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Conserved domains on  [gi|670357929|ref|XP_008673305|]
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uncharacterized protein LOC100191905 isoform X1 [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
SCOP:  4001128|3000844

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 ...
27-327 1.15e-175

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: 488.18  E-value: 1.15e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  27 QLQVGFYDTLCPAAEIIVQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDSSAGNQAEKDAAPNASLRGFEVID 106
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 107 SAKTRLEQACFGVVSCADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAGaNLPPPTASASQLTQAFGAKGLSQAE 186
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 187 MVALSGAHTVGAARCSSFAPRLYSYGPSGaGQDPSMDPAYLAALAQQCPPqgTGAADPPLPMDPVTPTAFDTNYYANLVA 266
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNFSGTG-DPDPTLDPAYAAQLRKKCPA--GGDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670357929 267 RRGLLASDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMGAIQVLTGTAGTVRTNCRV 327
Cdd:cd00693  237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
27-327 1.15e-175

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: 488.18  E-value: 1.15e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  27 QLQVGFYDTLCPAAEIIVQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDSSAGNQAEKDAAPNASLRGFEVID 106
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 107 SAKTRLEQACFGVVSCADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAGaNLPPPTASASQLTQAFGAKGLSQAE 186
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 187 MVALSGAHTVGAARCSSFAPRLYSYGPSGaGQDPSMDPAYLAALAQQCPPqgTGAADPPLPMDPVTPTAFDTNYYANLVA 266
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNFSGTG-DPDPTLDPAYAAQLRKKCPA--GGDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670357929 267 RRGLLASDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMGAIQVLTGTAGTVRTNCRV 327
Cdd:cd00693  237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
PLN03030 PLN03030
cationic peroxidase; Provisional
24-325 1.67e-92

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 278.38  E-value: 1.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  24 RAQQLQVGFYDTLCPAAEIIVQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDssaGNQAEKDAAPNASLRGFE 103
Cdd:PLN03030  21 QGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID---GSNTEKTALPNLLLRGYD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 104 VIDSAKTRLEQACFGVVSCADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAgANLPPPTASASQLTQAFGAKGLS 183
Cdd:PLN03030  98 VIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQKFAAKGLN 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 184 QAEMVALSGAHTVGAARCSSFAPRLYSYGPSGAGQDPSMDPAYLAALAQQCPPQGTGAADppLPMDPVTPTAFDTNYYAN 263
Cdd:PLN03030 177 TQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNGADPSIDASFVPQLQALCPQNGDGSRR--IALDTGSSNRFDASFFSN 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670357929 264 LVARRGLLASDQALLADPATAAQVLAYTN----SPATFQTDFVAAMIKMGAIQVLTGTAGTVRTNC 325
Cdd:PLN03030 255 LKNGRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVC 320
peroxidase pfam00141
Peroxidase;
44-293 1.47e-75

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 230.14  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929   44 VQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDssaGNQAEKDAAPNASLR-GFEVIDSAKTRLEQACFGVVSC 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  123 ADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAGANLPPPTASASQLTQAFGAKGLSQAEMVALSGAHTVGAARcs 202
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  203 sfaprlysygpsgagqdpsmdpaylaalaqqcppqgtgaadpplpmdpvtptafdtnyyANLVARRGLLASDQALLADPA 282
Cdd:pfam00141 156 -----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 670357929  283 TAAQVLAYTNS 293
Cdd:pfam00141 177 TRALVERYAAD 187
 
Name Accession Description Interval E-value
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
27-327 1.15e-175

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: 488.18  E-value: 1.15e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  27 QLQVGFYDTLCPAAEIIVQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDSSAGNQAEKDAAPNASLRGFEVID 106
Cdd:cd00693    1 QLSVGFYSKSCPNAESIVRSVVRAAVKADPRLAAALLRLHFHDCFVRGCDASVLLDSTANNTSEKDAPPNLSLRGFDVID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 107 SAKTRLEQACFGVVSCADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAGaNLPPPTASASQLTQAFGAKGLSQAE 186
Cdd:cd00693   81 DIKAALEAACPGVVSCADILALAARDAVVLAGGPSYEVPLGRRDGRVSSANDVG-NLPSPFFSVSQLISLFASKGLTVTD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 187 MVALSGAHTVGAARCSSFAPRLYSYGPSGaGQDPSMDPAYLAALAQQCPPqgTGAADPPLPMDPVTPTAFDTNYYANLVA 266
Cdd:cd00693  160 LVALSGAHTIGRAHCSSFSDRLYNFSGTG-DPDPTLDPAYAAQLRKKCPA--GGDDDTLVPLDPGTPNTFDNSYYKNLLA 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670357929 267 RRGLLASDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMGAIQVLTGTAGTVRTNCRV 327
Cdd:cd00693  237 GRGLLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIGVLTGSQGEIRKNCRV 297
PLN03030 PLN03030
cationic peroxidase; Provisional
24-325 1.67e-92

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 278.38  E-value: 1.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  24 RAQQLQVGFYDTLCPAAEIIVQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDssaGNQAEKDAAPNASLRGFE 103
Cdd:PLN03030  21 QGQGTRVGFYSTTCPQAESIVRKTVQSHFQSNPAIAPGLLRMHFHDCFVRGCDASILID---GSNTEKTALPNLLLRGYD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 104 VIDSAKTRLEQACFGVVSCADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAgANLPPPTASASQLTQAFGAKGLS 183
Cdd:PLN03030  98 VIDDAKTQLEAACPGVVSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDA-SNLPGFTDSIDVQKQKFAAKGLN 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 184 QAEMVALSGAHTVGAARCSSFAPRLYSYGPSGAGQDPSMDPAYLAALAQQCPPQGTGAADppLPMDPVTPTAFDTNYYAN 263
Cdd:PLN03030 177 TQDLVTLVGGHTIGTTACQFFRYRLYNFTTTGNGADPSIDASFVPQLQALCPQNGDGSRR--IALDTGSSNRFDASFFSN 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670357929 264 LVARRGLLASDQALLADPATAAQVLAYTN----SPATFQTDFVAAMIKMGAIQVLTGTAGTVRTNC 325
Cdd:PLN03030 255 LKNGRGILESDQKLWTDASTRTFVQRFLGvrglAGLNFNVEFGRSMVKMSNIGVKTGTNGEIRKVC 320
peroxidase pfam00141
Peroxidase;
44-293 1.47e-75

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 230.14  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929   44 VQEEVSKAASGNPGVAAGLLRLHFHDCFVRGCDASVLLDssaGNQAEKDAAPNASLR-GFEVIDSAKTRLEQACFGVVSC 122
Cdd:pfam00141   1 VRSVVRAAFKADPTMGPSLLRLHFHDCFVGGCDGSVLLD---GFKPEKDAPPNLGLRkGFEVIDDIKAKLEAACPGVVSC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  123 ADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQEAGANLPPPTASASQLTQAFGAKGLSQAEMVALSGAHTVGAARcs 202
Cdd:pfam00141  78 ADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  203 sfaprlysygpsgagqdpsmdpaylaalaqqcppqgtgaadpplpmdpvtptafdtnyyANLVARRGLLASDQALLADPA 282
Cdd:pfam00141 156 -----------------------------------------------------------KNLLDGRGLLTSDQALLSDPR 176
                         250
                  ....*....|.
gi 670357929  283 TAAQVLAYTNS 293
Cdd:pfam00141 177 TRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
44-309 3.26e-28

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: 109.94  E-value: 3.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  44 VQEEVSKAASGNPGVAAGLLRLHFHDCFVR--------GCDASVLLDssagnqAEKDAAPNASL-RGFEVIDSAKTRLEQ 114
Cdd:cd00314    3 IKAILEDLITQAGALAGSLLRLAFHDAGTYdiadgkggGADGSIRFE------PELDRPENGGLdKALRALEPIKSAYDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 115 ACfgVVSCADVLAFAARDA--LALVGGDAYQVPAGRRDGNVSSAQEA--GANLPPPTASASQLTQAFGAKGLSQAEMVAL 190
Cdd:cd00314   77 GN--PVSRADLIALAGAVAveSTFGGGPLIPFRFGRLDATEPDLGVPdpEGLLPNETSSATELRDKFKRMGLSPSELVAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 191 S-GAHTV-GAARCSSFAPRLYsygpsgagqdpsmdpaylaalaqqcppqgtgaadpplPMDPVTPTAFDTNYYANL---- 264
Cdd:cd00314  155 SaGAHTLgGKNHGDLLNYEGS-------------------------------------GLWTSTPFTFDNAYFKNLldmn 197
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 670357929 265 ------------VARRGLLASDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMG 309
Cdd:cd00314  198 wewrvgspdpdgVKGPGLLPSDYALLSDSETRALVERYASDQEKFFEDFAKAWIKMV 254
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
62-308 6.56e-12

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: 64.53  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  62 LLRLHFH-----DCFVR--GCDASVLLDssagnqAEKDAAPNASLrgfeviDSAKTRLEQ--ACFGVVSCADVLAFAARD 132
Cdd:cd00691   33 LVRLAWHdsgtyDKETKtgGSNGTIRFD------PELNHGANAGL------DIARKLLEPikKKYPDISYADLWQLAGVV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 133 ALALVGGDAYQVPAGRRDGNVSSAQEAGANLPPPTASASQLTQAFGAKGLSQAEMVALSGAHTVGaaRCssFAPRlysyg 212
Cdd:cd00691  101 AIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLG--RC--HKER----- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 213 pSGAGQdpsmdpaylaalaqqcpPQGTgaadpplpmdpvTPTAFDTNYYANLVARR------GL--LASDQALLADPATA 284
Cdd:cd00691  172 -SGYDG-----------------PWTK------------NPLKFDNSYFKELLEEDwklptpGLlmLPTDKALLEDPKFR 221
                        250       260
                 ....*....|....*....|....
gi 670357929 285 AQVLAYTNSPATFQTDFVAAMIKM 308
Cdd:cd00691  222 PYVELYAKDQDAFFKDYAEAHKKL 245
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
120-311 9.55e-10

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: 58.95  E-value: 9.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 120 VSCADVLAFAArdALALV---GGDAYQVPAGRRDgnvsSAQEAGANL-PPPTASASQLTQAFGAKGLSQAEMVALSGAHT 195
Cdd:cd00692  102 VSMADFIQFAG--AVAVSncpGAPRLEFYAGRKD----ATQPAPDGLvPEPFDSVDKILARFADAGFSPDELVALLAAHS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 196 VGAARcssfaprlysygpsgaGQDPSMdpaylaalaqqcppqgtgaadPPLPMDPvTPTAFDTNYY-------------- 261
Cdd:cd00692  176 VAAQD----------------FVDPSI---------------------AGTPFDS-TPGVFDTQFFietllkgtafpgsg 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 670357929 262 ------ANLVARRGLLASDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMGAI 311
Cdd:cd00692  218 gnqgevESPLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLL 273
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
58-218 2.04e-08

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: 54.40  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  58 VAAGLLRLHFHDCFVRGCDASVL-LDSS---AGNQAEK-DAAPNASLRGFEVIDSAKTrleqacfgvvSCADVLAFAARD 132
Cdd:cd08201   41 AAAEWLRTAFHDMATHNVDDGTGgLDASiqyELDRPENiGSGFNTTLNFFVNFYSPRS----------SMADLIAMGVVT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 133 ALALVGGDAYQVPAGRRDgnvssAQEAG-ANLPPPTASASQLTQAFGAKGLSQAEMVALSG-AHTVGAARCSSFaPRLYS 210
Cdd:cd08201  111 SVASCGGPVVPFRAGRID-----ATEAGqAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSEDF-PEIVP 184

                 ....*...
gi 670357929 211 YGPSGAGQ 218
Cdd:cd08201  185 PGSVPDTV 192
PLN02608 PLN02608
L-ascorbate peroxidase
62-308 5.07e-07

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 50.53  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929  62 LLRLHFHDcfvrgcdasvlldssAG--NQAEKDAAPNASLRG-FEVIDSAKTRLEQA---CFGV------VSCADVLAFA 129
Cdd:PLN02608  34 MLRLAWHD---------------AGtyDAKTKTGGPNGSIRNeEEYSHGANNGLKIAidlCEPVkakhpkITYADLYQLA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 130 ARDALALVGGDAYQVPAGRRDGNVSSAQeagANLPPPTASASQLTQAFGAKGLSQAEMVALSGAHTVGAARcssfaprly 209
Cdd:PLN02608  99 GVVAVEVTGGPTIDFVPGRKDSNACPEE---GRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAH--------- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 210 sygpsgagqdpsmdpaylaalaqqcpPQGTGaADPPLPMDPVTptaFDTNYYANLVA--RRGL--LASDQALLADPATAA 285
Cdd:PLN02608 167 --------------------------PERSG-FDGPWTKEPLK---FDNSYFVELLKgeSEGLlkLPTDKALLEDPEFRP 216
                        250       260
                 ....*....|....*....|...
gi 670357929 286 QVLAYTNSPATFQTDFVAAMIKM 308
Cdd:PLN02608 217 YVELYAKDEDAFFRDYAESHKKL 239
PLN02879 PLN02879
L-ascorbate peroxidase
117-311 1.81e-06

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 48.52  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 117 FGVVSCADVLAFAARDALALVGGDAYQVPAGRRDgNVSSAQEAgaNLPPPTASASQLTQAFGAKGLSQAEMVALSGAHTV 196
Cdd:PLN02879  89 FPILSYADFYQLAGVVAVEITGGPEIPFHPGRLD-KVEPPPEG--RLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTL 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 197 GaaRCSsfaprlysygpsgagqdpSMDPAYLAALAQQcppqgtgaadpplpmdpvtPTAFDTNYYANLVA--RRGLLA-- 272
Cdd:PLN02879 166 G--RCH------------------KERSGFEGAWTPN-------------------PLIFDNSYFKEILSgeKEGLLQlp 206
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 670357929 273 SDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMGAI 311
Cdd:PLN02879 207 TDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSEL 245
PLN02364 PLN02364
L-ascorbate peroxidase 1
117-316 6.57e-06

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 46.61  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 117 FGVVSCADVLAFAARDALALVGGDAYQVPAGRRDGNVSSAQeagANLPPPTASASQLTQAFGAK-GLSQAEMVALSGAHT 195
Cdd:PLN02364  88 FPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE---GRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357929 196 VGaaRCSSfaprlysygpsgagqdpsmdpaylaalaQQCPPQGTGAADPPLpmdpvtptaFDTNYYANLVA--RRGL--L 271
Cdd:PLN02364 165 LG--RCHK----------------------------DRSGFEGAWTSNPLI---------FDNSYFKELLSgeKEGLlqL 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 670357929 272 ASDQALLADPATAAQVLAYTNSPATFQTDFVAAMIKMGAIQVLTG 316
Cdd:PLN02364 206 VSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGFADA 250
 
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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