|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
1-250 |
0e+00 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 521.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
Cdd:PLN02364 1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
Cdd:PLN02364 81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
Cdd:PLN02364 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
|
250
....*....|
gi 186478248 241 KLSELGFADA 250
Cdd:PLN02364 241 KLSELGFADA 250
|
|
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
5-250 |
1.17e-156 |
|
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.
Pssm-ID: 173825 [Multi-domain] Cd Length: 253 Bit Score: 435.09 E-value: 1.17e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 5 YPTVSEDY-KKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDP 83
Cdd:cd00691 1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 84 IREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQP---PPEGRLPDATKGCDHLRDVFAkQMGLSDKDIVALS 160
Cdd:cd00691 81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFY-RMGFNDQEIVALS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEK----EGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYA 236
Cdd:cd00691 160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239
|
250
....*....|....
gi 186478248 237 EAHMKLSELGFADA 250
Cdd:cd00691 240 EAHKKLSELGVPFP 253
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
1-249 |
1.74e-151 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 422.16 E-value: 1.74e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 1 MTKNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRL 80
Cdd:PLN02879 2 VKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 81 LDPIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALS 160
Cdd:PLN02879 82 LDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHM 240
Cdd:PLN02879 161 GGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHL 240
|
....*....
gi 186478248 241 KLSELGFAD 249
Cdd:PLN02879 241 KLSELGFAD 249
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
6-247 |
4.29e-142 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 399.52 E-value: 4.29e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 6 PTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIR 85
Cdd:PLN02608 4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 86 EQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALSGAHTL 165
Cdd:PLN02608 84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFYR-MGLSDKDIVALSGGHTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 166 GRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSEL 245
Cdd:PLN02608 163 GRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSEL 242
|
..
gi 186478248 246 GF 247
Cdd:PLN02608 243 GF 244
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
23-244 |
9.05e-61 |
|
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.
Pssm-ID: 173823 [Multi-domain] Cd Length: 255 Bit Score: 191.98 E-value: 9.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 23 LRGLIAEKN-CAPIMVRLAWHSAGTFD-CQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFP---TISFADFH 97
Cdd:cd00314 7 LEDLITQAGaLAGSLLRLAFHDAGTYDiADGKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggnPVSRADLI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 98 QLAGVVAVEVT--GGPDIPFHPGREDKPQPP-----PEGRLPDATKGCDHLRDVFAKqMGLSDKDIVALS-GAHTL-GRC 168
Cdd:cd00314 87 ALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKFKR-MGLSPSELVALSaGAHTLgGKN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 169 HKDRSGFE--GAWTSNPLIFDNSYFKELLSGEKE------------GLLQLVSDKALLDDPVFRPLVEKYAADEDAFFAD 234
Cdd:cd00314 166 HGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQEKFFED 245
|
250
....*....|
gi 186478248 235 YAEAHMKLSE 244
Cdd:cd00314 246 FAKAWIKMVN 255
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
20-227 |
1.14e-53 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 171.59 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 20 RRKLRGLI-AEKNCAPIMVRLAWHSAGTfdcqsrtGGPFG-TMR--FDAEQAHGANSGIHIALRLLDPIREQFP-----T 90
Cdd:pfam00141 2 RSVVRAAFkADPTMGPSLLRLHFHDCFV-------GGCDGsVLLdgFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 91 ISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPE---GRLPDATKGCDHLRDVFAkQMGLSDKDIVALSGAHTLGR 167
Cdd:pfam00141 75 VSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRFA-RKGLTAEDLVALSGAHTIGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 168 CHkdrsgfegawtsnplifdnsyfKELLSGekEGLLQlvSDKALLDDPVFRPLVEKYAAD 227
Cdd:pfam00141 154 AH----------------------KNLLDG--RGLLT--SDQALLSDPRTRALVERYAAD 187
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
58-246 |
7.25e-31 |
|
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.
Pssm-ID: 173827 [Multi-domain] Cd Length: 298 Bit Score: 115.69 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 58 GTMRFDAEQAHGANSGIHiALRLLDPIREQF-----PTISFADFHQLAGVVAVEVTGGPDIPFHPGRED--KPQPPPEGR 130
Cdd:cd00693 57 STANNTSEKDAPPNLSLR-GFDVIDDIKAALeaacpGVVSCADILALAARDAVVLAGGPSYEVPLGRRDgrVSSANDVGN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 131 LPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLGRCH----KDR-SGFEGAWTSNPLI-------------------- 185
Cdd:cd00693 136 LPSPFFSVSQLISLFASK-GLTVTDLVALSGAHTIGRAHcssfSDRlYNFSGTGDPDPTLdpayaaqlrkkcpaggdddt 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186478248 186 -----------FDNSYFKELLSGekEGLLQlvSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELG 246
Cdd:cd00693 215 lvpldpgtpntFDNSYYKNLLAG--RGLLT--SDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
34-242 |
7.41e-26 |
|
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
Pssm-ID: 173824 [Multi-domain] Cd Length: 409 Bit Score: 104.31 E-value: 7.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 34 PIMVRLAWHSAGTFDCQS-RTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGGP 111
Cdd:cd00649 71 PLFIRMAWHSAGTYRIADgRGGAGTGQQRFAPLNSWPDNVNLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 112 DIPFHPGRED--------------------------KPQPP------------PEG--RLPDATKGCDHLRDVFAKqMGL 151
Cdd:cd00649 151 TFGFAGGREDvwepdedvywgpekewladkrysgdrDLENPlaavqmgliyvnPEGpdGNPDPLAAAKDIRETFAR-MAM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 152 SDKDIVAL-SGAHTLGRCH---------------------------------KDR--SGFEGAWTSNPLIFDNSYFKELL 195
Cdd:cd00649 230 NDEETVALiAGGHTFGKTHgagpashvgpepeaapieqqglgwknsygtgkgKDTitSGLEGAWTPTPTKWDNNYLKNLF 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478248 196 S--------------------------------GEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242
Cdd:cd00649 310 GyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKL 388
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
11-243 |
2.61e-23 |
|
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
Pssm-ID: 272957 [Multi-domain] Cd Length: 716 Bit Score: 98.46 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 11 DYKKAVEK-----CRRKLRGLIAEK---------NCAPIMVRLAWHSAGTFDC-QSRTGGPFGTMRFDAEQAHGANSGIH 75
Cdd:TIGR00198 44 DYAEEFQQldlaaVKQDLKHLMTDSqswwpadwgHYGGLFIRMAWHAAGTYRIaDGRGGAATGNQRFAPLNSWPDNVNLD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 76 IALRLLDPIREQF-PTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPP---------------------------- 126
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaa 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 127 ---------PEG--RLPDATKGCDHLRDVFAKqMGLSDKDIVAL-SGAHTLGRCHKD----------------------- 171
Cdd:TIGR00198 204 temgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 172 ------------RSGFEGAWTSNPLIFDNSYFKELLSGEKE------GLLQ------------------------LVSDK 209
Cdd:TIGR00198 283 nqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADL 362
|
330 340 350
....*....|....*....|....*....|....
gi 186478248 210 ALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLS 243
Cdd:TIGR00198 363 ALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
34-242 |
1.45e-19 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 87.50 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 34 PIMVRLAWHSAGTFdcqsRT-----GGPFGTMRF-------DaeqahgaNSGIHIALRLLDPIREQF-PTISFADFHQLA 100
Cdd:PRK15061 83 PLFIRMAWHSAGTY----RIgdgrgGAGGGQQRFaplnswpD-------NVNLDKARRLLWPIKQKYgNKISWADLMILA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 101 GVVAVEVTGGPDIPFHPGREDKPQP---------------------------P------------PEG--RLPDATKGCD 139
Cdd:PRK15061 152 GNVALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEGpnGNPDPLAAAR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 140 HLRDVFAKqMGLSDKDIVAL-SGAHTLGRCH---------------------------------KD--RSGFEGAWTSNP 183
Cdd:PRK15061 232 DIRETFAR-MAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgkgADtiTSGLEGAWTTTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 184 LIFDNSYFKELLSGEKE------GLLQ--------------------------LVSDKALLDDPVFRPLVEKYAADEDAf 231
Cdd:PRK15061 311 TQWDNGYFENLFGYEWEltkspaGAWQwvpkdgaaedtvpdahdpskkhaptmLTTDLALRFDPEYEKISRRFLENPEE- 389
|
330
....*....|..
gi 186478248 232 FAD-YAEAHMKL 242
Cdd:PRK15061 390 FADaFARAWFKL 401
|
|
| ligninase |
cd00692 |
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ... |
37-247 |
2.82e-19 |
|
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.
Pssm-ID: 173826 [Multi-domain] Cd Length: 328 Bit Score: 85.14 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 37 VRLAWHSAGTFDCQSRTGGPFGT------MRF-DAEQAHGANSGIHIALRLLDPIrEQFPTISFADFHQLAGVVAV-EVT 108
Cdd:cd00692 42 LRLTFHDAIGFSPALAAGQFGGGgadgsiVLFdDIETAFHANIGLDEIVEALRPF-HQKHNVSMADFIQFAGAVAVsNCP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 109 GGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQmGLSDKDIVALSGAHTLGRCHK-DRSGFEGAWTSNPLIFD 187
Cdd:cd00692 121 GAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARFADA-GFSPDELVALLAAHSVAAQDFvDPSIAGTPFDSTPGVFD 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478248 188 NSYFKE-LLSGE---------------KEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKLSELGF 247
Cdd:cd00692 200 TQFFIEtLLKGTafpgsggnqgevespLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
34-242 |
4.33e-19 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 85.94 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 34 PIMVRLAWHSAGTF---DcqSRTGGPFGTMRF-------DaeqahgaNSGIHIALRLLDPIREQF-PTISFADFHQLAGV 102
Cdd:COG0376 89 PLFIRMAWHSAGTYrigD--GRGGAGGGQQRFaplnswpD-------NANLDKARRLLWPIKQKYgNKISWADLMILAGN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 103 VAVEVTGGPDIPFHPGREDKPQP--------------------------P------------PEG--RLPDATKGCDHLR 142
Cdd:COG0376 160 VALESMGFKTFGFAGGREDVWEPeedvywgpetewlgderysgdrelenPlaavqmgliyvnPEGpnGNPDPLAAARDIR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 143 DVFAKqMGLSDKDIVAL-SGAHTLGRCH------------------------KDR-----------SGFEGAWTSNPLIF 186
Cdd:COG0376 240 ETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPTQW 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 187 DNSYFKELL--------------------------------SGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAfFAD 234
Cdd:COG0376 319 DNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-FAD 397
|
....*....
gi 186478248 235 -YAEAHMKL 242
Cdd:COG0376 398 aFARAWFKL 406
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
37-197 |
2.88e-12 |
|
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.
Pssm-ID: 173829 Cd Length: 264 Bit Score: 64.80 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 37 VRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIreQFPTISFADFHQLAGVVAVEVTGGPDIPFH 116
Cdd:cd08201 46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNF--YSPRSSMADLIAMGVVTSVASCGGPVVPFR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 117 PGREDKPQPPPEGrLPDATKGCDHLRDVFAKQmGLSDKDIVALSG-AHTLGRCHK-----------DRSGFEGAWTSNPl 184
Cdd:cd08201 124 AGRIDATEAGQAG-VPEPQTDLGTTTESFRRQ-GFSTSEMIALVAcGHTLGGVHSedfpeivppgsVPDTVLQFFDTTI- 200
|
170
....*....|...
gi 186478248 185 IFDNSYFKELLSG 197
Cdd:cd08201 201 QFDNKVVTEYLSG 213
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
36-245 |
6.95e-06 |
|
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
Pssm-ID: 272957 [Multi-domain] Cd Length: 716 Bit Score: 46.84 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 36 MVRLAWHSAGTFDCQSRTGGPFGT-MRFDAEQAHGANSGIHI--ALRLLDPIREQFPT--ISFADFHQLAGVVAVE---V 107
Cdd:TIGR00198 451 LVCTAWASASTFRSSDYRGGANGArIRLEPQKNWPVNEPTRLakVLAVLEKIQAEFAKgpVSLADLIVLGGGAAVEkaaL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 108 TGGPDI--PFHPGREDKPQ------------PPPEG----RLPDATKGCDHLRDVFAKQMGLSDKDIVAL-SGAHTLGRC 168
Cdd:TIGR00198 531 DAGISVnvPFLPGRVDATQamtdaesftplePIADGfrnyLKRDYAVTPEELLLDKAQLLTLTAPEMTVLiGGMRVLGAN 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 169 HKDRSgfEGAWTSNPLIFDNSYF----------------KELLSG--EKEGLLQLVSDKALL---DDPVFRPLVEKYAAD 227
Cdd:TIGR00198 611 HGGSK--HGVFTDRVGVLSNDFFvnlldmayewraadnnRYLFEGgdRQTGEVKWTATRVDLvfgSNSILRAVAEVYAQD 688
|
250 260
....*....|....*....|
gi 186478248 228 E--DAFFADYAEAHMKLSEL 245
Cdd:TIGR00198 689 DarEKFVKDFVAAWTKVMNL 708
|
|
| PLN03030 |
PLN03030 |
cationic peroxidase; Provisional |
90-246 |
3.41e-05 |
|
cationic peroxidase; Provisional
Pssm-ID: 215545 [Multi-domain] Cd Length: 324 Bit Score: 44.18 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 90 TISFADFHQLAGVVAVEVTGGPDIPFHPGREDkpqpppeGR---------LPDATKGCDHLRDVFAKQmGLSDKDIVALS 160
Cdd:PLN03030 113 VVSCADILALAARDSVVLTNGLTWPVPTGRRD-------GRvslasdasnLPGFTDSIDVQKQKFAAK-GLNTQDLVTLV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 161 GAHTLG---------RCHKDRSGFEGAwtsNPLI-------------------------------FDNSYFKELLSGekE 200
Cdd:PLN03030 185 GGHTIGttacqffryRLYNFTTTGNGA---DPSIdasfvpqlqalcpqngdgsrrialdtgssnrFDASFFSNLKNG--R 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 186478248 201 GLLQlvSDKALLDDPVFRPLVEKYAADED----AFFADYAEAHMKLSELG 246
Cdd:PLN03030 260 GILE--SDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIG 307
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
36-124 |
6.95e-04 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 40.51 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478248 36 MVRLAWHSAGTFdcqsRtggpfGT-MRfdaeqaHGANsGIHIAL------------RL------LDPIREQFPT------ 90
Cdd:PRK15061 458 LVSTAWASASTF----R-----GSdKR------GGAN-GARIRLapqkdwevnepaQLakvlavLEGIQAEFNAaqsggk 521
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186478248 91 -ISFADFHQLAGVVAVE---VTGGPDI--PFHPGREDKPQ 124
Cdd:PRK15061 522 kVSLADLIVLGGNAAVEqaaKAAGHDVtvPFTPGRTDATQ 561
|
|
|