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Conserved domains on  [gi|357480291|ref|XP_003610431|]
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peroxidase 42 [Medicago truncatula]

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 ...
31-326 2.76e-142

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: 404.20  E-value: 2.76e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  31 GLVMNYYKEACPQAEEIIKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTSTRRSLSEQEHDRSFGLRNFRYID 110
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 111 TIKEAVERECPGVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDlLEAYLPDHNESISAVLDKFGAMGIDTPG 190
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSAN-DVGNLPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 191 VVALLGAHSVGRTHCTKLVHRLYP-----EVDPALNPEHIPHMLKKCPDSIPDPkavQYVRNDRGTPMILDNNYYRNILD 265
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNfsgtgDPDPTLDPAYAAQLRKKCPAGGDDD---TLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357480291 266 NKGLLIVDHQLAHDKRTKPYVKKMAKSQEYFFKEFSRAITLLSENNPLTGTKGEIRKQCSV 326
Cdd:cd00693  237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
31-326 2.76e-142

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: 404.20  E-value: 2.76e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  31 GLVMNYYKEACPQAEEIIKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTSTRRSLSEQEHDRSFGLRNFRYID 110
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 111 TIKEAVERECPGVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDlLEAYLPDHNESISAVLDKFGAMGIDTPG 190
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSAN-DVGNLPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 191 VVALLGAHSVGRTHCTKLVHRLYP-----EVDPALNPEHIPHMLKKCPDSIPDPkavQYVRNDRGTPMILDNNYYRNILD 265
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNfsgtgDPDPTLDPAYAAQLRKKCPAGGDDD---TLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357480291 266 NKGLLIVDHQLAHDKRTKPYVKKMAKSQEYFFKEFSRAITLLSENNPLTGTKGEIRKQCSV 326
Cdd:cd00693  237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
peroxidase pfam00141
Peroxidase;
48-292 7.27e-66

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 205.49  E-value: 7.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291   48 IKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTStrrSLSEQEHDRSFGLRN-FRYIDTIKEAVERECPGVVSC 126
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKgFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  127 SDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDLLEAYLPDHNESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHct 206
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  207 klvhrlypevdpalnpehiphmlkkcpdsipdpkavqyvrndrgtpmildnnyyRNILDNKGLLIVDHQLAHDKRTKPYV 286
Cdd:pfam00141 156 ------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALV 181

                  ....*.
gi 357480291  287 KKMAKS 292
Cdd:pfam00141 182 ERYAAD 187
PLN03030 PLN03030
cationic peroxidase; Provisional
15-328 2.31e-59

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 193.64  E-value: 2.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  15 FSPQLFFIVSSAA----EDNGLVMNYYKEACPQAEEIIKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTSTRr 90
Cdd:PLN03030   4 FIVILFFLLAMMAttlvQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  91 slSEQEHDRSFGLRNFRYIDTIKEAVERECPGVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDLLEAyLPDH 170
Cdd:PLN03030  83 --TEKTALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 171 NESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHCTKLVHRLYPEV------DPALNPEHIPHMLKKCPDsipDPKAVQY 244
Cdd:PLN03030 160 TDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTttgngaDPSIDASFVPQLQALCPQ---NGDGSRR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 245 VRNDRGTPMILDNNYYRNILDNKGLLIVDHQLAHDKRTKPYVKKMAKSQEY----FFKEFSRAITLLSENNPLTGTKGEI 320
Cdd:PLN03030 237 IALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEI 316

                 ....*...
gi 357480291 321 RKQCSVSN 328
Cdd:PLN03030 317 RKVCSAIN 324
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
31-326 2.76e-142

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: 404.20  E-value: 2.76e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  31 GLVMNYYKEACPQAEEIIKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTSTRRSLSEQEHDRSFGLRNFRYID 110
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 111 TIKEAVERECPGVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDlLEAYLPDHNESISAVLDKFGAMGIDTPG 190
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSAN-DVGNLPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 191 VVALLGAHSVGRTHCTKLVHRLYP-----EVDPALNPEHIPHMLKKCPDSIPDPkavQYVRNDRGTPMILDNNYYRNILD 265
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNfsgtgDPDPTLDPAYAAQLRKKCPAGGDDD---TLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357480291 266 NKGLLIVDHQLAHDKRTKPYVKKMAKSQEYFFKEFSRAITLLSENNPLTGTKGEIRKQCSV 326
Cdd:cd00693  237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
peroxidase pfam00141
Peroxidase;
48-292 7.27e-66

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 205.49  E-value: 7.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291   48 IKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTStrrSLSEQEHDRSFGLRN-FRYIDTIKEAVERECPGVVSC 126
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLDG---FKPEKDAPPNLGLRKgFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  127 SDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDLLEAYLPDHNESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHct 206
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  207 klvhrlypevdpalnpehiphmlkkcpdsipdpkavqyvrndrgtpmildnnyyRNILDNKGLLIVDHQLAHDKRTKPYV 286
Cdd:pfam00141 156 ------------------------------------------------------KNLLDGRGLLTSDQALLSDPRTRALV 181

                  ....*.
gi 357480291  287 KKMAKS 292
Cdd:pfam00141 182 ERYAAD 187
PLN03030 PLN03030
cationic peroxidase; Provisional
15-328 2.31e-59

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 193.64  E-value: 2.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  15 FSPQLFFIVSSAA----EDNGLVMNYYKEACPQAEEIIKEQVKLLYKRHKNTAFSWLRNIFHDCAVQSCDASLLLTSTRr 90
Cdd:PLN03030   4 FIVILFFLLAMMAttlvQGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILIDGSN- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  91 slSEQEHDRSFGLRNFRYIDTIKEAVERECPGVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDLLEAyLPDH 170
Cdd:PLN03030  83 --TEKTALPNLLLRGYDVIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 171 NESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHCTKLVHRLYPEV------DPALNPEHIPHMLKKCPDsipDPKAVQY 244
Cdd:PLN03030 160 TDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRLYNFTttgngaDPSIDASFVPQLQALCPQ---NGDGSRR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 245 VRNDRGTPMILDNNYYRNILDNKGLLIVDHQLAHDKRTKPYVKKMAKSQEY----FFKEFSRAITLLSENNPLTGTKGEI 320
Cdd:PLN03030 237 IALDTGSSNRFDASFFSNLKNGRGILESDQKLWTDASTRTFVQRFLGVRGLaglnFNVEFGRSMVKMSNIGVKTGTNGEI 316

                 ....*...
gi 357480291 321 RKQCSVSN 328
Cdd:PLN03030 317 RKVCSAIN 324
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
65-303 2.27e-23

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: 96.84  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  65 SWLRNIFHDCAVQS--------CDASLlltstrRSLSEQEHDRSFGL-RNFRYIDTIKEAVERECPgvVSCSDILVLSAR 135
Cdd:cd00314   20 SLLRLAFHDAGTYDiadgkgggADGSI------RFEPELDRPENGGLdKALRALEPIKSAYDGGNP--VSRADLIALAGA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 136 EGIVSL--GGPYIPLKTGRRDGRKSRVDLLEAYLPDHNE--SISAVLDKFGAMGIDTPGVVALL-GAHSV-GRTHCTKLV 209
Cdd:cd00314   92 VAVESTfgGGPLIPFRFGRLDATEPDLGVPDPEGLLPNEtsSATELRDKFKRMGLSPSELVALSaGAHTLgGKNHGDLLN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 210 HRLYPEVDpalnpehiphmlkkcpdsipdpkavqyvrndrGTPMILDNNYYRNILDNK----------------GLLIVD 273
Cdd:cd00314  172 YEGSGLWT--------------------------------STPFTFDNAYFKNLLDMNwewrvgspdpdgvkgpGLLPSD 219
                        250       260       270
                 ....*....|....*....|....*....|
gi 357480291 274 HQLAHDKRTKPYVKKMAKSQEYFFKEFSRA 303
Cdd:cd00314  220 YALLSDSETRALVERYASDQEKFFEDFAKA 249
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
94-310 7.59e-18

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: 81.48  E-value: 7.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  94 EQEHDRSFGLRN-FRYIDTIKEaverECPGVvSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVDLLEAYLPDHNE 172
Cdd:cd00691   62 ELNHGANAGLDIaRKLLEPIKK----KYPDI-SYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 173 SISAVLDKFGAMGIDTPGVVALLGAHSVGRTHctklvhrlypevdpalnPEhiphmlkkcpdsipdpkavqyvRNDRG-- 250
Cdd:cd00691  137 GADHLRDVFYRMGFNDQEIVALSGAHTLGRCH-----------------KE----------------------RSGYDgp 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357480291 251 ---TPMILDNNYYRNILDNK------GLLIV--DHQLAHDKRTKPYVKKMAKSQEYFFKEFSRAITLLSEN 310
Cdd:cd00691  178 wtkNPLKFDNSYFKELLEEDwklptpGLLMLptDKALLEDPKFRPYVELYAKDQDAFFKDYAEAHKKLSEL 248
PLN02364 PLN02364
L-ascorbate peroxidase 1
88-309 4.65e-12

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 65.10  E-value: 4.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  88 TRRSLSEQEHDRSFGLR-NFRYIDTIKEAVErecpgVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVdllEAY 166
Cdd:PLN02364  59 TMRFDAEQAHGANSGIHiALRLLDPIREQFP-----TISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPP---EGR 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 167 LPDHNESISAVLDKFGA-MGIDTPGVVALLGAHSVGRTHctklvhrlypevdpalnpehiphmlkkcpdsiPDPKAVQYV 245
Cdd:PLN02364 131 LPDATKGCDHLRDVFAKqMGLSDKDIVALSGAHTLGRCH--------------------------------KDRSGFEGA 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357480291 246 RNDrgTPMILDNNYYRNIL--DNKGL--LIVDHQLAHDKRTKPYVKKMAKSQEYFFKEFSRAITLLSE 309
Cdd:PLN02364 179 WTS--NPLIFDNSYFKELLsgEKEGLlqLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSE 244
PLN02879 PLN02879
L-ascorbate peroxidase
88-309 1.62e-11

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 63.54  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  88 TRRSLSEQEHDRSFGLR-NFRYIDTIKEAVErecpgVVSCSDILVLSAREGIVSLGGPYIPLKTGRRDGRKSRVdllEAY 166
Cdd:PLN02879  60 TIRHPQELAHDANNGLDiAVRLLDPIKELFP-----ILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPP---EGR 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 167 LPDHNESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHCTKlvhrlypevdpalnpehiphmlkkcpdsipDPKAVQYVR 246
Cdd:PLN02879 132 LPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKER------------------------------SGFEGAWTP 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357480291 247 NdrgtPMILDNNYYRNIL--DNKGLLIV--DHQLAHDKRTKPYVKKMAKSQEYFFKEFSRAITLLSE 309
Cdd:PLN02879 182 N----PLIFDNSYFKEILsgEKEGLLQLptDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSE 244
PLN02608 PLN02608
L-ascorbate peroxidase
137-309 2.55e-10

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 60.55  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 137 GIVSL---GGPYIPLKTGRRDgrkSRVDLLEAYLPDHNESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHctklvhrly 213
Cdd:PLN02608  99 GVVAVevtGGPTIDFVPGRKD---SNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAH--------- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 214 PE---VDPALNPEhiphmlkkcpdsipdpkavqyvrndrgtPMILDNNYYRNIL--DNKGLLIV--DHQLAHDKRTKPYV 286
Cdd:PLN02608 167 PErsgFDGPWTKE----------------------------PLKFDNSYFVELLkgESEGLLKLptDKALLEDPEFRPYV 218
                        170       180
                 ....*....|....*....|...
gi 357480291 287 KKMAKSQEYFFKEFSRAITLLSE 309
Cdd:PLN02608 219 ELYAKDEDAFFRDYAESHKKLSE 241
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
67-314 5.97e-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: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  67 LRNIFHDCAVQS------------CDASLLLTSTRrslseqehdrsfgLRNFRYIDTIKEAVERECPGV----VSCSDIL 130
Cdd:cd00692   42 LRLTFHDAIGFSpalaagqfggggADGSIVLFDDI-------------ETAFHANIGLDEIVEALRPFHqkhnVSMADFI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 131 VLSAREGIVSL-GGPYIPLKTGRRDGRKSRVDLLeayLPDHNESISAVLDKFGAMGIDTPGVVALLGAHSVGRTHctklv 209
Cdd:cd00692  109 QFAGAVAVSNCpGAPRLEFYAGRKDATQPAPDGL---VPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQD----- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 210 hrlypEVDPALnpEHIPHmlkkcpDSIPDPKAVQYVRN--DRGTPMILDNNYYRNILDN-KGL--LIVDHQLAHDKRTKP 284
Cdd:cd00692  181 -----FVDPSI--AGTPF------DSTPGVFDTQFFIEtlLKGTAFPGSGGNQGEVESPlPGEfrLQSDFLLARDPRTAC 247
                        250       260       270
                 ....*....|....*....|....*....|....
gi 357480291 285 YVKKMAKSQEYFFKEFSRAITLLS----ENNPLT 314
Cdd:cd00692  248 EWQSFVNNQAKMNAAFAAAMLKLSllgqDNISLT 281
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
62-262 1.57e-05

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: 45.54  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291  62 TAFSWLRNIFHDCAVQSC-------DASLLLTSTRRSLSEQEHDRSFGlrNFRYIDTIKeaverecpgvVSCSDILVLSA 134
Cdd:cd08201   41 AAAEWLRTAFHDMATHNVddgtgglDASIQYELDRPENIGSGFNTTLN--FFVNFYSPR----------SSMADLIAMGV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357480291 135 REGIVSLGGPYIPLKTGRRDGRKSRvdllEAYLPDHNESISAVLDKFGAMGIDTPGVVALLG-AHSVGRTHCTKlvhrlY 213
Cdd:cd08201  109 VTSVASCGGPVVPFRAGRIDATEAG----QAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSED-----F 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357480291 214 PEVDPalnPEHIPHMLKKCPDSIP--DPKAV-QYVRNDRGTPMILDNNYYRN 262
Cdd:cd08201  180 PEIVP---PGSVPDTVLQFFDTTIqfDNKVVtEYLSGTTNNPLVVGPNNTTN 228
 
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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