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Conserved domains on  [gi|30694586|ref|NP_175380|]
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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 ...
47-348 4.48e-170

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: 475.08  E-value: 4.48e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  47 NLNYRFYDRSCPRLQTIVKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLNDSEDFKGEKNAQPNRnSVRGFEVI 126
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 127 EDIKSDIESSCPLTVSCADIVALAAREAVVLTGGPFWPVPLGRRDSLtASEQAANTNLPSPFEALENITAKFVTLGLDLK 206
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGR-VSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 207 DVVVLSGAHTIGFAQCFVIKHRLFNFKGSGQPDPNLaaSSALLSKLKDTCPNvDSSDSKLAALDAASSVKFDNAYYVNLM 286
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTL--DPAYAAQLRKKCPA-GGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694586 287 NNIGLLDSDQTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIGVMTGSDGVIRGKCGF 348
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
47-348 4.48e-170

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: 475.08  E-value: 4.48e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  47 NLNYRFYDRSCPRLQTIVKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLNDSEDFKGEKNAQPNRnSVRGFEVI 126
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 127 EDIKSDIESSCPLTVSCADIVALAAREAVVLTGGPFWPVPLGRRDSLtASEQAANTNLPSPFEALENITAKFVTLGLDLK 206
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGR-VSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 207 DVVVLSGAHTIGFAQCFVIKHRLFNFKGSGQPDPNLaaSSALLSKLKDTCPNvDSSDSKLAALDAASSVKFDNAYYVNLM 286
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTL--DPAYAAQLRKKCPA-GGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694586 287 NNIGLLDSDQTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIGVMTGSDGVIRGKCGF 348
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
PLN03030 PLN03030
cationic peroxidase; Provisional
52-346 8.57e-91

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 274.91  E-value: 8.57e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   52 FYDRSCPRLQTIVKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLNDSEDfkgEKNAQPNRnSVRGFEVIEDIKS 131
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT---EKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  132 DIESSCPLTVSCADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEQAANtNLPSPFEALENITAKFVTLGLDLKDVVVL 211
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  212 SGAHTIGFAQCFVIKHRLFNFKGSGQ-PDPNLAASsaLLSKLKDTCPNvDSSDSKLAALDAASSVKFDNAYYVNLMNNIG 290
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDAS--FVPQLQALCPQ-NGDGSRRIALDTGSSNRFDASFFSNLKNGRG 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  291 LLDSDQTLMTDPTAAALVKSYSENPYL----FSRDFAVSMVKMGNIGVMTGSDGVIRGKC 346
Cdd:PLN03030 261 ILESDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVC 320
peroxidase pfam00141
Peroxidase;
64-314 1.59e-79

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 240.93  E-value: 1.59e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586    64 VKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLndsEDFKGEKNAQPNRNSVRGFEVIEDIKSDIESSCPLTVSC 143
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLL---DGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   144 ADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEQAANTNLPSPFEALENITAKFVTLGLDLKDVVVLSGAHTIGFAQcf 223
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   224 vikhrlfnfkgsgqpdpnlaassallsklkdtcpnvdssdsklaaldaassvkfdnayyVNLMNNIGLLDSDQTLMTDPT 303
Cdd:pfam00141 156 -----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 30694586   304 AAALVKSYSEN 314
Cdd:pfam00141 177 TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
47-348 4.48e-170

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: 475.08  E-value: 4.48e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  47 NLNYRFYDRSCPRLQTIVKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLNDSEDFKGEKNAQPNRnSVRGFEVI 126
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 127 EDIKSDIESSCPLTVSCADIVALAAREAVVLTGGPFWPVPLGRRDSLtASEQAANTNLPSPFEALENITAKFVTLGLDLK 206
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGR-VSSANDVGNLPSPFFSVSQLISLFASKGLTVT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 207 DVVVLSGAHTIGFAQCFVIKHRLFNFKGSGQPDPNLaaSSALLSKLKDTCPNvDSSDSKLAALDAASSVKFDNAYYVNLM 286
Cdd:cd00693 159 DLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTL--DPAYAAQLRKKCPA-GGDDDTLVPLDPGTPNTFDNSYYKNLL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30694586 287 NNIGLLDSDQTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIGVMTGSDGVIRGKCGF 348
Cdd:cd00693 236 AGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
PLN03030 PLN03030
cationic peroxidase; Provisional
52-346 8.57e-91

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 274.91  E-value: 8.57e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   52 FYDRSCPRLQTIVKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLNDSEDfkgEKNAQPNRnSVRGFEVIEDIKS 131
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSNT---EKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  132 DIESSCPLTVSCADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEQAANtNLPSPFEALENITAKFVTLGLDLKDVVVL 211
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLNTQDLVTL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  212 SGAHTIGFAQCFVIKHRLFNFKGSGQ-PDPNLAASsaLLSKLKDTCPNvDSSDSKLAALDAASSVKFDNAYYVNLMNNIG 290
Cdd:PLN03030 184 VGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDAS--FVPQLQALCPQ-NGDGSRRIALDTGSSNRFDASFFSNLKNGRG 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  291 LLDSDQTLMTDPTAAALVKSYSENPYL----FSRDFAVSMVKMGNIGVMTGSDGVIRGKC 346
Cdd:PLN03030 261 ILESDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEIRKVC 320
peroxidase pfam00141
Peroxidase;
64-314 1.59e-79

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 240.93  E-value: 1.59e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586    64 VKSGVWRAFKDDSRIAASLLRLHFHDCFVNGCDGSILLndsEDFKGEKNAQPNRNSVRGFEVIEDIKSDIESSCPLTVSC 143
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLL---DGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   144 ADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEQAANTNLPSPFEALENITAKFVTLGLDLKDVVVLSGAHTIGFAQcf 223
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   224 vikhrlfnfkgsgqpdpnlaassallsklkdtcpnvdssdsklaaldaassvkfdnayyVNLMNNIGLLDSDQTLMTDPT 303
Cdd:pfam00141 156 -----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 30694586   304 AAALVKSYSEN 314
Cdd:pfam00141 177 TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
64-331 3.12e-37

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: 134.20  E-value: 3.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  64 VKSGVWRAFKDDSRIAASLLRLHFHDCFV--------NGCDGSILLNDsedfkgEKNAQPNRNSVRGFEVIEDIKSDIES 135
Cdd:cd00314   3 IKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRFEP------ELDRPENGGLDKALRALEPIKSAYDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 136 SCPltVSCADIVALAAREAVVLT--GGPFWPVPLGRRDSLTASEQAANT--NLPSPFEALENITAKFVTLGLDLKDVVVL 211
Cdd:cd00314  77 GNP--VSRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDLGVPDPegLLPNETSSATELRDKFKRMGLSPSELVAL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 212 S-GAHTI-GFAQCfvikhRLFNFKGSGQPDPNlaassallsklkdtcPNVdssdsklaaldaassvkFDNAYYVNLMNN- 288
Cdd:cd00314 155 SaGAHTLgGKNHG-----DLLNYEGSGLWTST---------------PFT-----------------FDNAYFKNLLDMn 197
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30694586 289 ---------------IGLLDSDQTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGN 331
Cdd:cd00314 198 wewrvgspdpdgvkgPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
70-334 2.15e-22

Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.


Pssm-ID: 173825 [Multi-domain]  Cd Length: 253  Bit Score: 94.58  E-value: 2.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  70 RAFKDDSRIAASLLRLHFH-----DCFVN--GCDGSIllndseDFKGEKNAQPNRNSVRGFEVIEDIK---SDIesscpl 139
Cdd:cd00691  21 AKLIDDKNCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAGLDIARKLLEPIKkkyPDI------ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 140 tvSCADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEQAANTNLPSPFEALENITAKFVTLGLDLKDVVVLSGAHTIGF 219
Cdd:cd00691  89 --SYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLGR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 220 AqcfvikHRLF-NFKGSGQPDPNlaassallsklkdtcpnvdssdsklaaldaassvKFDNAYYVNLMNNI------GL- 291
Cdd:cd00691 167 C------HKERsGYDGPWTKNPL----------------------------------KFDNSYFKELLEEDwklptpGLl 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 30694586 292 -LDSDQTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIGV 334
Cdd:cd00691 207 mLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSELGV 250
PLN02608 PLN02608
L-ascorbate peroxidase
70-346 9.38e-18

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 82.12  E-value: 9.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586   70 RAFKDDSRIAASLLRLHFHDC-------FVNGCDGSILlNDSEDFKGEKNaqpnrnsvrGFEVIEDIKSDIESSCPlTVS 142
Cdd:PLN02608  22 RALIASKNCAPIMLRLAWHDAgtydaktKTGGPNGSIR-NEEEYSHGANN---------GLKIAIDLCEPVKAKHP-KIT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  143 CADIVALAAREAVVLTGGP---FWPvplGRRDSLTASEQAantNLPSPFEALENITAKFVTLGLDLKDVVVLSGAHTIGF 219
Cdd:PLN02608  91 YADLYQLAGVVAVEVTGGPtidFVP---GRKDSNACPEEG---RLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  220 AQcfviKHRLfNFKGSGQPDPnlaassallsklkdtcpnvdssdsklaaldaassVKFDNAYYVNLM--NNIGLLD--SD 295
Cdd:PLN02608 165 AH----PERS-GFDGPWTKEP----------------------------------LKFDNSYFVELLkgESEGLLKlpTD 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30694586  296 QTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIGVMTGSDGVIRGKC 346
Cdd:PLN02608 206 KALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPSSAFKKKST 256
PLN02364 PLN02364
L-ascorbate peroxidase 1
140-337 1.40e-11

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 63.95  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  140 TVSCADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEQAANTNLPSPFEALENITAKfvTLGLDLKDVVVLSGAHTIGf 219
Cdd:PLN02364  90 TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAK--QMGLSDKDIVALSGAHTLG- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  220 aQCFviKHRlFNFKGSGQPDPNLaassallsklkdtcpnvdssdsklaaldaassvkFDNAYYVNLMN--NIGLLD--SD 295
Cdd:PLN02364 167 -RCH--KDR-SGFEGAWTSNPLI----------------------------------FDNSYFKELLSgeKEGLLQlvSD 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30694586  296 QTLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIGVMTG 337
Cdd:PLN02364 209 KALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
56-334 2.87e-11

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: 63.57  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  56 SCPRLQTIVKSG--VWRAFKDDSR-----------IAASLLRLHFHDCFV------------NGCDGSILLNDSEdfkgE 110
Cdd:cd00692   2 TCPGGQTVCNAAccVWFDILDDIQgnlfnggecgeEAHESLRLTFHDAIGfspalaagqfggGGADGSIVLFDDI----E 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 111 KNAQPNRnsvrGF-EVIEDIKSDIESScplTVSCADIVALAAREAVV-LTGGPFWPVPLGRRDsltASEQAANTNLPSPF 188
Cdd:cd00692  78 TAFHANI----GLdEIVEALRPFHQKH---NVSMADFIQFAGAVAVSnCPGAPRLEFYAGRKD---ATQPAPDGLVPEPF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 189 EALENITAKFVTLGLDLKDVVVLSGAHTIGfAQCFVikhrlfnfkgsgqpDPNLAASSallsklKDTCPNVdssdsklaa 268
Cdd:cd00692 148 DSVDKILARFADAGFSPDELVALLAAHSVA-AQDFV--------------DPSIAGTP------FDSTPGV--------- 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586 269 ldaassvkFDNAYYVNLM----------NNIGL----------LDSDQTLMTDPTAAALVKSYSENPYLFSRDFAVSMVK 328
Cdd:cd00692 198 --------FDTQFFIETLlkgtafpgsgGNQGEvesplpgefrLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLK 269

                ....*.
gi 30694586 329 MGNIGV 334
Cdd:cd00692 270 LSLLGQ 275
PLN02879 PLN02879
L-ascorbate peroxidase
141-333 8.65e-11

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 61.61  E-value: 8.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  141 VSCADIVALAAREAVVLTGGPFWPVPLGRRDSLtasEQAANTNLPSPFEALENITAKFVTLGLDLKDVVVLSGAHTIGfa 220
Cdd:PLN02879  92 LSYADFYQLAGVVAVEITGGPEIPFHPGRLDKV---EPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG-- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  221 QCFviKHRlFNFKGSGQPDPnlaassallsklkdtcpnvdssdsklaaldaassVKFDNAYYVNLMN--NIGLLD--SDQ 296
Cdd:PLN02879 167 RCH--KER-SGFEGAWTPNP----------------------------------LIFDNSYFKEILSgeKEGLLQlpTDK 209
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30694586  297 TLMTDPTAAALVKSYSENPYLFSRDFAVSMVKMGNIG 333
Cdd:PLN02879 210 ALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELG 246
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
71-218 1.09e-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: 52.47  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30694586  71 AFKDDSRIAASLLRLHFHDCF-------VNGCDGSIL--LNDSEDFKGEKNaqpnrNSVRGFEVIEDIKSdiesscpltv 141
Cdd:cd08201  34 APGPGRQAAAEWLRTAFHDMAthnvddgTGGLDASIQyeLDRPENIGSGFN-----TTLNFFVNFYSPRS---------- 98
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30694586 142 SCADIVALAAREAVVLTGGPFWPVPLGRRDSLTASEqaanTNLPSPFEALENITAKFVTLGLDLKDVVVLSG-AHTIG 218
Cdd:cd08201  99 SMADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQ----AGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLG 172
 
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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