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Conserved domains on  [gi|21730325|pdb|1H5L|A]
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Chain A, PEROXIDASE C1A

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 ...
1-304 1.39e-174

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: 484.71  E-value: 1.39e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        1 QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNaNSARGFPVI 80
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       81 DRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANaNLPAPFFTLPQLKDSFRNVGLNrS 160
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGLT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A      161 SDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQ 240
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1H5L_A      241 KGLIQSDQELFSSPnatDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVV 304
Cdd:cd00693 238 RGLLTSDQALLSDP---RTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
1-304 1.39e-174

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: 484.71  E-value: 1.39e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        1 QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNaNSARGFPVI 80
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       81 DRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANaNLPAPFFTLPQLKDSFRNVGLNrS 160
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGLT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A      161 SDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQ 240
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1H5L_A      241 KGLIQSDQELFSSPnatDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVV 304
Cdd:cd00693 238 RGLLTSDQALLSDP---RTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
6-305 1.04e-79

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 244.87  E-value: 1.04e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A         6 FYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTsfrTEKDAFGNAnSARGFPVIDRMKA 85
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        86 AVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANaNLPAPFFTLPQLKDSFRNVGLNrSSDLVA 165
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLN-TQDLVT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       166 LSGGHTFGKNQCRFIMDRLYNFSNTGL-PDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLI 244
Cdd:PLN03030 183 LVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGIL 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1H5L_A       245 QSDQELFSSpnaTDTIPLVRSFAN----STQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVN 305
Cdd:PLN03030 263 ESDQKLWTD---ASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
18-269 8.00e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 230.14  E-value: 8.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A         18 VRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNttsFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSC 97
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A         98 ADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNrSSDLVALSGGHTFGKNQc 177
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLT-AEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        178 rfimdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyVNLEEQKGLIQSDQELFSSPnat 257
Cdd:pfam00141 156 ---------------------------------------------------------KNLLDGRGLLTSDQALLSDP--- 175
                         250
                  ....*....|..
1H5L_A        258 DTIPLVRSFANS 269
Cdd:pfam00141 176 RTRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
1-304 1.39e-174

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: 484.71  E-value: 1.39e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        1 QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNaNSARGFPVI 80
Cdd:cd00693   1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPN-LSLRGFDVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       81 DRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANaNLPAPFFTLPQLKDSFRNVGLNrS 160
Cdd:cd00693  80 DDIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGLT-V 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A      161 SDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQ 240
Cdd:cd00693 158 TDLVALSGAHTIGRAHCSSFSDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGDDDTLVPLDPGTPNTFDNSYYKNLLAG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1H5L_A      241 KGLIQSDQELFSSPnatDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVV 304
Cdd:cd00693 238 RGLLTSDQALLSDP---RTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
6-305 1.04e-79

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 244.87  E-value: 1.04e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A         6 FYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTsfrTEKDAFGNAnSARGFPVIDRMKA 85
Cdd:PLN03030  29 FYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN---TEKTALPNL-LLRGYDVIDDAKT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        86 AVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANaNLPAPFFTLPQLKDSFRNVGLNrSSDLVA 165
Cdd:PLN03030 105 QLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDAS-NLPGFTDSIDVQKQKFAAKGLN-TQDLVT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       166 LSGGHTFGKNQCRFIMDRLYNFSNTGL-PDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLI 244
Cdd:PLN03030 183 LVGGHTIGTTACQFFRYRLYNFTTTGNgADPSIDASFVPQLQALCPQNGDGSRRIALDTGSSNRFDASFFSNLKNGRGIL 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1H5L_A       245 QSDQELFSSpnaTDTIPLVRSFAN----STQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVN 305
Cdd:PLN03030 263 ESDQKLWTD---ASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
18-269 8.00e-76

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 230.14  E-value: 8.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A         18 VRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNttsFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSC 97
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A         98 ADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNrSSDLVALSGGHTFGKNQc 177
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLT-AEDLVALSGAHTIGRAH- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        178 rfimdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyVNLEEQKGLIQSDQELFSSPnat 257
Cdd:pfam00141 156 ---------------------------------------------------------KNLLDGRGLLTSDQALLSDP--- 175
                         250
                  ....*....|..
1H5L_A        258 DTIPLVRSFANS 269
Cdd:pfam00141 176 RTRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
18-286 9.76e-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: 131.89  E-value: 9.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       18 VRDTIVNELRSDPRIAASILRLHFHDCFV--------NGCDASILLDNttsfrtEKDAFGNANSARGFPVIDRMKAAVES 89
Cdd:cd00314   3 IKAILEDLITQAGALAGSLLRLAFHDAGTydiadgkgGGADGSIRFEP------ELDRPENGGLDKALRALEPIKSAYDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       90 ACPrtVSCADLLTIAAQQSV--TLAGGPSWRVPLGRRDSLQAFLDLAN--ANLPAPFFTLPQLKDSFRNVGLNrSSDLVA 165
Cdd:cd00314  77 GNP--VSRADLIALAGAVAVesTFGGGPLIPFRFGRLDATEPDLGVPDpeGLLPNETSSATELRDKFKRMGLS-PSELVA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A      166 LS-GGHTF-GKNQCRFimdrlynfsntglpdptlnttylqtlrglcplngNLSALVDFDLRTPTIFDNKYYVNL------ 237
Cdd:cd00314 154 LSaGAHTLgGKNHGDL----------------------------------LNYEGSGLWTSTPFTFDNAYFKNLldmnwe 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
1H5L_A      238 ----------EEQKGLIQSDQELFSSPnatDTIPLVRSFANSTQTFFNAFVEAMDRMGN 286
Cdd:cd00314 200 wrvgspdpdgVKGPGLLPSDYALLSDS---ETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
24-280 4.05e-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: 73.39  E-value: 4.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       24 NELRS---DPRIAASILRLHFH-----DCFVN--GCDASIlldnttSFRTEKDAFGNA--NSARGF--PVIDRMkaaves 89
Cdd:cd00691  18 NDIAKlidDKNCAPILVRLAWHdsgtyDKETKtgGSNGTI------RFDPELNHGANAglDIARKLlePIKKKY------ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       90 acPRtVSCADLLTIAAQQSVTLAGGPS--WRvpLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNrSSDLVALS 167
Cdd:cd00691  86 --PD-ISYADLWQLAGVVAIEEMGGPKipFR--PGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFN-DQEIVALS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A      168 GGHTFGKnqCRfimdrlYNFSNTGLPdptlNTtylqtlrglcplngnlsalvdfdlRTPTIFDNKYYVNLEEQK------ 241
Cdd:cd00691 160 GAHTLGR--CH------KERSGYDGP----WT------------------------KNPLKFDNSYFKELLEEDwklptp 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
1H5L_A      242 GLIQ--SDQELFSSPnatDTIPLVRSFANSTQTFFNAFVEA 280
Cdd:cd00691 204 GLLMlpTDKALLEDP---KFRPYVELYAKDQDAFFKDYAEA 241
PLN02608 PLN02608
L-ascorbate peroxidase
33-280 4.34e-09

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 56.31  E-value: 4.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        33 AASILRLHFHDC-------FVNGCDASIlldnttsfRTEKDAFGNANSarGFPVIDRMKAAVESACPRtVSCADLLTIAA 105
Cdd:PLN02608  31 APIMLRLAWHDAgtydaktKTGGPNGSI--------RNEEEYSHGANN--GLKIAIDLCEPVKAKHPK-ITYADLYQLAG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       106 QQSVTLAGGPSWRVPLGRRDSLQAFLD--LANANLPAPfftlpQLKDSFRNVGLNrSSDLVALSGGHTFGKNQcrfiMDR 183
Cdd:PLN02608 100 VVAVEVTGGPTIDFVPGRKDSNACPEEgrLPDAKKGAK-----HLRDVFYRMGLS-DKDIVALSGGHTLGRAH----PER 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       184 lynfsnTGLPDPTlnttylqtlrglcplngnlsalvdfdLRTPTIFDNKYYVNL--EEQKGLIQ--SDQELFSSPnatDT 259
Cdd:PLN02608 170 ------SGFDGPW--------------------------TKEPLKFDNSYFVELlkGESEGLLKlpTDKALLEDP---EF 214
                        250       260
                 ....*....|....*....|.
1H5L_A       260 IPLVRSFANSTQTFFNAFVEA 280
Cdd:PLN02608 215 RPYVELYAKDEDAFFRDYAES 235
PLN02879 PLN02879
L-ascorbate peroxidase
76-280 6.23e-09

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 55.84  E-value: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        76 GFPVIDRMKAAVESACPrTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQafldlananlPAPFFTLPQ-------L 148
Cdd:PLN02879  74 GLDIAVRLLDPIKELFP-ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVE----------PPPEGRLPQatkgvdhL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       149 KDSFRNVGLNrSSDLVALSGGHTFGKnqcrfimdrlynfsntglpdptlnttylqtlrglcpLNGNLSALVDFDLRTPTI 228
Cdd:PLN02879 143 RDVFGRMGLN-DKDIVALSGGHTLGR------------------------------------CHKERSGFEGAWTPNPLI 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
1H5L_A       229 FDNKYYVNL--EEQKGLIQ--SDQELFSSPNATdtiPLVRSFANSTQTFFNAFVEA 280
Cdd:PLN02879 186 FDNSYFKEIlsGEKEGLLQlpTDKALLDDPLFL---PFVEKYAADEDAFFEDYTEA 238
PLN02364 PLN02364
L-ascorbate peroxidase 1
60-292 3.94e-08

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 53.16  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A        60 SFRTEKDAFGNANSarGFPVIDRMKAAVESACPrTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQafldlananlP 139
Cdd:PLN02364  59 TMRFDAEQAHGANS--GIHIALRLLDPIREQFP-TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQ----------P 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       140 APFFTLP-------QLKDSF-RNVGLNrSSDLVALSGGHTFGKnqCRfiMDRlynfsntglpdptlnttylQTLRGLCPL 211
Cdd:PLN02364 126 PPEGRLPdatkgcdHLRDVFaKQMGLS-DKDIVALSGAHTLGR--CH--KDR-------------------SGFEGAWTS 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       212 NgnlsalvdfdlrtPTIFDNKYYVNL--EEQKGLIQ--SDQELFSSPNATdtiPLVRSFANSTQTFFNAFVEAMDRMGNI 287
Cdd:PLN02364 182 N-------------PLIFDNSYFKELlsGEKEGLLQlvSDKALLDDPVFR---PLVEKYAADEDAFFADYAEAHMKLSEL 245

                 ....*
1H5L_A       288 TPLTG 292
Cdd:PLN02364 246 GFADA 250
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
32-173 3.15e-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: 41.68  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A       32 IAASILRLHFHDCF-------VNGCDASILLDNTtsfRTEKDAFGNANSARGFpvidrmkaaVESACPRTvSCADLLTIA 104
Cdd:cd08201  41 AAAEWLRTAFHDMAthnvddgTGGLDASIQYELD---RPENIGSGFNTTLNFF---------VNFYSPRS-SMADLIAMG 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1H5L_A      105 AQQSVTLAGGPSWRVPLGRRDSLQAfldlANANLPAPFFTLPQLKDSFRNVGLNrSSDLVALSG-GHTFG 173
Cdd:cd08201 108 VVTSVASCGGPVVPFRAGRIDATEA----GQAGVPEPQTDLGTTTESFRRQGFS-TSEMIALVAcGHTLG 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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