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Conserved domains on  [gi|30680940|ref|NP_187575|]
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ascorbate peroxidase 2 [Arabidopsis thaliana]

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

CATH:  1.10.420.10|1.10.520.10
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 ...
 1-251 0e+00

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 PLN02879:

Pssm-ID: 444739 [Multi-domain]  Cd Length: 251  Bit Score: 503.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80
Cdd:PLN02879   1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS 160
Cdd:PLN02879  81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240
Cdd:PLN02879 161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240

                        250
                 ....*....|.
gi 30680940  241 KLSELGFADKE 251
Cdd:PLN02879 241 KLSELGFADKE 251
 
Name Accession Description Interval E-value
PLN02879 PLN02879
L-ascorbate peroxidase
 1-251 0e+00

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 503.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80
Cdd:PLN02879   1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS 160
Cdd:PLN02879  81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240
Cdd:PLN02879 161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240

                        250
                 ....*....|.
gi 30680940  241 KLSELGFADKE 251
Cdd:PLN02879 241 KLSELGFADKE 251
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 6-247 4.83e-152

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: 423.54  E-value: 4.83e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   6 YPEVKEEY-KKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDP 84
Cdd:cd00691   1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  85 IKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEP---PPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSG 161
Cdd:cd00691  81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 162 GHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEK----EGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTE 237
Cdd:cd00691 161 AHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAE 240

                       250
                ....*....|
gi 30680940 238 AHLKLSELGF 247
Cdd:cd00691 241 AHKKLSELGV 250
peroxidase pfam00141
Peroxidase;
27-227 9.48e-56

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 176.60  E-value: 9.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    27 LIAEKHCAPIVLRLAWHSAGTfdvktktGGPFGTI---RHPQELAHDANNGLDIAVRLLDPIKELFP-----ILSYADFY 98
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    99 QLAGVVAVEITGGPEIPFHPGRLDKVEPPPE---GRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHkersgf 175
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH------ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30680940   176 egawtpnplifdnsyfKEILSGekEGLlqLPTDKALLDDPLFLPFVEKYAAD 227
Cdd:pfam00141 156 ----------------KNLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 12-243 3.28e-27

catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]


Pssm-ID: 272957 [Multi-domain]  Cd Length: 716  Bit Score: 109.63  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    12 EYKKAVQR-----CKRKLRGLIAEK---------HCAPIVLRLAWHSAGTFDVKTKTGGPF-GTIRHPQELAHDANNGLD 76
Cdd:TIGR00198  44 DYAEEFQQldlaaVKQDLKHLMTDSqswwpadwgHYGGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    77 IAVRLLDPIKELF-PILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPP------PE------GRLPQAT------- 136
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgAEkewltsSREDRESlenplaa 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   137 ----------KGVDH----------LRDVFGRMGLNDKDIVAL-SGGHTLGRCHKE------------------------ 171
Cdd:TIGR00198 204 temgliyvnpEGPDGhpdplctaqdIRTTFARMGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhn 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   172 -----------RSGFEGAWTPNPLIFDNSYFKEILSGEKE------GLLQ------------------------LPTDKA 210
Cdd:TIGR00198 284 qygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLA 363

                         330       340       350
                  ....*....|....*....|....*....|...
gi 30680940   211 LLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLS 243
Cdd:TIGR00198 364 LRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
32-242 5.11e-20

Catalase (peroxidase I) [Inorganic ion transport and metabolism];


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 88.64  E-value: 5.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  32 HCAPIVLRLAWHSAGTFDVKTKTGGpfgtirhpqelAHDAN-----------NG-LDIAVRLLDPIKELF-PILSYADFY 98
Cdd:COG0376  86 HYGPLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLM 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  99 QLAGVVAVEITGGPEIPFHPGRLDKVEP--------------------------P------------PEGRL----PQAT 136
Cdd:COG0376 155 ILAGNVALESMGFKTFGFAGGREDVWEPeedvywgpetewlgderysgdrelenPlaavqmgliyvnPEGPNgnpdPLAA 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 137 kGVDhLRDVFGRMGLNDKDIVAL-SGGHTLGRCH------------------------KER-----------SGFEGAWT 180
Cdd:COG0376 235 -ARD-IRETFGRMAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWT 312

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 181 PNPLIFDNSYFkEIL---------------------------------SGEKEGLLQLPTDKALLDDPLFLPFVEKYAAD 227
Cdd:COG0376 313 PTPTQWDNGYF-DNLfgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLEN 391

                       330
                ....*....|....*
gi 30680940 228 EDAFFEDYTEAHLKL 242
Cdd:COG0376 392 PEEFADAFARAWFKL 406
 
Name Accession Description Interval E-value
PLN02879 PLN02879
L-ascorbate peroxidase
 1-251 0e+00

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 503.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80
Cdd:PLN02879   1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS 160
Cdd:PLN02879  81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240
Cdd:PLN02879 161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240

                        250
                 ....*....|.
gi 30680940  241 KLSELGFADKE 251
Cdd:PLN02879 241 KLSELGFADKE 251
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 6-247 4.83e-152

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: 423.54  E-value: 4.83e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   6 YPEVKEEY-KKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDP 84
Cdd:cd00691   1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  85 IKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEP---PPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSG 161
Cdd:cd00691  81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 162 GHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEK----EGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTE 237
Cdd:cd00691 161 AHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYAE 240

                       250
                ....*....|
gi 30680940 238 AHLKLSELGF 247
Cdd:cd00691 241 AHKKLSELGV 250
PLN02364 PLN02364
L-ascorbate peroxidase 1
 4-247 2.19e-148

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 414.09  E-value: 2.19e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83
Cdd:PLN02364   3 KNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162
Cdd:PLN02364  83 PIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALSGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242
Cdd:PLN02364 163 HTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242


                 ....*
gi 30680940  243 SELGF 247
Cdd:PLN02364 243 SELGF 247
PLN02608 PLN02608
L-ascorbate peroxidase
 7-247 2.70e-142

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 400.29  E-value: 2.70e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    7 PEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDPIK 86
Cdd:PLN02608   4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   87 ELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG 166
Cdd:PLN02608  84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  167 RCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELG 246
Cdd:PLN02608 164 RAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSELG 243


                 .
gi 30680940  247 F 247
Cdd:PLN02608 244 F 244
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
 21-244 1.42e-69

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: 214.32  E-value: 1.42e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  21 KRKLRGLIAE-KHCAPIVLRLAWHSAGTFDVKT-KTGGPFGTIRHPQELAHDANNGLDIAVRLLDPIKELFP---ILSYA 95
Cdd:cd00314   4 KAILEDLITQaGALAGSLLRLAFHDAGTYDIADgKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggnPVSRA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  96 DFYQLAGVVAVEIT--GGPEIPFHPGRLDKVEPP-----PEGRLPQATKGVDHLRDVFGRMGLNDKDIVALS-GGHTL-G 166
Cdd:cd00314  84 DLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKFKRMGLSPSELVALSaGAHTLgG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 167 RCHKERSGFE--GAWTPNPLIFDNSYFKEILSGEKE------------GLLQLPTDKALLDDPLFLPFVEKYAADEDAFF 232
Cdd:cd00314 164 KNHGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQEKFF 243

                       250
                ....*....|..
gi 30680940 233 EDYTEAHLKLSE 244
Cdd:cd00314 244 EDFAKAWIKMVN 255
peroxidase pfam00141
Peroxidase;
27-227 9.48e-56

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 176.60  E-value: 9.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    27 LIAEKHCAPIVLRLAWHSAGTfdvktktGGPFGTI---RHPQELAHDANNGLDIAVRLLDPIKELFP-----ILSYADFY 98
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    99 QLAGVVAVEITGGPEIPFHPGRLDKVEPPPE---GRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHkersgf 175
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH------ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30680940   176 egawtpnplifdnsyfKEILSGekEGLlqLPTDKALLDDPLFLPFVEKYAAD 227
Cdd:pfam00141 156 ----------------KNLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
 105-246 9.99e-29

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: 110.30  E-value: 9.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 105 AVEITGGP--EIPFhpGRLD--KVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCH----KER-SGF 175
Cdd:cd00693 107 AVVLAGGPsyEVPL--GRRDgrVSSANDVGNLPSPFFSVSQLISLFASKGLTVTDLVALSGAHTIGRAHcssfSDRlYNF 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 176 EGAWTPNPLI-------------------------------FDNSYFKEILSGekEGLLQlpTDKALLDDPLFLPFVEKY 224
Cdd:cd00693 185 SGTGDPDPTLdpayaaqlrkkcpaggdddtlvpldpgtpntFDNSYYKNLLAG--RGLLT--SDQALLSDPRTRAIVNRY 260

                       170       180
                ....*....|....*....|..
gi 30680940 225 AADEDAFFEDYTEAHLKLSELG 246
Cdd:cd00693 261 AANQDAFFRDFAAAMVKMGNIG 282
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 12-243 3.28e-27

catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]


Pssm-ID: 272957 [Multi-domain]  Cd Length: 716  Bit Score: 109.63  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    12 EYKKAVQR-----CKRKLRGLIAEK---------HCAPIVLRLAWHSAGTFDVKTKTGGPF-GTIRHPQELAHDANNGLD 76
Cdd:TIGR00198  44 DYAEEFQQldlaaVKQDLKHLMTDSqswwpadwgHYGGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    77 IAVRLLDPIKELF-PILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPP------PE------GRLPQAT------- 136
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgAEkewltsSREDRESlenplaa 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   137 ----------KGVDH----------LRDVFGRMGLNDKDIVAL-SGGHTLGRCHKE------------------------ 171
Cdd:TIGR00198 204 temgliyvnpEGPDGhpdplctaqdIRTTFARMGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhn 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   172 -----------RSGFEGAWTPNPLIFDNSYFKEILSGEKE------GLLQ------------------------LPTDKA 210
Cdd:TIGR00198 284 qygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLA 363

                         330       340       350
                  ....*....|....*....|....*....|...
gi 30680940   211 LLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLS 243
Cdd:TIGR00198 364 LRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
catalase_peroxidase_1 cd00649
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 32-242 6.23e-27

N-terminal catalytic domain of catalase-peroxidases; This is 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. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.


Pssm-ID: 173824 [Multi-domain]  Cd Length: 409  Bit Score: 107.39  E-value: 6.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  32 HCAPIVLRLAWHSAGTFDVKTKTGGP-FGTIRHPQELAHDANNGLDIAVRLLDPIKELF-PILSYADFYQLAGVVAVEIT 109
Cdd:cd00649  68 HYGPLFIRMAWHSAGTYRIADGRGGAgTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYgNKISWADLMILAGNVALESM 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 110 GGPEIPFHPGRLD--------------------------KVEPP------------PEG--RLPQATKGVDHLRDVFGRM 149
Cdd:cd00649 148 GFKTFGFAGGREDvwepdedvywgpekewladkrysgdrDLENPlaavqmgliyvnPEGpdGNPDPLAAAKDIRETFARM 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 150 GLNDKDIVAL-SGGHTLGRCH---------KE--------------------------RSGFEGAWTPNPLIFDNSYFKE 193
Cdd:cd00649 228 AMNDEETVALiAGGHTFGKTHgagpashvgPEpeaapieqqglgwknsygtgkgkdtiTSGLEGAWTPTPTKWDNNYLKN 307

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 194 ILS--------------------------------GEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLK 241
Cdd:cd00649 308 LFGyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFK 387


                .
gi 30680940 242 L 242
Cdd:cd00649 388 L 388
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
 37-247 3.42e-20

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: 87.84  E-value: 3.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  37 VLRLAWHSAGTFDVKTKTGGPFGT------IRHPQ-ELAHDANNGLDIAVRLLDPIkELFPILSYADFYQLAGVVAV-EI 108
Cdd:cd00692  41 SLRLTFHDAIGFSPALAAGQFGGGgadgsiVLFDDiETAFHANIGLDEIVEALRPF-HQKHNVSMADFIQFAGAVAVsNC 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 109 TGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGawTP---NPLI 185
Cdd:cd00692 120 PGAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQDFVDPSIAG--TPfdsTPGV 197

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30680940 186 FDNSYFKEIL------------SGEKE----GLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELGF 247
Cdd:cd00692 198 FDTQFFIETLlkgtafpgsggnQGEVEsplpGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
PRK15061 PRK15061
catalase/peroxidase;
32-242 4.54e-20

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 89.04  E-value: 4.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   32 HCAPIVLRLAWHSAGTFDVKTKTGGP-FGTIRH------PqelahDaNNGLDIAVRLLDPIKELF-PILSYADFYQLAGV 103
Cdd:PRK15061  80 HYGPLFIRMAWHSAGTYRIGDGRGGAgGGQQRFaplnswP-----D-NVNLDKARRLLWPIKQKYgNKISWADLMILAGN 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  104 VAVEITGGPEIPFHPGRLDKVEP---------------------------P------------PEGRL----PQATkGVD 140
Cdd:PRK15061 154 VALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEGPNgnpdPLAA-ARD 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  141 hLRDVFGRMGLNDKDIVAL-SGGHTLGRCH-------------------------------KER----SGFEGAWTPNPL 184
Cdd:PRK15061 233 -IRETFARMAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgKGAdtitSGLEGAWTTTPT 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  185 IFDNSYFkEIL---------------------------------SGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAF 231
Cdd:PRK15061 312 QWDNGYF-ENLfgyeweltkspagawqwvpkdgaaedtvpdahdPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPEEF 390

                        330
                 ....*....|.
gi 30680940  232 FEDYTEAHLKL 242
Cdd:PRK15061 391 ADAFARAWFKL 401
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
32-242 5.11e-20

Catalase (peroxidase I) [Inorganic ion transport and metabolism];


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 88.64  E-value: 5.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  32 HCAPIVLRLAWHSAGTFDVKTKTGGpfgtirhpqelAHDAN-----------NG-LDIAVRLLDPIKELF-PILSYADFY 98
Cdd:COG0376  86 HYGPLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLM 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  99 QLAGVVAVEITGGPEIPFHPGRLDKVEP--------------------------P------------PEGRL----PQAT 136
Cdd:COG0376 155 ILAGNVALESMGFKTFGFAGGREDVWEPeedvywgpetewlgderysgdrelenPlaavqmgliyvnPEGPNgnpdPLAA 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 137 kGVDhLRDVFGRMGLNDKDIVAL-SGGHTLGRCH------------------------KER-----------SGFEGAWT 180
Cdd:COG0376 235 -ARD-IRETFGRMAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWT 312

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 181 PNPLIFDNSYFkEIL---------------------------------SGEKEGLLQLPTDKALLDDPLFLPFVEKYAAD 227
Cdd:COG0376 313 PTPTQWDNGYF-DNLfgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLEN 391

                       330
                ....*....|....*
gi 30680940 228 EDAFFEDYTEAHLKL 242
Cdd:COG0376 392 PEEFADAFARAWFKL 406
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
 38-197 6.04e-17

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: 77.89  E-value: 6.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  38 LRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDPIKElfPILSYADFYQLAGVVAVEITGGPEIPFH 117
Cdd:cd08201  46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNFYS--PRSSMADLIAMGVVTSVASCGGPVVPFR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940 118 PGRLDKVEPPPEGrLPQATKGVDHLRDVFGRMGLNDKDIVALSG-GHTLGRCHKERsgFEGAWTPNPLI----------- 185
Cdd:cd08201 124 AGRIDATEAGQAG-VPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHSED--FPEIVPPGSVPdtvlqffdtti 200

                       170
                ....*....|...
gi 30680940 186 -FDNSYFKEILSG 197
Cdd:cd08201 201 qFDNKVVTEYLSG 213
PLN03030 PLN03030
cationic peroxidase; Provisional
 91-166 6.51e-07

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 49.57  E-value: 6.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30680940   91 ILSYADFYQLAGVVAVEITGGPEIPFHPGRLD-KVEPPPE-GRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLG 166
Cdd:PLN03030 113 VVSCADILALAARDSVVLTNGLTWPVPTGRRDgRVSLASDaSNLPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIG 190
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 41-195 1.09e-03

catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]


Pssm-ID: 272957 [Multi-domain]  Cd Length: 716  Bit Score: 39.91  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940    41 AWHSAGTFDVKTKTGGPFGT-----------IRHPQELAHdanngldiAVRLLDPIKELFPI--LSYADFYQLAGVVAVE 107
Cdd:TIGR00198 455 AWASASTFRSSDYRGGANGArirlepqknwpVNEPTRLAK--------VLAVLEKIQAEFAKgpVSLADLIVLGGGAAVE 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940   108 ---ITGGPEI--PFHPGRLDK------------VEPPPEG-----RLPQATKGVDHLRDVFGRMGLNDKDIVALSGG-HT 164
Cdd:TIGR00198 527 kaaLDAGISVnvPFLPGRVDAtqamtdaesftpLEPIADGfrnylKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGmRV 606

                         170       180       190
                  ....*....|....*....|....*....|.
gi 30680940   165 LGRCHKERSgfEGAWTPNPLIFDNSYFKEIL 195
Cdd:TIGR00198 607 LGANHGGSK--HGVFTDRVGVLSNDFFVNLL 635
catalase_peroxidase_2 cd08200
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 39-122 3.16e-03

C-terminal non-catalytic domain of catalase-peroxidases; This is 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. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.


Pssm-ID: 173828  Cd Length: 297  Bit Score: 37.98  E-value: 3.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680940  39 RLAWHSAGTFDVKTKTGGPFGT-IR----------HPQELAHdanngldiAVRLLDPIKELFPI-------LSYADFYQL 100
Cdd:cd08200  35 STAWASASTFRNSDKRGGANGArIRlapqkdwevnEPEELAK--------VLAVLEGIQKEFNEsqsggkkVSLADLIVL 106

                        90       100
                ....*....|....*....|....*..
gi 30680940 101 AGVVAVEIT---GGPEI--PFHPGRLD 122
Cdd:cd08200 107 GGCAAVEKAakdAGVDIkvPFTPGRTD 133
 
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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