|
Name |
Accession |
Description |
Interval |
E-value |
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
39-284 |
4.49e-148 |
|
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: 415.45 E-value: 4.49e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 39 YPTVSADY-QDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 117
Cdd:cd00691 1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 118 LKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEP---PPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALS 194
Cdd:cd00691 81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 195 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYA 270
Cdd:cd00691 160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239
|
250
....*....|....
gi 1912456256 271 EAHQKLSELGFADA 284
Cdd:cd00691 240 EAHKKLSELGVPFP 253
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
37-283 |
6.17e-145 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 407.52 E-value: 6.17e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 37 KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 116
Cdd:PLN02879 4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 117 PLKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALSGG 196
Cdd:PLN02879 84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 197 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:PLN02879 163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242
|
....*..
gi 1912456256 277 SELGFAD 283
Cdd:PLN02879 243 SELGFAD 249
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
60-261 |
4.77e-55 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 176.60 E-value: 4.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 60 FIAEKRCAPLMLRLAFHSAGTfdkgtktGGPFGTI---KHPAELAHSANNGLDIAVRLLEPLKAEFP-----ILSYADFY 131
Cdd:pfam00141 9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGPKVPFHPGREDKPEPPPE---GRLPDPTKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAHKersg 208
Cdd:pfam00141 82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHK---- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1912456256 209 fegpwtsnplifdnsyftELLSGekEGLlqLPSDKALFSDPVFRPLVDKYAAD 261
Cdd:pfam00141 157 ------------------NLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
67-277 |
3.23e-20 |
|
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: 90.76 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 67 APLMLRLAFHSAGTFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGG 144
Cdd:TIGR00198 80 GGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 145 PKVPFHPGREDKPEPP-------------------------------------PEG--RLPDPTKGSDHLRDVFGKaMGL 185
Cdd:TIGR00198 160 KVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaatemgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 186 TDQDIVAL-SGGHTIGAAHKE-----------------------------------RSGFEGPWTSNPLIFDNSYFTELL 229
Cdd:TIGR00198 239 NDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhnqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLF 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1912456256 230 SGEKE------GLLQ------------------------LPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLS 277
Cdd:TIGR00198 319 NYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
68-276 |
6.05e-16 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 77.85 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 68 PLMLRLAFHSAGTFDKGTKTGGpfgtikhpaelAHSAN-----------NG-LDIAVRLLEPLKAEF-PILSYADFYQLA 134
Cdd:COG0376 89 PLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLMILA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 135 GVVAVEVTGGPKVPFHPGREDKPEPP--------------------------------------PEG--RLPDPTKGSDH 174
Cdd:COG0376 158 GNVALESMGFKTFGFAGGREDVWEPEedvywgpetewlgderysgdrelenplaavqmgliyvnPEGpnGNPDPLAAARD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 175 LRDVFGKaMGLTDQDIVAL-SGGHTIGAAH------------------------KER-----------SGFEGPWTSNPL 218
Cdd:COG0376 238 IRETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 219 IFDNSYFTELL--------------------------------SGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAfF 266
Cdd:COG0376 317 QWDNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-F 395
|
330
....*....|.
gi 1912456256 267 AD-YAEAHQKL 276
Cdd:COG0376 396 ADaFARAWFKL 406
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
39-284 |
4.49e-148 |
|
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: 415.45 E-value: 4.49e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 39 YPTVSADY-QDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 117
Cdd:cd00691 1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 118 LKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEP---PPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALS 194
Cdd:cd00691 81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 195 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYA 270
Cdd:cd00691 160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239
|
250
....*....|....
gi 1912456256 271 EAHQKLSELGFADA 284
Cdd:cd00691 240 EAHKKLSELGVPFP 253
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
37-283 |
6.17e-145 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 407.52 E-value: 6.17e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 37 KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 116
Cdd:PLN02879 4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 117 PLKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALSGG 196
Cdd:PLN02879 84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 197 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:PLN02879 163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242
|
....*..
gi 1912456256 277 SELGFAD 283
Cdd:PLN02879 243 SELGFAD 249
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
37-284 |
1.37e-142 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 401.38 E-value: 1.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 37 KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 116
Cdd:PLN02364 3 KNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 117 PLKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKAMGLTDQDIVALSGG 196
Cdd:PLN02364 83 PIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 197 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:PLN02364 163 HTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242
|
....*...
gi 1912456256 277 SELGFADA 284
Cdd:PLN02364 243 SELGFADA 250
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
40-281 |
5.17e-136 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 386.04 E-value: 5.17e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 40 PTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLK 119
Cdd:PLN02608 4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 120 AEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALSGGHTI 199
Cdd:PLN02608 84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFYR-MGLSDKDIVALSGGHTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 200 GAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLSEL 279
Cdd:PLN02608 163 GRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSEL 242
|
..
gi 1912456256 280 GF 281
Cdd:PLN02608 243 GF 244
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
51-278 |
5.79e-65 |
|
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: 204.31 E-value: 5.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 51 EKAKKKLRGFIAE-KRCAPLMLRLAFHSAGTFDKGT-KTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFP---IL 125
Cdd:cd00314 1 DAIKAILEDLITQaGALAGSLLRLAFHDAGTYDIADgKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggnPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 126 SYADFYQLAGVVAVEVT--GGPKVPFHPGREDKPEPP-----PEGRLPDPTKGSDHLRDVFgKAMGLTDQDIVALS-GGH 197
Cdd:cd00314 81 SRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKF-KRMGLSPSELVALSaGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 198 TI-GAAHKERSGFE--GPWTSNPLIFDNSYFTELLSGEKE------------GLLQLPSDKALFSDPVFRPLVDKYAADE 262
Cdd:cd00314 160 TLgGKNHGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQ 239
|
250
....*....|....*.
gi 1912456256 263 DAFFADYAEAHQKLSE 278
Cdd:cd00314 240 EKFFEDFAKAWIKMVN 255
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
60-261 |
4.77e-55 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 176.60 E-value: 4.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 60 FIAEKRCAPLMLRLAFHSAGTfdkgtktGGPFGTI---KHPAELAHSANNGLDIAVRLLEPLKAEFP-----ILSYADFY 131
Cdd:pfam00141 9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGPKVPFHPGREDKPEPPPE---GRLPDPTKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAHKersg 208
Cdd:pfam00141 82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHK---- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1912456256 209 fegpwtsnplifdnsyftELLSGekEGLlqLPSDKALFSDPVFRPLVDKYAAD 261
Cdd:pfam00141 157 ------------------NLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
47-280 |
9.09e-33 |
|
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: 122.24 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 47 QDAVEKAkkklrgFIAEKRCAPLMLRLAFHSAgtFDKG-------TKTGGPfgtikhPAELAHSANNGL------DIAVR 113
Cdd:cd00693 19 RSVVRAA------VKADPRLAAALLRLHFHDC--FVRGcdasvllDSTANN------TSEKDAPPNLSLrgfdviDDIKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 114 LLEplkAEFP-ILSYADFYQLAGVVAVEVTGGP--KVPFhpGRED--KPEPPPEGRLPDPTKGSDHLRDVFgKAMGLTDQ 188
Cdd:cd00693 85 ALE---AACPgVVSCADILALAARDAVVLAGGPsyEVPL--GRRDgrVSSANDVGNLPSPFFSVSQLISLF-ASKGLTVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 189 DIVALSGGHTIGAAH----KER-SGFEG--------------------PWTSN-----------PLIFDNSYFTELLSGe 232
Cdd:cd00693 159 DLVALSGAHTIGRAHcssfSDRlYNFSGtgdpdptldpayaaqlrkkcPAGGDddtlvpldpgtPNTFDNSYYKNLLAG- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1912456256 233 kEGLLQlpSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELG 280
Cdd:cd00693 238 -RGLLT--SDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
|
|
| ligninase |
cd00692 |
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ... |
71-281 |
2.83e-26 |
|
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: 105.56 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 71 LRLAFHSAGTFDK----GTKTGG-------PFGTIkhpaELAHSANNGLDIAVRLLEPLKAEFPIlSYADFYQLAGVVAV 139
Cdd:cd00692 42 LRLTFHDAIGFSPalaaGQFGGGgadgsivLFDDI----ETAFHANIGLDEIVEALRPFHQKHNV-SMADFIQFAGAVAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 140 -EVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKAmGLTDQDIVALSGGHTIGAAHKERSGFEG-PWTSNP 217
Cdd:cd00692 117 sNCPGAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARFADA-GFSPDELVALLAAHSVAAQDFVDPSIAGtPFDSTP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 218 LIFDNSYFTE-LLSGE---------------KEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGF 281
Cdd:cd00692 196 GVFDTQFFIEtLLKGTafpgsggnqgevespLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
68-276 |
1.02e-21 |
|
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: 93.91 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 68 PLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNG-LDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGGP 145
Cdd:cd00649 71 PLFIRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVnLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 146 KVPFHPGREDKPEPP--------------------------------------PEG--RLPDPTKGSDHLRDVFGKaMGL 185
Cdd:cd00649 151 TFGFAGGREDVWEPDedvywgpekewladkrysgdrdlenplaavqmgliyvnPEGpdGNPDPLAAAKDIRETFAR-MAM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 186 TDQDIVAL-SGGHTIGAAH---------KE--------------------------RSGFEGPWTSNPLIFDNSYFTELL 229
Cdd:cd00649 230 NDEETVALiAGGHTFGKTHgagpashvgPEpeaapieqqglgwknsygtgkgkdtiTSGLEGAWTPTPTKWDNNYLKNLF 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1912456256 230 S--------------------------------GEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:cd00649 310 GyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKL 388
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
67-277 |
3.23e-20 |
|
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: 90.76 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 67 APLMLRLAFHSAGTFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGG 144
Cdd:TIGR00198 80 GGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 145 PKVPFHPGREDKPEPP-------------------------------------PEG--RLPDPTKGSDHLRDVFGKaMGL 185
Cdd:TIGR00198 160 KVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaatemgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 186 TDQDIVAL-SGGHTIGAAHKE-----------------------------------RSGFEGPWTSNPLIFDNSYFTELL 229
Cdd:TIGR00198 239 NDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhnqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLF 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1912456256 230 SGEKE------GLLQ------------------------LPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLS 277
Cdd:TIGR00198 319 NYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
71-247 |
4.48e-17 |
|
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.
Pssm-ID: 173829 Cd Length: 264 Bit Score: 79.05 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 71 LRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAefPILSYADFYQLAGVVAVEVTGGPKVPFH 150
Cdd:cd08201 46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNFYS--PRSSMADLIAMGVVTSVASCGGPVVPFR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 151 PGREDKPEPPPEGrLPDPTKGSDHLRDVFGKaMGLTDQDIVALSG-GHTIGAAHKER-----------SGFEGPWTSNPl 218
Cdd:cd08201 124 AGRIDATEAGQAG-VPEPQTDLGTTTESFRR-QGFSTSEMIALVAcGHTLGGVHSEDfpeivppgsvpDTVLQFFDTTI- 200
|
170 180 190
....*....|....*....|....*....|....*
gi 1912456256 219 IFDNSYFTELLSGEKEGLL------QLPSDKALFS 247
Cdd:cd08201 201 QFDNKVVTEYLSGTTNNPLvvgpnnTTNSDLRIFS 235
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
68-276 |
2.17e-16 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 79.03 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 68 PLMLRLAFHSAGTFDKGTKTGGpfgtikhpaelahsANNG---------------LDIAVRLLEPLKAEF-PILSYADFY 131
Cdd:PRK15061 83 PLFIRMAWHSAGTYRIGDGRGG--------------AGGGqqrfaplnswpdnvnLDKARRLLWPIKQKYgNKISWADLM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGPKVPFHPGREDKPEP---------------------------P------------PEG--RLPDPTK 170
Cdd:PRK15061 149 ILAGNVALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEGpnGNPDPLA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 171 GSDHLRDVFGKaMGLTDQDIVAL-SGGHTIGAAH-------------------------------KER----SGFEGPWT 214
Cdd:PRK15061 229 AARDIRETFAR-MAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgKGAdtitSGLEGAWT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 215 SNPLIFDNSYFTELLSGEKE------GLLQ--------------------------LPSDKALFSDPVFRPLVDKYAADE 262
Cdd:PRK15061 308 TTPTQWDNGYFENLFGYEWEltkspaGAWQwvpkdgaaedtvpdahdpskkhaptmLTTDLALRFDPEYEKISRRFLENP 387
|
330
....*....|....*
gi 1912456256 263 DAfFAD-YAEAHQKL 276
Cdd:PRK15061 388 EE-FADaFARAWFKL 401
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
68-276 |
6.05e-16 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 77.85 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 68 PLMLRLAFHSAGTFDKGTKTGGpfgtikhpaelAHSAN-----------NG-LDIAVRLLEPLKAEF-PILSYADFYQLA 134
Cdd:COG0376 89 PLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLMILA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 135 GVVAVEVTGGPKVPFHPGREDKPEPP--------------------------------------PEG--RLPDPTKGSDH 174
Cdd:COG0376 158 GNVALESMGFKTFGFAGGREDVWEPEedvywgpetewlgderysgdrelenplaavqmgliyvnPEGpnGNPDPLAAARD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 175 LRDVFGKaMGLTDQDIVAL-SGGHTIGAAH------------------------KER-----------SGFEGPWTSNPL 218
Cdd:COG0376 238 IRETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 219 IFDNSYFTELL--------------------------------SGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAfF 266
Cdd:COG0376 317 QWDNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-F 395
|
330
....*....|.
gi 1912456256 267 AD-YAEAHQKL 276
Cdd:COG0376 396 ADaFARAWFKL 406
|
|
| PLN03030 |
PLN03030 |
cationic peroxidase; Provisional |
60-280 |
5.25e-10 |
|
cationic peroxidase; Provisional
Pssm-ID: 215545 [Multi-domain] Cd Length: 324 Bit Score: 59.20 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 60 FIAEKRCAPLMLRLAFHSAgtFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEFP-ILSYADFYQLAGVV 137
Cdd:PLN03030 49 FQSNPAIAPGLLRMHFHDC--FVRGCDASILIdGSNTEKTALPNLLLRGYDVIDDAKTQLEAACPgVVSCADILALAARD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 138 AVEVTGGPKVPFHPGREDkpepppeGR---------LPDPTKGSDHLRDVFGkAMGLTDQDIVALSGGHTIGAAH----- 203
Cdd:PLN03030 127 SVVLTNGLTWPVPTGRRD-------GRvslasdasnLPGFTDSIDVQKQKFA-AKGLNTQDLVTLVGGHTIGTTAcqffr 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 204 -----------------------------------KERSGFEgpwTSNPLIFDNSYFTELLSGekEGLLQlpSDKALFSD 248
Cdd:PLN03030 199 yrlynftttgngadpsidasfvpqlqalcpqngdgSRRIALD---TGSSNRFDASFFSNLKNG--RGILE--SDQKLWTD 271
|
250 260 270
....*....|....*....|....*....|....*.
gi 1912456256 249 PVFRPLVDKYAADED----AFFADYAEAHQKLSELG 280
Cdd:PLN03030 272 ASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIG 307
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
74-229 |
1.52e-05 |
|
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: 46.46 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 74 AFHSAGTFDKGTKTGGPFGT-----------IKHPAELAHsanngldiAVRLLEPLKAEFPI--LSYADFYQLAGVVAVE 140
Cdd:TIGR00198 455 AWASASTFRSSDYRGGANGArirlepqknwpVNEPTRLAK--------VLAVLEKIQAEFAKgpVSLADLIVLGGGAAVE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 141 ---VTGG--PKVPFHPGREDKPEPPPEGRLPDPTKG-SDHLRDVFGK---------------AMGLTDQDIVALSGGHTI 199
Cdd:TIGR00198 527 kaaLDAGisVNVPFLPGRVDATQAMTDAESFTPLEPiADGFRNYLKRdyavtpeellldkaqLLTLTAPEMTVLIGGMRV 606
|
170 180 190
....*....|....*....|....*....|
gi 1912456256 200 GAAHKERSGFeGPWTSNPLIFDNSYFTELL 229
Cdd:TIGR00198 607 LGANHGGSKH-GVFTDRVGVLSNDFFVNLL 635
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
70-279 |
1.43e-04 |
|
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: 42.60 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 70 MLRLAFHSAGTFDKGTKTGGPFG-----------TIKHPAELAHsanngldiAVRLLEPLKAEFPI-------LSYADFY 131
Cdd:cd08200 33 LVSTAWASASTFRNSDKRGGANGarirlapqkdwEVNEPEELAK--------VLAVLEGIQKEFNEsqsggkkVSLADLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGP-----KVPFHPGREDKP------------EPPPEG-----RLPDPTKGSDHLRDvfgKA--MGLTD 187
Cdd:cd08200 105 VLGGCAAVEKAAKDagvdiKVPFTPGRTDATqeqtdvesfevlEPKADGfrnylKKGYRVPPEEMLVD---KAqlLTLTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 188 QDIVALSGG-HTIGAAHKERSgfEGPWTSNPLIFDNSYFTELL--------SGEKEGLLQL-------PSDKALFSDPVF 251
Cdd:cd08200 182 PEMTVLVGGlRVLGANYGGSK--HGVFTDRPGVLTNDFFVNLLdmstewkpADEDDGLFEGrdrktgeVKWTATRVDLVF 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 1912456256 252 ------RPLVDKYAAD--EDAFFADYAEAHQKLSEL 279
Cdd:cd08200 260 gsnselRAVAEVYASDdaQEKFVKDFVAAWTKVMNL 295
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
70-155 |
4.10e-03 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 38.58 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 70 MLRLAFHSAGTFDKGTKTGGPFG-----------TIKHPAELAHsanngldiAVRLLEPLKAEFPI-------LSYADFY 131
Cdd:PRK15061 458 LVSTAWASASTFRGSDKRGGANGarirlapqkdwEVNEPAQLAK--------VLAVLEGIQAEFNAaqsggkkVSLADLI 529
|
90 100 110
....*....|....*....|....*....|...
gi 1912456256 132 QLAGVVAVE---------VTggpkVPFHPGRED 155
Cdd:PRK15061 530 VLGGNAAVEqaakaaghdVT----VPFTPGRTD 558
|
|
|