NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|45685301|gb|AAS75410|]
View 

peroxidase, partial [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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
24-334 9.37e-177

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: 492.41  E-value: 9.37e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  24 LDVGFYDRTCPTAETIVQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDTVGNLTAEKDAPPNNpSLRFFDVVD 103
Cdd:cd00693   2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 104 RAKASLEAQCPGVVSCADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEAlNNLPPPFFNATELADRFASKNLSIED 183
Cdd:cd00693  81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGLTVTD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 184 LVVLSGAHTIGVSHCSGFagptdlngpVDRLYNFSSPDGIDPTLSKAYAFLLKSICPANTSqffPNTTVFMDLITPERFD 263
Cdd:cd00693 160 LVALSGAHTIGRAHCSSF---------SDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGD---DDTLVPLDPGTPNTFD 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45685301 264 NKYYVGLTNNLGLFKSDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQIEVLTGTQGEIRRNCRVI 334
Cdd:cd00693 228 NSYYKNLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
24-334 9.37e-177

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: 492.41  E-value: 9.37e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  24 LDVGFYDRTCPTAETIVQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDTVGNLTAEKDAPPNNpSLRFFDVVD 103
Cdd:cd00693   2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 104 RAKASLEAQCPGVVSCADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEAlNNLPPPFFNATELADRFASKNLSIED 183
Cdd:cd00693  81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGLTVTD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 184 LVVLSGAHTIGVSHCSGFagptdlngpVDRLYNFSSPDGIDPTLSKAYAFLLKSICPANTSqffPNTTVFMDLITPERFD 263
Cdd:cd00693 160 LVALSGAHTIGRAHCSSF---------SDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGD---DDTLVPLDPGTPNTFD 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45685301 264 NKYYVGLTNNLGLFKSDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQIEVLTGTQGEIRRNCRVI 334
Cdd:cd00693 228 NSYYKNLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
9-335 3.13e-95

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 286.47  E-value: 3.13e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301    9 TTVLATTLLSATAACL------DVGFYDRTCPTAETIVQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDtvGN 82
Cdd:PLN03030   4 FIVILFFLLAMMATTLvqgqgtRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID--GS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301   83 LTaEKDAPPNNpSLRFFDVVDRAKASLEAQCPGVVSCADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEAlNNLPP 162
Cdd:PLN03030  82 NT-EKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA-SNLPG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  163 PFFNATELADRFASKNLSIEDLVVLSGAHTIGVSHCSGFAGptdlngpvdRLYNFSSP-DGIDPTLSKAYAFLLKSICPA 241
Cdd:PLN03030 159 FTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRY---------RLYNFTTTgNGADPSIDASFVPQLQALCPQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  242 NTSQffpNTTVFMDLITPERFDNKYYVGLTNNLGLFKSDVALLTNATMKALVDSF--VRSEA--TFRTKFARSMIKMGQI 317
Cdd:PLN03030 230 NGDG---SRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFlgVRGLAglNFNVEFGRSMVKMSNI 306
                        330
                 ....*....|....*...
gi 45685301  318 EVLTGTQGEIRRNCRVIN 335
Cdd:PLN03030 307 GVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
40-197 3.12e-78

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 237.85  E-value: 3.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301    40 VQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDtvgNLTAEKDAPPNNpSLRF-FDVVDRAKASLEAQCPGVVS 118
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNL-GLRKgFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45685301   119 CADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEALNNLPPPFFNATELADRFASKNLSIEDLVVLSGAHTIGVSH 197
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH 155
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
24-334 9.37e-177

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: 492.41  E-value: 9.37e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  24 LDVGFYDRTCPTAETIVQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDTVGNLTAEKDAPPNNpSLRFFDVVD 103
Cdd:cd00693   2 LSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNL-SLRGFDVID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 104 RAKASLEAQCPGVVSCADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEAlNNLPPPFFNATELADRFASKNLSIED 183
Cdd:cd00693  81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDV-GNLPSPFFSVSQLISLFASKGLTVTD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 184 LVVLSGAHTIGVSHCSGFagptdlngpVDRLYNFSSPDGIDPTLSKAYAFLLKSICPANTSqffPNTTVFMDLITPERFD 263
Cdd:cd00693 160 LVALSGAHTIGRAHCSSF---------SDRLYNFSGTGDPDPTLDPAYAAQLRKKCPAGGD---DDTLVPLDPGTPNTFD 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45685301 264 NKYYVGLTNNLGLFKSDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQIEVLTGTQGEIRRNCRVI 334
Cdd:cd00693 228 NSYYKNLLAGRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRVV 298
PLN03030 PLN03030
cationic peroxidase; Provisional
9-335 3.13e-95

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 286.47  E-value: 3.13e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301    9 TTVLATTLLSATAACL------DVGFYDRTCPTAETIVQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDtvGN 82
Cdd:PLN03030   4 FIVILFFLLAMMATTLvqgqgtRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID--GS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301   83 LTaEKDAPPNNpSLRFFDVVDRAKASLEAQCPGVVSCADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEAlNNLPP 162
Cdd:PLN03030  82 NT-EKTALPNL-LLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA-SNLPG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  163 PFFNATELADRFASKNLSIEDLVVLSGAHTIGVSHCSGFAGptdlngpvdRLYNFSSP-DGIDPTLSKAYAFLLKSICPA 241
Cdd:PLN03030 159 FTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRY---------RLYNFTTTgNGADPSIDASFVPQLQALCPQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  242 NTSQffpNTTVFMDLITPERFDNKYYVGLTNNLGLFKSDVALLTNATMKALVDSF--VRSEA--TFRTKFARSMIKMGQI 317
Cdd:PLN03030 230 NGDG---SRRIALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFlgVRGLAglNFNVEFGRSMVKMSNI 306
                        330
                 ....*....|....*...
gi 45685301  318 EVLTGTQGEIRRNCRVIN 335
Cdd:PLN03030 307 GVKTGTNGEIRKVCSAIN 324
peroxidase pfam00141
Peroxidase;
40-197 3.12e-78

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 237.85  E-value: 3.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301    40 VQQTVAAAFRNNSGVAPALIRMHFHDCFVRGCDGSVLIDtvgNLTAEKDAPPNNpSLRF-FDVVDRAKASLEAQCPGVVS 118
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNL-GLRKgFEVIDDIKAKLEAACPGVVS 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45685301   119 CADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTEALNNLPPPFFNATELADRFASKNLSIEDLVVLSGAHTIGVSH 197
Cdd:pfam00141  77 CADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH 155
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
40-316 4.53e-27

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: 107.24  E-value: 4.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  40 VQQTVAAAFRNNSGVAPALIRMHFHDCFVR--------GCDGSVlidtvgNLTAEKDAPPNNPSLRFFDVVDRAKASLEA 111
Cdd:cd00314   3 IKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSI------RFEPELDRPENGGLDKALRALEPIKSAYDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 112 QCPgvVSCADVLAFAARDSVVLSGGLGYQVP--AGRRDGRISND--TEALNNLPPPFFNATELADRFASKNLSIEDLVVL 187
Cdd:cd00314  77 GNP--VSRADLIALAGAVAVESTFGGGPLIPfrFGRLDATEPDLgvPDPEGLLPNETSSATELRDKFKRMGLSPSELVAL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 188 S-GAHTI-GVSHCSGFAGPTdlngpvdrlynfsspdgidptlskayafllksiCPANTSqffpnttvfmdliTPERFDNK 265
Cdd:cd00314 155 SaGAHTLgGKNHGDLLNYEG---------------------------------SGLWTS-------------TPFTFDNA 188
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45685301 266 YYVGLTNN----------------LGLFKSDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQ 316
Cdd:cd00314 189 YFKNLLDMnwewrvgspdpdgvkgPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMVN 255
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
46-314 8.68e-11

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: 61.45  E-value: 8.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  46 AAFRNNSGVAPALIRMHFH-----DCFVR--GCDGSVLIDtvgnltAEKDAPPNNPslrffdvVDRAKASLE---AQCPG 115
Cdd:cd00691  21 AKLIDDKNCAPILVRLAWHdsgtyDKETKtgGSNGTIRFD------PELNHGANAG-------LDIARKLLEpikKKYPD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 116 VvSCADVLAFAARDSVVLSGGlgyqvPA-----GRRDGRISNDTEALNNLPPPFFNATELADRFASKNLSIEDLVVLSGA 190
Cdd:cd00691  88 I-SYADLWQLAGVVAIEEMGG-----PKipfrpGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 191 HTIGVSHC--SGFAGPtdlngpvdrlynfsspdgidptlskayafllksicpaNTSQffpnttvfmdlitPERFDNKYYV 268
Cdd:cd00691 162 HTLGRCHKerSGYDGP-------------------------------------WTKN-------------PLKFDNSYFK 191
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 45685301 269 GL--------TNNLGLFKSDVALLTNATMKALVDSFVRSEATFRTKFARSMIKM 314
Cdd:cd00691 192 ELleedwklpTPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
59-317 6.52e-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: 56.64  E-value: 6.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  59 IRMHFHDC--FVR----------GCDGSVLIdtvgnLTAEKDAPPNNPSLRffDVVDRAKASLEAQCpgvVSCADVLAFA 126
Cdd:cd00692  42 LRLTFHDAigFSPalaagqfgggGADGSIVL-----FDDIETAFHANIGLD--EIVEALRPFHQKHN---VSMADFIQFA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 127 ARDSVVlSGGLGYQVP--AGRRDgrisNDTEALNNL-PPPFFNATELADRFASKNLSIEDLVVLSGAHTIgvshcsgfag 203
Cdd:cd00692 112 GAVAVS-NCPGAPRLEfyAGRKD----ATQPAPDGLvPEPFDSVDKILARFADAGFSPDELVALLAAHSV---------- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 204 ptdlngpvdrlynfSSPDGIDPTLSKAyafllksicPANTsqffpnttvfmdliTPERFDNKYYV----------GLTNN 273
Cdd:cd00692 177 --------------AAQDFVDPSIAGT---------PFDS--------------TPGVFDTQFFIetllkgtafpGSGGN 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 45685301 274 LGL----------FKSDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQI 317
Cdd:cd00692 220 QGEvesplpgefrLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLL 273
PLN02608 PLN02608
L-ascorbate peroxidase
117-357 2.67e-08

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 54.38  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  117 VSCADVLAFAARDSVVLSGGLGYQVPAGRRDgriSNDTEALNNLPPPFFNATELADRFASKNLSIEDLVVLSGAHTIGVS 196
Cdd:PLN02608  89 ITYADLYQLAGVVAVEVTGGPTIDFVPGRKD---SNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  197 HC--SGFAGPTdlngpvdrlynfsspdgidptlskayafllksicpanTSQffpnttvfmdlitPERFDNKYYVGLT--N 272
Cdd:PLN02608 166 HPerSGFDGPW-------------------------------------TKE-------------PLKFDNSYFVELLkgE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  273 NLGLFK--SDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQIEVLTGTQGeirrncrvINPVSATDDVVLARPSG 350
Cdd:PLN02608 196 SEGLLKlpTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSELGFTPPSSA--------FKKKSTSTSTVLAQSAV 267

                 ....*..
gi 45685301  351 FTGVAAS 357
Cdd:PLN02608 268 GVAVAAA 274
PLN02364 PLN02364
L-ascorbate peroxidase 1
55-322 2.78e-05

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 45.07  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301   55 APALIRMHFH-----DCFVR--GCDGSVLIDtvgnltAEKDAPPNNP---SLRFFDvvdrakaSLEAQCPgVVSCADVLA 124
Cdd:PLN02364  33 APIMVRLAWHsagtfDCQSRtgGPFGTMRFD------AEQAHGANSGihiALRLLD-------PIREQFP-TISFADFHQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  125 FAARDSVVLSGGLGYQVPAGRRD-------GRISNDTEALNNLPPPFFNATELADRfasknlsieDLVVLSGAHTIGVSH 197
Cdd:PLN02364  99 LAGVVAVEVTGGPDIPFHPGREDkpqpppeGRLPDATKGCDHLRDVFAKQMGLSDK---------DIVALSGAHTLGRCH 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  198 C--SGFAGPTDLNgpvdrlynfsspdgidptlskayafllksicpantsqffpnttvfmdlitPERFDNKYYVGLTN--N 273
Cdd:PLN02364 170 KdrSGFEGAWTSN--------------------------------------------------PLIFDNSYFKELLSgeK 199
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 45685301  274 LGLFK--SDVALLTNATMKALVDSFVRSEATFRTKFARSMIKMGQIEVLTG 322
Cdd:PLN02364 200 EGLLQlvSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
32-314 1.56e-03

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: 39.76  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301  32 TCPTAETIVQQTVAAAfrnnsgvapALIRMHFHDCFVRGCDgsvliDTVGNLTA----EKDAPPN-----NPSLRFFDVV 102
Cdd:cd08201  28 TPCTDCAPGPGRQAAA---------EWLRTAFHDMATHNVD-----DGTGGLDAsiqyELDRPENigsgfNTTLNFFVNF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 103 DRAKASLeaqcpgvvscADVLAFAARDSVVLSGGLGYQVPAGRRDGRISNDTealnNLPPPFFNATELADRFASKNLSIE 182
Cdd:cd08201  94 YSPRSSM----------ADLIAMGVVTSVASCGGPVVPFRAGRIDATEAGQA----GVPEPQTDLGTTTESFRRQGFSTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45685301 183 DLVVLSG-AHTIGVSHCSGFagptdlngpvdrlynfssPDGIDPTLSkayafllksicPANTSQFFPNTTVFMDLITPEr 261
Cdd:cd08201 160 EMIALVAcGHTLGGVHSEDF------------------PEIVPPGSV-----------PDTVLQFFDTTIQFDNKVVTE- 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45685301 262 fdnkYYVGLTNN-------------LGLFKSDvallTNATMKALVDsfvrsEATFRTKFARSMIKM 314
Cdd:cd08201 210 ----YLSGTTNNplvvgpnnttnsdLRIFSSD----GNVTMNELAS-----PDTFQKTCADILQRM 262
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH