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Conserved domains on  [gi|297809375|ref|XP_002872571|]
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peroxidase 39 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

peroxidase( domain architecture ID 10091046)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
25-326 1.80e-178

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


:

Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 495.11  E-value: 1.80e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  25 QLKMGFYDQTCPYAEKIVQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSNQqVEKLAPPNLTVRGFDFI 104
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNT-SEKDAPPNLSLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 105 DKVKSALESKCPGIVSCADIITLATRDSIVAIGGPTWNVPTGRRDGRISNfAEARNNIPPPFGNFTTLITLFGNQGLDVK 184
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSS-ANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 185 DLVLLSGAHTIGVSHCSSFSNRLFNFTGVGDQDPSMDSEYVDNLKsRRCLALADNTTTVEMDPGSRNTFDLSYYRLVLKR 264
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLR-KKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297809375 265 RGLFESDAALTMNPAALAQVKRFSgGSEQEFFAEFSKSMEKMGRIGVKTGSDGEIRRTCAFV 326
Cdd:cd00693  238 RGLLTSDQALLSDPRTRAIVNRYA-ANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
25-326 1.80e-178

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 495.11  E-value: 1.80e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  25 QLKMGFYDQTCPYAEKIVQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSNQqVEKLAPPNLTVRGFDFI 104
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNT-SEKDAPPNLSLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 105 DKVKSALESKCPGIVSCADIITLATRDSIVAIGGPTWNVPTGRRDGRISNfAEARNNIPPPFGNFTTLITLFGNQGLDVK 184
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSS-ANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 185 DLVLLSGAHTIGVSHCSSFSNRLFNFTGVGDQDPSMDSEYVDNLKsRRCLALADNTTTVEMDPGSRNTFDLSYYRLVLKR 264
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLR-KKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297809375 265 RGLFESDAALTMNPAALAQVKRFSgGSEQEFFAEFSKSMEKMGRIGVKTGSDGEIRRTCAFV 326
Cdd:cd00693  238 RGLLTSDQALLSDPRTRAIVNRYA-ANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
8-327 8.33e-103

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 304.57  E-value: 8.33e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375   8 LVMMILVIQGFVRFSEAQ-LKMGFYDQTCPYAEKIVQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSnq 86
Cdd:PLN03030   6 VILFFLLAMMATTLVQGQgTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  87 qvEKLAPPNLTVRGFDFIDKVKSALESKCPGIVSCADIITLATRDSIVAIGGPTWNVPTGRRDGRISnFAEARNNIPPPF 166
Cdd:PLN03030  84 --EKTALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVS-LASDASNLPGFT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 167 GNFTTLITLFGNQGLDVKDLVLLSGAHTIGVSHCSSFSNRLFNFTGVGD-QDPSMDSEYVDNLKSrRCLALADNTTTVEM 245
Cdd:PLN03030 161 DSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQA-LCPQNGDGSRRIAL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 246 DPGSRNTFDLSYYRLVLKRRGLFESDAALTMNPAALAQVKRF---SGGSEQEFFAEFSKSMEKMGRIGVKTGSDGEIRRT 322
Cdd:PLN03030 240 DTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFlgvRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKV 319

                 ....*
gi 297809375 323 CAFVN 327
Cdd:PLN03030 320 CSAIN 324
peroxidase pfam00141
Peroxidase;
42-199 8.35e-79

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 238.23  E-value: 8.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375   42 VQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSnqqvEKLAPPNLTVR-GFDFIDKVKSALESKCPGIVS 120
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKP----EKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297809375  121 CADIITLATRDSIVAIGGPTWNVPTGRRDGRISNFAEARNNIPPPFGNFTTLITLFGNQGLDVKDLVLLSGAHTIGVSH 199
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH 155
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
25-326 1.80e-178

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 495.11  E-value: 1.80e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  25 QLKMGFYDQTCPYAEKIVQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSNQqVEKLAPPNLTVRGFDFI 104
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNT-SEKDAPPNLSLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 105 DKVKSALESKCPGIVSCADIITLATRDSIVAIGGPTWNVPTGRRDGRISNfAEARNNIPPPFGNFTTLITLFGNQGLDVK 184
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSS-ANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 185 DLVLLSGAHTIGVSHCSSFSNRLFNFTGVGDQDPSMDSEYVDNLKsRRCLALADNTTTVEMDPGSRNTFDLSYYRLVLKR 264
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLR-KKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297809375 265 RGLFESDAALTMNPAALAQVKRFSgGSEQEFFAEFSKSMEKMGRIGVKTGSDGEIRRTCAFV 326
Cdd:cd00693  238 RGLLTSDQALLSDPRTRAIVNRYA-ANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
8-327 8.33e-103

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 304.57  E-value: 8.33e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375   8 LVMMILVIQGFVRFSEAQ-LKMGFYDQTCPYAEKIVQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSnq 86
Cdd:PLN03030   6 VILFFLLAMMATTLVQGQgTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  87 qvEKLAPPNLTVRGFDFIDKVKSALESKCPGIVSCADIITLATRDSIVAIGGPTWNVPTGRRDGRISnFAEARNNIPPPF 166
Cdd:PLN03030  84 --EKTALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVS-LASDASNLPGFT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 167 GNFTTLITLFGNQGLDVKDLVLLSGAHTIGVSHCSSFSNRLFNFTGVGD-QDPSMDSEYVDNLKSrRCLALADNTTTVEM 245
Cdd:PLN03030 161 DSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQA-LCPQNGDGSRRIAL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 246 DPGSRNTFDLSYYRLVLKRRGLFESDAALTMNPAALAQVKRF---SGGSEQEFFAEFSKSMEKMGRIGVKTGSDGEIRRT 322
Cdd:PLN03030 240 DTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFlgvRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKV 319

                 ....*
gi 297809375 323 CAFVN 327
Cdd:PLN03030 320 CSAIN 324
peroxidase pfam00141
Peroxidase;
42-199 8.35e-79

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 238.23  E-value: 8.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375   42 VQDVVNQHIHNAPSLAAGLIRMHFHDCFVRGCDGSILINATSSnqqvEKLAPPNLTVR-GFDFIDKVKSALESKCPGIVS 120
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKP----EKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297809375  121 CADIITLATRDSIVAIGGPTWNVPTGRRDGRISNFAEARNNIPPPFGNFTTLITLFGNQGLDVKDLVLLSGAHTIGVSH 199
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH 155
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
42-308 6.44e-26

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: 103.77  E-value: 6.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  42 VQDVVNQHIHNAPSLAAGLIRMHFHDCFVR--------GCDGSILINAtssnqqvEKLAPPNLTV-RGFDFIDKVKSALE 112
Cdd:cd00314    3 IKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIRFEP-------ELDRPENGGLdKALRALEPIKSAYD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 113 SKCPgiVSCADIITLAtrdSIVAI-----GGPTWNVPTGRRDGRISNF--AEARNNIPPPFGNFTTLITLFGNQGLDVKD 185
Cdd:cd00314   76 GGNP--VSRADLIALA---GAVAVestfgGGPLIPFRFGRLDATEPDLgvPDPEGLLPNETSSATELRDKFKRMGLSPSE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 186 LV-LLSGAHTI-GVSHCssfsnRLFNFTGVGDQDPSM---DSEYVDNLKsrrclaladNTTTVEMDPGSRNTFDLSYYRL 260
Cdd:cd00314  151 LVaLSAGAHTLgGKNHG-----DLLNYEGSGLWTSTPftfDNAYFKNLL---------DMNWEWRVGSPDPDGVKGPGLL 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 297809375 261 vlkrrglfESDAALTMNPAALAQVKRFsGGSEQEFFAEFSKSMEKMGR 308
Cdd:cd00314  217 --------PSDYALLSDSETRALVERY-ASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
100-312 1.40e-15

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: 74.93  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 100 GFDFIDKVKSalesKCPGIvSCADIITLAtrdSIVAI---GGPTWNVPTGRRDGRISNFAEARNNIPPPFGNFTTLITLF 176
Cdd:cd00691   74 ARKLLEPIKK----KYPDI-SYADLWQLA---GVVAIeemGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVF 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 177 GNQGLDVKDLVLLSGAHTIGVSHCssfsnrlfNFTGVGdqdpsmdseyvdnlksrrclalADNTTtvemdpgSRNTFDLS 256
Cdd:cd00691  146 YRMGFNDQEIVALSGAHTLGRCHK--------ERSGYD----------------------GPWTK-------NPLKFDNS 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297809375 257 YYRLVLKRR------GL--FESDAALTMNPAALAQVKRFSgGSEQEFFAEFSKSMEKMGRIGVK 312
Cdd:cd00691  189 YFKELLEEDwklptpGLlmLPTDKALLEDPKFRPYVELYA-KDQDAFFKDYAEAHKKLSELGVP 251
PLN02608 PLN02608
L-ascorbate peroxidase
102-317 6.29e-09

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 56.31  E-value: 6.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 102 DFIDKVKSalesKCPGIvSCADIITLAtrdSIVAI---GGPTWNVPTGRRDGRISNfAEARnnIPPPFGNFTTLITLFGN 178
Cdd:PLN02608  77 DLCEPVKA----KHPKI-TYADLYQLA---GVVAVevtGGPTIDFVPGRKDSNACP-EEGR--LPDAKKGAKHLRDVFYR 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 179 QGLDVKDLVLLSGAHTIGVSHcssfSNRLfNFTGVGDQDPsmdseyvdnLKsrrclaladntttvemdpgsrntFDLSYY 258
Cdd:PLN02608 146 MGLSDKDIVALSGGHTLGRAH----PERS-GFDGPWTKEP---------LK-----------------------FDNSYF 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297809375 259 RLVLK--RRGLFE--SDAALTMNPAALAQVKRFSgGSEQEFFAEFSKSMEKMGRIGVKTGSDG 317
Cdd:PLN02608 189 VELLKgeSEGLLKlpTDKALLEDPEFRPYVELYA-KDEDAFFRDYAESHKKLSELGFTPPSSA 250
PLN02879 PLN02879
L-ascorbate peroxidase
100-310 2.17e-07

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 51.21  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 100 GFDFIDKVKSALESKCPgIVSCADIITLATRDSIVAIGGPTWNVPTGRRDgRISNFAEARnnIPPPFGNFTTLITLFGNQ 179
Cdd:PLN02879  74 GLDIAVRLLDPIKELFP-ILSYADFYQLAGVVAVEITGGPEIPFHPGRLD-KVEPPPEGR--LPQATKGVDHLRDVFGRM 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 180 GLDVKDLVLLSGAHTIGVSHcssfsNRLFNFTGVGDQDPSMdseyvdnlksrrclaladntttvemdpgsrntFDLSYYR 259
Cdd:PLN02879 150 GLNDKDIVALSGGHTLGRCH-----KERSGFEGAWTPNPLI--------------------------------FDNSYFK 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 297809375 260 LVL--KRRGLFE--SDAALTMNPAALAQVKRFSgGSEQEFFAEFSKSMEKMGRIG 310
Cdd:PLN02879 193 EILsgEKEGLLQlpTDKALLDDPLFLPFVEKYA-ADEDAFFEDYTEAHLKLSELG 246
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
61-311 4.53e-07

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: 50.86  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  61 IRMHFHDC--FVR----------GCDGSILINATssnqqVEKLAPPNLtvrGFDFIDKVKSALESKCPgiVSCADIITLA 128
Cdd:cd00692   42 LRLTFHDAigFSPalaagqfgggGADGSIVLFDD-----IETAFHANI---GLDEIVEALRPFHQKHN--VSMADFIQFA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 129 TRdsiVAI----GGPTWNVPTGRRDgriSNFAEARNNIPPPFGNFTTLITLFGNQGLDVKDLVLLSGAHTIGVshcSSFS 204
Cdd:cd00692  112 GA---VAVsncpGAPRLEFYAGRKD---ATQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAA---QDFV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 205 NRlfnfTGVGD-QD--PS-MDSE-YVDNLksrrclalaDNTTTVemdPGSRNTFDLSYYRLVLKRRglFESDAALTMNPA 279
Cdd:cd00692  183 DP----SIAGTpFDstPGvFDTQfFIETL---------LKGTAF---PGSGGNQGEVESPLPGEFR--LQSDFLLARDPR 244
                        250       260       270
                 ....*....|....*....|....*....|...
gi 297809375 280 ALAQVKRFSGGseQEFFAE-FSKSMEKMGRIGV 311
Cdd:cd00692  245 TACEWQSFVNN--QAKMNAaFAAAMLKLSLLGQ 275
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
55-203 1.31e-03

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


Pssm-ID: 173829  Cd Length: 264  Bit Score: 39.76  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375  55 SLAAGLIRMHFHDCF-------VRGCDGSIlinatssnqQVEKLAPPNL------TVRGFDFIDKVKSaleskcpgivSC 121
Cdd:cd08201   40 QAAAEWLRTAFHDMAthnvddgTGGLDASI---------QYELDRPENIgsgfntTLNFFVNFYSPRS----------SM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297809375 122 ADIITLATRDSIVAIGGPTwnVPTgrRDGRISNFAEARNNIPPPFGNFTTLITLFGNQGLDVKDLV-LLSGAHTIGVSHC 200
Cdd:cd08201  101 ADLIAMGVVTSVASCGGPV--VPF--RAGRIDATEAGQAGVPEPQTDLGTTTESFRRQGFSTSEMIaLVACGHTLGGVHS 176

                 ...
gi 297809375 201 SSF 203
Cdd:cd08201  177 EDF 179
 
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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