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Conserved domains on  [gi|186478248|ref|NP_001117244|]
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ascorbate peroxidase 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02364 PLN02364
L-ascorbate peroxidase 1
1-250 0e+00

L-ascorbate peroxidase 1


:

Pssm-ID: 166005  Cd Length: 250  Bit Score: 521.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
Cdd:PLN02364   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
Cdd:PLN02364  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
Cdd:PLN02364 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
                        250
                 ....*....|
gi 186478248 241 KLSELGFADA 250
Cdd:PLN02364 241 KLSELGFADA 250
 
Name Accession Description Interval E-value
PLN02364 PLN02364
L-ascorbate peroxidase 1
1-250 0e+00

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 521.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
Cdd:PLN02364   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
Cdd:PLN02364  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
Cdd:PLN02364 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
                        250
                 ....*....|
gi 186478248 241 KLSELGFADA 250
Cdd:PLN02364 241 KLSELGFADA 250
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
5-250 1.17e-156

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: 435.09  E-value: 1.17e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   5 YPTVSEDY-KKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDP 83
Cdd:cd00691    1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  84 IREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQP---PPEGRLPDATKGCDHLRDVFAkQMGLSDKDIVALS 160
Cdd:cd00691   81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFY-RMGFNDQEIVALS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEK----EGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYA 236
Cdd:cd00691  160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239
                        250
                 ....*....|....
gi 186478248 237 EAHMKLSELGFADA 250
Cdd:cd00691  240 EAHKKLSELGVPFP 253
peroxidase pfam00141
Peroxidase;
20-227 1.14e-53

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 171.59  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   20 RRKLRGLI-AEKNCAPIMVRLAWHSAGTfdcqsrtGGPFG-TMR--FDAEQAHGANSGIHIALRLLDPIREQFP-----T 90
Cdd:pfam00141   2 RSVVRAAFkADPTMGPSLLRLHFHDCFV-------GGCDGsVLLdgFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   91 ISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE---GRLPDATKGCDHLRDVFAkQMGLSDKDIVALSGAHTLGR 167
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRFA-RKGLTAEDLVALSGAHTIGR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  168 CHkdrsgfegawtsnplifdnsyfKELLSGekEGLLQlvSDKALLDDPVFRPLVEKYAAD 227
Cdd:pfam00141 154 AH----------------------KNLLDG--RGLLT--SDQALLSDPRTRALVERYAAD 187
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
11-243 2.61e-23

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: 98.46  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   11 DYKKAVEK-----CRRKLRGLIAEK---------NCAPIMVRLAWHSAGTFDC-QSRTGGPFGTMRFDAEQAHGANSGIH 75
Cdd:TIGR00198  44 DYAEEFQQldlaaVKQDLKHLMTDSqswwpadwgHYGGLFIRMAWHAAGTYRIaDGRGGAATGNQRFAPLNSWPDNVNLD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   76 IALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPP---------------------------- 126
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaa 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  127 ---------PEG--RLPDATKGCDHLRDVFAKqMGLSDKDIVAL-SGAHTLGRCHKD----------------------- 171
Cdd:TIGR00198 204 temgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwh 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  172 ------------RSGFEGAWTSNPLIFDNSYFKELLSGEKE------GLLQ------------------------LVSDK 209
Cdd:TIGR00198 283 nqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADL 362
                         330       340       350
                  ....*....|....*....|....*....|....
gi 186478248  210 ALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLS 243
Cdd:TIGR00198 363 ALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
34-242 4.33e-19

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 85.94  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  34 PIMVRLAWHSAGTF---DcqSRTGGPFGTMRF-------DaeqahgaNSGIHIALRLLDPIREQF-PTISFADFHQLAGV 102
Cdd:COG0376   89 PLFIRMAWHSAGTYrigD--GRGGAGGGQQRFaplnswpD-------NANLDKARRLLWPIKQKYgNKISWADLMILAGN 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 103 VAVEVTGGPDIPFHPGREDKPQP--------------------------P------------PEG--RLPDATKGCDHLR 142
Cdd:COG0376  160 VALESMGFKTFGFAGGREDVWEPeedvywgpetewlgderysgdrelenPlaavqmgliyvnPEGpnGNPDPLAAARDIR 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 143 DVFAKqMGLSDKDIVAL-SGAHTLGRCH------------------------KDR-----------SGFEGAWTSNPLIF 186
Cdd:COG0376  240 ETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPTQW 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 187 DNSYFKELL--------------------------------SGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAfFAD 234
Cdd:COG0376  319 DNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-FAD 397

                 ....*....
gi 186478248 235 -YAEAHMKL 242
Cdd:COG0376  398 aFARAWFKL 406
 
Name Accession Description Interval E-value
PLN02364 PLN02364
L-ascorbate peroxidase 1
1-250 0e+00

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 521.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
Cdd:PLN02364   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
Cdd:PLN02364  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
Cdd:PLN02364 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
                        250
                 ....*....|
gi 186478248 241 KLSELGFADA 250
Cdd:PLN02364 241 KLSELGFADA 250
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
5-250 1.17e-156

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: 435.09  E-value: 1.17e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   5 YPTVSEDY-KKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDP 83
Cdd:cd00691    1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  84 IREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQP---PPEGRLPDATKGCDHLRDVFAkQMGLSDKDIVALS 160
Cdd:cd00691   81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFY-RMGFNDQEIVALS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEK----EGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYA 236
Cdd:cd00691  160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239
                        250
                 ....*....|....
gi 186478248 237 EAHMKLSELGFADA 250
Cdd:cd00691  240 EAHKKLSELGVPFP 253
PLN02879 PLN02879
L-ascorbate peroxidase
1-249 1.74e-151

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 422.16  E-value: 1.74e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
Cdd:PLN02879   2 VKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALS 160
Cdd:PLN02879  82 LDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
Cdd:PLN02879 161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240

                 ....*....
gi 186478248 241 KLSELGFAD 249
Cdd:PLN02879 241 KLSELGFAD 249
PLN02608 PLN02608
L-ascorbate peroxidase
6-247 4.29e-142

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 399.52  E-value: 4.29e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   6 PTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIR 85
Cdd:PLN02608   4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  86 EQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALSGAHTL 165
Cdd:PLN02608  84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFYR-MGLSDKDIVALSGGHTL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 166 GRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSEL 245
Cdd:PLN02608 163 GRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSEL 242

                 ..
gi 186478248 246 GF 247
Cdd:PLN02608 243 GF 244
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
23-244 9.05e-61

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: 191.98  E-value: 9.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  23 LRGLIAEKN-CAPIMVRLAWHSAGTFD-CQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFP---TISFADFH 97
Cdd:cd00314    7 LEDLITQAGaLAGSLLRLAFHDAGTYDiADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggnPVSRADLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  98 QLAGVVAVEVT--GGPDIPFHPGREDKPQPP-----PEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALS-GAHTL-GRC 168
Cdd:cd00314   87 ALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKFKR-MGLSPSELVALSaGAHTLgGKN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 169 HKDRSGFE--GAWTSNPLIFDNSYFKELLSGEKE------------GLLQLVSDKALLDDPVFRPLVEKYAADEDAFFAD 234
Cdd:cd00314  166 HGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQEKFFED 245
                        250
                 ....*....|
gi 186478248 235 YAEAHMKLSE 244
Cdd:cd00314  246 FAKAWIKMVN 255
peroxidase pfam00141
Peroxidase;
20-227 1.14e-53

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 171.59  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   20 RRKLRGLI-AEKNCAPIMVRLAWHSAGTfdcqsrtGGPFG-TMR--FDAEQAHGANSGIHIALRLLDPIREQFP-----T 90
Cdd:pfam00141   2 RSVVRAAFkADPTMGPSLLRLHFHDCFV-------GGCDGsVLLdgFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   91 ISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE---GRLPDATKGCDHLRDVFAkQMGLSDKDIVALSGAHTLGR 167
Cdd:pfam00141  75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRFA-RKGLTAEDLVALSGAHTIGR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  168 CHkdrsgfegawtsnplifdnsyfKELLSGekEGLLQlvSDKALLDDPVFRPLVEKYAAD 227
Cdd:pfam00141 154 AH----------------------KNLLDG--RGLLT--SDQALLSDPRTRALVERYAAD 187
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
58-246 7.25e-31

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: 115.69  E-value: 7.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  58 GTMRFDAEQAHGANSGIHiALRLLDPIREQF-----PTISFADFHQLAGVVAVEVTGGPDIPFHPGRED--KPQPPPEGR 130
Cdd:cd00693   57 STANNTSEKDAPPNLSLR-GFDVIDDIKAALeaacpGVVSCADILALAARDAVVLAGGPSYEVPLGRRDgrVSSANDVGN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 131 LPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLGRCH----KDR-SGFEGAWTSNPLI-------------------- 185
Cdd:cd00693  136 LPSPFFSVSQLISLFASK-GLTVTDLVALSGAHTIGRAHcssfSDRlYNFSGTGDPDPTLdpayaaqlrkkcpaggdddt 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186478248 186 -----------FDNSYFKELLSGekEGLLQlvSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELG 246
Cdd:cd00693  215 lvpldpgtpntFDNSYYKNLLAG--RGLLT--SDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
catalase_peroxidase_1 cd00649
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
34-242 7.41e-26

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: 104.31  E-value: 7.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  34 PIMVRLAWHSAGTFDCQS-RTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGGP 111
Cdd:cd00649   71 PLFIRMAWHSAGTYRIADgRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFK 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 112 DIPFHPGRED--------------------------KPQPP------------PEG--RLPDATKGCDHLRDVFAKqMGL 151
Cdd:cd00649  151 TFGFAGGREDvwepdedvywgpekewladkrysgdrDLENPlaavqmgliyvnPEGpdGNPDPLAAAKDIRETFAR-MAM 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 152 SDKDIVAL-SGAHTLGRCH---------------------------------KDR--SGFEGAWTSNPLIFDNSYFKELL 195
Cdd:cd00649  230 NDEETVALiAGGHTFGKTHgagpashvgpepeaapieqqglgwknsygtgkgKDTitSGLEGAWTPTPTKWDNNYLKNLF 309
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478248 196 S--------------------------------GEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242
Cdd:cd00649  310 GyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKL 388
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
11-243 2.61e-23

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: 98.46  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   11 DYKKAVEK-----CRRKLRGLIAEK---------NCAPIMVRLAWHSAGTFDC-QSRTGGPFGTMRFDAEQAHGANSGIH 75
Cdd:TIGR00198  44 DYAEEFQQldlaaVKQDLKHLMTDSqswwpadwgHYGGLFIRMAWHAAGTYRIaDGRGGAATGNQRFAPLNSWPDNVNLD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   76 IALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPP---------------------------- 126
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaa 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  127 ---------PEG--RLPDATKGCDHLRDVFAKqMGLSDKDIVAL-SGAHTLGRCHKD----------------------- 171
Cdd:TIGR00198 204 temgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwh 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  172 ------------RSGFEGAWTSNPLIFDNSYFKELLSGEKE------GLLQ------------------------LVSDK 209
Cdd:TIGR00198 283 nqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADL 362
                         330       340       350
                  ....*....|....*....|....*....|....
gi 186478248  210 ALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLS 243
Cdd:TIGR00198 363 ALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
PRK15061 PRK15061
catalase/peroxidase;
34-242 1.45e-19

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 87.50  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  34 PIMVRLAWHSAGTFdcqsRT-----GGPFGTMRF-------DaeqahgaNSGIHIALRLLDPIREQF-PTISFADFHQLA 100
Cdd:PRK15061  83 PLFIRMAWHSAGTY----RIgdgrgGAGGGQQRFaplnswpD-------NVNLDKARRLLWPIKQKYgNKISWADLMILA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 101 GVVAVEVTGGPDIPFHPGREDKPQP---------------------------P------------PEG--RLPDATKGCD 139
Cdd:PRK15061 152 GNVALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEGpnGNPDPLAAAR 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 140 HLRDVFAKqMGLSDKDIVAL-SGAHTLGRCH---------------------------------KD--RSGFEGAWTSNP 183
Cdd:PRK15061 232 DIRETFAR-MAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgkgADtiTSGLEGAWTTTP 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 184 LIFDNSYFKELLSGEKE------GLLQ--------------------------LVSDKALLDDPVFRPLVEKYAADEDAf 231
Cdd:PRK15061 311 TQWDNGYFENLFGYEWEltkspaGAWQwvpkdgaaedtvpdahdpskkhaptmLTTDLALRFDPEYEKISRRFLENPEE- 389
                        330
                 ....*....|..
gi 186478248 232 FAD-YAEAHMKL 242
Cdd:PRK15061 390 FADaFARAWFKL 401
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
37-247 2.82e-19

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: 85.14  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  37 VRLAWHSAGTFDCQSRTGGPFGT------MRF-DAEQAHGANSGIHIALRLLDPIrEQFPTISFADFHQLAGVVAV-EVT 108
Cdd:cd00692   42 LRLTFHDAIGFSPALAAGQFGGGgadgsiVLFdDIETAFHANIGLDEIVEALRPF-HQKHNVSMADFIQFAGAVAVsNCP 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 109 GGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLGRCHK-DRSGFEGAWTSNPLIFD 187
Cdd:cd00692  121 GAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARFADA-GFSPDELVALLAAHSVAAQDFvDPSIAGTPFDSTPGVFD 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478248 188 NSYFKE-LLSGE---------------KEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGF 247
Cdd:cd00692  200 TQFFIEtLLKGTafpgsggnqgevespLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
34-242 4.33e-19

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 85.94  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  34 PIMVRLAWHSAGTF---DcqSRTGGPFGTMRF-------DaeqahgaNSGIHIALRLLDPIREQF-PTISFADFHQLAGV 102
Cdd:COG0376   89 PLFIRMAWHSAGTYrigD--GRGGAGGGQQRFaplnswpD-------NANLDKARRLLWPIKQKYgNKISWADLMILAGN 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 103 VAVEVTGGPDIPFHPGREDKPQP--------------------------P------------PEG--RLPDATKGCDHLR 142
Cdd:COG0376  160 VALESMGFKTFGFAGGREDVWEPeedvywgpetewlgderysgdrelenPlaavqmgliyvnPEGpnGNPDPLAAARDIR 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 143 DVFAKqMGLSDKDIVAL-SGAHTLGRCH------------------------KDR-----------SGFEGAWTSNPLIF 186
Cdd:COG0376  240 ETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPTQW 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 187 DNSYFKELL--------------------------------SGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAfFAD 234
Cdd:COG0376  319 DNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-FAD 397

                 ....*....
gi 186478248 235 -YAEAHMKL 242
Cdd:COG0376  398 aFARAWFKL 406
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
37-197 2.88e-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: 64.80  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  37 VRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIreQFPTISFADFHQLAGVVAVEVTGGPDIPFH 116
Cdd:cd08201   46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNF--YSPRSSMADLIAMGVVTSVASCGGPVVPFR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 117 PGREDKPQPPPEGrLPDATKGCDHLRDVFAKQmGLSDKDIVALSG-AHTLGRCHK-----------DRSGFEGAWTSNPl 184
Cdd:cd08201  124 AGRIDATEAGQAG-VPEPQTDLGTTTESFRRQ-GFSTSEMIALVAcGHTLGGVHSedfpeivppgsVPDTVLQFFDTTI- 200
                        170
                 ....*....|...
gi 186478248 185 IFDNSYFKELLSG 197
Cdd:cd08201  201 QFDNKVVTEYLSG 213
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
36-245 6.95e-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: 46.84  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248   36 MVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGANSGIHI--ALRLLDPIREQFPT--ISFADFHQLAGVVAVE---V 107
Cdd:TIGR00198 451 LVCTAWASASTFRSSDYRGGANGArIRLEPQKNWPVNEPTRLakVLAVLEKIQAEFAKgpVSLADLIVLGGGAAVEkaaL 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  108 TGGPDI--PFHPGREDKPQ------------PPPEG----RLPDATKGCDHLRDVFAKQMGLSDKDIVAL-SGAHTLGRC 168
Cdd:TIGR00198 531 DAGISVnvPFLPGRVDATQamtdaesftplePIADGfrnyLKRDYAVTPEELLLDKAQLLTLTAPEMTVLiGGMRVLGAN 610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  169 HKDRSgfEGAWTSNPLIFDNSYF----------------KELLSG--EKEGLLQLVSDKALL---DDPVFRPLVEKYAAD 227
Cdd:TIGR00198 611 HGGSK--HGVFTDRVGVLSNDFFvnlldmayewraadnnRYLFEGgdRQTGEVKWTATRVDLvfgSNSILRAVAEVYAQD 688
                         250       260
                  ....*....|....*....|
gi 186478248  228 E--DAFFADYAEAHMKLSEL 245
Cdd:TIGR00198 689 DarEKFVKDFVAAWTKVMNL 708
PLN03030 PLN03030
cationic peroxidase; Provisional
90-246 3.41e-05

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 44.18  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  90 TISFADFHQLAGVVAVEVTGGPDIPFHPGREDkpqpppeGR---------LPDATKGCDHLRDVFAKQmGLSDKDIVALS 160
Cdd:PLN03030 113 VVSCADILALAARDSVVLTNGLTWPVPTGRRD-------GRvslasdasnLPGFTDSIDVQKQKFAAK-GLNTQDLVTLV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLG---------RCHKDRSGFEGAwtsNPLI-------------------------------FDNSYFKELLSGekE 200
Cdd:PLN03030 185 GGHTIGttacqffryRLYNFTTTGNGA---DPSIdasfvpqlqalcpqngdgsrrialdtgssnrFDASFFSNLKNG--R 259
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 186478248 201 GLLQlvSDKALLDDPVFRPLVEKYAADED----AFFADYAEAHMKLSELG 246
Cdd:PLN03030 260 GILE--SDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIG 307
PRK15061 PRK15061
catalase/peroxidase;
36-124 6.95e-04

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 40.51  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248  36 MVRLAWHSAGTFdcqsRtggpfGT-MRfdaeqaHGANsGIHIAL------------RL------LDPIREQFPT------ 90
Cdd:PRK15061 458 LVSTAWASASTF----R-----GSdKR------GGAN-GARIRLapqkdwevnepaQLakvlavLEGIQAEFNAaqsggk 521
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 186478248  91 -ISFADFHQLAGVVAVE---VTGGPDI--PFHPGREDKPQ 124
Cdd:PRK15061 522 kVSLADLIVLGGNAAVEqaaKAAGHDVtvPFTPGRTDATQ 561
 
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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