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Conserved domains on  [gi|30984554|gb|AAP42740|]
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At2g41480 [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 30984554  29 LKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKS---AEQAALPNLGLRGLEVIDD 105
Cdd:cd00693   2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTAnntSEKDAPPNLSLRGFDVIDD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 106 AKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLV 185
Cdd:cd00693  82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 186 TLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAIL 265
Cdd:cd00693 162 ALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGLL 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30984554 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 30984554  29 LKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKS---AEQAALPNLGLRGLEVIDD 105
Cdd:cd00693   2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTAnntSEKDAPPNLSLRGFDVIDD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 106 AKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLV 185
Cdd:cd00693  82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 186 TLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAIL 265
Cdd:cd00693 162 ALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGLL 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30984554 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 30984554   11 IMIIMLVLVLGKEVRSQLLKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQA 90
Cdd:PLN03030   7 ILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNTEKT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554   91 ALPNLGLRGLEVIDDAKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQ 170
Cdd:PLN03030  87 ALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASNLPGFTDSIDVQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554  171 KQKFQDKGLDTHDLVTLLGAHTIGQTDCLFFRYRLYNFTVTGN-SDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSK 249
Cdd:PLN03030 167 KQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNR 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30984554  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 30984554    45 VRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQAALPNLGLR-GLEVIDDAKARLEAVCPGVVSCADI 123
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVSCADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554   124 LALAARDSVDLSDGPSWRVPTGRKDGRISLATEA-SNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDclffr 202
Cdd:pfam00141  81 LALAARDAVELAGGPSWPVPLGRRDGTVSSAVEAnSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554   203 yrlynftvtgnsdptispsfltqlktlcppngdgskrvaldigspskfdesffKNLRDGNAILESDQRLWSDAETNAVVK 282
Cdd:pfam00141 156 -----------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVE 182

                  ....
gi 30984554   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 30984554  29 LKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKS---AEQAALPNLGLRGLEVIDD 105
Cdd:cd00693   2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTAnntSEKDAPPNLSLRGFDVIDD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 106 AKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQKQKFQDKGLDTHDLV 185
Cdd:cd00693  82 IKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 186 TLLGAHTIGQTDCLFFRYRLYNFTVTGNSDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSKFDESFFKNLRDGNAIL 265
Cdd:cd00693 162 ALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAGRGLL 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30984554 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 30984554   11 IMIIMLVLVLGKEVRSQLLKNGYYSTSCPKAESIVRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQA 90
Cdd:PLN03030   7 ILFFLLAMMATTLVQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNTEKT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554   91 ALPNLGLRGLEVIDDAKARLEAVCPGVVSCADILALAARDSVDLSDGPSWRVPTGRKDGRISLATEASNLPSPLDSVAVQ 170
Cdd:PLN03030  87 ALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASNLPGFTDSIDVQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554  171 KQKFQDKGLDTHDLVTLLGAHTIGQTDCLFFRYRLYNFTVTGN-SDPTISPSFLTQLKTLCPPNGDGSKRVALDIGSPSK 249
Cdd:PLN03030 167 KQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNR 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30984554  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 30984554    45 VRSTVESHFDSDPTISPGLLRLHFHDCFVQGCDGSVLIKGKSAEQAALPNLGLR-GLEVIDDAKARLEAVCPGVVSCADI 123
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDGFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVSCADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554   124 LALAARDSVDLSDGPSWRVPTGRKDGRISLATEA-SNLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDclffr 202
Cdd:pfam00141  81 LALAARDAVELAGGPSWPVPLGRRDGTVSSAVEAnSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554   203 yrlynftvtgnsdptispsfltqlktlcppngdgskrvaldigspskfdesffKNLRDGNAILESDQRLWSDAETNAVVK 282
Cdd:pfam00141 156 -----------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALVE 182

                  ....
gi 30984554   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 30984554  43 SIVRSTVESHFDSDPTISPGLLRLHFHDCFVQ--------GCDGSVLikgKSAEQAALPNLGL-RGLEVIDDAKARLEAV 113
Cdd:cd00314   1 DAIKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIR---FEPELDRPENGGLdKALRALEPIKSAYDGG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 114 CPgvVSCADILALAARDSVDLSDGPS--WRVPTGRKDGRISLATEAS---NLPSPLDSVAVQKQKFQDKGLDTHDLVTLL 188
Cdd:cd00314  78 NP--VSRADLIALAGAVAVESTFGGGplIPFRFGRLDATEPDLGVPDpegLLPNETSSATELRDKFKRMGLSPSELVALS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 189 -GAHTI-GQTDCLFFRYRLYNftvtgnsdptispsfltqlktlcppngdgskrvaLDIGSPSKFDESFFKNLRDGN---- 262
Cdd:cd00314 156 aGAHTLgGKNHGDLLNYEGSG----------------------------------LWTSTPFTFDNAYFKNLLDMNwewr 201
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30984554 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 30984554  64 LRLHFHDCFV------------QGCDGSVLIKGkSAEQAALPNLGLrgLEVIDDAKARLEAvcpGVVSCADILALAArdS 131
Cdd:cd00692  42 LRLTFHDAIGfspalaagqfggGGADGSIVLFD-DIETAFHANIGL--DEIVEALRPFHQK---HNVSMADFIQFAG--A 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 132 VDLSD---GPSWRVPTGRKDgrislATEASN---LPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTDCLffryrl 205
Cdd:cd00692 114 VAVSNcpgAPRLEFYAGRKD-----ATQPAPdglVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQDFV------ 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 206 yNFTVTG---NSDPTI--SPSFL-TQLKTlcpPNGDGSKRVALDIGSPSKfdesffknlrdGNAILESDQRLWSDAETNA 279
Cdd:cd00692 183 -DPSIAGtpfDSTPGVfdTQFFIeTLLKG---TAFPGSGGNQGEVESPLP-----------GEFRLQSDFLLARDPRTAC 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 30984554 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 30984554  61 PGLLRLHFH-----DCFVQ--GCDGSVLIKgksAEQAALPNLGLrgleviDDAKARLEAV---CPGVvSCADILALAARD 130
Cdd:cd00691  31 PILVRLAWHdsgtyDKETKtgGSNGTIRFD---PELNHGANAGL------DIARKLLEPIkkkYPDI-SYADLWQLAGVV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 131 SVDLSDGPS--WRVptGRKDgrISLATEAS---NLPSPLDSVAVQKQKFQDKGLDTHDLVTLLGAHTIGQTdclfFRYRl 205
Cdd:cd00691 101 AIEEMGGPKipFRP--GRVD--ASDPEECPpegRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLGRC----HKER- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30984554 206 ynftvTGnsdptispsFltqlktlcppNGDGSKrvaldigSPSKFDESFFKNLRDGNAILESDQRLW--------SDAET 277
Cdd:cd00691 172 -----SG---------Y----------DGPWTK-------NPLKFDNSYFKELLEEDWKLPTPGLLMlptdkallEDPKF 220
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 30984554 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 30984554  64 LRLHFHDCF-------VQGCDGSVLIKGKSAEqaalpNLGLRGLEVIDDakarLEAVCPGVVSCADILALAARDSVDLSD 136
Cdd:cd08201  46 LRTAFHDMAthnvddgTGGLDASIQYELDRPE-----NIGSGFNTTLNF----FVNFYSPRSSMADLIAMGVVTSVASCG 116
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30984554 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 30984554   60 SPGLLRLHFHDCFVQ-------GCDGSVLIKgksAEQAALPNLGLR-GLEVIDDAKARLEavcpgVVSCADILALAARDS 131
Cdd:PLN02608  31 APIMLRLAWHDAGTYdaktktgGPNGSIRNE---EEYSHGANNGLKiAIDLCEPVKAKHP-----KITYADLYQLAGVVA 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30984554  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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