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Conserved domains on  [gi|1327848626|ref|NP_001346441|]
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Peroxidase 72 precursor [Zea mays]

Protein Classification

peroxidase( domain architecture ID 10091046)

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

EC:  1.11.1.7
Gene Ontology:  GO:0004601|GO:0006979|GO:0020037
PubMed:  11054546
SCOP:  4001128|3000844

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
36-337 5.99e-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: 497.04  E-value: 5.99e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  36 LLPHFYGHACPQMEAIVGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDadGSGRFVTEKRSNPNKdSLRGFEV 115
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLD--STANNTSEKDAPPNL-SLRGFDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 116 IDEIKAALEHACPHTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLiPAPNDSLPTIIGKFANQGLDI 195
Cdd:cd00693    79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 196 VDLVALSGGHTIGDSRCVSFRQRLYGQNNNGQVDRTLNPAYAAELRGRCPRSGGDQNLFALDLVTQFRFDNQYYHNILAM 275
Cdd:cd00693   158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327848626 276 NGLLSSDEILLTQSReTMDLVHRYAADQGLFFDHFAKSMVKMGNISPLTGSAGEIRHNCRRV 337
Cdd:cd00693   238 RGLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
36-337 5.99e-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: 497.04  E-value: 5.99e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  36 LLPHFYGHACPQMEAIVGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDadGSGRFVTEKRSNPNKdSLRGFEV 115
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLD--STANNTSEKDAPPNL-SLRGFDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 116 IDEIKAALEHACPHTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLiPAPNDSLPTIIGKFANQGLDI 195
Cdd:cd00693    79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 196 VDLVALSGGHTIGDSRCVSFRQRLYGQNNNGQVDRTLNPAYAAELRGRCPRSGGDQNLFALDLVTQFRFDNQYYHNILAM 275
Cdd:cd00693   158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327848626 276 NGLLSSDEILLTQSReTMDLVHRYAADQGLFFDHFAKSMVKMGNISPLTGSAGEIRHNCRRV 337
Cdd:cd00693   238 RGLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
40-338 1.48e-90

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 273.76  E-value: 1.48e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  40 FYGHACPQMEAIVGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDadGSGrfvTEKRSNPNKdSLRGFEVIDEI 119
Cdd:PLN03030   29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID--GSN---TEKTALPNL-LLRGYDVIDDA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 120 KAALEHACPHTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLiPAPNDSLPTIIGKFANQGLDIVDLV 199
Cdd:PLN03030  103 KTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASNL-PGFTDSIDVQKQKFAAKGLNTQDLV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 200 ALSGGHTIGDSRCVSFRQRLYGQNNNGQ-VDRTLNPAYAAELRGRCPRSGGDQNLFALDLVTQFRFDNQYYHNILAMNGL 278
Cdd:PLN03030  182 TLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGI 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327848626 279 LSSDEILLTQSrETMDLVHRYAADQGL----FFDHFAKSMVKMGNISPLTGSAGEIRHNCRRVN 338
Cdd:PLN03030  262 LESDQKLWTDA-STRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
52-302 3.25e-75

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 229.76  E-value: 3.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  52 VGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDAdgsgrFVTEKRSNPNKdSLR-GFEVIDEIKAALEHACPHT 130
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG-----FKPEKDAPPNL-GLRkGFEVIDDIKAKLEAACPGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 131 VSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLIPAPNDSLPTIIGKFANQGLDIVDLVALSGGHTIGDS 210
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 211 RcvsfrqrlygqnnngqvdrtlnpayaaelrgrcprsggdqnlfaldlvtqfrfdnqyyHNILAMNGLLSSDEILLTQSR 290
Cdd:pfam00141 155 H----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|..
gi 1327848626 291 eTMDLVHRYAAD 302
Cdd:pfam00141 177 -TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
36-337 5.99e-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: 497.04  E-value: 5.99e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  36 LLPHFYGHACPQMEAIVGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDadGSGRFVTEKRSNPNKdSLRGFEV 115
Cdd:cd00693     2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLD--STANNTSEKDAPPNL-SLRGFDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 116 IDEIKAALEHACPHTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLiPAPNDSLPTIIGKFANQGLDI 195
Cdd:cd00693    79 IDDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNL-PSPFFSVSQLISLFASKGLTV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 196 VDLVALSGGHTIGDSRCVSFRQRLYGQNNNGQVDRTLNPAYAAELRGRCPRSGGDQNLFALDLVTQFRFDNQYYHNILAM 275
Cdd:cd00693   158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327848626 276 NGLLSSDEILLTQSReTMDLVHRYAADQGLFFDHFAKSMVKMGNISPLTGSAGEIRHNCRRV 337
Cdd:cd00693   238 RGLLTSDQALLSDPR-TRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
40-338 1.48e-90

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 273.76  E-value: 1.48e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  40 FYGHACPQMEAIVGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDadGSGrfvTEKRSNPNKdSLRGFEVIDEI 119
Cdd:PLN03030   29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID--GSN---TEKTALPNL-LLRGYDVIDDA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 120 KAALEHACPHTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLiPAPNDSLPTIIGKFANQGLDIVDLV 199
Cdd:PLN03030  103 KTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASNL-PGFTDSIDVQKQKFAAKGLNTQDLV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 200 ALSGGHTIGDSRCVSFRQRLYGQNNNGQ-VDRTLNPAYAAELRGRCPRSGGDQNLFALDLVTQFRFDNQYYHNILAMNGL 278
Cdd:PLN03030  182 TLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGI 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327848626 279 LSSDEILLTQSrETMDLVHRYAADQGL----FFDHFAKSMVKMGNISPLTGSAGEIRHNCRRVN 338
Cdd:PLN03030  262 LESDQKLWTDA-STRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
52-302 3.25e-75

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 229.76  E-value: 3.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  52 VGSLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDAdgsgrFVTEKRSNPNKdSLR-GFEVIDEIKAALEHACPHT 130
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG-----FKPEKDAPPNL-GLRkGFEVIDDIKAKLEAACPGV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 131 VSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSNNLIPAPNDSLPTIIGKFANQGLDIVDLVALSGGHTIGDS 210
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 211 RcvsfrqrlygqnnngqvdrtlnpayaaelrgrcprsggdqnlfaldlvtqfrfdnqyyHNILAMNGLLSSDEILLTQSR 290
Cdd:pfam00141 155 H----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|..
gi 1327848626 291 eTMDLVHRYAAD 302
Cdd:pfam00141 177 -TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
54-319 3.95e-42

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: 146.91  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  54 SLVAKAHAEDPRMAASLLRMHFHDCFVQGCDASVLLDADGSGRFVTEKRSNPNKDSLRGFEVIDEIKAALEHACPhtVSC 133
Cdd:cd00314     5 AILEDLITQAGALAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDGGNP--VSR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 134 ADIVAVAARDSVVLT--GGPGWEVPLGRRDSLTASLSGSN--NLIPAPNDSLPTIIGKFANQGLDIVDLVALS-GGHTIG 208
Cdd:cd00314    83 ADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGVPDpeGLLPNETSSATELRDKFKRMGLSPSELVALSaGAHTLG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 209 dsrcvsfrqrlygqnnngqvdrtlnpayaaelrGRCPRSGGDQNLFALDLVTQFRFDNQYYHNILAMN------------ 276
Cdd:cd00314   163 ---------------------------------GKNHGDLLNYEGSGLWTSTPFTFDNAYFKNLLDMNwewrvgspdpdg 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1327848626 277 ----GLLSSDEILLTQSrETMDLVHRYAADQGLFFDHFAKSMVKMGN 319
Cdd:cd00314   210 vkgpGLLPSDYALLSDS-ETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
62-317 9.14e-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: 73.01  E-value: 9.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  62 EDPRMAASLLRMHFHDCfvqGC-DASVllDADGSG---RFVTEKRSNPNKDSLRGFEVIDEIKAalEHAcphTVSCADIV 137
Cdd:cd00691    25 DDKNCAPILVRLAWHDS---GTyDKET--KTGGSNgtiRFDPELNHGANAGLDIARKLLEPIKK--KYP---DISYADLW 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 138 AVAARDSVVLTGGPgwEVP--LGRRDSLTASLSGSNNLIP---APNDSLPTIigkFANQGLDIVDLVALSGGHTIGdsRC 212
Cdd:cd00691    95 QLAGVVAIEEMGGP--KIPfrPGRVDASDPEECPPEGRLPdasKGADHLRDV---FYRMGFNDQEIVALSGAHTLG--RC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 213 VSFRQRLYGQNnngqvdrTLNPayaaelrgrcprsggdqnlfaldlvtqFRFDNQYYHNIL------AMNGL--LSSDEI 284
Cdd:cd00691   168 HKERSGYDGPW-------TKNP---------------------------LKFDNSYFKELLeedwklPTPGLlmLPTDKA 213
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1327848626 285 LLTQSrETMDLVHRYAADQGLFFDHFAKSMVKM 317
Cdd:cd00691   214 LLEDP-KFRPYVELYAKDQDAFFKDYAEAHKKL 245
PLN02879 PLN02879
L-ascorbate peroxidase
131-320 1.24e-09

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 58.15  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 131 VSCADIVAVAARDSVVLTGGPgwEVPL--GRRDSLTASLSGSnnlIPAPNDSLPTIIGKFANQGLDIVDLVALSGGHTIG 208
Cdd:PLN02879   92 LSYADFYQLAGVVAVEITGGP--EIPFhpGRLDKVEPPPEGR---LPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 209 dsRCVSFRQRLYGQnnngqvdRTLNPayaaelrgrcprsggdqnlfaldlvtqFRFDNQYYHNILA--MNGLLS--SDEI 284
Cdd:PLN02879  167 --RCHKERSGFEGA-------WTPNP---------------------------LIFDNSYFKEILSgeKEGLLQlpTDKA 210
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1327848626 285 LLTQSReTMDLVHRYAADQGLFFDHFAKSMVKMGNI 320
Cdd:PLN02879  211 LLDDPL-FLPFVEKYAADEDAFFEDYTEAHLKLSEL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
71-213 1.37e-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: 58.56  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  71 LRMHFHDCFV------------QGCDASVLLDADgsgrfvTEKRSNPNKDslrgfevIDEIKAALE-HACPHTVSCADIV 137
Cdd:cd00692    42 LRLTFHDAIGfspalaagqfggGGADGSIVLFDD------IETAFHANIG-------LDEIVEALRpFHQKHNVSMADFI 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848626 138 AVAARDSVV-LTGGPGWEVPLGRRDSLTASlsgSNNLIPAPNDSLPTIIGKFANQGLDIVDLVALSGGHTIGDSRCV 213
Cdd:cd00692   109 QFAGAVAVSnCPGAPRLEFYAGRKDATQPA---PDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQDFV 182
PLN02608 PLN02608
L-ascorbate peroxidase
91-317 9.35e-09

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 55.54  E-value: 9.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  91 ADGSGRFVTEKRSNPNKDSLRGFEVIDEIKAalEHAcphTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGS 170
Cdd:PLN02608   54 PNGSIRNEEEYSHGANNGLKIAIDLCEPVKA--KHP---KITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 171 nnlIPAPNDSLPTIIGKFANQGLDIVDLVALSGGHTIGdsrcvsfrqrlygqnnngqvdrtlnpayaaelRGRCPRSGGD 250
Cdd:PLN02608  129 ---LPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLG--------------------------------RAHPERSGFD 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327848626 251 QNLfaldlvTQ--FRFDNQYYHNILAMN--GL--LSSDEILLtQSRETMDLVHRYAADQGLFFDHFAKSMVKM 317
Cdd:PLN02608  174 GPW------TKepLKFDNSYFVELLKGEseGLlkLPTDKALL-EDPEFRPYVELYAKDEDAFFRDYAESHKKL 239
PLN02364 PLN02364
L-ascorbate peroxidase 1
93-325 1.60e-08

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 54.70  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626  93 GSGRFVTEKRSNPNKDSLRGFEVIDEIKAALEhacphTVSCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGSnn 172
Cdd:PLN02364   58 GTMRFDAEQAHGANSGIHIALRLLDPIREQFP-----TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGR-- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 173 lIPAPNDSLPTIIGKFANQ-GLDIVDLVALSGGHTIGdsRCVSFRQRLYGQnnngqvdRTLNPayaaelrgrcprsggdq 251
Cdd:PLN02364  131 -LPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLG--RCHKDRSGFEGA-------WTSNP----------------- 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848626 252 nlfaldlvtqFRFDNQYYHNILA--MNGLLS--SDEILLTQSrETMDLVHRYAADQGLFFDHFAKSMVKMGNISPLTG 325
Cdd:PLN02364  184 ----------LIFDNSYFKELLSgeKEGLLQlvSDKALLDDP-VFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
132-217 2.94e-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: 50.93  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848626 132 SCADIVAVAARDSVVLTGGPGWEVPLGRRDSLTASLSGsnnlIPAPNDSLPTIIGKFANQGLDIVDLVALSG-GHTIGDS 210
Cdd:cd08201    99 SMADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQAG----VPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGV 174

                  ....*..
gi 1327848626 211 RCVSFRQ 217
Cdd:cd08201   175 HSEDFPE 181
 
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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