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Conserved domains on  [gi|1063699078|ref|NP_181679|]
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peroxidase superfamily protein [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 ...
29-327 3.00e-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: 494.73  E-value: 3.00e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  29 LKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKS---AEQAALPNLGLRGLEVIDD 105
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTAnntSEKDAPPNLSLRGFDVIDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 106 AKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLV 185
Cdd:cd00693    82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 186 TLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAIL 265
Cdd:cd00693   162 ALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGLL 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063699078 266 ESDQRLWSDAETNAVVKKYASRlrgllGFRFDYEFGKAMIKMSSIDVKTDVDGEVRKVCSKV 327
Cdd:cd00693   242 TSDQALLSDPRTRAIVNRYAAN-----QDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-327 3.00e-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: 494.73  E-value: 3.00e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  29 LKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKS---AEQAALPNLGLRGLEVIDD 105
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTAnntSEKDAPPNLSLRGFDVIDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 106 AKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLV 185
Cdd:cd00693    82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 186 TLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAIL 265
Cdd:cd00693   162 ALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGLL 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063699078 266 ESDQRLWSDAETNAVVKKYASRlrgllGFRFDYEFGKAMIKMSSIDVKTDVDGEVRKVCSKV 327
Cdd:cd00693   242 TSDQALLSDPRTRAIVNRYAAN-----QDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
11-328 2.52e-173

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 483.31  E-value: 2.52e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  11 IMIIMLVLVLGKEVRSQLLKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQA 90
Cdd:PLN03030    7 ILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNTEKT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  91 ALPNLGLRGLEVIDDAKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQ 170
Cdd:PLN03030   87 ALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASNLPGFTDSIDVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 171 KQKFQDKGLDTHDLVTLLGAHTIGQTDCLFFRYRLYNFTVTGN-SDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSK 249
Cdd:PLN03030  167 KQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNR 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063699078 250 FDESFFKNLRDGNAILESDQRLWSDAETNAVVKKYASrLRGLLGFRFDYEFGKAMIKMSSIDVKTDVDGEVRKVCSKVN 328
Cdd:PLN03030  247 FDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLG-VRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
45-286 2.70e-81

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 244.78  E-value: 2.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  45 VRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQAALPNLGLR-GLEVIDDAKARLEAVCPGVVSCADI 123
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVSCADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 124 LALAARDSVDLSDGPSWRVPTGRKDGRISLATEA-SNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDclffr 202
Cdd:pfam00141  81 LALAARDAVELAGGPSWPVPLGRRDGTVSSAVEAnSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 203 yrlynftvtgnsdptispsfltqlktlcppngdgskrvaldigspskfdesffKNLRDGNAILESDQRLWSDAETNAVVK 282
Cdd:pfam00141 156 -----------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVE 182

                  ....
gi 1063699078 283 KYAS 286
Cdd:pfam00141 183 RYAA 186
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
29-327 3.00e-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: 494.73  E-value: 3.00e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  29 LKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKS---AEQAALPNLGLRGLEVIDD 105
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTAnntSEKDAPPNLSLRGFDVIDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 106 AKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLV 185
Cdd:cd00693    82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 186 TLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAIL 265
Cdd:cd00693   162 ALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGLL 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063699078 266 ESDQRLWSDAETNAVVKKYASRlrgllGFRFDYEFGKAMIKMSSIDVKTDVDGEVRKVCSKV 327
Cdd:cd00693   242 TSDQALLSDPRTRAIVNRYAAN-----QDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
11-328 2.52e-173

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 483.31  E-value: 2.52e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  11 IMIIMLVLVLGKEVRSQLLKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQA 90
Cdd:PLN03030    7 ILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNTEKT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  91 ALPNLGLRGLEVIDDAKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQ 170
Cdd:PLN03030   87 ALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASNLPGFTDSIDVQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 171 KQKFQDKGLDTHDLVTLLGAHTIGQTDCLFFRYRLYNFTVTGN-SDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSK 249
Cdd:PLN03030  167 KQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNR 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063699078 250 FDESFFKNLRDGNAILESDQRLWSDAETNAVVKKYASrLRGLLGFRFDYEFGKAMIKMSSIDVKTDVDGEVRKVCSKVN 328
Cdd:PLN03030  247 FDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLG-VRGLAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
45-286 2.70e-81

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 244.78  E-value: 2.70e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  45 VRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQAALPNLGLR-GLEVIDDAKARLEAVCPGVVSCADI 123
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVSCADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 124 LALAARDSVDLSDGPSWRVPTGRKDGRISLATEA-SNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDclffr 202
Cdd:pfam00141  81 LALAARDAVELAGGPSWPVPLGRRDGTVSSAVEAnSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 203 yrlynftvtgnsdptispsfltqlktlcppngdgskrvaldigspskfdesffKNLRDGNAILESDQRLWSDAETNAVVK 282
Cdd:pfam00141 156 -----------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVE 182

                  ....
gi 1063699078 283 KYAS 286
Cdd:pfam00141 183 RYAA 186
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
43-309 2.37e-35

Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.


Pssm-ID: 173823 [Multi-domain]  Cd Length: 255  Bit Score: 128.81  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  43 SIVRSTVESHFDSDPTISPGLLRLHFHDCFVQ--------GCDGSVLikgKSAEQAALPNLGL-RGLEVIDDAKARLEAV 113
Cdd:cd00314     1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIR---FEPELDRPENGGLdKALRALEPIKSAYDGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 114 CPgvVSCADILALAARDSVDLSDGPS--WRVPTGRKDGRISLATEAS---NLPSPLDSVAVQKQKFQDKGLDTHDLVTLL 188
Cdd:cd00314    78 NP--VSRADLIALAGAVAVESTFGGGplIPFRFGRLDATEPDLGVPDpegLLPNETSSATELRDKFKRMGLSPSELVALS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 189 -GAHTI-GQTDCLFFRYRLYNftvtgnsdptispsfltqlktlcppngdgskrvaLDIGSPSKFDESFFKNLRDGN---- 262
Cdd:cd00314   156 aGAHTLgGKNHGDLLNYEGSG----------------------------------LWTSTPFTFDNAYFKNLLDMNwewr 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063699078 263 ------------AILESDQRLWSDAETNAVVKKYASRlrgllGFRFDYEFGKAMIKMSS 309
Cdd:cd00314   202 vgspdpdgvkgpGLLPSDYALLSDSETRALVERYASD-----QEKFFEDFAKAWIKMVN 255
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
64-327 1.61e-09

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: 58.18  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  64 LRLHFHDCFV------------QGCDGSVLIKGkSAEQAALPNLGLrgLEVIDDAKARLEAvcpGVVSCADILALAArdS 131
Cdd:cd00692    42 LRLTFHDAIGfspalaagqfggGGADGSIVLFD-DIETAFHANIGL--DEIVEALRPFHQK---HNVSMADFIQFAG--A 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 132 VDLSD---GPSWRVPTGRKDgrislATEASN---LPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDCLffryrl 205
Cdd:cd00692   114 VAVSNcpgAPRLEFYAGRKD-----ATQPAPdglVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQDFV------ 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 206 yNFTVTG---NSDPTI--SPSFL-TQLKTlcpPNGDGSKRVALDIGSPSKfdesffknlrdGNAILESDQRLWSDAETNA 279
Cdd:cd00692   183 -DPSIAGtpfDSTPGVfdTQFFIeTLLKG---TAFPGSGGNQGEVESPLP-----------GEFRLQSDFLLARDPRTAC 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063699078 280 VVKKYASRlRGLLGFRFDyefgKAMIKMSSIDVK----TDvdgevrkvCSKV 327
Cdd:cd00692   248 EWQSFVNN-QAKMNAAFA----AAMLKLSLLGQDnislTD--------CSDV 286
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
61-313 9.88e-06

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: 46.04  E-value: 9.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  61 PGLLRLHFH-----DCFVQ--GCDGSVLIKgksAEQAALPNLGLrgleviDDAKARLEAV---CPGVvSCADILALAARD 130
Cdd:cd00691    31 PILVRLAWHdsgtyDKETKtgGSNGTIRFD---PELNHGANAGL------DIARKLLEPIkkkYPDI-SYADLWQLAGVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 131 SVDLSDGPS--WRVptGRKDgrISLATEAS---NLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTdclfFRYRl 205
Cdd:cd00691   101 AIEEMGGPKipFRP--GRVD--ASDPEECPpegRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLGRC----HKER- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078 206 ynftvTGnsdptispsFltqlktlcppNGDGSKrvaldigSPSKFDESFFKNLRDGNAILESDQRLW--------SDAET 277
Cdd:cd00691   172 -----SG---------Y----------DGPWTK-------NPLKFDNSYFKELLEEDWKLPTPGLLMlptdkallEDPKF 220
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1063699078 278 NAVVKKYASRLRgllgfRFDYEFGKAMIKMSSIDVK 313
Cdd:cd00691   221 RPYVELYAKDQD-----AFFKDYAEAHKKLSELGVP 251
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
64-194 6.18e-04

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: 40.91  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  64 LRLHFHDCF-------VQGCDGSVLIKGKSAEqaalpNLGLRGLEVIDDakarLEAVCPGVVSCADILALAARDSVDLSD 136
Cdd:cd08201    46 LRTAFHDMAthnvddgTGGLDASIQYELDRPE-----NIGSGFNTTLNF----FVNFYSPRSSMADLIAMGVVTSVASCG 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063699078 137 GPSWRVPTGRKDgrislATEA--SNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLG-AHTIG 194
Cdd:cd08201   117 GPVVPFRAGRID-----ATEAgqAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLG 172
PLN02608 PLN02608
L-ascorbate peroxidase
60-195 1.54e-03

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 39.75  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699078  60 SPGLLRLHFHDCFVQ-------GCDGSVLIKgksAEQAALPNLGLR-GLEVIDDAKARLEavcpgVVSCADILALAARDS 131
Cdd:PLN02608   31 APIMLRLAWHDAGTYdaktktgGPNGSIRNE---EEYSHGANNGLKiAIDLCEPVKAKHP-----KITYADLYQLAGVVA 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063699078 132 VDLSDGPSWRVPTGRKDGRISlaTEASNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQ 195
Cdd:PLN02608  103 VEVTGGPTIDFVPGRKDSNAC--PEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGR 164
 
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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