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Conserved domains on  [gi|670406530|ref|XP_008644819|]
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peroxidase N [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 ...
28-330 2.55e-158

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: 444.65  E-value: 2.55e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  28 QLTSDFYDSTCPQLYYVVQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASILLDG---DDGEKFALPNLnSVRGYEVI 104
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDStanNTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 105 DAIKADLESACPEVVSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADNgLPSPFEPVDSIIQKFAAVGLNTT 184
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 185 DVVVLSGAHTIGRARCALFSNRLSNFSATDSADPTLEASLADSLQSLCAGGNGDGNeTAALDVSSPYVFDNDYYKNLLTE 264
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDT-LVPLDPGTPNTFDNSYYKNLLAG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670406530 265 RGLLSSDLGLFSSPEgvaasTKDLVEAYSSDGDQFFYDFVWSMIRMGNIPLAAGSDGEVRKNCRVV 330
Cdd:cd00693  238 RGLLTSDQALLSDPR-----TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
28-330 2.55e-158

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: 444.65  E-value: 2.55e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  28 QLTSDFYDSTCPQLYYVVQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASILLDG---DDGEKFALPNLnSVRGYEVI 104
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDStanNTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 105 DAIKADLESACPEVVSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADNgLPSPFEPVDSIIQKFAAVGLNTT 184
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 185 DVVVLSGAHTIGRARCALFSNRLSNFSATDSADPTLEASLADSLQSLCAGGNGDGNeTAALDVSSPYVFDNDYYKNLLTE 264
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDT-LVPLDPGTPNTFDNSYYKNLLAG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670406530 265 RGLLSSDLGLFSSPEgvaasTKDLVEAYSSDGDQFFYDFVWSMIRMGNIPLAAGSDGEVRKNCRVV 330
Cdd:cd00693  238 RGLLTSDQALLSDPR-----TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
1-331 4.32e-91

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 274.91  E-value: 4.32e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530   1 MERYSCCRWVLACSILALcLGGQGARCqltsDFYDSTCPQLYYVVQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASI 80
Cdd:PLN03030   2 QRFIVILFFLLAMMATTL-VQGQGTRV----GFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  81 LLDGDDGEKFALPNLnSVRGYEVIDAIKADLESACPEVVSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADN 160
Cdd:PLN03030  77 LIDGSNTEKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 161 gLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAHTIGRARCALFSNRLSNFSAT-DSADPTLEASLADSLQSLCAgGNGDG 239
Cdd:PLN03030 156 -LPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTgNGADPSIDASFVPQLQALCP-QNGDG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 240 NETAALDVSSPYVFDNDYYKNLLTERGLLSSDLGLFSSpegvaASTKDLVEAY----SSDGDQFFYDFVWSMIRMGNIPL 315
Cdd:PLN03030 234 SRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTD-----ASTRTFVQRFlgvrGLAGLNFNVEFGRSMVKMSNIGV 308
                        330
                 ....*....|....*.
gi 670406530 316 AAGSDGEVRKNCRVVN 331
Cdd:PLN03030 309 KTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
45-295 5.60e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 231.30  E-value: 5.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530   45 VQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASILLDGDDGEKFALPNLNSVRGYEVIDAIKADLESACPEVVSCADV 124
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSCADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  125 VALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADNGLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAHTIGRARcalfs 204
Cdd:pfam00141  81 LALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  205 nrlsnfsatdsadptleasladslqslcaggngdgnetaaldvsspyvfdndyyKNLLTERGLLSSDLGLFSSPEgvaas 284
Cdd:pfam00141 156 ------------------------------------------------------KNLLDGRGLLTSDQALLSDPR----- 176
                         250
                  ....*....|.
gi 670406530  285 TKDLVEAYSSD 295
Cdd:pfam00141 177 TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
28-330 2.55e-158

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: 444.65  E-value: 2.55e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  28 QLTSDFYDSTCPQLYYVVQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASILLDG---DDGEKFALPNLnSVRGYEVI 104
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDStanNTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 105 DAIKADLESACPEVVSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADNgLPSPFEPVDSIIQKFAAVGLNTT 184
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGN-LPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 185 DVVVLSGAHTIGRARCALFSNRLSNFSATDSADPTLEASLADSLQSLCAGGNGDGNeTAALDVSSPYVFDNDYYKNLLTE 264
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDT-LVPLDPGTPNTFDNSYYKNLLAG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670406530 265 RGLLSSDLGLFSSPEgvaasTKDLVEAYSSDGDQFFYDFVWSMIRMGNIPLAAGSDGEVRKNCRVV 330
Cdd:cd00693  238 RGLLTSDQALLSDPR-----TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
1-331 4.32e-91

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 274.91  E-value: 4.32e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530   1 MERYSCCRWVLACSILALcLGGQGARCqltsDFYDSTCPQLYYVVQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASI 80
Cdd:PLN03030   2 QRFIVILFFLLAMMATTL-VQGQGTRV----GFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  81 LLDGDDGEKFALPNLnSVRGYEVIDAIKADLESACPEVVSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADN 160
Cdd:PLN03030  77 LIDGSNTEKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 161 gLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAHTIGRARCALFSNRLSNFSAT-DSADPTLEASLADSLQSLCAgGNGDG 239
Cdd:PLN03030 156 -LPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTgNGADPSIDASFVPQLQALCP-QNGDG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 240 NETAALDVSSPYVFDNDYYKNLLTERGLLSSDLGLFSSpegvaASTKDLVEAY----SSDGDQFFYDFVWSMIRMGNIPL 315
Cdd:PLN03030 234 SRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTD-----ASTRTFVQRFlgvrGLAGLNFNVEFGRSMVKMSNIGV 308
                        330
                 ....*....|....*.
gi 670406530 316 AAGSDGEVRKNCRVVN 331
Cdd:PLN03030 309 KTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
45-295 5.60e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 231.30  E-value: 5.60e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530   45 VQQHVFDAMREEMRMGASLLRLHFHDCFVNGCDASILLDGDDGEKFALPNLNSVRGYEVIDAIKADLESACPEVVSCADV 124
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSCADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  125 VALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADNGLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAHTIGRARcalfs 204
Cdd:pfam00141  81 LALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  205 nrlsnfsatdsadptleasladslqslcaggngdgnetaaldvsspyvfdndyyKNLLTERGLLSSDLGLFSSPEgvaas 284
Cdd:pfam00141 156 ------------------------------------------------------KNLLDGRGLLTSDQALLSDPR----- 176
                         250
                  ....*....|.
gi 670406530  285 TKDLVEAYSSD 295
Cdd:pfam00141 177 TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
49-312 1.72e-35

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: 129.20  E-value: 1.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  49 VFDAMREEMRMGASLLRLHFHDCFV--------NGCDASILLdgdDGEKFALPNLNSVRGYEVIDAIKADLESACPevVS 120
Cdd:cd00314    7 LEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRF---EPELDRPENGGLDKALRALEPIKSAYDGGNP--VS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 121 CADVVALAASYGV--LFSGGPYYDVLLGRLDgrvanQSGADNGLPSPFEPVDS-------IIQKFAAVGLNTTDVVVLS- 190
Cdd:cd00314   82 RADLIALAGAVAVesTFGGGPLIPFRFGRLD-----ATEPDLGVPDPEGLLPNetssateLRDKFKRMGLSPSELVALSa 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 191 GAHTIGRArcalfsnrlsnfsatdsadptleasladslqslcAGGNGDGNETAALDVSSPYVFDNDYYKNLLT------- 263
Cdd:cd00314  157 GAHTLGGK----------------------------------NHGDLLNYEGSGLWTSTPFTFDNAYFKNLLDmnwewrv 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 670406530 264 ---------ERGLLSSDLGLFSSPEgvaasTKDLVEAYSSDGDQFFYDFVWSMIRMGN 312
Cdd:cd00314  203 gspdpdgvkGPGLLPSDYALLSDSE-----TRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
50-303 1.03e-21

Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.


Pssm-ID: 173825 [Multi-domain]  Cd Length: 253  Bit Score: 92.27  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  50 FDAMREEMR-------MGASLLRLHFH-----DCFVN--GCDASILLDG--DDGEKFALPNlnsvrGYEVIDAIKADLes 113
Cdd:cd00691   13 LEAARNDIAkliddknCAPILVRLAWHdsgtyDKETKtgGSNGTIRFDPelNHGANAGLDI-----ARKLLEPIKKKY-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 114 acPEVvSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGADNGLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAH 193
Cdd:cd00691   86 --PDI-SYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 194 TIGRArcalFSNRlSNFsatdsadptleasladslqslcaggngDGNETaaldvSSPYVFDNDYYKNLLTER------GL 267
Cdd:cd00691  163 TLGRC----HKER-SGY---------------------------DGPWT-----KNPLKFDNSYFKELLEEDwklptpGL 205
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 670406530 268 --LSSDLGLFSSPEgvaasTKDLVEAYSSDGDQFFYDF 303
Cdd:cd00691  206 lmLPTDKALLEDPK-----FRPYVELYAKDQDAFFKDY 238
PLN02879 PLN02879
L-ascorbate peroxidase
118-316 3.34e-12

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 65.47  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 118 VVSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGAdngLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAHTIGR 197
Cdd:PLN02879  91 ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGR---LPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 198 ARcalfsNRLSNFsatdsadptleasladslqslcaggngDGNETaaldvSSPYVFDNDYYKNLLT--ERGLLS--SDLG 273
Cdd:PLN02879 168 CH-----KERSGF---------------------------EGAWT-----PNPLIFDNSYFKEILSgeKEGLLQlpTDKA 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 670406530 274 LFSSPegvaaSTKDLVEAYSSDGDQFFYDFVWSMIRMGNIPLA 316
Cdd:PLN02879 211 LLDDP-----LFLPFVEKYAADEDAFFEDYTEAHLKLSELGFA 248
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
35-250 4.21e-12

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: 65.88  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  35 DSTCPQLYYV---VQQHVFDAMR--EEMRmgaSLLRLHFHDCFV------------NGCDASILLDGDDGEKFAlPNLns 97
Cdd:cd00692   11 NAACCVWFDIlddIQGNLFNGGEcgEEAH---ESLRLTFHDAIGfspalaagqfggGGADGSIVLFDDIETAFH-ANI-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  98 vrGY-EVIDAIKADLESacpEVVSCADVVALAASYGVL-FSGGPYYDVLLGRLDgrvANQSGADNGLPSPFEPVDSIIQK 175
Cdd:cd00692   85 --GLdEIVEALRPFHQK---HNVSMADFIQFAGAVAVSnCPGAPRLEFYAGRKD---ATQPAPDGLVPEPFDSVDKILAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 176 FAAVGLNTTDVVVLSGAHTIgrarcalfsnrlsnfSATDSADPTLEASLADS----------LQSLCAGGNGDGNETAAL 245
Cdd:cd00692  157 FADAGFSPDELVALLAAHSV---------------AAQDFVDPSIAGTPFDStpgvfdtqffIETLLKGTAFPGSGGNQG 221

                 ....*
gi 670406530 246 DVSSP 250
Cdd:cd00692  222 EVESP 226
PLN02364 PLN02364
L-ascorbate peroxidase 1
119-313 1.18e-10

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 60.86  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 119 VSCADVVALAASYGVLFSGGPYYDVLLGRLDgrvANQSGADNGLPSPFEPVDSIIQKFAA-VGLNTTDVVVLSGAHTIGR 197
Cdd:PLN02364  91 ISFADFHQLAGVVAVEVTGGPDIPFHPGRED---KPQPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALSGAHTLGR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 198 ARcalfsnrlsnfsatdsadptleasladslqslcagGNGDGNETAAldVSSPYVFDNDYYKNLLT--ERGLLS--SDLG 273
Cdd:PLN02364 168 CH-----------------------------------KDRSGFEGAW--TSNPLIFDNSYFKELLSgeKEGLLQlvSDKA 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 670406530 274 LFSSPegvaaSTKDLVEAYSSDGDQFFYDFVWSMIRMGNI 313
Cdd:PLN02364 211 LLDDP-----VFRPLVEKYAADEDAFFADYAEAHMKLSEL 245
PLN02608 PLN02608
L-ascorbate peroxidase
119-306 5.86e-10

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 59.39  E-value: 5.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 119 VSCADVVALAASYGVLFSGGPYYDVLLGRLDGRVANQSGAdngLPSPFEPVDSIIQKFAAVGLNTTDVVVLSGAHTIGRA 198
Cdd:PLN02608  89 ITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGR---LPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 199 RcalfSNRlSNFsatdsadptleasladslqslcaggngDGNETaaldvSSPYVFDNDYYKNLLTE--RGL--LSSDLGL 274
Cdd:PLN02608 166 H----PER-SGF---------------------------DGPWT-----KEPLKFDNSYFVELLKGesEGLlkLPTDKAL 208
                        170       180       190
                 ....*....|....*....|....*....|..
gi 670406530 275 FSSPEgvaasTKDLVEAYSSDGDQFFYDFVWS 306
Cdd:PLN02608 209 LEDPE-----FRPYVELYAKDEDAFFRDYAES 235
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
61-277 1.56e-09

Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.


Pssm-ID: 173829  Cd Length: 264  Bit Score: 57.86  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530  61 ASLLRLHFHDCF-------VNGCDASILLDGDDGEKFALPNLNSVRGYEVIDAIKAdlesacpevvSCADVVALAASYGV 133
Cdd:cd08201   43 AEWLRTAFHDMAthnvddgTGGLDASIQYELDRPENIGSGFNTTLNFFVNFYSPRS----------SMADLIAMGVVTSV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670406530 134 LFSGGPYYDVLLGRLDgrvANQSGAdNGLPSPFEPVDSIIQKFAAVGLNTTDVVVLSG-AHTIGRARCALFSNRLSNFSA 212
Cdd:cd08201  113 ASCGGPVVPFRAGRID---ATEAGQ-AGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDFPEIVPPGSV 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 670406530 213 TDSaDPTLEASladslqslcaggngdgneTAALD--VSSPYVFDNDyyKNLLT--ERGLLSSDLGLFSS 277
Cdd:cd08201  189 PDT-VLQFFDT------------------TIQFDnkVVTEYLSGTT--NNPLVvgPNNTTNSDLRIFSS 236
 
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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