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Conserved domains on  [gi|217407588|gb|EEC47524|]
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l-ascorbate peroxidase, partial [Phaeodactylum tricornutum CCAP 1055/1]

Protein Classification

peroxidase( domain architecture ID 10091038)

peroxidase catalyzes an oxidative reaction involving hydrogen peroxide as the electron acceptor, such as plant ascorbate peroxidase and fungal cytochrome c peroxidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 8-245 4.14e-135

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: 381.55  E-value: 4.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   8 DEFYDNAARAEVSRAIVNKkvNVCPFTVRLAWHASGTFDQSDASGGSdGARMRYAPELSDGANAGLALMQDIIKPVKEKF 87
Cdd:cd00691    9 AAKDLEAARNDIAKLIDDK--NCAPILVRLAWHDSGTYDKETKTGGS-NGTIRFDPELNHGANAGLDIARKLLEPIKKKY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  88 PDMSYADLWTMAGTQAIKLTGGPDIPFNYGRTDDADNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLG 167
Cdd:cd00691   86 PDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLG 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 168 SCHRLRSGFDGPWTTNPLKFDNEYFKNLLEIDWKPrewegplqyqdPSGKLMMLPTDMALIQDEAFLPFVKKYAEDEQ 245
Cdd:cd00691  166 RCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWKL-----------PTPGLLMLPTDKALLEDPKFRPYVELYAKDQD 232
 
Name Accession Description Interval E-value
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 8-245 4.14e-135

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: 381.55  E-value: 4.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   8 DEFYDNAARAEVSRAIVNKkvNVCPFTVRLAWHASGTFDQSDASGGSdGARMRYAPELSDGANAGLALMQDIIKPVKEKF 87
Cdd:cd00691    9 AAKDLEAARNDIAKLIDDK--NCAPILVRLAWHDSGTYDKETKTGGS-NGTIRFDPELNHGANAGLDIARKLLEPIKKKY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  88 PDMSYADLWTMAGTQAIKLTGGPDIPFNYGRTDDADNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLG 167
Cdd:cd00691   86 PDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLG 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 168 SCHRLRSGFDGPWTTNPLKFDNEYFKNLLEIDWKPrewegplqyqdPSGKLMMLPTDMALIQDEAFLPFVKKYAEDEQ 245
Cdd:cd00691  166 RCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWKL-----------PTPGLLMLPTDKALLEDPKFRPYVELYAKDQD 232
PLN02608 PLN02608
L-ascorbate peroxidase
 15-244 2.58e-84

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 254.30  E-value: 2.58e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  15 ARAEVsRAIVNKKvNVCPFTVRLAWHASGTFDQSDASGGSDGArMRYAPELSDGANAGLALMQDIIKPVKEKFPDMSYAD 94
Cdd:PLN02608  17 ARRDL-RALIASK-NCAPIMLRLAWHDAGTYDAKTKTGGPNGS-IRNEEEYSHGANNGLKIAIDLCEPVKAKHPKITYAD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  95 LWTMAGTQAIKLTGGPDIPFNYGRTDdadNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLGSCHRLRS 174
Cdd:PLN02608  94 LYQLAGVVAVEVTGGPTIDFVPGRKD---SNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAHPERS 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 175 GFDGPWTTNPLKFDNEYFKNLLEidwkpREWEGplqyqdpsgkLMMLPTDMALIQDEAFLPFVKKYAEDE 244
Cdd:PLN02608 171 GFDGPWTKEPLKFDNSYFVELLK-----GESEG----------LLKLPTDKALLEDPEFRPYVELYAKDE 225
peroxidase pfam00141
Peroxidase;
15-243 2.33e-53

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 171.59  E-value: 2.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   15 ARAEVsRAIVNKKVNVCPFTVRLAWHASGTfdqsdasGGSDGARMR--YAPELSDGANAGLALMQDIIKPVKEKFPDM-- 90
Cdd:pfam00141   1 VRSVV-RAAFKADPTMGPSLLRLHFHDCFV-------GGCDGSVLLdgFKPEKDAPPNLGLRKGFEVIDDIKAKLEAAcp 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   91 ---SYADLWTMAGTQAIKLTGGPDIPFNYGRTDDADNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLG 167
Cdd:pfam00141  73 gvvSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIG 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217407588  168 SCHrlrsgfdgpwttnplkfdneyfKNLLEidwkprewegplqyqdpsgKLMMLPTDMALIQDEAFLPFVKKYAED 243
Cdd:pfam00141 153 RAH----------------------KNLLD-------------------GRGLLTSDQALLSDPRTRALVERYAAD 187
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
32-243 2.45e-24

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 102.12  E-value: 2.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  32 PFTVRLAWHASGTFDQSDASGGSDGARMRYAPELS--DGAN---AGLALMqdiikPVKEKFPD-MSYADLWTMAGTQAIK 105
Cdd:COG0376   89 PLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSwpDNANldkARRLLW-----PIKQKYGNkISWADLMILAGNVALE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 106 LTGGPDIPFNYGRTDD---------------ADNNKCPANGRL----------------------PDATQGAEHLRDVFY 148
Cdd:COG0376  164 SMGFKTFGFAGGREDVwepeedvywgpetewLGDERYSGDRELenplaavqmgliyvnpegpngnPDPLAAARDIRETFG 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 149 RMGFGDKEIVAL-SGAHTLGSCH-----------------------------------RLRSGFDGPWTTNPLKFDNEYF 192
Cdd:COG0376  244 RMAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwknsfgsgkgedTITSGLEGAWTPTPTQWDNGYF 323

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 193 KNLLEIDW------------KPREWEGPLQY---QDPSGK--LMMLPTDMALIQDEAFLPFVKKYAED 243
Cdd:COG0376  324 DNLFGYEWeltkspagahqwVPKDGAAADTVpdaHDPSKRhaPMMLTTDLALRFDPAYEKISRRFLEN 391
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 32-245 4.24e-24

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: 101.54  E-value: 4.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   32 PFTVRLAWHASGTFDQSDASGGSDGARMRYAPELSDGANAGLALMQDIIKPVKEKFPD-MSYADLWTMAGTQAIKLTGGP 110
Cdd:TIGR00198  81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNkLSWADLIILAGTVAYESMGLK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  111 DIPFNYGRTD----DADNNKCPANGRL--------------------------------PDATQGAEHLRDVFYRMGFGD 154
Cdd:TIGR00198 161 VFGFAGGREDiwepDKDIYWGAEKEWLtssredreslenplaatemgliyvnpegpdghPDPLCTAQDIRTTFARMGMND 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  155 KEIVAL-SGAHTLGSCH-----------------------------------RLRSGFDGPWTTNPLKFDNEYFKNLLEI 198
Cdd:TIGR00198 241 EETVALiAGGHTVGKCHgagpaeligpdpegapieeqglgwhnqygkgvgrdTMTSGLEVAWTTTPTQWDNGYFYMLFNY 320

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217407588  199 DWK-PREWEGPLQYQ------------DPSGKL--MMLPTDMALIQDEAFLPFVKKYAEDEQ 245
Cdd:TIGR00198 321 EWElKKSPAGAWQWEavdapeiipdveDPNKKHnpIMLDADLALRFDPEFRKISRRFLREPD 382
 
Name Accession Description Interval E-value
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 8-245 4.14e-135

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: 381.55  E-value: 4.14e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   8 DEFYDNAARAEVSRAIVNKkvNVCPFTVRLAWHASGTFDQSDASGGSdGARMRYAPELSDGANAGLALMQDIIKPVKEKF 87
Cdd:cd00691    9 AAKDLEAARNDIAKLIDDK--NCAPILVRLAWHDSGTYDKETKTGGS-NGTIRFDPELNHGANAGLDIARKLLEPIKKKY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  88 PDMSYADLWTMAGTQAIKLTGGPDIPFNYGRTDDADNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLG 167
Cdd:cd00691   86 PDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASKGADHLRDVFYRMGFNDQEIVALSGAHTLG 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 168 SCHRLRSGFDGPWTTNPLKFDNEYFKNLLEIDWKPrewegplqyqdPSGKLMMLPTDMALIQDEAFLPFVKKYAEDEQ 245
Cdd:cd00691  166 RCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWKL-----------PTPGLLMLPTDKALLEDPKFRPYVELYAKDQD 232
PLN02608 PLN02608
L-ascorbate peroxidase
 15-244 2.58e-84

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 254.30  E-value: 2.58e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  15 ARAEVsRAIVNKKvNVCPFTVRLAWHASGTFDQSDASGGSDGArMRYAPELSDGANAGLALMQDIIKPVKEKFPDMSYAD 94
Cdd:PLN02608  17 ARRDL-RALIASK-NCAPIMLRLAWHDAGTYDAKTKTGGPNGS-IRNEEEYSHGANNGLKIAIDLCEPVKAKHPKITYAD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  95 LWTMAGTQAIKLTGGPDIPFNYGRTDdadNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLGSCHRLRS 174
Cdd:PLN02608  94 LYQLAGVVAVEVTGGPTIDFVPGRKD---SNACPEEGRLPDAKKGAKHLRDVFYRMGLSDKDIVALSGGHTLGRAHPERS 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 175 GFDGPWTTNPLKFDNEYFKNLLEidwkpREWEGplqyqdpsgkLMMLPTDMALIQDEAFLPFVKKYAEDE 244
Cdd:PLN02608 171 GFDGPWTKEPLKFDNSYFVELLK-----GESEG----------LLKLPTDKALLEDPEFRPYVELYAKDE 225
PLN02879 PLN02879
L-ascorbate peroxidase
 21-244 1.62e-70

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 217.62  E-value: 1.62e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  21 RAIVNKKvNVCPFTVRLAWHASGTFDQSDASGGSDGArMRYAPELSDGANAGLALMQDIIKPVKEKFPDMSYADLWTMAG 100
Cdd:PLN02879  25 RGLIAEK-HCAPIVLRLAWHSAGTFDVKTKTGGPFGT-IRHPQELAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 101 TQAIKLTGGPDIPFNYGRTDDADNnkcPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLGSCHRLRSGFDGPW 180
Cdd:PLN02879 103 VVAVEITGGPEIPFHPGRLDKVEP---PPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGAW 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 217407588 181 TTNPLKFDNEYFKNLLEidwkpREWEGPLQyqdpsgklmmLPTDMALIQDEAFLPFVKKYAEDE 244
Cdd:PLN02879 180 TPNPLIFDNSYFKEILS-----GEKEGLLQ----------LPTDKALLDDPLFLPFVEKYAADE 228
PLN02364 PLN02364
L-ascorbate peroxidase 1
 21-244 1.26e-68

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 213.02  E-value: 1.26e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  21 RAIVNKKvNVCPFTVRLAWHASGTFDQSDASGGSDGArMRYAPELSDGANAGLALMQDIIKPVKEKFPDMSYADLWTMAG 100
Cdd:PLN02364  24 RGLIAEK-NCAPIMVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGANSGIHIALRLLDPIREQFPTISFADFHQLAG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 101 TQAIKLTGGPDIPFNYGRTDDAdnnKCPANGRLPDATQGAEHLRDVFYR-MGFGDKEIVALSGAHTLGSCHRLRSGFDGP 179
Cdd:PLN02364 102 VVAVEVTGGPDIPFHPGREDKP---QPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALSGAHTLGRCHKDRSGFEGA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217407588 180 WTTNPLKFDNEYFKNLLEidwkpREWEGPLQyqdpsgklmmLPTDMALIQDEAFLPFVKKYAEDE 244
Cdd:PLN02364 179 WTSNPLIFDNSYFKELLS-----GEKEGLLQ----------LVSDKALLDDPVFRPLVEKYAADE 228
peroxidase pfam00141
Peroxidase;
15-243 2.33e-53

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 171.59  E-value: 2.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   15 ARAEVsRAIVNKKVNVCPFTVRLAWHASGTfdqsdasGGSDGARMR--YAPELSDGANAGLALMQDIIKPVKEKFPDM-- 90
Cdd:pfam00141   1 VRSVV-RAAFKADPTMGPSLLRLHFHDCFV-------GGCDGSVLLdgFKPEKDAPPNLGLRKGFEVIDDIKAKLEAAcp 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   91 ---SYADLWTMAGTQAIKLTGGPDIPFNYGRTDDADNNKCPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLG 167
Cdd:pfam00141  73 gvvSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPAPTDSLDQLRDRFARKGLTAEDLVALSGAHTIG 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217407588  168 SCHrlrsgfdgpwttnplkfdneyfKNLLEidwkprewegplqyqdpsgKLMMLPTDMALIQDEAFLPFVKKYAED 243
Cdd:pfam00141 153 RAH----------------------KNLLD-------------------GRGLLTSDQALLSDPRTRALVERYAAD 187
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
 30-244 3.15e-53

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: 173.49  E-value: 3.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  30 VCPFTVRLAWHASGTFDQSDASGGSDGARMRYAPELSDGANAGLALMQDIIKPVKEKFPD---MSYADLWTMAGTQAIKL 106
Cdd:cd00314   17 LAGSLLRLAFHDAGTYDIADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDGgnpVSRADLIALAGAVAVES 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 107 T--GGPDIPFNYGRTDDADNNKCPAN--GRLPDATQGAEHLRDVFYRMGFGDKEIVALS-GAHTL-GSCHRLRSGF--DG 178
Cdd:cd00314   97 TfgGGPLIPFRFGRLDATEPDLGVPDpeGLLPNETSSATELRDKFKRMGLSPSELVALSaGAHTLgGKNHGDLLNYegSG 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217407588 179 PWTTNPLKFDNEYFKNLLEIDWkprEWEGPLQYQDPSGKLMMLPTDMALIQDEAFLPFVKKYAEDE 244
Cdd:cd00314  177 LWTSTPFTFDNAYFKNLLDMNW---EWRVGSPDPDGVKGPGLLPSDYALLSDSETRALVERYASDQ 239
catalase_peroxidase_1 cd00649
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 32-243 5.59e-31

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: 118.95  E-value: 5.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  32 PFTVRLAWHASGTFDQSDASGGSDGARMRYAPELSDGANAGLALMQDIIKPVKEKFPD-MSYADLWTMAGTQAIKLTGGP 110
Cdd:cd00649   71 PLFIRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYGNkISWADLMILAGNVALESMGFK 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 111 DIPFNYGRTDD--AD-------------NNKCPANGRL----------------------PDATQGAEHLRDVFYRMGFG 153
Cdd:cd00649  151 TFGFAGGREDVwePDedvywgpekewlaDKRYSGDRDLenplaavqmgliyvnpegpdgnPDPLAAAKDIRETFARMAMN 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 154 DKEIVAL-SGAHTLGSCH-----------------------------------RLRSGFDGPWTTNPLKFDNEYFKNLLE 197
Cdd:cd00649  231 DEETVALiAGGHTFGKTHgagpashvgpepeaapieqqglgwknsygtgkgkdTITSGLEGAWTPTPTKWDNNYLKNLFG 310

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217407588 198 IDWKPREW-EGPLQY--------------QDPSGK--LMMLPTDMALIQDEAFLPFVKKYAED 243
Cdd:cd00649  311 YEWELTKSpAGAWQWvpknaagentvpdaHDPSKKhaPMMLTTDLALRFDPEYEKISRRFLEN 373
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
32-243 2.45e-24

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 102.12  E-value: 2.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  32 PFTVRLAWHASGTFDQSDASGGSDGARMRYAPELS--DGAN---AGLALMqdiikPVKEKFPD-MSYADLWTMAGTQAIK 105
Cdd:COG0376   89 PLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSwpDNANldkARRLLW-----PIKQKYGNkISWADLMILAGNVALE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 106 LTGGPDIPFNYGRTDD---------------ADNNKCPANGRL----------------------PDATQGAEHLRDVFY 148
Cdd:COG0376  164 SMGFKTFGFAGGREDVwepeedvywgpetewLGDERYSGDRELenplaavqmgliyvnpegpngnPDPLAAARDIRETFG 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 149 RMGFGDKEIVAL-SGAHTLGSCH-----------------------------------RLRSGFDGPWTTNPLKFDNEYF 192
Cdd:COG0376  244 RMAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwknsfgsgkgedTITSGLEGAWTPTPTQWDNGYF 323

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 193 KNLLEIDW------------KPREWEGPLQY---QDPSGK--LMMLPTDMALIQDEAFLPFVKKYAED 243
Cdd:COG0376  324 DNLFGYEWeltkspagahqwVPKDGAAADTVpdaHDPSKRhaPMMLTTDLALRFDPAYEKISRRFLEN 391
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 32-245 4.24e-24

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: 101.54  E-value: 4.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   32 PFTVRLAWHASGTFDQSDASGGSDGARMRYAPELSDGANAGLALMQDIIKPVKEKFPD-MSYADLWTMAGTQAIKLTGGP 110
Cdd:TIGR00198  81 GLFIRMAWHAAGTYRIADGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYGNkLSWADLIILAGTVAYESMGLK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  111 DIPFNYGRTD----DADNNKCPANGRL--------------------------------PDATQGAEHLRDVFYRMGFGD 154
Cdd:TIGR00198 161 VFGFAGGREDiwepDKDIYWGAEKEWLtssredreslenplaatemgliyvnpegpdghPDPLCTAQDIRTTFARMGMND 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  155 KEIVAL-SGAHTLGSCH-----------------------------------RLRSGFDGPWTTNPLKFDNEYFKNLLEI 198
Cdd:TIGR00198 241 EETVALiAGGHTVGKCHgagpaeligpdpegapieeqglgwhnqygkgvgrdTMTSGLEVAWTTTPTQWDNGYFYMLFNY 320

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217407588  199 DWK-PREWEGPLQYQ------------DPSGKL--MMLPTDMALIQDEAFLPFVKKYAEDEQ 245
Cdd:TIGR00198 321 EWElKKSPAGAWQWEavdapeiipdveDPNKKHnpIMLDADLALRFDPEFRKISRRFLREPD 382
PRK15061 PRK15061
catalase/peroxidase;
32-243 1.60e-23

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 99.83  E-value: 1.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  32 PFTVRLAWHASGTFDQSDASGGSDGARMRYAPELS--DGANAGLA--LMQdiikPVKEKFPD-MSYADLWTMAGTQAIKL 106
Cdd:PRK15061  83 PLFIRMAWHSAGTYRIGDGRGGAGGGQQRFAPLNSwpDNVNLDKArrLLW----PIKQKYGNkISWADLMILAGNVALES 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 107 TGGPDIPFNYGRTDD----------------ADNNKCPANGRL----------------------PDATQGAEHLRDVFY 148
Cdd:PRK15061 159 MGFKTFGFAGGREDVwepeedvywgpekewlGGDERYSGERDLenplaavqmgliyvnpegpngnPDPLAAARDIRETFA 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 149 RMGFGDKEIVAL-SGAHTLGSCH-----------------------------------RLRSGFDGPWTTNPLKFDNEYF 192
Cdd:PRK15061 239 RMAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgkgadTITSGLEGAWTTTPTQWDNGYF 318

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 193 KNLLEIDWKP-REWEGPLQYQ--------------DPSGKL--MMLPTDMALIQDEAFLPFVKKYAED 243
Cdd:PRK15061 319 ENLFGYEWELtKSPAGAWQWVpkdgaaedtvpdahDPSKKHapTMLTTDLALRFDPEYEKISRRFLEN 386
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
 91-245 2.17e-16

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: 77.17  E-value: 2.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  91 SYADLWTMAGTQAIKLTGGPDIPFNYGRTD----DADNNkcpanGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTL 166
Cdd:cd00693   95 SCADILALAARDAVVLAGGPSYEVPLGRRDgrvsSANDV-----GNLPSPFFSVSQLISLFASKGLTVTDLVALSGAHTI 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 167 G--SC----HRL--------------------------RSGFDGPwTTN-----PLKFDNEYFKNLLEidwkprewegpl 209
Cdd:cd00693  170 GraHCssfsDRLynfsgtgdpdptldpayaaqlrkkcpAGGDDDT-LVPldpgtPNTFDNSYYKNLLA------------ 236

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 217407588 210 qyqdpsgKLMMLPTDMALIQDEAFLPFVKKYAEDEQ 245
Cdd:cd00693  237 -------GRGLLTSDQALLSDPRTRAIVNRYAANQD 265
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
 35-171 1.58e-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: 65.95  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  35 VRLAWHASGTFDQSDASGGSDGArMRYapELSDGANAGLALMQDIIKPVKEKFPDMSYADLWTMAGTQAIKLTGGPDIPF 114
Cdd:cd08201   46 LRTAFHDMATHNVDDGTGGLDAS-IQY--ELDRPENIGSGFNTTLNFFVNFYSPRSSMADLIAMGVVTSVASCGGPVVPF 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 217407588 115 NYGRTDDADnnkcPANGRLPDATQGAEHLRDVFYRMGFGDKEIVALSG-AHTLGSCHR 171
Cdd:cd08201  123 RAGRIDATE----AGQAGVPEPQTDLGTTTESFRRQGFSTSEMIALVAcGHTLGGVHS 176
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
 33-232 3.36e-12

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: 65.50  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  33 FTVRLAWHASGTFDQSDAS-----GGSDGARMRYAP-ELSDGANAGLALMQDIIKPVKEKFpDMSYADLWTMAGTQAI-K 105
Cdd:cd00692   40 ESLRLTFHDAIGFSPALAAgqfggGGADGSIVLFDDiETAFHANIGLDEIVEALRPFHQKH-NVSMADFIQFAGAVAVsN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588 106 LTGGPDIPFNYGRTDDADnnkcPA-NGRLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLGSCHRLRSGFDG-PWTTN 183
Cdd:cd00692  119 CPGAPRLEFYAGRKDATQ----PApDGLVPEPFDSVDKILARFADAGFSPDELVALLAAHSVAAQDFVDPSIAGtPFDST 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 217407588 184 PLKFDNEYF-KNLLEIDWKPREWEGPLQYQDPSGKLMMLPTDMALIQDEA 232
Cdd:cd00692  195 PGVFDTQFFiETLLKGTAFPGSGGNQGEVESPLPGEFRLQSDFLLARDPR 244
catalase_peroxidase_2 cd08200
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 12-202 2.67e-09

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: 56.85  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  12 DNAARAEVSRAIVNKKVNVCPFtVRLAWHASGTFDQSDASGGSDGARMRYAPELSDGAN--AGLALMQDIIKPVKEKFPD 89
Cdd:cd08200   12 DDADIAALKAKILASGLTVSEL-VSTAWASASTFRNSDKRGGANGARIRLAPQKDWEVNepEELAKVLAVLEGIQKEFNE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  90 -------MSYADLWTMAGT----QAIKlTGGPDI--PFNYGRTD------D----------ADNNKcpaNGRLPDATQGA 140
Cdd:cd08200   91 sqsggkkVSLADLIVLGGCaaveKAAK-DAGVDIkvPFTPGRTDatqeqtDvesfevlepkADGFR---NYLKKGYRVPP 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 217407588 141 EH-LRDVFYRMGFGDKEIVALSG------AHTLGSCHrlrsgfdGPWTTNPLKFDNEYFKNLLEID--WKP 202
Cdd:cd08200  167 EEmLVDKAQLLTLTAPEMTVLVGglrvlgANYGGSKH-------GVFTDRPGVLTNDFFVNLLDMSteWKP 230
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 18-202 2.16e-06

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: 48.77  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   18 EVSRAIVNKKVNVCPFtVRLAWHASGTFDQSDASGGSDGARMRYAPELSDGANAGLALMQDIikPVKEKF------PDMS 91
Cdd:TIGR00198 436 ELKQQILASGLSVSEL-VCTAWASASTFRSSDYRGGANGARIRLEPQKNWPVNEPTRLAKVL--AVLEKIqaefakGPVS 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588   92 YADLWTMAGTQAIK---LTGGPDI--PFNYGRTD------DADNNKC--P-ANG-----RLPDATQGAEHLRDVFYRMGF 152
Cdd:TIGR00198 513 LADLIVLGGGAAVEkaaLDAGISVnvPFLPGRVDatqamtDAESFTPlePiADGfrnylKRDYAVTPEELLLDKAQLLTL 592

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 217407588  153 GDKEIVAL-SGAHTLGSCHrlrSGFD-GPWTTNPLKFDNEYFKNLLEI--DWKP 202
Cdd:TIGR00198 593 TAPEMTVLiGGMRVLGANH---GGSKhGVFTDRVGVLSNDFFVNLLDMayEWRA 643
PRK15061 PRK15061
catalase/peroxidase;
35-120 4.80e-06

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 47.44  E-value: 4.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  35 VRLAWHASGTFDQSDASGGSDGARMRYAPELSDGAN--AGLALMQDIIKPVKEKFPDM-------SYADLWTMAGT---- 101
Cdd:PRK15061 459 VSTAWASASTFRGSDKRGGANGARIRLAPQKDWEVNepAQLAKVLAVLEGIQAEFNAAqsggkkvSLADLIVLGGNaave 538

                         90       100
                 ....*....|....*....|.
gi 217407588 102 QAIKlTGGPDI--PFNYGRTD 120
Cdd:PRK15061 539 QAAK-AAGHDVtvPFTPGRTD 558
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
35-120 7.09e-05

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 43.96  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217407588  35 VRLAWHASGTFDQSDASGGSDGARMRYAPELSDGAN--AGLALMQDIIKPVKEKFPDM-------SYADLWTMAGTQAIK 105
Cdd:COG0376  464 VSTAWASASTFRGSDKRGGANGARIRLAPQKDWEVNepEQLAKVLAVLEGIQKDFNAAqsggkkvSLADLIVLGGCAAVE 543

                         90       100
                 ....*....|....*....|
gi 217407588 106 LT---GGPDI--PFNYGRTD 120
Cdd:COG0376  544 KAakdAGHDVtvPFTPGRTD 563
PLN03030 PLN03030
cationic peroxidase; Provisional
 90-168 1.53e-03

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 39.56  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217407588  90 MSYADLWTMAGTQAIKLTGGPDIPFNYGRTDDADNNKCPANGrLPDATQGAEHLRDVFYRMGFGDKEIVALSGAHTLGS 168
Cdd:PLN03030 114 VSCADILALAARDSVVLTNGLTWPVPTGRRDGRVSLASDASN-LPGFTDSIDVQKQKFAAKGLNTQDLVTLVGGHTIGT 191
 
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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