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Conserved domains on  [gi|485929919|gb|EOD53169|]
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putative ligninase h2 protein [Neofusicoccum parvum UCRNP2]

Protein Classification

peroxidase( domain architecture ID 396)

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.-
Gene Ontology:  GO:0004601|GO:0006979|GO:0020037
PubMed:  11054546
SCOP:  4001128|3000844

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
plant_peroxidase_like super family cl00196
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
49-326 3.47e-79

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.


The actual alignment was detected with superfamily member cd00692:

Pssm-ID: 444739 [Multi-domain]  Cd Length: 328  Bit Score: 245.00  E-value: 3.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  49 PRKTPACPA---IWTTVSADLTKDFLLNGECTDLARAAIRYAFHDAGTFSTKLPTVAPASGGADGSLLLAPEIDRAE--N 123
Cdd:cd00692    4 PGGQTVCNAaccVWFDILDDIQGNLFNGGECGEEAHESLRLTFHDAIGFSPALAAGQFGGGGADGSIVLFDDIETAFhaN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 124 GGLQDyhsyIGGKYAQYKGR-GVGAADLIQFAGSHAVVTCPGGPTVRTVVGRTDSSAPSPAGVMPpgfGPGSDHDSLLQL 202
Cdd:cd00692   84 IGLDE----IVEALRPFHQKhNVSMADFIQFAGAVAVSNCPGAPRLEFYAGRKDATQPAPDGLVP---EPFDSVDKILAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 203 FVDKGFSAADLAALIGAHTTSRS-FAQRQLPvGTPQDSTPGRWDVKYYGET-----------------YAPPAGVGRFDS 264
Cdd:cd00692  157 FADAGFSPDELVALLAAHSVAAQdFVDPSIA-GTPFDSTPGVFDTQFFIETllkgtafpgsggnqgevESPLPGEFRLQS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485929919 265 DIALSdRTKAVGKEFNGFVNNQGKWVGKFADAMFRLSVLGIPPatyNTFADCTGVLPKATSA 326
Cdd:cd00692  236 DFLLA-RDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQDN---ISLTDCSDVIPPPKPL 293
 
Name Accession Description Interval E-value
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
49-326 3.47e-79

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: 245.00  E-value: 3.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  49 PRKTPACPA---IWTTVSADLTKDFLLNGECTDLARAAIRYAFHDAGTFSTKLPTVAPASGGADGSLLLAPEIDRAE--N 123
Cdd:cd00692    4 PGGQTVCNAaccVWFDILDDIQGNLFNGGECGEEAHESLRLTFHDAIGFSPALAAGQFGGGGADGSIVLFDDIETAFhaN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 124 GGLQDyhsyIGGKYAQYKGR-GVGAADLIQFAGSHAVVTCPGGPTVRTVVGRTDSSAPSPAGVMPpgfGPGSDHDSLLQL 202
Cdd:cd00692   84 IGLDE----IVEALRPFHQKhNVSMADFIQFAGAVAVSNCPGAPRLEFYAGRKDATQPAPDGLVP---EPFDSVDKILAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 203 FVDKGFSAADLAALIGAHTTSRS-FAQRQLPvGTPQDSTPGRWDVKYYGET-----------------YAPPAGVGRFDS 264
Cdd:cd00692  157 FADAGFSPDELVALLAAHSVAAQdFVDPSIA-GTPFDSTPGVFDTQFFIETllkgtafpgsggnqgevESPLPGEFRLQS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485929919 265 DIALSdRTKAVGKEFNGFVNNQGKWVGKFADAMFRLSVLGIPPatyNTFADCTGVLPKATSA 326
Cdd:cd00692  236 DFLLA-RDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQDN---ISLTDCSDVIPPPKPL 293
peroxidase pfam00141
Peroxidase;
78-221 7.33e-23

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 93.78  E-value: 7.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919   78 DLARAAIRYAFHDAGTfstklptvapasGGADGSLLL---APEIDRAENGGLQDYHSYIGG---KYAQYKGRGVGAADLI 151
Cdd:pfam00141  14 TMGPSLLRLHFHDCFV------------GGCDGSVLLdgfKPEKDAPPNLGLRKGFEVIDDikaKLEAACPGVVSCADIL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  152 QFAGSHAVVTCpGGPTVRTVVGRTDSSAPSPAGVMPPGFGPGSDHDSLLQLFVDKGFSAADLAALIGAHT 221
Cdd:pfam00141  82 ALAARDAVELA-GGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHT 150
PLN02608 PLN02608
L-ascorbate peroxidase
84-251 3.79e-15

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 74.80  E-value: 3.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  84 IRYAFHDAGTFSTKLPTvapasGGADGSLLLAPEIDRAENGGLQ---DYHSYIGGKYAQykgrgVGAADLIQFAGSHAV- 159
Cdd:PLN02608  35 LRLAWHDAGTYDAKTKT-----GGPNGSIRNEEEYSHGANNGLKiaiDLCEPVKAKHPK-----ITYADLYQLAGVVAVe 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 160 VTcpGGPTVRTVVGRTDSSAPSPAGVMPPGfGPGSDHdsLLQLFVDKGFSAADLAALIGAHTTSRSFAQRQLPVGtPQDS 239
Cdd:PLN02608 105 VT--GGPTIDFVPGRKDSNACPEEGRLPDA-KKGAKH--LRDVFYRMGLSDKDIVALSGGHTLGRAHPERSGFDG-PWTK 178
                        170
                 ....*....|..
gi 485929919 240 TPGRWDVKYYGE 251
Cdd:PLN02608 179 EPLKFDNSYFVE 190
 
Name Accession Description Interval E-value
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
49-326 3.47e-79

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: 245.00  E-value: 3.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  49 PRKTPACPA---IWTTVSADLTKDFLLNGECTDLARAAIRYAFHDAGTFSTKLPTVAPASGGADGSLLLAPEIDRAE--N 123
Cdd:cd00692    4 PGGQTVCNAaccVWFDILDDIQGNLFNGGECGEEAHESLRLTFHDAIGFSPALAAGQFGGGGADGSIVLFDDIETAFhaN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 124 GGLQDyhsyIGGKYAQYKGR-GVGAADLIQFAGSHAVVTCPGGPTVRTVVGRTDSSAPSPAGVMPpgfGPGSDHDSLLQL 202
Cdd:cd00692   84 IGLDE----IVEALRPFHQKhNVSMADFIQFAGAVAVSNCPGAPRLEFYAGRKDATQPAPDGLVP---EPFDSVDKILAR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 203 FVDKGFSAADLAALIGAHTTSRS-FAQRQLPvGTPQDSTPGRWDVKYYGET-----------------YAPPAGVGRFDS 264
Cdd:cd00692  157 FADAGFSPDELVALLAAHSVAAQdFVDPSIA-GTPFDSTPGVFDTQFFIETllkgtafpgsggnqgevESPLPGEFRLQS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485929919 265 DIALSdRTKAVGKEFNGFVNNQGKWVGKFADAMFRLSVLGIPPatyNTFADCTGVLPKATSA 326
Cdd:cd00692  236 DFLLA-RDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQDN---ISLTDCSDVIPPPKPL 293
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
61-301 7.04e-31

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: 117.25  E-value: 7.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  61 TVSADLTKDFllnGECTDLARAAIRYAFHDAGTFSTklptVAPASGGADGSLLLAPEIDRAENGGLQDYHSYIGGKYAQY 140
Cdd:cd00314    2 AIKAILEDLI---TQAGALAGSLLRLAFHDAGTYDI----ADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 141 KGRG-VGAADLIQFAGSHAVVTCP-GGPTVRTVVGRTDSSAPSPAGVMPPG--FGPGSDHDSLLQLFVDKGFSAADLAAL 216
Cdd:cd00314   75 DGGNpVSRADLIALAGAVAVESTFgGGPLIPFRFGRLDATEPDLGVPDPEGllPNETSSATELRDKFKRMGLSPSELVAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 217 I-GAHT---TSRSFAqRQLPVGTPQDSTPGRWDVKYYGETY-------------APPAGVGRFDSDIALS--DRTKAVGK 277
Cdd:cd00314  155 SaGAHTlggKNHGDL-LNYEGSGLWTSTPFTFDNAYFKNLLdmnwewrvgspdpDGVKGPGLLPSDYALLsdSETRALVE 233
                        250       260
                 ....*....|....*....|....
gi 485929919 278 EFNgfvNNQGKWVGKFADAMFRLS 301
Cdd:cd00314  234 RYA---SDQEKFFEDFAKAWIKMV 254
peroxidase pfam00141
Peroxidase;
78-221 7.33e-23

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 93.78  E-value: 7.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919   78 DLARAAIRYAFHDAGTfstklptvapasGGADGSLLL---APEIDRAENGGLQDYHSYIGG---KYAQYKGRGVGAADLI 151
Cdd:pfam00141  14 TMGPSLLRLHFHDCFV------------GGCDGSVLLdgfKPEKDAPPNLGLRKGFEVIDDikaKLEAACPGVVSCADIL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  152 QFAGSHAVVTCpGGPTVRTVVGRTDSSAPSPAGVMPPGFGPGSDHDSLLQLFVDKGFSAADLAALIGAHT 221
Cdd:pfam00141  82 ALAARDAVELA-GGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHT 150
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
84-308 4.11e-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: 93.42  E-value: 4.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  84 IRYAFHDAGTFSTKLPTvapasGGADGSLLLAPEIDRAENGGLQDYHSYIGGKYAQYkgRGVGAADLIQFAGSHAVVTCp 163
Cdd:cd00691   34 VRLAWHDSGTYDKETKT-----GGSNGTIRFDPELNHGANAGLDIARKLLEPIKKKY--PDISYADLWQLAGVVAIEEM- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 164 GGPTVRTVVGRTDSSAPS---PAGVMPPGfGPGSDHdsLLQLFVDKGFSAADLAALIGAHTTSRSFAQRQlPVGTPQDST 240
Cdd:cd00691  106 GGPKIPFRPGRVDASDPEecpPEGRLPDA-SKGADH--LRDVFYRMGFNDQEIVALSGAHTLGRCHKERS-GYDGPWTKN 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485929919 241 PGRWDVKYY-----GETYAPPAGVGRFDSDIAL-SDrtkavgKEFNGFV----NNQGKWVGKFADAMFRLSVLGIPPA 308
Cdd:cd00691  182 PLKFDNSYFkelleEDWKLPTPGLLMLPTDKALlED------PKFRPYVelyaKDQDAFFKDYAEAHKKLSELGVPFP 253
PLN02608 PLN02608
L-ascorbate peroxidase
84-251 3.79e-15

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 74.80  E-value: 3.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  84 IRYAFHDAGTFSTKLPTvapasGGADGSLLLAPEIDRAENGGLQ---DYHSYIGGKYAQykgrgVGAADLIQFAGSHAV- 159
Cdd:PLN02608  35 LRLAWHDAGTYDAKTKT-----GGPNGSIRNEEEYSHGANNGLKiaiDLCEPVKAKHPK-----ITYADLYQLAGVVAVe 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 160 VTcpGGPTVRTVVGRTDSSAPSPAGVMPPGfGPGSDHdsLLQLFVDKGFSAADLAALIGAHTTSRSFAQRQLPVGtPQDS 239
Cdd:PLN02608 105 VT--GGPTIDFVPGRKDSNACPEEGRLPDA-KKGAKH--LRDVFYRMGLSDKDIVALSGGHTLGRAHPERSGFDG-PWTK 178
                        170
                 ....*....|..
gi 485929919 240 TPGRWDVKYYGE 251
Cdd:PLN02608 179 EPLKFDNSYFVE 190
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
148-306 3.91e-13

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: 68.69  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 148 ADLIQFAGSHAVVTCpGGPTVRTVVGRTDS--SAPSPAGVMPPgfgPGSDHDSLLQLFVDKGFSAADLAALIGAHT--TS 223
Cdd:cd00693   97 ADILALAARDAVVLA-GGPSYEVPLGRRDGrvSSANDVGNLPS---PFFSVSQLISLFASKGLTVTDLVALSGAHTigRA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 224 R--SFAQR--------------------QL----PVGTPQD-------STPGRWDVKYYGETyapPAGVGRFDSDIAL-- 268
Cdd:cd00693  173 HcsSFSDRlynfsgtgdpdptldpayaaQLrkkcPAGGDDDtlvpldpGTPNTFDNSYYKNL---LAGRGLLTSDQALls 249
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 485929919 269 SDRTKA-VgkefNGFVNNQGKWVGKFADAMFRLSVLGIP 306
Cdd:cd00693  250 DPRTRAiV----NRYAANQDAFFRDFAAAMVKMGNIGVL 284
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
84-221 2.13e-12

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: 66.34  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  84 IRYAFHDAGTFStklptVAPASGGADGSLllAPEIDRAENGGLQdyHSYIGGKYAQYKGRGVGAADLIQFAGSHAVVTCp 163
Cdd:cd08201   46 LRTAFHDMATHN-----VDDGTGGLDASI--QYELDRPENIGSG--FNTTLNFFVNFYSPRSSMADLIAMGVVTSVASC- 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 485929919 164 GGPTVRTVVGRTDSSAPSPAGVmPPgfgPGSDHDSLLQLFVDKGFSAADLAALIG-AHT 221
Cdd:cd08201  116 GGPVVPFRAGRIDATEAGQAGV-PE---PQTDLGTTTESFRRQGFSTSEMIALVAcGHT 170
PLN02364 PLN02364
L-ascorbate peroxidase 1
84-304 9.70e-10

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 58.17  E-value: 9.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  84 IRYAFHDAGTFSTKLPTvapasGGADGSLLLAPEIDRAENGGLQDYHSYIGGKYAQYKGrgVGAADLIQFAGSHAVvTCP 163
Cdd:PLN02364  37 VRLAWHSAGTFDCQSRT-----GGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFPT--ISFADFHQLAGVVAV-EVT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 164 GGPTVRTVVGRTDSSAPSPAGVMPPGfGPGSDHdsLLQLFVDK-GFSAADLAALIGAHTTSRSFAQRQLPVGTpQDSTPG 242
Cdd:PLN02364 109 GGPDIPFHPGREDKPQPPPEGRLPDA-TKGCDH--LRDVFAKQmGLSDKDIVALSGAHTLGRCHKDRSGFEGA-WTSNPL 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485929919 243 RWDVKYYGETYA-PPAGVGRFDSDIALSDrTKAVGKEFNGFVNNQGKWVGKFADAMFRLSVLG 304
Cdd:PLN02364 185 IFDNSYFKELLSgEKEGLLQLVSDKALLD-DPVFRPLVEKYAADEDAFFADYAEAHMKLSELG 246
PLN02879 PLN02879
L-ascorbate peroxidase
80-304 3.70e-09

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 56.61  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919  80 ARAAIRYAFHDAGTFSTKLPTvapasGGADGSLLLAPEIDRAENGGLQDYHSYIGGKYAQYKGrgVGAADLIQFAGSHAV 159
Cdd:PLN02879  34 APIVLRLAWHSAGTFDVKTKT-----GGPFGTIRHPQELAHDANNGLDIAVRLLDPIKELFPI--LSYADFYQLAGVVAV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 160 vTCPGGPTVRTVVGRTDSSAPSPAGVMPPGfGPGSDHdsLLQLFVDKGFSAADLAALIGAHTTSRSFAQRQLPVGTpQDS 239
Cdd:PLN02879 107 -EITGGPEIPFHPGRLDKVEPPPEGRLPQA-TKGVDH--LRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGA-WTP 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 240 TPGRWDVKYYGETYA-PPAGVGRFDSDIALSDRTKavgkeFNGFVN----NQGKWVGKFADAMFRLSVLG 304
Cdd:PLN02879 182 NPLIFDNSYFKEILSgEKEGLLQLPTDKALLDDPL-----FLPFVEkyaaDEDAFFEDYTEAHLKLSELG 246
PLN03030 PLN03030
cationic peroxidase; Provisional
145-228 1.96e-03

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 39.56  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929919 145 VGAADLIQFAGSHAVVTCpGGPTVRTVVGRTDS--SAPSPAGVMPpgfGPGSDHDSLLQLFVDKGFSAADLAALIGAHTT 222
Cdd:PLN03030 114 VSCADILALAARDSVVLT-NGLTWPVPTGRRDGrvSLASDASNLP---GFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTI 189

                 ....*.
gi 485929919 223 SRSFAQ 228
Cdd:PLN03030 190 GTTACQ 195
 
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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