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Conserved domains on  [gi|257632751|emb|CBD24422|]
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unnamed protein product [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 ...
34-334 1.24e-179

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: 498.58  E-value: 1.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  34 NLFPDFYRSSCPRAEEIVRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGSIVTEKNSNPNsRSARGFEVV 113
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 114 DEIKAALENECPNTVSCADALTLAARDSSVLTGGPSWTVPLGRRDSaTASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLT 193
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDG-RVSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 194 DLVALSGSHTIGFSRCTSFRQRLYNQSGSGSPDTTLEKSYAAILRQRCPRSGGDQNLSELDINSAGRFDNSYFKNLIENM 273
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257632751 274 GLLNSDQVLFSSNEqSRELVKKYAEDQEEFFEQFAESMIKMGKISPLTGSSGEIRKKCRKI 334
Cdd:cd00693  239 GLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
34-334 1.24e-179

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: 498.58  E-value: 1.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  34 NLFPDFYRSSCPRAEEIVRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGSIVTEKNSNPNsRSARGFEVV 113
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 114 DEIKAALENECPNTVSCADALTLAARDSSVLTGGPSWTVPLGRRDSaTASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLT 193
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDG-RVSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 194 DLVALSGSHTIGFSRCTSFRQRLYNQSGSGSPDTTLEKSYAAILRQRCPRSGGDQNLSELDINSAGRFDNSYFKNLIENM 273
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257632751 274 GLLNSDQVLFSSNEqSRELVKKYAEDQEEFFEQFAESMIKMGKISPLTGSSGEIRKKCRKI 334
Cdd:cd00693  239 GLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
39-335 5.65e-84

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 256.81  E-value: 5.65e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  39 FYRSSCPRAEEIVRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGsivTEKNSNPNsRSARGFEVVDEIKA 118
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPN-LLLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 119 ALENECPNTVSCADALTLAARDSSVLTGGPSWTVPLGRRDsATASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLTDLVAL 198
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRD-GRVSLASDASNLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 199 SGSHTIGFSRCTSFRQRLYNQSGSGS-PDTTLEKSYAAILRQRCPRSGGDQNLSELDINSAGRFDNSYFKNLIENMGLLN 277
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILE 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257632751 278 SDQVLFsSNEQSRELVKKYAEDQE----EFFEQFAESMIKMGKISPLTGSSGEIRKKCRKIN 335
Cdd:PLN03030 264 SDQKLW-TDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
51-299 2.22e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 232.45  E-value: 2.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751   51 VRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGSivtEKNSNPNSRSARGFEVVDEIKAALENECPNTVSC 130
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKP---EKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  131 ADALTLAARDSSVLTGGPSWTVPLGRRDSATASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLTDLVALSGSHTIGFSRct 210
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  211 sfrqrlynqsgsgspdttleksyaailrqrcprsggdqnlseldinsagrfdnsyfKNLIENMGLLNSDQVLFsSNEQSR 290
Cdd:pfam00141 156 --------------------------------------------------------KNLLDGRGLLTSDQALL-SDPRTR 178

                  ....*....
gi 257632751  291 ELVKKYAED 299
Cdd:pfam00141 179 ALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
34-334 1.24e-179

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: 498.58  E-value: 1.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  34 NLFPDFYRSSCPRAEEIVRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGSIVTEKNSNPNsRSARGFEVV 113
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 114 DEIKAALENECPNTVSCADALTLAARDSSVLTGGPSWTVPLGRRDSaTASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLT 193
Cdd:cd00693   80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDG-RVSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 194 DLVALSGSHTIGFSRCTSFRQRLYNQSGSGSPDTTLEKSYAAILRQRCPRSGGDQNLSELDINSAGRFDNSYFKNLIENM 273
Cdd:cd00693  159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGR 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257632751 274 GLLNSDQVLFSSNEqSRELVKKYAEDQEEFFEQFAESMIKMGKISPLTGSSGEIRKKCRKI 334
Cdd:cd00693  239 GLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
39-335 5.65e-84

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 256.81  E-value: 5.65e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  39 FYRSSCPRAEEIVRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGsivTEKNSNPNsRSARGFEVVDEIKA 118
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPN-LLLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 119 ALENECPNTVSCADALTLAARDSSVLTGGPSWTVPLGRRDsATASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLTDLVAL 198
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRD-GRVSLASDASNLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 199 SGSHTIGFSRCTSFRQRLYNQSGSGS-PDTTLEKSYAAILRQRCPRSGGDQNLSELDINSAGRFDNSYFKNLIENMGLLN 277
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGILE 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257632751 278 SDQVLFsSNEQSRELVKKYAEDQE----EFFEQFAESMIKMGKISPLTGSSGEIRKKCRKIN 335
Cdd:PLN03030 264 SDQKLW-TDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
51-299 2.22e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 232.45  E-value: 2.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751   51 VRSVVAKAFERETRMAASLMRLHFHDCFVQGCDGSLLLDTSGSivtEKNSNPNSRSARGFEVVDEIKAALENECPNTVSC 130
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKP---EKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  131 ADALTLAARDSSVLTGGPSWTVPLGRRDSATASRAKPNKDLPEPDNLFDTIFLRFSNEGLNLTDLVALSGSHTIGFSRct 210
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  211 sfrqrlynqsgsgspdttleksyaailrqrcprsggdqnlseldinsagrfdnsyfKNLIENMGLLNSDQVLFsSNEQSR 290
Cdd:pfam00141 156 --------------------------------------------------------KNLLDGRGLLTSDQALL-SDPRTR 178

                  ....*....
gi 257632751  291 ELVKKYAED 299
Cdd:pfam00141 179 ALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
49-316 2.36e-34

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: 126.50  E-value: 2.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  49 EIVRSVVAKAFERETRMAASLMRLHFHDCFVQ--------GCDGSLLLDtsgsivTEKNSNPNSRSARGFEVVDEIKAAL 120
Cdd:cd00314    1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIRFE------PELDRPENGGLDKALRALEPIKSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 121 ENECPntVSCADALTLAA--RDSSVLTGGPSWTVPLGRRDSATASR--AKPNKDLPEPDNLFDTIFLRFSNEGLNLTDLV 196
Cdd:cd00314   75 DGGNP--VSRADLIALAGavAVESTFGGGPLIPFRFGRLDATEPDLgvPDPEGLLPNETSSATELRDKFKRMGLSPSELV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 197 ALS-GSHTI-GFSRCTSFRQRLYNQSgSGSPDTtleksyaailrqrcprsggdqnlseldinsagrFDNSYFKNLIEN-- 272
Cdd:cd00314  153 ALSaGAHTLgGKNHGDLLNYEGSGLW-TSTPFT---------------------------------FDNAYFKNLLDMnw 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 257632751 273 --------------MGLLNSDQVLFSSNEqSRELVKKYAEDQEEFFEQFAESMIKMGK 316
Cdd:cd00314  199 ewrvgspdpdgvkgPGLLPSDYALLSDSE-TRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
43-314 1.92e-26

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: 105.36  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  43 SCPRAEEIVRSVVAKAFErETRMAASLMRLHFH-----DCFVqGCDGSllldtSGSI--VTEKNSNPNSRSARGFEVVDE 115
Cdd:cd00691    8 YAAKDLEAARNDIAKLID-DKNCAPILVRLAWHdsgtyDKET-KTGGS-----NGTIrfDPELNHGANAGLDIARKLLEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 116 IKAalenECPNtVSCADALTLAARDSSVLTGGPswTVP--LGRRDSATASRAKPNKDLPEPDNLFD---TIFLRFsneGL 190
Cdd:cd00691   81 IKK----KYPD-ISYADLWQLAGVVAIEEMGGP--KIPfrPGRVDASDPEECPPEGRLPDASKGADhlrDVFYRM---GF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 191 NLTDLVALSGSHTIGfsRCtsFRQRlynqSGSGSPDTTleksyaailrqrcprsggdqnlSELdinsagRFDNSYFKNLI 270
Cdd:cd00691  151 NDQEIVALSGAHTLG--RC--HKER----SGYDGPWTK----------------------NPL------KFDNSYFKELL 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 257632751 271 ENM------GL--LNSDQVLFsSNEQSRELVKKYAEDQEEFFEQFAESMIKM 314
Cdd:cd00691  195 EEDwklptpGLlmLPTDKALL-EDPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
40-322 2.04e-13

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 68.95  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  40 YRSSCPRAEEIVRSVVAkaferETRMAASLMRLHFHDCFVQGCDGSllldTSGSIVTEKNSNPNSRSAR-GFEVVDEIKA 118
Cdd:PLN02364  12 YKKAVEKCRRKLRGLIA-----EKNCAPIMVRLAWHSAGTFDCQSR----TGGPFGTMRFDAEQAHGANsGIHIALRLLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 119 ALENECPnTVSCADALTLAARDSSVLTGGPSWTVPLGRRDSataSRAKPNKDLPEPDNLFDTIFLRFSNE-GLNLTDLVA 197
Cdd:PLN02364  83 PIREQFP-TISFADFHQLAGVVAVEVTGGPDIPFHPGREDK---PQPPPEGRLPDATKGCDHLRDVFAKQmGLSDKDIVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 198 LSGSHTIGfsRCTSFRQRLynqSGSGSPDTTLeksyaailrqrcprsggdqnlseldinsagrFDNSYFKNLI--ENMGL 275
Cdd:PLN02364 159 LSGAHTLG--RCHKDRSGF---EGAWTSNPLI-------------------------------FDNSYFKELLsgEKEGL 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 257632751 276 LN--SDQVLFsSNEQSRELVKKYAEDQEEFFEQFAESMIKMGKISPLTG 322
Cdd:PLN02364 203 LQlvSDKALL-DDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
PLN02608 PLN02608
L-ascorbate peroxidase
127-331 5.36e-13

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 68.25  E-value: 5.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 127 TVSCADALTLAARDSSVLTGGPSWTVPLGRRDSATASrakPNKDLPE----PDNLFDtIFLRFsneGLNLTDLVALSGSH 202
Cdd:PLN02608  88 KITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACP---EEGRLPDakkgAKHLRD-VFYRM---GLSDKDIVALSGGH 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 203 TIGfsrctsfrqrlynqsgsgspdttleksyaailRQRCPRSGGDQNLSELDInsagRFDNSYFKNLI--ENMGLLN--S 278
Cdd:PLN02608 161 TLG--------------------------------RAHPERSGFDGPWTKEPL----KFDNSYFVELLkgESEGLLKlpT 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 257632751 279 DQVLFSSNEqSRELVKKYAEDQEEFFEQFAESMIKMGKISPLTGSSGEIRKKC 331
Cdd:PLN02608 205 DKALLEDPE-FRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKST 256
PLN02879 PLN02879
L-ascorbate peroxidase
40-317 1.06e-12

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 67.01  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  40 YRSSCPRAEEIVRSVVAkaferETRMAASLMRLHFHDCfvqgcdGSLLLDTS--GSIVTEKNSNPNSRSAR-GFEVVDEI 116
Cdd:PLN02879  13 YKKAVQRCKRKLRGLIA-----EKHCAPIVLRLAWHSA------GTFDVKTKtgGPFGTIRHPQELAHDANnGLDIAVRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 117 KAALENECPnTVSCADALTLAARDSSVLTGGPSWTVPLGRRDSAtasRAKPNKDLPEPDNLFDTIFLRFSNEGLNLTDLV 196
Cdd:PLN02879  82 LDPIKELFP-ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKV---EPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 197 ALSGSHTIGfsRCTSFRQRLynqSGSGSPDTTLeksyaailrqrcprsggdqnlseldinsagrFDNSYFKNLI--ENMG 274
Cdd:PLN02879 158 ALSGGHTLG--RCHKERSGF---EGAWTPNPLI-------------------------------FDNSYFKEILsgEKEG 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 257632751 275 LLN--SDQVLFsSNEQSRELVKKYAEDQEEFFEQFAESMIKMGKI 317
Cdd:PLN02879 202 LLQlpTDKALL-DDPLFLPFVEKYAADEDAFFEDYTEAHLKLSEL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
70-228 4.17e-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: 60.10  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  70 MRLHFHDCFV------------QGCDGSLLLdtSGSIvtEKNSNPNSRSArgfEVVDEIKAALENecpNTVSCADALTLA 137
Cdd:cd00692   42 LRLTFHDAIGfspalaagqfggGGADGSIVL--FDDI--ETAFHANIGLD---EIVEALRPFHQK---HNVSMADFIQFA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 138 ArdsSVLT----GGPSWTVPLGRRDSATASrakPNKDLPEPDNLFDTIFLRFSNEGLNLTDLVALSGSHTIGfsrctsfR 213
Cdd:cd00692  112 G---AVAVsncpGAPRLEFYAGRKDATQPA---PDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVA-------A 178
                        170
                 ....*....|....*.
gi 257632751 214 QRLYNQSGSGSP-DTT 228
Cdd:cd00692  179 QDFVDPSIAGTPfDST 194
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
57-221 6.73e-06

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


Pssm-ID: 173829  Cd Length: 264  Bit Score: 46.69  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751  57 KAFERETRMAASLMRLHFHDCFVQGCD-GSLLLDtsGSIVTEKNSNPNSRSARGFEVVDeikaaLENECPNTVSCADALT 135
Cdd:cd08201   33 CAPGPGRQAAAEWLRTAFHDMATHNVDdGTGGLD--ASIQYELDRPENIGSGFNTTLNF-----FVNFYSPRSSMADLIA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257632751 136 LAARDSSVLTGGPSWTVPLGRRDSATASRAkpnkDLPEPDNLFDTIFLRFSNEGLNLTDLVALSG-SHTIGFSRCTSFRQ 214
Cdd:cd08201  106 MGVVTSVASCGGPVVPFRAGRIDATEAGQA----GVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDFPE 181

                 ....*..
gi 257632751 215 RLYNQSG 221
Cdd:cd08201  182 IVPPGSV 188
 
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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