFHDCFVQGCDASVLLkpDNDTNPQPEMLGVPNLSLRGFEVI 128
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAvkaDPRLAAALLRLHFHDCFVRGCDASVLL--DSTANNTSEKDAPPNLSLRGFDVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 129 DAAKAAVEARCPGVVSCADIVAFAGRDASAfLSGGaINFTMPAGRYDGTVSLANETlPNLPPPFADVRRLKAMFAAKGLD 208
Cdd:cd00693    80 DDIKAALEAACPGVVSCADILALAARDAVV-LAGG-PSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 209 TVDMVALSGAHSIGRSHCSSFSSDRLPPSNTSD----MDPAFAATLQASCasSANGAADNTVVQDYRTPDQLDNQYYRNV 284
Cdd:cd00693   157 VTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDpdptLDPAYAAQLRKKC--PAGGDDDTLVPLDPGTPNTFDNSYYKNL 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162490558 285 ISHKVLFASDAALLKSSDTLGLVYVAAFSQKLWQDKFGEAMVKMGGVQVKTAANGEIRRMCGYV 348
Cdd:cd00693   235 LAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
52-348 4.24e-148

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: 419.61  E-value: 4.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  52 LSVGYYKDKCAEAETIVQEAVRAA---DAGTKAGLLRLFFHDCFVQGCDASVLLkpDNDTNPQPEMLGVPNLSLRGFEVI 128
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAvkaDPRLAAALLRLHFHDCFVRGCDASVLL--DSTANNTSEKDAPPNLSLRGFDVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 129 DAAKAAVEARCPGVVSCADIVAFAGRDASAfLSGGaINFTMPAGRYDGTVSLANETlPNLPPPFADVRRLKAMFAAKGLD 208
Cdd:cd00693    80 DDIKAALEAACPGVVSCADILALAARDAVV-LAGG-PSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 209 TVDMVALSGAHSIGRSHCSSFSSDRLPPSNTSD----MDPAFAATLQASCasSANGAADNTVVQDYRTPDQLDNQYYRNV 284
Cdd:cd00693   157 VTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDpdptLDPAYAAQLRKKC--PAGGDDDTLVPLDPGTPNTFDNSYYKNL 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162490558 285 ISHKVLFASDAALLKSSDTLGLVYVAAFSQKLWQDKFGEAMVKMGGVQVKTAANGEIRRMCGYV 348
Cdd:cd00693   235 LAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
54-349 1.60e-70

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 222.91  E-value: 1.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  54 VGYYKDKCAEAETIVQEAVRA---ADAGTKAGLLRLFFHDCFVQGCDASVLLKPDNDtnpqpEMLGVPNLSLRGFEVIDA 130
Cdd:PLN03030   27 VGFYSTTCPQAESIVRKTVQShfqSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT-----EKTALPNLLLRGYDVIDD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 131 AKAAVEARCPGVVSCADIVAFAGRDASAFLSGGAinFTMPAGRYDGTVSLANETlPNLPPPFADVRRLKAMFAAKGLDTV 210
Cdd:PLN03030  102 AKTQLEAACPGVVSCADILALAARDSVVLTNGLT--WPVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQKFAAKGLNTQ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 211 DMVALSGAHSIGRSHCSSFSSdRL----PPSNTSD--MDPAFAATLQASCasSANGAADNTVVQDYRTPDQLDNQYYRNV 284
Cdd:PLN03030  179 DLVTLVGGHTIGTTACQFFRY-RLynftTTGNGADpsIDASFVPQLQALC--PQNGDGSRRIALDTGSSNRFDASFFSNL 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162490558 285 ISHKVLFASDAALLKSSDTLGLVY----VAAFSQKLWQDKFGEAMVKMGGVQVKTAANGEIRRMCGYVN 349
Cdd:PLN03030  256 KNGRGILESDQKLWTDASTRTFVQrflgVRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
68-313 1.44e-63

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 200.10  E-value: 1.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  68 VQEAVRAA---DAGTKAGLLRLFFHDCFVQGCDASVLLkpdndTNPQPEMLGVPNLSLR-GFEVIDAAKAAVEARCPGVV 143
Cdd:pfam00141   1 VRSVVRAAfkaDPTMGPSLLRLHFHDCFVGGCDGSVLL-----DGFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 144 SCADIVAFAGRDASAFLSGGAINFtmPAGRYDGTVSLANETLPNLPPPFADVRRLKAMFAAKGLDTVDMVALSGAHSIGR 223
Cdd:pfam00141  76 SCADILALAARDAVELAGGPSWPV--PLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 224 SHcssfssdrlppsntsdmdpafaatlqascassangaadntvvqdyrtpdqldnqyyRNVISHKVLFASDAALLKSSDT 303
Cdd:pfam00141 154 AH--------------------------------------------------------KNLLDGRGLLTSDQALLSDPRT 177
                         250
                  ....*....|
gi 1162490558 304 LGLVYVAAFS 313
Cdd:pfam00141 178 RALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
52-348 4.24e-148

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: 419.61  E-value: 4.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  52 LSVGYYKDKCAEAETIVQEAVRAA---DAGTKAGLLRLFFHDCFVQGCDASVLLkpDNDTNPQPEMLGVPNLSLRGFEVI 128
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAvkaDPRLAAALLRLHFHDCFVRGCDASVLL--DSTANNTSEKDAPPNLSLRGFDVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 129 DAAKAAVEARCPGVVSCADIVAFAGRDASAfLSGGaINFTMPAGRYDGTVSLANETlPNLPPPFADVRRLKAMFAAKGLD 208
Cdd:cd00693    80 DDIKAALEAACPGVVSCADILALAARDAVV-LAGG-PSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 209 TVDMVALSGAHSIGRSHCSSFSSDRLPPSNTSD----MDPAFAATLQASCasSANGAADNTVVQDYRTPDQLDNQYYRNV 284
Cdd:cd00693   157 VTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDpdptLDPAYAAQLRKKC--PAGGDDDTLVPLDPGTPNTFDNSYYKNL 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162490558 285 ISHKVLFASDAALLKSSDTLGLVYVAAFSQKLWQDKFGEAMVKMGGVQVKTAANGEIRRMCGYV 348
Cdd:cd00693   235 LAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
54-349 1.60e-70

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 222.91  E-value: 1.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  54 VGYYKDKCAEAETIVQEAVRA---ADAGTKAGLLRLFFHDCFVQGCDASVLLKPDNDtnpqpEMLGVPNLSLRGFEVIDA 130
Cdd:PLN03030   27 VGFYSTTCPQAESIVRKTVQShfqSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT-----EKTALPNLLLRGYDVIDD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 131 AKAAVEARCPGVVSCADIVAFAGRDASAFLSGGAinFTMPAGRYDGTVSLANETlPNLPPPFADVRRLKAMFAAKGLDTV 210
Cdd:PLN03030  102 AKTQLEAACPGVVSCADILALAARDSVVLTNGLT--WPVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQKFAAKGLNTQ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 211 DMVALSGAHSIGRSHCSSFSSdRL----PPSNTSD--MDPAFAATLQASCasSANGAADNTVVQDYRTPDQLDNQYYRNV 284
Cdd:PLN03030  179 DLVTLVGGHTIGTTACQFFRY-RLynftTTGNGADpsIDASFVPQLQALC--PQNGDGSRRIALDTGSSNRFDASFFSNL 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162490558 285 ISHKVLFASDAALLKSSDTLGLVY----VAAFSQKLWQDKFGEAMVKMGGVQVKTAANGEIRRMCGYVN 349
Cdd:PLN03030  256 KNGRGILESDQKLWTDASTRTFVQrflgVRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
68-313 1.44e-63

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 200.10  E-value: 1.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  68 VQEAVRAA---DAGTKAGLLRLFFHDCFVQGCDASVLLkpdndTNPQPEMLGVPNLSLR-GFEVIDAAKAAVEARCPGVV 143
Cdd:pfam00141   1 VRSVVRAAfkaDPTMGPSLLRLHFHDCFVGGCDGSVLL-----DGFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 144 SCADIVAFAGRDASAFLSGGAINFtmPAGRYDGTVSLANETLPNLPPPFADVRRLKAMFAAKGLDTVDMVALSGAHSIGR 223
Cdd:pfam00141  76 SCADILALAARDAVELAGGPSWPV--PLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 224 SHcssfssdrlppsntsdmdpafaatlqascassangaadntvvqdyrtpdqldnqyyRNVISHKVLFASDAALLKSSDT 303
Cdd:pfam00141 154 AH--------------------------------------------------------KNLLDGRGLLTSDQALLSDPRT 177
                         250
                  ....*....|
gi 1162490558 304 LGLVYVAAFS 313
Cdd:pfam00141 178 RALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
81-329 3.17e-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: 99.54  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  81 AGLLRLFFHDCFVQ--------GCDASVLLKPDNDtnpQPEMLGVpnlsLRGFEVIDAAKAAVEARCPgvVSCADIVAFA 152
Cdd:cd00314    19 GSLLRLAFHDAGTYdiadgkggGADGSIRFEPELD---RPENGGL----DKALRALEPIKSAYDGGNP--VSRADLIALA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 153 GRDASAFLSGGAINFTMPAGRYDGTVSLANETLP--NLPPPFADVRRLKAMFAAKGLDTVDMVALS-GAHSI-GRSHCSS 228
Cdd:cd00314    90 GAVAVESTFGGGPLIPFRFGRLDATEPDLGVPDPegLLPNETSSATELRDKFKRMGLSPSELVALSaGAHTLgGKNHGDL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 229 FSSDRLPPsntsdmdpafaatlqascassangaadntvvqDYRTPDQLDNQYYRNVIS-----------------HKVLF 291
Cdd:cd00314   170 LNYEGSGL--------------------------------WTSTPFTFDNAYFKNLLDmnwewrvgspdpdgvkgPGLLP 217
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1162490558 292 aSDAALLKSSDTLGLVYVAAFSQKLWQDKFGEAMVKMG 329
Cdd:cd00314   218 -SDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMV 254
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
84-331 2.44e-09

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: 57.79  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  84 LRLFFHDCFV------------QGCDASVLLKPDNDTNPQPEMlgvpnlslrGFEVIDAAKAAVEARcpGVVSCADIVAF 151
Cdd:cd00692    42 LRLTFHDAIGfspalaagqfggGGADGSIVLFDDIETAFHANI---------GLDEIVEALRPFHQK--HNVSMADFIQF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 152 AGRDASAFLSGGA-INFTmpAGRYDGTVSlANETLpnLPPPFADVRRLKAMFAAKGLDTVDMVALSGAHSIGRShcssfs 230
Cdd:cd00692   111 AGAVAVSNCPGAPrLEFY--AGRKDATQP-APDGL--VPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQ------ 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 231 sdrlppsntSDMDPAFAATLQAScassangaadntvvqdyrTPDQLDNQYYRNVISHKVLFA------------------ 292
Cdd:cd00692   180 ---------DFVDPSIAGTPFDS------------------TPGVFDTQFFIETLLKGTAFPgsggnqgevesplpgefr 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1162490558 293 --SDAALLKSSDTLGLVYVAAFSQKLWQDKFGEAMVKMGGV 331
Cdd:cd00692   233 lqSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLL 273
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
143-328 2.13e-07

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: 51.44  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 143 VSCADIVAFAGRDASAFLSGGAINFTMpaGRYD---GTVSLANETLPNLPPPFADVRRLkamFAAKGLDTVDMVALSGAH 219
Cdd:cd00691    88 ISYADLWQLAGVVAIEEMGGPKIPFRP--GRVDasdPEECPPEGRLPDASKGADHLRDV---FYRMGFNDQEIVALSGAH 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 220 SIGRSHcssfsSDRlppsntsdmdpafaatlqascaSSANGAadNTvvqdyRTPDQLDNQYYRNVISHK--------VLF 291
Cdd:cd00691   163 TLGRCH-----KER----------------------SGYDGP--WT-----KNPLKFDNSYFKELLEEDwklptpglLML 208
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1162490558 292 ASDAALLKSSDTLGLVYVAAFSQKLWQDKFGEAMVKM 328
Cdd:cd00691   209 PTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
84-294 9.40e-06

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: 46.69  E-value: 9.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558  84 LRLFFHDCF-------VQGCDASVLLKPDNDTNPQPEMlgvpNLSLRGFEVIDAAKAavearcpgvvSCADIVAFAGRDA 156
Cdd:cd08201    46 LRTAFHDMAthnvddgTGGLDASIQYELDRPENIGSGF----NTTLNFFVNFYSPRS----------SMADLIAMGVVTS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 157 SAFLSGGAINFTmpAGRYDGTVSLAnetlPNLPPPFADVRRLKAMFAAKGLDTVDMVALSG-AHSIGRSHCSSFsSDRLP 235
Cdd:cd08201   112 VASCGGPVVPFR--AGRIDATEAGQ----AGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDF-PEIVP 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162490558 236 PSNTSDMDPAFAATlqascassaNGAADNTVVQDY---RTPDQLDNQYYRNVISHKVLFASD 294
Cdd:cd08201   185 PGSVPDTVLQFFDT---------TIQFDNKVVTEYlsgTTNNPLVVGPNNTTNSDLRIFSSD 237
PLN02608 PLN02608
L-ascorbate peroxidase
134-225 7.03e-05

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 43.98  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 134 AVEARCPgVVSCADIVAFAGRDASAFLSGGAINFTmpAGRYDGTVSLANETLPNLPPPFAdvrRLKAMFAAKGLDTVDMV 213
Cdd:PLN02608   81 PVKAKHP-KITYADLYQLAGVVAVEVTGGPTIDFV--PGRKDSNACPEEGRLPDAKKGAK---HLRDVFYRMGLSDKDIV 154
                          90
                  ....*....|..
gi 1162490558 214 ALSGAHSIGRSH 225
Cdd:PLN02608  155 ALSGGHTLGRAH 166
PLN02879 PLN02879
L-ascorbate peroxidase
142-225 2.96e-04

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 41.97  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162490558 142 VVSCADIVAFAGRDASAFLSGGAINFTmpAGRYDGTvslanETLPN--LPPPFADVRRLKAMFAAKGLDTVDMVALSGAH 219
Cdd:PLN02879   91 ILSYADFYQLAGVVAVEITGGPEIPFH--PGRLDKV-----EPPPEgrLPQATKGVDHLRDVFGRMGLNDKDIVALSGGH 163

                  ....*.
gi 1162490558 220 SIGRSH 225
Cdd:PLN02879  164 TLGRCH 169
 
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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