|
Name |
Accession |
Description |
Interval |
E-value |
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
78-344 |
1.02e-143 |
|
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: 409.67 E-value: 1.02e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 78 CAASDAAQLISAKEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEewplRGGANGSLRFEAELKHAANAGLLNALKLIQP 157
Cdd:cd00691 5 SAAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETK----TGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 158 LKDKYPNISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEGRLPDAGPpsPADHLRDVFYRMGLDDKEIVAL 237
Cdd:cd00691 81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASK--GADHLRDVFYRMGFNDQEIVAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 238 SGAHTLGRARPDRSGWGKPetkytktgpgeaggqsWTVKWLKFDNSYFKDIKEKR----DDDLLVLPTDAALFEDPSFKN 313
Cdd:cd00691 159 SGAHTLGRCHKERSGYDGP----------------WTKNPLKFDNSYFKELLEEDwklpTPGLLMLPTDKALLEDPKFRP 222
|
250 260 270
....*....|....*....|....*....|.
gi 118572831 314 YAEKYAEDVAAFFKDYAEAHAKLSNLGAKFD 344
Cdd:cd00691 223 YVELYAKDQDAFFKDYAEAHKKLSELGVPFP 253
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
73-346 |
5.49e-98 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 294.75 E-value: 5.49e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 73 MISPKCAASDAAQLISAKEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEEwplrGGANGSLRFEAELKHAANAGLLNAL 152
Cdd:PLN02608 1 MAAPVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKT----GGPNGSIRNEEEYSHGANNGLKIAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 153 KLIQPLKDKYPNISYADLFQLASATAIEEAGGPDIPMKYGRVDVVApeqCPEEGRLPDA--GPPspadHLRDVFYRMGLD 230
Cdd:PLN02608 77 DLCEPVKAKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNA---CPEEGRLPDAkkGAK----HLRDVFYRMGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 231 DKEIVALSGAHTLGRARPDRSGWGKPetkytktgpgeaggqsWTVKWLKFDNSYFKDIKEKRDDDLLVLPTDAALFEDPS 310
Cdd:PLN02608 150 DKDIVALSGGHTLGRAHPERSGFDGP----------------WTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPE 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 118572831 311 FKNYAEKYAEDVAAFFKDYAEAHAKLSNLGakFDPP 346
Cdd:PLN02608 214 FRPYVELYAKDEDAFFRDYAESHKKLSELG--FTPP 247
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
102-321 |
7.78e-50 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 166.97 E-value: 7.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 102 CHPILVRLGWHDAGTynknieewplrGGANGSL---RFEAELKHAANAGLLNALKLIQPLKDKYPN-----ISYADLFQL 173
Cdd:pfam00141 15 MGPSLLRLHFHDCFV-----------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAacpgvVSCADILAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 174 ASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEGRLPDagPPSPADHLRDVFYRMGLDDKEIVALSGAHTLGRARpdrsgw 253
Cdd:pfam00141 84 AARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPA--PTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH------ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572831 254 gkpetkytktgpgeaggqswtvkwlkfdnsyfKDIKEKRdddlLVLPTDAALFEDPSFKNYAEKYAED 321
Cdd:pfam00141 156 --------------------------------KNLLDGR----GLLTSDQALLSDPRTRALVERYAAD 187
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
90-342 |
8.59e-22 |
|
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: 98.08 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTK-------FCH--PILVRLGWHDAGTYnKNIEEwplRGGA-NGSLRFEAELKHAANAGLLNALKLIQPLK 159
Cdd:TIGR00198 58 KQDLKHLMTDSqswwpadWGHygGLFIRMAWHAAGTY-RIADG---RGGAaTGNQRFAPLNSWPDNVNLDKARRLLWPIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 160 DKYPN-ISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEG---------RLPDA------------------ 211
Cdd:TIGR00198 134 KKYGNkLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDKDIYWGaekewltssREDREslenplaatemgliyvnp 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 212 ----GPPSP---ADHLRDVFYRMGLDDKEIVAL-SGAHTLGRAR---------PDRS---------GW----GKPETKYT 261
Cdd:TIGR00198 214 egpdGHPDPlctAQDIRTTFARMGMNDEETVALiAGGHTVGKCHgagpaeligPDPEgapieeqglGWhnqyGKGVGRDT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 262 KTGPGEAggqSWTVKWLKFDNSYF----------------------KDIKEKRDD--------DLLVLPTDAALFEDPSF 311
Cdd:TIGR00198 294 MTSGLEV---AWTTTPTQWDNGYFymlfnyewelkkspagawqweaVDAPEIIPDvedpnkkhNPIMLDADLALRFDPEF 370
|
330 340 350
....*....|....*....|....*....|...
gi 118572831 312 KNYAEKYAEDVAAFFKDYAEAHAKLS--NLGAK 342
Cdd:TIGR00198 371 RKISRRFLREPDYFAEAFAKAWFKLThrDMGPK 403
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
90-335 |
2.62e-18 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 87.48 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTK-------FCH--PILVRLGWHDAGTYnkNIEEWplRGGAN-GSLRFeaelkhaA-------NAGLLNAL 152
Cdd:COG0376 66 KKDLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY--RIGDG--RGGAGgGQQRF-------AplnswpdNANLDKAR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 153 KLIQPLKDKYPN-ISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQC----PEEGRLPDA---------------- 211
Cdd:COG0376 135 RLLWPIKQKYGNkISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDvywgPETEWLGDErysgdrelenplaavq 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 212 ---------GP---PSP---ADHLRDVFYRMGLDDKEIVAL-SGAHTLGRARpdrsGWGKPE------------------ 257
Cdd:COG0376 215 mgliyvnpeGPngnPDPlaaARDIRETFGRMAMNDEETVALiAGGHTFGKTH----GAGDAEhvgpepeaapieeqglgw 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 258 -TKYtKTGPGE---AGG--QSWTVKWLKFDNSYF----------------------KDIKEKR------DDDLLVLP--- 300
Cdd:COG0376 291 kNSF-GSGKGEdtiTSGleGAWTPTPTQWDNGYFdnlfgyeweltkspagahqwvpKDGAAADtvpdahDPSKRHAPmml 369
|
330 340 350
....*....|....*....|....*....|....*.
gi 118572831 301 -TDAALFEDPSFKNYAEKYAEDVAAFfkdyAEAHAK 335
Cdd:COG0376 370 tTDLALRFDPAYEKISRRFLENPEEF----ADAFAR 401
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
78-344 |
1.02e-143 |
|
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: 409.67 E-value: 1.02e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 78 CAASDAAQLISAKEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEewplRGGANGSLRFEAELKHAANAGLLNALKLIQP 157
Cdd:cd00691 5 SAAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETK----TGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 158 LKDKYPNISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEGRLPDAGPpsPADHLRDVFYRMGLDDKEIVAL 237
Cdd:cd00691 81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASK--GADHLRDVFYRMGFNDQEIVAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 238 SGAHTLGRARPDRSGWGKPetkytktgpgeaggqsWTVKWLKFDNSYFKDIKEKR----DDDLLVLPTDAALFEDPSFKN 313
Cdd:cd00691 159 SGAHTLGRCHKERSGYDGP----------------WTKNPLKFDNSYFKELLEEDwklpTPGLLMLPTDKALLEDPKFRP 222
|
250 260 270
....*....|....*....|....*....|.
gi 118572831 314 YAEKYAEDVAAFFKDYAEAHAKLSNLGAKFD 344
Cdd:cd00691 223 YVELYAKDQDAFFKDYAEAHKKLSELGVPFP 253
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
73-346 |
5.49e-98 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 294.75 E-value: 5.49e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 73 MISPKCAASDAAQLISAKEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEEwplrGGANGSLRFEAELKHAANAGLLNAL 152
Cdd:PLN02608 1 MAAPVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKT----GGPNGSIRNEEEYSHGANNGLKIAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 153 KLIQPLKDKYPNISYADLFQLASATAIEEAGGPDIPMKYGRVDVVApeqCPEEGRLPDA--GPPspadHLRDVFYRMGLD 230
Cdd:PLN02608 77 DLCEPVKAKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNA---CPEEGRLPDAkkGAK----HLRDVFYRMGLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 231 DKEIVALSGAHTLGRARPDRSGWGKPetkytktgpgeaggqsWTVKWLKFDNSYFKDIKEKRDDDLLVLPTDAALFEDPS 310
Cdd:PLN02608 150 DKDIVALSGGHTLGRAHPERSGFDGP----------------WTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPE 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 118572831 311 FKNYAEKYAEDVAAFFKDYAEAHAKLSNLGakFDPP 346
Cdd:PLN02608 214 FRPYVELYAKDEDAFFRDYAESHKKLSELG--FTPP 247
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
90-340 |
2.31e-71 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 225.32 E-value: 2.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEEwplrGGANGSLRFEAELKHAANAGLLNALKLIQPLKDKYPNISYAD 169
Cdd:PLN02879 21 KRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKT----GGPFGTIRHPQELAHDANNGLDIAVRLLDPIKELFPILSYAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 170 LFQLASATAIEEAGGPDIPMKYGRVDVVAPeqcPEEGRLPDAgpPSPADHLRDVFYRMGLDDKEIVALSGAHTLGRARPD 249
Cdd:PLN02879 97 FYQLAGVVAVEITGGPEIPFHPGRLDKVEP---PPEGRLPQA--TKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 250 RSGWGKpetkytktgpgeaggqSWTVKWLKFDNSYFKDIKEKRDDDLLVLPTDAALFEDPSFKNYAEKYAEDVAAFFKDY 329
Cdd:PLN02879 172 RSGFEG----------------AWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDY 235
|
250
....*....|.
gi 118572831 330 AEAHAKLSNLG 340
Cdd:PLN02879 236 TEAHLKLSELG 246
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
90-340 |
6.01e-70 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 221.49 E-value: 6.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTKFCHPILVRLGWHDAGTYNKNIEEwplrGGANGSLRFEAELKHAANAGLLNALKLIQPLKDKYPNISYAD 169
Cdd:PLN02364 20 RRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRT----GGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFPTISFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 170 LFQLASATAIEEAGGPDIPMKYGRVDVVAPeqcPEEGRLPDAgpPSPADHLRDVFYR-MGLDDKEIVALSGAHTLGRARP 248
Cdd:PLN02364 96 FHQLAGVVAVEVTGGPDIPFHPGREDKPQP---PPEGRLPDA--TKGCDHLRDVFAKqMGLSDKDIVALSGAHTLGRCHK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 249 DRSGWGKpetkytktgpgeaggqSWTVKWLKFDNSYFKDIKEKRDDDLLVLPTDAALFEDPSFKNYAEKYAEDVAAFFKD 328
Cdd:PLN02364 171 DRSGFEG----------------AWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFAD 234
|
250
....*....|..
gi 118572831 329 YAEAHAKLSNLG 340
Cdd:PLN02364 235 YAEAHMKLSELG 246
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
102-321 |
7.78e-50 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 166.97 E-value: 7.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 102 CHPILVRLGWHDAGTynknieewplrGGANGSL---RFEAELKHAANAGLLNALKLIQPLKDKYPN-----ISYADLFQL 173
Cdd:pfam00141 15 MGPSLLRLHFHDCFV-----------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEAacpgvVSCADILAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 174 ASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEGRLPDagPPSPADHLRDVFYRMGLDDKEIVALSGAHTLGRARpdrsgw 253
Cdd:pfam00141 84 AARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPA--PTDSLDQLRDRFARKGLTAEDLVALSGAHTIGRAH------ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572831 254 gkpetkytktgpgeaggqswtvkwlkfdnsyfKDIKEKRdddlLVLPTDAALFEDPSFKNYAEKYAED 321
Cdd:pfam00141 156 --------------------------------KNLLDGR----GLLTSDQALLSDPRTRALVERYAAD 187
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
106-338 |
8.02e-48 |
|
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: 164.25 E-value: 8.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 106 LVRLGWHDAGTYNKNIeewPLRGGANGSLRFEAELKHAANAGLLNALKLIQPLKDKYPN---ISYADLFQLASATAIEEA 182
Cdd:cd00314 21 LLRLAFHDAGTYDIAD---GKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDGgnpVSRADLIALAGAVAVEST 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 183 --GGPDIPMKYGRVDVVAPEQCPEEGRLPDAGPPSPADHLRDVFYRMGLDDKEIVALS-GAHTL-GRArpdrSGWGKPET 258
Cdd:cd00314 98 fgGGPLIPFRFGRLDATEPDLGVPDPEGLLPNETSSATELRDKFKRMGLSPSELVALSaGAHTLgGKN----HGDLLNYE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 259 KYTKtgpgeaggqsWTVKWLKFDNSYFKDIKEK------------RDDDLLVLPTDAALFEDPSFKNYAEKYAEDVAAFF 326
Cdd:cd00314 174 GSGL----------WTSTPFTFDNAYFKNLLDMnwewrvgspdpdGVKGPGLLPSDYALLSDSETRALVERYASDQEKFF 243
|
250
....*....|..
gi 118572831 327 KDYAEAHAKLSN 338
Cdd:cd00314 244 EDFAKAWIKMVN 255
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
131-340 |
1.21e-26 |
|
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: 108.37 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 131 NGSLRFEAELKHAANAGLlNALKLIQPLKDKY----PNI-SYADLfqLASAT--AIEEAGGPDIPMKYGRVD-VVApeQC 202
Cdd:cd00693 56 DSTANNTSEKDAPPNLSL-RGFDVIDDIKAALeaacPGVvSCADI--LALAArdAVVLAGGPSYEVPLGRRDgRVS--SA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 203 PEEGRLPdaGPPSPADHLRDVFYRMGLDDKEIVALSGAHTLGRAR----PDR----SGWGKP----ETKY----TKTGPG 266
Cdd:cd00693 131 NDVGNLP--SPFFSVSQLISLFASKGLTVTDLVALSGAHTIGRAHcssfSDRlynfSGTGDPdptlDPAYaaqlRKKCPA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 267 EAGGQS------WTVkwLKFDNSYFKDIKEKRDddllVLPTDAALFEDPSFKNYAEKYAEDVAAFFKDYAEAHAKLSNLG 340
Cdd:cd00693 209 GGDDDTlvpldpGTP--NTFDNSYYKNLLAGRG----LLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
90-336 |
3.50e-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: 109.32 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTK-------FCH--PILVRLGWHDAGTYNknIEEWplRGGAN-GSLRFEAELKHAANAGLLNALKLIQPLK 159
Cdd:cd00649 48 KEDLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTYR--IADG--RGGAGtGQQRFAPLNSWPDNVNLDKARRLLWPIK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 160 DKYPN-ISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQC----PEEGRLPDA----------------------- 211
Cdd:cd00649 124 QKYGNkISWADLMILAGNVALESMGFKTFGFAGGREDVWEPDEDvywgPEKEWLADKrysgdrdlenplaavqmgliyvn 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 212 --GP---PSP---ADHLRDVFYRMGLDDKEIVAL-SGAHTLGRAR-----------PDRS-------GW----GKPETKY 260
Cdd:cd00649 204 peGPdgnPDPlaaAKDIRETFARMAMNDEETVALiAGGHTFGKTHgagpashvgpePEAApieqqglGWknsyGTGKGKD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 261 TKTGPGEAggqSWTVKWLKFDNSYFKDI-------------------KEKRDDDLLV-------------LPTDAALFED 308
Cdd:cd00649 284 TITSGLEG---AWTPTPTKWDNNYLKNLfgyeweltkspagawqwvpKNAAGENTVPdahdpskkhapmmLTTDLALRFD 360
|
330 340
....*....|....*....|....*...
gi 118572831 309 PSFKNYAEKYAEDVAAFFKDYAEAHAKL 336
Cdd:cd00649 361 PEYEKISRRFLENPDEFADAFAKAWFKL 388
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
90-342 |
8.59e-22 |
|
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: 98.08 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTK-------FCH--PILVRLGWHDAGTYnKNIEEwplRGGA-NGSLRFEAELKHAANAGLLNALKLIQPLK 159
Cdd:TIGR00198 58 KQDLKHLMTDSqswwpadWGHygGLFIRMAWHAAGTY-RIADG---RGGAaTGNQRFAPLNSWPDNVNLDKARRLLWPIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 160 DKYPN-ISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQCPEEG---------RLPDA------------------ 211
Cdd:TIGR00198 134 KKYGNkLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDKDIYWGaekewltssREDREslenplaatemgliyvnp 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 212 ----GPPSP---ADHLRDVFYRMGLDDKEIVAL-SGAHTLGRAR---------PDRS---------GW----GKPETKYT 261
Cdd:TIGR00198 214 egpdGHPDPlctAQDIRTTFARMGMNDEETVALiAGGHTVGKCHgagpaeligPDPEgapieeqglGWhnqyGKGVGRDT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 262 KTGPGEAggqSWTVKWLKFDNSYF----------------------KDIKEKRDD--------DLLVLPTDAALFEDPSF 311
Cdd:TIGR00198 294 MTSGLEV---AWTTTPTQWDNGYFymlfnyewelkkspagawqweaVDAPEIIPDvedpnkkhNPIMLDADLALRFDPEF 370
|
330 340 350
....*....|....*....|....*....|...
gi 118572831 312 KNYAEKYAEDVAAFFKDYAEAHAKLS--NLGAK 342
Cdd:TIGR00198 371 RKISRRFLREPDYFAEAFAKAWFKLThrDMGPK 403
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
90-335 |
7.36e-19 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 89.04 E-value: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTK-------FCH--PILVRLGWHDAGTYnkNIEEWplRGGAN-GSLRFeaelkhaA-------NAGLLNAL 152
Cdd:PRK15061 60 KKDLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY--RIGDG--RGGAGgGQQRF-------AplnswpdNVNLDKAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 153 KLIQPLKDKYPN-ISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQC----PE----------------------- 204
Cdd:PRK15061 129 RLLWPIKQKYGNkISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDvywgPEkewlggderysgerdlenplaav 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 205 ---------EGrlPDaGPPSP---ADHLRDVFYRMGLDDKEIVAL-SGAHTLGRARpdrsGWGKPEtkytKTGPG-EAGG 270
Cdd:PRK15061 209 qmgliyvnpEG--PN-GNPDPlaaARDIRETFARMAMNDEETVALiAGGHTFGKTH----GAGDAS----HVGPEpEAAP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 271 ---Q-----------------------SWTVKWLKFDNSYF----------------------KDIKEKR------DDDL 296
Cdd:PRK15061 278 ieeQglgwknsygsgkgadtitsglegAWTTTPTQWDNGYFenlfgyeweltkspagawqwvpKDGAAEDtvpdahDPSK 357
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 118572831 297 LVLP----TDAALFEDPSFKNYAEKYAEDVAAFfkdyAEAHAK 335
Cdd:PRK15061 358 KHAPtmltTDLALRFDPEYEKISRRFLENPEEF----ADAFAR 396
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
90-335 |
2.62e-18 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 87.48 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 90 KEDIKVLLRTK-------FCH--PILVRLGWHDAGTYnkNIEEWplRGGAN-GSLRFeaelkhaA-------NAGLLNAL 152
Cdd:COG0376 66 KKDLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY--RIGDG--RGGAGgGQQRF-------AplnswpdNANLDKAR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 153 KLIQPLKDKYPN-ISYADLFQLASATAIEEAGGPDIPMKYGRVDVVAPEQC----PEEGRLPDA---------------- 211
Cdd:COG0376 135 RLLWPIKQKYGNkISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDvywgPETEWLGDErysgdrelenplaavq 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 212 ---------GP---PSP---ADHLRDVFYRMGLDDKEIVAL-SGAHTLGRARpdrsGWGKPE------------------ 257
Cdd:COG0376 215 mgliyvnpeGPngnPDPlaaARDIRETFGRMAMNDEETVALiAGGHTFGKTH----GAGDAEhvgpepeaapieeqglgw 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 258 -TKYtKTGPGE---AGG--QSWTVKWLKFDNSYF----------------------KDIKEKR------DDDLLVLP--- 300
Cdd:COG0376 291 kNSF-GSGKGEdtiTSGleGAWTPTPTQWDNGYFdnlfgyeweltkspagahqwvpKDGAAADtvpdahDPSKRHAPmml 369
|
330 340 350
....*....|....*....|....*....|....*.
gi 118572831 301 -TDAALFEDPSFKNYAEKYAEDVAAFfkdyAEAHAK 335
Cdd:COG0376 370 tTDLALRFDPAYEKISRRFLENPEEF----ADAFAR 401
|
|
| ligninase |
cd00692 |
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ... |
107-340 |
1.85e-17 |
|
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: 82.83 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 107 VRLGWHDAGTYNKNIEEWPLRG-GANGSLRF--EAELKHAANAGLLNALKLIQPLKDKYpNISYADLFQLASATAIEE-A 182
Cdd:cd00692 42 LRLTFHDAIGFSPALAAGQFGGgGADGSIVLfdDIETAFHANIGLDEIVEALRPFHQKH-NVSMADFIQFAGAVAVSNcP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 183 GGPDIPMKYGRVDVVAPEqcpeegrlPDAGPPSPADHLRDVFYRM---GLDDKEIVALSGAHTLGRARP-DRSGWGKP-- 256
Cdd:cd00692 121 GAPRLEFYAGRKDATQPA--------PDGLVPEPFDSVDKILARFadaGFSPDELVALLAAHSVAAQDFvDPSIAGTPfd 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 257 ------ETKY-------TKTGPGEAGGQSWTVKWLKfdnsyfkdiKEKRdddllvLPTDAALFEDPSFKNYAEKYAEDVA 323
Cdd:cd00692 193 stpgvfDTQFfietllkGTAFPGSGGNQGEVESPLP---------GEFR------LQSDFLLARDPRTACEWQSFVNNQA 257
|
250
....*....|....*..
gi 118572831 324 AFFKDYAEAHAKLSNLG 340
Cdd:cd00692 258 KMNAAFAAAMLKLSLLG 274
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
107-244 |
1.88e-11 |
|
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: 64.03 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 107 VRLGWHDAGTYNKNIEEwplrGGANGSLRFEaeLKHAAN--AGLLNALKLIQPLKDKYpnISYADLFQLASATAIEEAGG 184
Cdd:cd08201 46 LRTAFHDMATHNVDDGT----GGLDASIQYE--LDRPENigSGFNTTLNFFVNFYSPR--SSMADLIAMGVVTSVASCGG 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572831 185 PDIPMKYGRVDVVAPEQcpeegrlpdAGPPSP---ADHLRDVFYRMGLDDKEIVALSG-AHTLG 244
Cdd:cd08201 118 PVVPFRAGRIDATEAGQ---------AGVPEPqtdLGTTTESFRRQGFSTSEMIALVAcGHTLG 172
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
85-195 |
3.92e-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: 42.22 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 85 QLISAKeDIKVL----LRTKFCHPILVRLGWHDAGTYNKNieewPLRGGANGS-LRFEAELKHAAN-----AGLLNALKL 154
Cdd:cd08200 9 ELIDDA-DIAALkakiLASGLTVSELVSTAWASASTFRNS----DKRGGANGArIRLAPQKDWEVNepeelAKVLAVLEG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 118572831 155 IQplkDKYPN-------ISYADLFQLASATAIEEA---GGPDIPMKY--GRVD 195
Cdd:cd08200 84 IQ---KEFNEsqsggkkVSLADLIVLGGCAAVEKAakdAGVDIKVPFtpGRTD 133
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
80-195 |
7.39e-03 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 38.56 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572831 80 ASDAAQLisaKEDIkvlLRTKFCHPILVRLGWHDAGTY---NKnieewplRGGANGS-LRFEAELKHAAN-----AGLLN 150
Cdd:COG0376 443 DADIAAL---KAKI---LASGLSVSELVSTAWASASTFrgsDK-------RGGANGArIRLAPQKDWEVNepeqlAKVLA 509
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 118572831 151 ALKLIQ------PLKDKypNISYADLFQLASATAIEEA---GGPDI--PMKYGRVD 195
Cdd:COG0376 510 VLEGIQkdfnaaQSGGK--KVSLADLIVLGGCAAVEKAakdAGHDVtvPFTPGRTD 563
|
|
| |
