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Conserved domains on  [gi|460364898|ref|XP_004228346|]
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peroxidase N [Solanum lycopersicum]

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 ...
27-329 4.93e-173

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: 481.63  E-value: 4.93e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  27 QLTTDFYAKTCPNVLKVVRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNST-TSEKFAAGNInSARGFEVI 105
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANnTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 106 DNIKKAVEDACSGVVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVgniSGANSG--LPAPFHSRDTIISMFQDVGLN 183
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV---SSANDVgnLPSPFFSVSQLISLFASKGLT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 184 VTDVVSLSGAHTIGLAKCATFDNRLTNFNGSGEPDTTLDTALVTELQNLCPSTSDGNNTAPLDRNSTDLFDNHYFKNLIN 263
Cdd:cd00693  157 VTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460364898 264 QRGLLESDQILFSSNDaiatTKTLVEIYSNSSSVFFSDFVNSMIKMGNISPLTGSNGEIRKNCRVI 329
Cdd:cd00693  237 GRGLLTSDQALLSDPR----TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
27-329 4.93e-173

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: 481.63  E-value: 4.93e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  27 QLTTDFYAKTCPNVLKVVRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNST-TSEKFAAGNInSARGFEVI 105
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANnTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 106 DNIKKAVEDACSGVVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVgniSGANSG--LPAPFHSRDTIISMFQDVGLN 183
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV---SSANDVgnLPSPFFSVSQLISLFASKGLT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 184 VTDVVSLSGAHTIGLAKCATFDNRLTNFNGSGEPDTTLDTALVTELQNLCPSTSDGNNTAPLDRNSTDLFDNHYFKNLIN 263
Cdd:cd00693  157 VTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460364898 264 QRGLLESDQILFSSNDaiatTKTLVEIYSNSSSVFFSDFVNSMIKMGNISPLTGSNGEIRKNCRVI 329
Cdd:cd00693  237 GRGLLTSDQALLSDPR----TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
13-330 3.17e-93

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 280.31  E-value: 3.17e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  13 LFVTFMIMFVVVNSQLT-TDFYAKTCPNVLKVVRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNSTtsEKF 91
Cdd:PLN03030   9 FFLLAMMATTLVQGQGTrVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT--EKT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  92 AAGNInSARGFEVIDNIKKAVEDACSGVVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVGNISGANSgLPAPFHSRD 171
Cdd:PLN03030  87 ALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSID 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 172 TIISMFQDVGLNVTDVVSLSGAHTIGLAKCATFDNRLTNFNGSGE-PDTTLDTALVTELQNLCPSTSDGNNTAPLDRNST 250
Cdd:PLN03030 165 VQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 251 DLFDNHYFKNLINQRGLLESDQILFSSndaiATTKTLVEIYSNSSSV----FFSDFVNSMIKMGNISPLTGSNGEIRKNC 326
Cdd:PLN03030 245 NRFDASFFSNLKNGRGILESDQKLWTD----ASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVC 320

                 ....
gi 460364898 327 RVIN 330
Cdd:PLN03030 321 SAIN 324
peroxidase pfam00141
Peroxidase;
44-294 5.16e-80

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 241.70  E-value: 5.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898   44 VRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNstTSEKFAAGNINSARGFEVIDNIKKAVEDACSGVVSCA 123
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGF--KPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  124 DILAIAARDAVLLSGGPTWKVRLGRRDGLVGNISGANSGLPAPFHSRDTIISMFQDVGLNVTDVVSLSGAHTIGLAkcat 203
Cdd:pfam00141  79 DILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  204 fdnrltnfngsgepdttldtalvtelqnlcpstsdgnntapldrnstdlfdnHyfKNLINQRGLLESDQILFSSNDaiat 283
Cdd:pfam00141 155 ----------------------------------------------------H--KNLLDGRGLLTSDQALLSDPR---- 176
                         250
                  ....*....|.
gi 460364898  284 TKTLVEIYSNS 294
Cdd:pfam00141 177 TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
27-329 4.93e-173

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: 481.63  E-value: 4.93e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  27 QLTTDFYAKTCPNVLKVVRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNST-TSEKFAAGNInSARGFEVI 105
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANnTSEKDAPPNL-SLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 106 DNIKKAVEDACSGVVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVgniSGANSG--LPAPFHSRDTIISMFQDVGLN 183
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRV---SSANDVgnLPSPFFSVSQLISLFASKGLT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 184 VTDVVSLSGAHTIGLAKCATFDNRLTNFNGSGEPDTTLDTALVTELQNLCPSTSDGNNTAPLDRNSTDLFDNHYFKNLIN 263
Cdd:cd00693  157 VTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460364898 264 QRGLLESDQILFSSNDaiatTKTLVEIYSNSSSVFFSDFVNSMIKMGNISPLTGSNGEIRKNCRVI 329
Cdd:cd00693  237 GRGLLTSDQALLSDPR----TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
13-330 3.17e-93

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 280.31  E-value: 3.17e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  13 LFVTFMIMFVVVNSQLT-TDFYAKTCPNVLKVVRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNSTtsEKF 91
Cdd:PLN03030   9 FFLLAMMATTLVQGQGTrVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT--EKT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  92 AAGNInSARGFEVIDNIKKAVEDACSGVVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVGNISGANSgLPAPFHSRD 171
Cdd:PLN03030  87 ALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSID 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 172 TIISMFQDVGLNVTDVVSLSGAHTIGLAKCATFDNRLTNFNGSGE-PDTTLDTALVTELQNLCPSTSDGNNTAPLDRNST 250
Cdd:PLN03030 165 VQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 251 DLFDNHYFKNLINQRGLLESDQILFSSndaiATTKTLVEIYSNSSSV----FFSDFVNSMIKMGNISPLTGSNGEIRKNC 326
Cdd:PLN03030 245 NRFDASFFSNLKNGRGILESDQKLWTD----ASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVC 320

                 ....
gi 460364898 327 RVIN 330
Cdd:PLN03030 321 SAIN 324
peroxidase pfam00141
Peroxidase;
44-294 5.16e-80

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 241.70  E-value: 5.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898   44 VRKEVQNAIKNEMRMAASLLRLHFHDCFVNGCDGSLLLDGNstTSEKFAAGNINSARGFEVIDNIKKAVEDACSGVVSCA 123
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGF--KPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  124 DILAIAARDAVLLSGGPTWKVRLGRRDGLVGNISGANSGLPAPFHSRDTIISMFQDVGLNVTDVVSLSGAHTIGLAkcat 203
Cdd:pfam00141  79 DILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA---- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  204 fdnrltnfngsgepdttldtalvtelqnlcpstsdgnntapldrnstdlfdnHyfKNLINQRGLLESDQILFSSNDaiat 283
Cdd:pfam00141 155 ----------------------------------------------------H--KNLLDGRGLLTSDQALLSDPR---- 176
                         250
                  ....*....|.
gi 460364898  284 TKTLVEIYSNS 294
Cdd:pfam00141 177 TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
44-311 2.25e-32

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: 121.11  E-value: 2.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  44 VRKEVQNAIKNEMRMAASLLRLHFHDCFV--------NGCDGSLLLDgnsttSEKFAAGNINSARGFEVIDNIKKAVEDa 115
Cdd:cd00314    3 IKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRFE-----PELDRPENGGLDKALRALEPIKSAYDG- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 116 cSGVVSCADILAIAARDAV--LLSGGPTWKVRLGRRDGLVGNISGAN--SGLPAPFHSRDTIISMFQDVGLNVTDVVSLS 191
Cdd:cd00314   77 -GNPVSRADLIALAGAVAVesTFGGGPLIPFRFGRLDATEPDLGVPDpeGLLPNETSSATELRDKFKRMGLSPSELVALS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 192 -GAHTIGlAKCAtfdNRLTNFNGSGEPDTTLDTalvtelqnlcpstsdgnntapldrnstdlFDNHYFKNLIN------- 263
Cdd:cd00314  156 aGAHTLG-GKNH---GDLLNYEGSGLWTSTPFT-----------------------------FDNAYFKNLLDmnwewrv 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 460364898 264 ---------QRGLLESDQILFSsndaIATTKTLVEIYSNSSSVFFSDFVNSMIKMGN 311
Cdd:cd00314  203 gspdpdgvkGPGLLPSDYALLS----DSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
34-309 2.60e-22

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: 93.81  E-value: 2.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  34 AKTCPNVLKVVRKEVQNAIKnEMRMAASLLRLHFH-----DCFVN--GCDGSLLLDgnsttSEKFAAGN--INSARGFev 104
Cdd:cd00691    6 AAYAAKDLEAARNDIAKLID-DKNCAPILVRLAWHdsgtyDKETKtgGSNGTIRFD-----PELNHGANagLDIARKL-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 105 IDNIKKAVEDacsgvVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVGNISGANSGLPAPFHSRDTIISMFQDVGLNV 184
Cdd:cd00691   78 LEPIKKKYPD-----ISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFND 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 185 TDVVSLSGAHTIGlaKCatFDNRlTNFNGsgepdttldtalvtelqnlcPSTSDgnntaPLdrnstdLFDNHYFKNLINQ 264
Cdd:cd00691  153 QEIVALSGAHTLG--RC--HKER-SGYDG--------------------PWTKN-----PL------KFDNSYFKELLEE 196
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 460364898 265 RGLLESDQIL-FSSNDAIAT---TKTLVEIYSNSSSVFFSDFVNSMIKM 309
Cdd:cd00691  197 DWKLPTPGLLmLPTDKALLEdpkFRPYVELYAKDQDAFFKDYAEAHKKL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
29-197 1.12e-11

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: 64.72  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  29 TTDFYAKTCpnVLKVVRKEVQNAIKNEMR---MAASLLRLHFHDCFV------------NGCDGSLLLDGNSTTseKFAA 93
Cdd:cd00692    7 QTVCNAACC--VWFDILDDIQGNLFNGGEcgeEAHESLRLTFHDAIGfspalaagqfggGGADGSIVLFDDIET--AFHA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  94 GNinsarGFEVIDNIKKAVEDacSGVVSCADILAIAArdAVLLS---GGPTWKVRLGRRDglvgNISGANSGL-PAPFHS 169
Cdd:cd00692   83 NI-----GLDEIVEALRPFHQ--KHNVSMADFIQFAG--AVAVSncpGAPRLEFYAGRKD----ATQPAPDGLvPEPFDS 149
                        170       180
                 ....*....|....*....|....*...
gi 460364898 170 RDTIISMFQDVGLNVTDVVSLSGAHTIG 197
Cdd:cd00692  150 VDKILARFADAGFSPDELVALLAAHSVA 177
PLN02608 PLN02608
L-ascorbate peroxidase
59-309 5.75e-11

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 62.09  E-value: 5.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  59 AASLLRLHFHDCfvngcdGSLllDGNSTTSEkfAAGNINSARGFEVIDN--IKKAVeDACSGV------VSCADILAIAA 130
Cdd:PLN02608  31 APIMLRLAWHDA------GTY--DAKTKTGG--PNGSIRNEEEYSHGANngLKIAI-DLCEPVkakhpkITYADLYQLAG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 131 RDAVLLSGGPTWKVRLGRRDGLV----GNISGANSGLPapfHSRDtiisMFQDVGLNVTDVVSLSGAHTIGLAKcatfDN 206
Cdd:PLN02608 100 VVAVEVTGGPTIDFVPGRKDSNAcpeeGRLPDAKKGAK---HLRD----VFYRMGLSDKDIVALSGGHTLGRAH----PE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 207 RlTNFNGsgepdttldtalvtelqnlcPSTSDgnntaPLDrnstdlFDNHYFKNLI--NQRGLLE--SDQILFSSndaiA 282
Cdd:PLN02608 169 R-SGFDG--------------------PWTKE-----PLK------FDNSYFVELLkgESEGLLKlpTDKALLED----P 212
                        250       260
                 ....*....|....*....|....*..
gi 460364898 283 TTKTLVEIYSNSSSVFFSDFVNSMIKM 309
Cdd:PLN02608 213 EFRPYVELYAKDEDAFFRDYAESHKKL 239
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
59-197 7.13e-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: 55.94  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  59 AASLLRLHFHDCF-------VNGCDGSLLLDGNSttSEKFAAGNINSARGFEVIDNIKkavedacsgvVSCADILAIAAR 131
Cdd:cd08201   42 AAEWLRTAFHDMAthnvddgTGGLDASIQYELDR--PENIGSGFNTTLNFFVNFYSPR----------SSMADLIAMGVV 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 460364898 132 DAVLLSGGPTWKVRLGRRDGlvgnISGANSGLPAPFHSRDTIISMFQDVGLNVTDVVSLSG-AHTIG 197
Cdd:cd08201  110 TSVASCGGPVVPFRAGRIDA----TEAGQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLG 172
PLN02879 PLN02879
L-ascorbate peroxidase
119-312 1.37e-08

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 54.68  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 119 VVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLVGNISGAnsgLPAPFHSRDTIISMFQDVGLNVTDVVSLSGAHTIGl 198
Cdd:PLN02879  91 ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGR---LPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 199 aKCatfDNRLTNFNGSGEpdttldtalvtelQNlcpstsdgnntaPLdrnstdLFDNHYFKNLIN--QRGLLE--SDQIL 274
Cdd:PLN02879 167 -RC---HKERSGFEGAWT-------------PN------------PL------IFDNSYFKEILSgeKEGLLQlpTDKAL 211
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 460364898 275 FssNDAIatTKTLVEIYSNSSSVFFSDFVNSMIKMGNI 312
Cdd:PLN02879 212 L--DDPL--FLPFVEKYAADEDAFFEDYTEAHLKLSEL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
35-317 2.79e-08

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 53.93  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898  35 KTCPNVLKVVRKEVQNAIKN------EMRMAASLLRLHFH-----DC--FVNGCDGSLLLDgnsttSEKFAAGNINSARG 101
Cdd:PLN02364   3 KNYPTVSEDYKKAVEKCRRKlrgliaEKNCAPIMVRLAWHsagtfDCqsRTGGPFGTMRFD-----AEQAHGANSGIHIA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 102 FEVIDNIKKAVEdacsgVVSCADILAIAARDAVLLSGGPTWKVRLGRRDGLV----GNISGANSGLPapfHSRDTIIsmf 177
Cdd:PLN02364  78 LRLLDPIREQFP-----TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQpppeGRLPDATKGCD---HLRDVFA--- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460364898 178 QDVGLNVTDVVSLSGAHTIGlaKCatfDNRLTNFNGSGepdttldtalvtelqnlcpstsdgnNTAPLdrnstdLFDNHY 257
Cdd:PLN02364 147 KQMGLSDKDIVALSGAHTLG--RC---HKDRSGFEGAW-------------------------TSNPL------IFDNSY 190
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 460364898 258 FKNLIN--QRGLLE--SDQILFssNDAIatTKTLVEIYSNSSSVFFSDFVNSMIKMGNISPLTG 317
Cdd:PLN02364 191 FKELLSgeKEGLLQlvSDKALL--DDPV--FRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
 
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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