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Conserved domains on  [gi|937928460|dbj|BAT03377|]
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Os07g0694700 [Oryza sativa Japonica Group]

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 ...
 3-248 4.84e-153

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 PLN02364:

Pssm-ID: 444739  Cd Length: 250  Bit Score: 426.03  E-value: 4.84e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   3 SKSYPTVSDEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLL 82
Cdd:PLN02364   2 TKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  83 DPIKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFSAQMGLSDKDIVALSG 162
Cdd:PLN02364  82 DPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 163 GHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLK 242
Cdd:PLN02364 162 AHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMK 241


                 ....*.
gi 937928460 243 LSELGF 248
Cdd:PLN02364 242 LSELGF 247
 
Name Accession Description Interval E-value
PLN02364 PLN02364
L-ascorbate peroxidase 1
 3-248 4.84e-153

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 426.03  E-value: 4.84e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   3 SKSYPTVSDEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLL 82
Cdd:PLN02364   2 TKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  83 DPIKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFSAQMGLSDKDIVALSG 162
Cdd:PLN02364  82 DPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 163 GHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLK 242
Cdd:PLN02364 162 AHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMK 241


                 ....*.
gi 937928460 243 LSELGF 248
Cdd:PLN02364 242 LSELGF 247
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 6-251 3.66e-147

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: 411.21  E-value: 3.66e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   6 YPTVS-DEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDP 84
Cdd:cd00691    1 APVVSaAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  85 IKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEP---PPEGRLPDATQGSDHLRQVFsAQMGLSDKDIVALS 161
Cdd:cd00691   81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVF-YRMGFNDQEIVALS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 162 GGHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEK----EGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYA 237
Cdd:cd00691  160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                        250
                 ....*....|....
gi 937928460 238 EAHLKLSELGFAEE 251
Cdd:cd00691  240 EAHKKLSELGVPFP 253
peroxidase pfam00141
Peroxidase;
27-228 6.62e-55

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 174.68  E-value: 6.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   27 LIAEKNCAPLMLRLAWHSAGTfdvssrtGGPFGTM---KNPGEQSHAANAGLDIAVRLLDPIKDQLP-----ILSYADFY 98
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   99 QLAGVVAVEVTGGPEVPFHPGRQDKPEPPPE---GRLPDATQGSDHLRQVFsAQMGLSDKDIVALSGGHTLGRCHKErsg 175
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHKN--- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937928460  176 fegawtsnpLIfdnsyftelvsgEKEGLlqLPSDKALMADPAFRPLVEKYAAD 228
Cdd:pfam00141 158 ---------LL------------DGRGL--LTSDQALLSDPRTRALVERYAAD 187
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 34-244 3.88e-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: 100.77  E-value: 3.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   34 APLMLRLAWHSAGTFDV-SSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDPIKDQL-PILSYADFYQLAGVVAVEVTGG 111
Cdd:TIGR00198  80 GGLFIRMAWHAAGTYRIaDGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  112 PEVPFHPGRQDKPEPP-------------------------------------PEG--RLPDATQGSDHLRQVFsAQMGL 152
Cdd:TIGR00198 160 KVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaatemgliyvnPEGpdGHPDPLCTAQDIRTTF-ARMGM 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  153 SDKDIVAL-SGGHTLGRCHKE-----------------------------------RSGFEGAWTSNPLIFDNSYFTELV 196
Cdd:TIGR00198 239 NDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhnqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLF 318

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937928460  197 SGEKE------GLLQ------------------------LPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLKLS 244
Cdd:TIGR00198 319 NYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
35-243 1.56e-22

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 95.96  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  35 PLMLRLAWHSAGTFDVSS-RTGGpfGTmknpGEQSHAA------NAGLDIAVRLLDPIK----DQlpiLSYADFYQLAGV 103
Cdd:COG0376   89 PLFIRMAWHSAGTYRIGDgRGGA--GG----GQQRFAPlnswpdNANLDKARRLLWPIKqkygNK---ISWADLMILAGN 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 104 VAVEVTGGPEVPFHPGRQDKPEPP------PEGR-LPD--------------ATQ---------GSD----------HLR 143
Cdd:COG0376  160 VALESMGFKTFGFAGGREDVWEPEedvywgPETEwLGDerysgdrelenplaAVQmgliyvnpeGPNgnpdplaaarDIR 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 144 QVFsAQMGLSDKDIVAL-SGGHTLGRCH------------------------KER-----------SGFEGAWTSNPLIF 187
Cdd:COG0376  240 ETF-GRMAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPTQW 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 188 DNSYFT-------ELV-------------------------SGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAfFAD 235
Cdd:COG0376  319 DNGYFDnlfgyewELTkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-FAD 397


                 ....*....
gi 937928460 236 -YAEAHLKL 243
Cdd:COG0376  398 aFARAWFKL 406
 
Name Accession Description Interval E-value
PLN02364 PLN02364
L-ascorbate peroxidase 1
 3-248 4.84e-153

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 426.03  E-value: 4.84e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   3 SKSYPTVSDEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLL 82
Cdd:PLN02364   2 TKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  83 DPIKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFSAQMGLSDKDIVALSG 162
Cdd:PLN02364  82 DPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 163 GHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLK 242
Cdd:PLN02364 162 AHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMK 241


                 ....*.
gi 937928460 243 LSELGF 248
Cdd:PLN02364 242 LSELGF 247
PLN02879 PLN02879
L-ascorbate peroxidase
 1-251 1.55e-150

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 419.47  E-value: 1.55e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   1 MGSKSYPTVSDEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVR 80
Cdd:PLN02879   1 MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  81 LLDPIKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFSaQMGLSDKDIVAL 160
Cdd:PLN02879  81 LLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFG-RMGLNDKDIVAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 161 SGGHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAH 240
Cdd:PLN02879 160 SGGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAH 239

                        250
                 ....*....|.
gi 937928460 241 LKLSELGFAEE 251
Cdd:PLN02879 240 LKLSELGFADK 250
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 6-251 3.66e-147

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: 411.21  E-value: 3.66e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   6 YPTVS-DEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDP 84
Cdd:cd00691    1 APVVSaAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  85 IKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEP---PPEGRLPDATQGSDHLRQVFsAQMGLSDKDIVALS 161
Cdd:cd00691   81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVF-YRMGFNDQEIVALS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 162 GGHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEK----EGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYA 237
Cdd:cd00691  160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                        250
                 ....*....|....
gi 937928460 238 EAHLKLSELGFAEE 251
Cdd:cd00691  240 EAHKKLSELGVPFP 253
PLN02608 PLN02608
L-ascorbate peroxidase
 7-248 5.73e-141

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 396.83  E-value: 5.73e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   7 PTVSDEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDPIK 86
Cdd:PLN02608   4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  87 DQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFSaQMGLSDKDIVALSGGHTL 166
Cdd:PLN02608  84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFY-RMGLSDKDIVALSGGHTL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 167 GRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLKLSEL 246
Cdd:PLN02608 163 GRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSEL 242


                 ..
gi 937928460 247 GF 248
Cdd:PLN02608 243 GF 244
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
 21-245 1.58e-60

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: 191.21  E-value: 1.58e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  21 KRKLRGLIAEKN-CAPLMLRLAWHSAGTFDVSS-RTGGPFGTMKNPGEQSHAANAGLDIAVRLLDPIK---DQLPILSYA 95
Cdd:cd00314    4 KAILEDLITQAGaLAGSLLRLAFHDAGTYDIADgKGGGADGSIRFEPELDRPENGGLDKALRALEPIKsayDGGNPVSRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  96 DFYQLAGVVAVEVT--GGPEVPFHPGRQDKPEPP-----PEGRLPDATQGSDHLRQVFSAqMGLSDKDIVALS-GGHTL- 166
Cdd:cd00314   84 DLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKFKR-MGLSPSELVALSaGAHTLg 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 167 GRCHKERSGFE--GAWTSNPLIFDNSYFTELVSGEKE------------GLLQLPSDKALMADPAFRPLVEKYAADEDAF 232
Cdd:cd00314  163 GKNHGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQEKF 242

                        250
                 ....*....|...
gi 937928460 233 FADYAEAHLKLSE 245
Cdd:cd00314  243 FEDFAKAWIKMVN 255
peroxidase pfam00141
Peroxidase;
27-228 6.62e-55

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 174.68  E-value: 6.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   27 LIAEKNCAPLMLRLAWHSAGTfdvssrtGGPFGTM---KNPGEQSHAANAGLDIAVRLLDPIKDQLP-----ILSYADFY 98
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   99 QLAGVVAVEVTGGPEVPFHPGRQDKPEPPPE---GRLPDATQGSDHLRQVFsAQMGLSDKDIVALSGGHTLGRCHKErsg 175
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHKN--- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937928460  176 fegawtsnpLIfdnsyftelvsgEKEGLlqLPSDKALMADPAFRPLVEKYAAD 228
Cdd:pfam00141 158 ---------LL------------DGRGL--LTSDQALLSDPRTRALVERYAAD 187
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
 59-247 6.74e-34

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: 123.78  E-value: 6.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  59 GTMKNPGEQSHAANAGLDiAVRLLDPIKDQL-----PILSYADFYQLAGVVAVEVTGGP--EVPFhpGRQD--KPEPPPE 129
Cdd:cd00693   57 STANNTSEKDAPPNLSLR-GFDVIDDIKAALeaacpGVVSCADILALAARDAVVLAGGPsyEVPL--GRRDgrVSSANDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 130 GRLPDATQGSDHLRQVFsAQMGLSDKDIVALSGGHTLGRCH----KER-SGFEGAWTSNPLI------------------ 186
Cdd:cd00693  134 GNLPSPFFSVSQLISLF-ASKGLTVTDLVALSGAHTIGRAHcssfSDRlYNFSGTGDPDPTLdpayaaqlrkkcpaggdd 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937928460 187 -------------FDNSYFTELVSGekEGLLQlpSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLKLSELG 247
Cdd:cd00693  213 dtlvpldpgtpntFDNSYYKNLLAG--RGLLT--SDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
catalase_peroxidase_1 cd00649
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 35-243 5.04e-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: 5.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  35 PLMLRLAWHSAGTFDVSSRTGGpfgtmKNPGEQSHAA------NAGLDIAVRLLDPIKDQL-PILSYADFYQLAGVVAVE 107
Cdd:cd00649   71 PLFIRMAWHSAGTYRIADGRGG-----AGTGQQRFAPlnswpdNVNLDKARRLLWPIKQKYgNKISWADLMILAGNVALE 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 108 VTGGPEVPFHPGRQDKPEPP--------------------------------------PEG--RLPDATQGSDHLRQVFs 147
Cdd:cd00649  146 SMGFKTFGFAGGREDVWEPDedvywgpekewladkrysgdrdlenplaavqmgliyvnPEGpdGNPDPLAAAKDIRETF- 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 148 AQMGLSDKDIVAL-SGGHTLGRCH---------KE--------------------------RSGFEGAWTSNPLIFDNSY 191
Cdd:cd00649  225 ARMAMNDEETVALiAGGHTFGKTHgagpashvgPEpeaapieqqglgwknsygtgkgkdtiTSGLEGAWTPTPTKWDNNY 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 192 FTELVS--------------------------------GEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEA 239
Cdd:cd00649  305 LKNLFGyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKA 384


                 ....
gi 937928460 240 HLKL 243
Cdd:cd00649  385 WFKL 388
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 34-244 3.88e-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: 100.77  E-value: 3.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   34 APLMLRLAWHSAGTFDV-SSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDPIKDQL-PILSYADFYQLAGVVAVEVTGG 111
Cdd:TIGR00198  80 GGLFIRMAWHAAGTYRIaDGRGGAATGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  112 PEVPFHPGRQDKPEPP-------------------------------------PEG--RLPDATQGSDHLRQVFsAQMGL 152
Cdd:TIGR00198 160 KVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaatemgliyvnPEGpdGHPDPLCTAQDIRTTF-ARMGM 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  153 SDKDIVAL-SGGHTLGRCHKE-----------------------------------RSGFEGAWTSNPLIFDNSYFTELV 196
Cdd:TIGR00198 239 NDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhnqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLF 318

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937928460  197 SGEKE------GLLQ------------------------LPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLKLS 244
Cdd:TIGR00198 319 NYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
35-243 1.56e-22

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 95.96  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  35 PLMLRLAWHSAGTFDVSS-RTGGpfGTmknpGEQSHAA------NAGLDIAVRLLDPIK----DQlpiLSYADFYQLAGV 103
Cdd:COG0376   89 PLFIRMAWHSAGTYRIGDgRGGA--GG----GQQRFAPlnswpdNANLDKARRLLWPIKqkygNK---ISWADLMILAGN 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 104 VAVEVTGGPEVPFHPGRQDKPEPP------PEGR-LPD--------------ATQ---------GSD----------HLR 143
Cdd:COG0376  160 VALESMGFKTFGFAGGREDVWEPEedvywgPETEwLGDerysgdrelenplaAVQmgliyvnpeGPNgnpdplaaarDIR 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 144 QVFsAQMGLSDKDIVAL-SGGHTLGRCH------------------------KER-----------SGFEGAWTSNPLIF 187
Cdd:COG0376  240 ETF-GRMAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPTQW 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 188 DNSYFT-------ELV-------------------------SGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAfFAD 235
Cdd:COG0376  319 DNGYFDnlfgyewELTkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-FAD 397


                 ....*....
gi 937928460 236 -YAEAHLKL 243
Cdd:COG0376  398 aFARAWFKL 406
PRK15061 PRK15061
catalase/peroxidase;
35-243 5.70e-22

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 94.44  E-value: 5.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  35 PLMLRLAWHSAGTFdvssRTG---GPFGTmknpGEQSHAA------NAGLDIAVRLLDPIK----DQlpiLSYADFYQLA 101
Cdd:PRK15061  83 PLFIRMAWHSAGTY----RIGdgrGGAGG----GQQRFAPlnswpdNVNLDKARRLLWPIKqkygNK---ISWADLMILA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 102 GVVAVEVTGGPEVPFHPGRQDKPEP---------------------------P------------PEGrlPDAT---QGS 139
Cdd:PRK15061 152 GNVALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEG--PNGNpdpLAA 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 140 DH-LRQVFsAQMGLSDKDIVAL-SGGHTLGRCH-------------------------------KER----SGFEGAWTS 182
Cdd:PRK15061 230 ARdIRETF-ARMAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgKGAdtitSGLEGAWTT 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 183 NPLIFDNSYFTEL--------------------------------VSGEKEGLLQLPSDKALMADPAFRPLVEKYAADED 230
Cdd:PRK15061 309 TPTQWDNGYFENLfgyeweltkspagawqwvpkdgaaedtvpdahDPSKKHAPTMLTTDLALRFDPEYEKISRRFLENPE 388

                        330
                 ....*....|....
gi 937928460 231 AfFAD-YAEAHLKL 243
Cdd:PRK15061 389 E-FADaFARAWFKL 401
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
 38-248 7.48e-21

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: 89.38  E-value: 7.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  38 LRLAWHSAGTFDVSSRTGgPFGTMKNPG--------EQSHAANAGLDIAVRLLDPIKDQLPIlSYADFYQLAGVVAV-EV 108
Cdd:cd00692   42 LRLTFHDAIGFSPALAAG-QFGGGGADGsivlfddiETAFHANIGLDEIVEALRPFHQKHNV-SMADFIQFAGAVAVsNC 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 109 TGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFsAQMGLSDKDIVALSGGHTLGRCHKERSGFEGA-WTSNPLIF 187
Cdd:cd00692  120 PGAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARF-ADAGFSPDELVALLAAHSVAAQDFVDPSIAGTpFDSTPGVF 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937928460 188 DNSYFTE----------------LVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLKLSELGF 248
Cdd:cd00692  199 DTQFFIEtllkgtafpgsggnqgEVESPLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
 38-198 1.18e-14

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: 71.34  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  38 LRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDPIkdQLPILSYADFYQLAGVVAVEVTGGPEVPFH 117
Cdd:cd08201   46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNF--YSPRSSMADLIAMGVVTSVASCGGPVVPFR 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 118 PGRQDKPEPPPEGrLPDATQGSDHLRQVFsAQMGLSDKDIVALSG-GHTLGRCHKER-----------SGFEGAWTSNPl 185
Cdd:cd08201  124 AGRIDATEAGQAG-VPEPQTDLGTTTESF-RRQGFSTSEMIALVAcGHTLGGVHSEDfpeivppgsvpDTVLQFFDTTI- 200

                        170
                 ....*....|...
gi 937928460 186 IFDNSYFTELVSG 198
Cdd:cd08201  201 QFDNKVVTEYLSG 213
PLN03030 PLN03030
cationic peroxidase; Provisional
 81-247 2.19e-08

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 53.81  E-value: 2.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  81 LLDPIKDQLP-----ILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDkpepppeGR---------LPDATQGSDHLRQVF 146
Cdd:PLN03030  98 VIDDAKTQLEaacpgVVSCADILALAARDSVVLTNGLTWPVPTGRRD-------GRvslasdasnLPGFTDSIDVQKQKF 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460 147 SAQmGLSDKDIVALSGGHTLG---------RCHKERSGFEGAwtsNPLI------------------------------- 186
Cdd:PLN03030 171 AAK-GLNTQDLVTLVGGHTIGttacqffryRLYNFTTTGNGA---DPSIdasfvpqlqalcpqngdgsrrialdtgssnr 246

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937928460 187 FDNSYFTELVSGekEGLLQlpSDKALMADPAFRPLVEKYAADED----AFFADYAEAHLKLSELG 247
Cdd:PLN03030 247 FDASFFSNLKNG--RGILE--SDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIG 307
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 41-196 2.10e-04

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: 42.22  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460   41 AWHSAGTFDVSSRTGGPFGT------MKNpGEQSHAANAGLDIAVrlLDPIKDQLPI--LSYADFYQLAGVVAVE---VT 109
Cdd:TIGR00198 455 AWASASTFRSSDYRGGANGArirlepQKN-WPVNEPTRLAKVLAV--LEKIQAEFAKgpVSLADLIVLGGGAAVEkaaLD 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937928460  110 GGPE--VPFHPGRQDKP------------EPPPEG----RLPDATQGSDHLRQVFSAQMGLSDKDIVALSGG-HTLGRCH 170
Cdd:TIGR00198 532 AGISvnVPFLPGRVDATqamtdaesftplEPIADGfrnyLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGmRVLGANH 611

                         170       180
                  ....*....|....*....|....*.
gi 937928460  171 KERSgfEGAWTSNPLIFDNSYFTELV 196
Cdd:TIGR00198 612 GGSK--HGVFTDRVGVLSNDFFVNLL 635
 
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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