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Conserved domains on  [gi|110743356|dbj|BAE99565|]
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peroxidase ATP21a [Arabidopsis thaliana]

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 ...
26-328 4.97e-165

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: 461.21  E-value: 4.97e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  26 QLSRGFYSKTCPNVEQIVRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVMIQSTPKNKAEKDHPDNISLagDGFDV 105
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 106 VIQAKKALDSnpSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTASSVeGNLPGPSDNVDKLNALFTKNKL 185
Cdd:cd00693   79 IDDIKAALEA--ACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 186 TQEDMIALSAAHTLGFAHCGKVFKRIHKFNGINSVDPTLNKAYAIELQKACPKNVDPRIAINMDPVTPKTFDNTYFKNLQ 265
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110743356 266 QGKGLFTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVGVKNSSNGNIRRDCGAF 328
Cdd:cd00693  236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
26-328 4.97e-165

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: 461.21  E-value: 4.97e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  26 QLSRGFYSKTCPNVEQIVRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVMIQSTPKNKAEKDHPDNISLagDGFDV 105
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 106 VIQAKKALDSnpSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTASSVeGNLPGPSDNVDKLNALFTKNKL 185
Cdd:cd00693   79 IDDIKAALEA--ACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 186 TQEDMIALSAAHTLGFAHCGKVFKRIHKFNGINSVDPTLNKAYAIELQKACPKNVDPRIAINMDPVTPKTFDNTYFKNLQ 265
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110743356 266 QGKGLFTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVGVKNSSNGNIRRDCGAF 328
Cdd:cd00693  236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
1-329 5.10e-74

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 231.00  E-value: 5.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356   1 MARFDIVLLIGLCLIISVFpdtTTAQLSR-GFYSKTCPNVEQIVRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVM 79
Cdd:PLN03030   1 GQRFIVILFFLLAMMATTL---VQGQGTRvGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  80 IQSTpknKAEKDHPDNISLagDGFDVVIQAKKALDSnpSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTA 159
Cdd:PLN03030  78 IDGS---NTEKTALPNLLL--RGYDVIDDAKTQLEA--ACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 160 SSVeGNLPGPSDNVDKLNALFTKNKLTQEDMIALSAAHTLGFAHCGKVFKRIHKFNGI-NSVDPTLNKAYAIELQKACPK 238
Cdd:PLN03030 151 SDA-SNLPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTgNGADPSIDASFVPQLQALCPQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 239 NVDPRIAINMDPVTPKTFDNTYFKNLQQGKGLFTSDQVLFTDGRSRPTVNAWAS----NSTAFNRAFVIAMTKLGRVGVK 314
Cdd:PLN03030 230 NGDGSRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVK 309
                        330
                 ....*....|....*
gi 110743356 315 NSSNGNIRRDCGAFN 329
Cdd:PLN03030 310 TGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-293 2.69e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 221.67  E-value: 2.69e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356   43 VRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVMIQStpkNKAEKDHPDNISLAgDGFDVVIQAKKALDSnpSCRNK 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLR-KGFEVIDDIKAKLEA--ACPGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  123 VSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTASSVEGNLPGPSDNVDKLNALFTKNKLTQEDMIALSAAHTLGFA 202
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  203 HcgkvfkrihkfnginsvdptlnkayaielqkacpknvdpriainmdpvtpktfdntyfKNLQQGKGLFTSDQVLFTDGR 282
Cdd:pfam00141 155 H----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 110743356  283 SRPTVNAWASN 293
Cdd:pfam00141 177 TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
26-328 4.97e-165

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: 461.21  E-value: 4.97e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  26 QLSRGFYSKTCPNVEQIVRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVMIQSTPKNKAEKDHPDNISLagDGFDV 105
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSL--RGFDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 106 VIQAKKALDSnpSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTASSVeGNLPGPSDNVDKLNALFTKNKL 185
Cdd:cd00693   79 IDDIKAALEA--ACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 186 TQEDMIALSAAHTLGFAHCGKVFKRIHKFNGINSVDPTLNKAYAIELQKACPKNVDPRIAINMDPVTPKTFDNTYFKNLQ 265
Cdd:cd00693  156 TVTDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110743356 266 QGKGLFTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVGVKNSSNGNIRRDCGAF 328
Cdd:cd00693  236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
1-329 5.10e-74

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 231.00  E-value: 5.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356   1 MARFDIVLLIGLCLIISVFpdtTTAQLSR-GFYSKTCPNVEQIVRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVM 79
Cdd:PLN03030   1 GQRFIVILFFLLAMMATTL---VQGQGTRvGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  80 IQSTpknKAEKDHPDNISLagDGFDVVIQAKKALDSnpSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTA 159
Cdd:PLN03030  78 IDGS---NTEKTALPNLLL--RGYDVIDDAKTQLEA--ACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 160 SSVeGNLPGPSDNVDKLNALFTKNKLTQEDMIALSAAHTLGFAHCGKVFKRIHKFNGI-NSVDPTLNKAYAIELQKACPK 238
Cdd:PLN03030 151 SDA-SNLPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTgNGADPSIDASFVPQLQALCPQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 239 NVDPRIAINMDPVTPKTFDNTYFKNLQQGKGLFTSDQVLFTDGRSRPTVNAWAS----NSTAFNRAFVIAMTKLGRVGVK 314
Cdd:PLN03030 230 NGDGSRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVK 309
                        330
                 ....*....|....*
gi 110743356 315 NSSNGNIRRDCGAFN 329
Cdd:PLN03030 310 TGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
43-293 2.69e-72

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 221.67  E-value: 2.69e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356   43 VRNAVQKKIKKTFVAVPATLRLFFHDCFVNGCDASVMIQStpkNKAEKDHPDNISLAgDGFDVVIQAKKALDSnpSCRNK 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLR-KGFEVIDDIKAKLEA--ACPGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  123 VSCADILTLATRDVVVAAGGPSYEVELGRFDGLVSTASSVEGNLPGPSDNVDKLNALFTKNKLTQEDMIALSAAHTLGFA 202
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  203 HcgkvfkrihkfnginsvdptlnkayaielqkacpknvdpriainmdpvtpktfdntyfKNLQQGKGLFTSDQVLFTDGR 282
Cdd:pfam00141 155 H----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 110743356  283 SRPTVNAWASN 293
Cdd:pfam00141 177 TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
41-310 1.64e-23

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: 97.22  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  41 QIVRNAVQKKIKKTFVAVPATLRLFFHDCFV--------NGCDASVmiqstpKNKAEKDHPDNIslagdGFDVVIQAKKA 112
Cdd:cd00314    1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSI------RFEPELDRPENG-----GLDKALRALEP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 113 LDSNPSCRNKVSCADILTLATrdvVVAA-----GGPSYEVELGRFDGLVSTASSV--EGNLPGPSDNVDKLNALFTKNKL 185
Cdd:cd00314   70 IKSAYDGGNPVSRADLIALAG---AVAVestfgGGPLIPFRFGRLDATEPDLGVPdpEGLLPNETSSATELRDKFKRMGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 186 TQEDMIALSA-AHTL-GFAHCgkvfkrihkfnginsvdptlnkayaielqkacpkNVDPRIAINMDPVTPKTFDNTYFKN 263
Cdd:cd00314  147 SPSELVALSAgAHTLgGKNHG----------------------------------DLLNYEGSGLWTSTPFTFDNAYFKN 192
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110743356 264 L----------------QQGKGLFTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGR 310
Cdd:cd00314  193 LldmnwewrvgspdpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
43-314 3.04e-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: 3.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  43 VRNAVQKKIKKTFVAvPATLRLFFH-----DCFVN--GCDASVmiqstpKNKAEKDHPDNISLAGdgfdvviqAKKAL-- 113
Cdd:cd00691   16 ARNDIAKLIDDKNCA-PILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAGLDI--------ARKLLep 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 114 --DSNPscrnKVSCADILTLATrdvVVA---AGGPSYEVELGRFDGLVSTASSVEGNLPGPSDNVDKLNALFTKNKLTQE 188
Cdd:cd00691   81 ikKKYP----DISYADLWQLAG---VVAieeMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 189 DMIALSAAHTLGFAHcgkvfKRIHKFNGINSVDPTlnkayaielqkacpknvdpriainmdpvtpkTFDNTYFKNLQQGK 268
Cdd:cd00691  154 EIVALSGAHTLGRCH-----KERSGYDGPWTKNPL-------------------------------KFDNSYFKELLEED 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110743356 269 ------GL--FTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVGVK 314
Cdd:cd00691  198 wklptpGLlmLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGVP 251
PLN02879 PLN02879
L-ascorbate peroxidase
33-312 2.75e-14

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 71.63  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  33 SKTCPNVEQIVRNAVQ--KKIKKTFVA----VPATLRLFFHDCfvngcdASVMIQS-TPKNKAEKDHPDNISL-AGDGFD 104
Cdd:PLN02879   3 KKSYPEVKEEYKKAVQrcKRKLRGLIAekhcAPIVLRLAWHSA------GTFDVKTkTGGPFGTIRHPQELAHdANNGLD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 105 VVIqakKALDSNPSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDglvSTASSVEGNLPGPSDNVDKLNALFTKNK 184
Cdd:PLN02879  77 IAV---RLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLD---KVEPPPEGRLPQATKGVDHLRDVFGRMG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 185 LTQEDMIALSAAHTLGFAHcgkvfKRIHKFNGINSVDPTLnkayaielqkacpknvdpriainmdpvtpktFDNTYFKNL 264
Cdd:PLN02879 151 LNDKDIVALSGGHTLGRCH-----KERSGFEGAWTPNPLI-------------------------------FDNSYFKEI 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110743356 265 QQG--KGLFT--SDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVG 312
Cdd:PLN02879 195 LSGekEGLLQlpTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELG 246
PLN02608 PLN02608
L-ascorbate peroxidase
59-325 1.95e-13

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 69.41  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  59 PATLRLFFHDC-------FVNGCDASVmiqstpKNKAEKDHPDNISLagdgfdvviqaKKALDSNPSCRNK---VSCADI 128
Cdd:PLN02608  32 PIMLRLAWHDAgtydaktKTGGPNGSI------RNEEEYSHGANNGL-----------KIAIDLCEPVKAKhpkITYADL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 129 LTLATRDVVVAAGGPSYEVELGRFDglvSTASSVEGNLPGPSDNVDKLNALFTKNKLTQEDMIALSAAHTLGFAHcgkvf 208
Cdd:PLN02608  95 YQLAGVVAVEVTGGPTIDFVPGRKD---SNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAH----- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 209 KRIHKFNGinsvdptlnkayaielqkacpknvdpriainmdPVT--PKTFDNTYFKNLQQG--KGL--FTSDQVLFTDGR 282
Cdd:PLN02608 167 PERSGFDG---------------------------------PWTkePLKFDNSYFVELLKGesEGLlkLPTDKALLEDPE 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 110743356 283 SRPTVNAWASNSTAFNRAFVIAMTKLGRVGVKNSSNGNIRRDC 325
Cdd:PLN02608 214 FRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKST 256
PLN02364 PLN02364
L-ascorbate peroxidase 1
33-312 4.30e-13

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 68.18  E-value: 4.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  33 SKTCPNVEQIVRNAVQKKIKKT--FVA----VPATLRLFFHDCFVNGCDASVMIQ-STPKNKAEKDHPDNislagDGFDV 105
Cdd:PLN02364   2 TKNYPTVSEDYKKAVEKCRRKLrgLIAekncAPIMVRLAWHSAGTFDCQSRTGGPfGTMRFDAEQAHGAN-----SGIHI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 106 viqAKKALDSNPSCRNKVSCADILTLATRDVVVAAGGPSYEVELGRFDglvSTASSVEGNLPGPSDNVDKLNALFTKNK- 184
Cdd:PLN02364  77 ---ALRLLDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGRED---KPQPPPEGRLPDATKGCDHLRDVFAKQMg 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 185 LTQEDMIALSAAHTLGFAHcgkvfKRIHKFNGINSVDPTLnkayaielqkacpknvdpriainmdpvtpktFDNTYFKNL 264
Cdd:PLN02364 151 LSDKDIVALSGAHTLGRCH-----KDRSGFEGAWTSNPLI-------------------------------FDNSYFKEL 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110743356 265 QQG--KGL--FTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVG 312
Cdd:PLN02364 195 LSGekEGLlqLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELG 246
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
60-317 6.74e-10

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: 59.33  E-value: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  60 ATLRLFFHDCFV------------NGCDASVMIQSTpknkAEKDHPDNIslagdGFDVVIQAKKALDSNpscrNKVSCAD 127
Cdd:cd00692   40 ESLRLTFHDAIGfspalaagqfggGGADGSIVLFDD----IETAFHANI-----GLDEIVEALRPFHQK----HNVSMAD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 128 ILTLATR-DVVVAAGGPSYEVELGRFDglvSTASSVEGNLPGPSDNVDKLNALFTKNKLTQEDMIALSAAHTLgfahcgk 206
Cdd:cd00692  107 FIQFAGAvAVSNCPGAPRLEFYAGRKD---ATQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSV------- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 207 vfkrihkfnginsvdptlnkayaielqkACPKNVDPRIAinMDPV--TPKTFDNTYF-----KN-LQQGKGL-------- 270
Cdd:cd00692  177 ----------------------------AAQDFVDPSIA--GTPFdsTPGVFDTQFFietllKGtAFPGSGGnqgevesp 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110743356 271 ------FTSDQVLFTDGRSRPTVNAWASNSTAFNRAFVIAMTKLGRVGVKNSS 317
Cdd:cd00692  227 lpgefrLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQDNIS 279
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
62-203 3.55e-07

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: 50.54  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356  62 LRLFFHDCF-------VNGCDASVMIqstpknkaEKDHPDNIslaGDGFDVVIQakkalDSNPSCRNKVSCADILTLATR 134
Cdd:cd08201   46 LRTAFHDMAthnvddgTGGLDASIQY--------ELDRPENI---GSGFNTTLN-----FFVNFYSPRSSMADLIAMGVV 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110743356 135 DVVVAAGGPSYEVELGRFDglvsTASSVEGNLPGPSDNVDKLNALFTKNKLTQEDMIALSA-AHTLGFAH 203
Cdd:cd08201  110 TSVASCGGPVVPFRAGRID----ATEAGQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVH 175
 
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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