|
Name |
Accession |
Description |
Interval |
E-value |
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
95-365 |
7.43e-144 |
|
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: 407.75 E-value: 7.43e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 95 AATKSSSSDPDQLKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNIKewpqRGGANGSLRFDIELKHAANAGLVNALN 174
Cdd:cd00691 1 APVVSAAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETK----TGGSNGTIRFDPELNHGANAGLDIARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 175 LIKDIKEKYSGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEGRLPDAGPpsPATHLREVFYRMGLDDKD 254
Cdd:cd00691 77 LLEPIKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASK--GADHLRDVFYRMGFNDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 255 IVALSGAHTLGRSRPERSGWGKPetkytkegpgapggqsWTPEWLKFDNSYFKEIKEKR----DEDLLVLPTDAAIFEDS 330
Cdd:cd00691 155 IVALSGAHTLGRCHKERSGYDGP----------------WTKNPLKFDNSYFKELLEEDwklpTPGLLMLPTDKALLEDP 218
|
250 260 270
....*....|....*....|....*....|....*
gi 42572847 331 SFKVYAEKYAADQDAFFKDYAVAHAKLSNLGAEFN 365
Cdd:cd00691 219 KFRPYVELYAKDQDAFFKDYAEAHKKLSELGVPFP 253
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
106-367 |
3.82e-99 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 295.52 E-value: 3.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 106 QLKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNIKEwpqrGGANGSLRFDIELKHAANAGLVNALNLIKDIKEKYSG 185
Cdd:PLN02608 13 EIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKT----GGPNGSIRNEEEYSHGANNGLKIAIDLCEPVKAKHPK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 186 ISYADLFQLASATAIEEAGGPKIPMKYGRVDASgpeDCPEEGRLPDA--GPPspatHLREVFYRMGLDDKDIVALSGAHT 263
Cdd:PLN02608 89 ITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSN---ACPEEGRLPDAkkGAK----HLRDVFYRMGLSDKDIVALSGGHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 264 LGRSRPERSGWgkpetkytkEGPgapggqsWTPEWLKFDNSYFKEIKEKRDEDLLVLPTDAAIFEDSSFKVYAEKYAADQ 343
Cdd:PLN02608 162 LGRAHPERSGF---------DGP-------WTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDE 225
|
250 260
....*....|....*....|....
gi 42572847 344 DAFFKDYAVAHAKLSNLGaeFNPP 367
Cdd:PLN02608 226 DAFFRDYAESHKKLSELG--FTPP 247
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
110-342 |
5.32e-49 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 163.50 E-value: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 110 AREDIKELLSTKF-CHPILVRLGWHDAGTynknikewpqrGGANGSL---RFDIELKHAANAGLVNALNLIKDIKEKY-- 183
Cdd:pfam00141 1 VRSVVRAAFKADPtMGPSLLRLHFHDCFV-----------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLea 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 184 ---SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEGRLPDagPPSPATHLREVFYRMGLDDKDIVALSG 260
Cdd:pfam00141 70 acpGVVSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPA--PTDSLDQLRDRFARKGLTAEDLVALSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 261 AHTLGRSRpersgwgkpetkytkegpgapggqswtpewlkfdnsyfKEIKEKRdedlLVLPTDAAIFEDSSFKVYAEKYA 340
Cdd:pfam00141 148 AHTIGRAH--------------------------------------KNLLDGR----GLLTSDQALLSDPRTRALVERYA 185
|
..
gi 42572847 341 AD 342
Cdd:pfam00141 186 AD 187
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
111-359 |
1.42e-16 |
|
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: 81.13 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 111 REDIKELLSTK-------FCH--PILVRLGWHDAGTYnkniKEWPQRGGA-NGSLRFDIELKHAANAGLVNALNLIKDIK 180
Cdd:TIGR00198 58 KQDLKHLMTDSqswwpadWGHygGLFIRMAWHAAGTY----RIADGRGGAaTGNQRFAPLNSWPDNVNLDKARRLLWPIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 181 EKY-SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEG---------RLPDA------------------ 232
Cdd:TIGR00198 134 KKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDKDIYWGaekewltssREDREslenplaatemgliyvnp 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 233 ----GPPSP---ATHLREVFYRMGLDDKDIVAL-SGAHTLGRSR-----------PERS-------GWgkpETKYTKeGP 286
Cdd:TIGR00198 214 egpdGHPDPlctAQDIRTTFARMGMNDEETVALiAGGHTVGKCHgagpaeligpdPEGApieeqglGW---HNQYGK-GV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 287 GAPGGQS-----WTPEWLKFDNSYF--------------------------KEIKEKRDEDL----LVLPTDAAIFEDSS 331
Cdd:TIGR00198 290 GRDTMTSglevaWTTTPTQWDNGYFymlfnyewelkkspagawqweavdapEIIPDVEDPNKkhnpIMLDADLALRFDPE 369
|
330 340
....*....|....*....|....*...
gi 42572847 332 FKVYAEKYAADQDAFFKDYAVAHAKLSN 359
Cdd:TIGR00198 370 FRKISRRFLREPDYFAEAFAKAWFKLTH 397
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
103-306 |
1.24e-14 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 75.16 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 103 DPDQLKNareDIKELLSTK-------FCH--PILVRLGWHDAGTYnkniKEWPQRGGAN-GSLRF-------Dielkhaa 165
Cdd:COG0376 61 DLDAVKK---DLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY----RIGDGRGGAGgGQQRFaplnswpD------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 166 NAGLVNALNLIKDIKEKY-SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDC----PEEGRLPDA-------- 232
Cdd:COG0376 127 NANLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDvywgPETEWLGDErysgdrel 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 233 -----------------GP---PSP---ATHLREVFYRMGLDDKDIVAL-SGAHTLGRSR-----------PERS----- 272
Cdd:COG0376 207 enplaavqmgliyvnpeGPngnPDPlaaARDIRETFGRMAMNDEETVALiAGGHTFGKTHgagdaehvgpePEAApieeq 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 42572847 273 --GW------GKPETKYTK--EGpgapggqSWTPEWLKFDNSYF 306
Cdd:COG0376 287 glGWknsfgsGKGEDTITSglEG-------AWTPTPTQWDNGYF 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ascorbate_peroxidase |
cd00691 |
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ... |
95-365 |
7.43e-144 |
|
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: 407.75 E-value: 7.43e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 95 AATKSSSSDPDQLKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNIKewpqRGGANGSLRFDIELKHAANAGLVNALN 174
Cdd:cd00691 1 APVVSAAYAAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETK----TGGSNGTIRFDPELNHGANAGLDIARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 175 LIKDIKEKYSGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEGRLPDAGPpsPATHLREVFYRMGLDDKD 254
Cdd:cd00691 77 LLEPIKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPEECPPEGRLPDASK--GADHLRDVFYRMGFNDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 255 IVALSGAHTLGRSRPERSGWGKPetkytkegpgapggqsWTPEWLKFDNSYFKEIKEKR----DEDLLVLPTDAAIFEDS 330
Cdd:cd00691 155 IVALSGAHTLGRCHKERSGYDGP----------------WTKNPLKFDNSYFKELLEEDwklpTPGLLMLPTDKALLEDP 218
|
250 260 270
....*....|....*....|....*....|....*
gi 42572847 331 SFKVYAEKYAADQDAFFKDYAVAHAKLSNLGAEFN 365
Cdd:cd00691 219 KFRPYVELYAKDQDAFFKDYAEAHKKLSELGVPFP 253
|
|
| PLN02608 |
PLN02608 |
L-ascorbate peroxidase |
106-367 |
3.82e-99 |
|
L-ascorbate peroxidase
Pssm-ID: 178218 [Multi-domain] Cd Length: 289 Bit Score: 295.52 E-value: 3.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 106 QLKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNIKEwpqrGGANGSLRFDIELKHAANAGLVNALNLIKDIKEKYSG 185
Cdd:PLN02608 13 EIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKT----GGPNGSIRNEEEYSHGANNGLKIAIDLCEPVKAKHPK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 186 ISYADLFQLASATAIEEAGGPKIPMKYGRVDASgpeDCPEEGRLPDA--GPPspatHLREVFYRMGLDDKDIVALSGAHT 263
Cdd:PLN02608 89 ITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSN---ACPEEGRLPDAkkGAK----HLRDVFYRMGLSDKDIVALSGGHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 264 LGRSRPERSGWgkpetkytkEGPgapggqsWTPEWLKFDNSYFKEIKEKRDEDLLVLPTDAAIFEDSSFKVYAEKYAADQ 343
Cdd:PLN02608 162 LGRAHPERSGF---------DGP-------WTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDE 225
|
250 260
....*....|....*....|....
gi 42572847 344 DAFFKDYAVAHAKLSNLGaeFNPP 367
Cdd:PLN02608 226 DAFFRDYAESHKKLSELG--FTPP 247
|
|
| PLN02879 |
PLN02879 |
L-ascorbate peroxidase |
86-361 |
1.28e-69 |
|
L-ascorbate peroxidase
Pssm-ID: 178467 [Multi-domain] Cd Length: 251 Bit Score: 218.78 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 86 VNRSFNSTTAATKSSssdpdqLKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNIKEwpqrGGANGSLRFDIELKHAA 165
Cdd:PLN02879 2 VKKSYPEVKEEYKKA------VQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKT----GGPFGTIRHPQELAHDA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 166 NAGLVNALNLIKDIKEKYSGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPedcPEEGRLPDAgpPSPATHLREVF 245
Cdd:PLN02879 72 NNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEP---PPEGRLPQA--TKGVDHLRDVF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 246 YRMGLDDKDIVALSGAHTLGRSRPERSGWgkpetkytkEGpgapggqSWTPEWLKFDNSYFKEIKEKRDEDLLVLPTDAA 325
Cdd:PLN02879 147 GRMGLNDKDIVALSGGHTLGRCHKERSGF---------EG-------AWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKA 210
|
250 260 270
....*....|....*....|....*....|....*.
gi 42572847 326 IFEDSSFKVYAEKYAADQDAFFKDYAVAHAKLSNLG 361
Cdd:PLN02879 211 LLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELG 246
|
|
| PLN02364 |
PLN02364 |
L-ascorbate peroxidase 1 |
107-361 |
7.19e-68 |
|
L-ascorbate peroxidase 1
Pssm-ID: 166005 Cd Length: 250 Bit Score: 214.56 E-value: 7.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 107 LKNAREDIKELLSTKFCHPILVRLGWHDAGTYNKNikewPQRGGANGSLRFDIELKHAANAGLVNALNLIKDIKEKYSGI 186
Cdd:PLN02364 16 VEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQ----SRTGGPFGTMRFDAEQAHGANSGIHIALRLLDPIREQFPTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 187 SYADLFQLASATAIEEAGGPKIPMKYGRVDASGPedcPEEGRLPDAgpPSPATHLREVFYR-MGLDDKDIVALSGAHTLG 265
Cdd:PLN02364 92 SFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQP---PPEGRLPDA--TKGCDHLRDVFAKqMGLSDKDIVALSGAHTLG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 266 RSRPERSGWgkpetkytkEGpgapggqSWTPEWLKFDNSYFKEIKEKRDEDLLVLPTDAAIFEDSSFKVYAEKYAADQDA 345
Cdd:PLN02364 167 RCHKDRSGF---------EG-------AWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDA 230
|
250
....*....|....*.
gi 42572847 346 FFKDYAVAHAKLSNLG 361
Cdd:PLN02364 231 FFADYAEAHMKLSELG 246
|
|
| peroxidase |
pfam00141 |
Peroxidase; |
110-342 |
5.32e-49 |
|
Peroxidase;
Pssm-ID: 425483 [Multi-domain] Cd Length: 187 Bit Score: 163.50 E-value: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 110 AREDIKELLSTKF-CHPILVRLGWHDAGTynknikewpqrGGANGSL---RFDIELKHAANAGLVNALNLIKDIKEKY-- 183
Cdd:pfam00141 1 VRSVVRAAFKADPtMGPSLLRLHFHDCFV-----------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLea 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 184 ---SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEGRLPDagPPSPATHLREVFYRMGLDDKDIVALSG 260
Cdd:pfam00141 70 acpGVVSCADILALAARDAVELAGGPSWPVPLGRRDGTVSSAVEANSNLPA--PTDSLDQLRDRFARKGLTAEDLVALSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 261 AHTLGRSRpersgwgkpetkytkegpgapggqswtpewlkfdnsyfKEIKEKRdedlLVLPTDAAIFEDSSFKVYAEKYA 340
Cdd:pfam00141 148 AHTIGRAH--------------------------------------KNLLDGR----GLLTSDQALLSDPRTRALVERYA 185
|
..
gi 42572847 341 AD 342
Cdd:pfam00141 186 AD 187
|
|
| plant_peroxidase_like |
cd00314 |
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ... |
127-359 |
1.35e-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: 164.63 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 127 LVRLGWHDAGTYNKNIKewpQRGGANGSLRFDIELKHAANAGLVNALNLIKDIKEKYSG---ISYADLFQLASATAIEEA 203
Cdd:cd00314 21 LLRLAFHDAGTYDIADG---KGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDGgnpVSRADLIALAGAVAVEST 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 204 --GGPKIPMKYGRVDASGPE-DCPEEGRLPDAGPPSpATHLREVFYRMGLDDKDIVALS-GAHTL-GRSrperSGWGKPE 278
Cdd:cd00314 98 fgGGPLIPFRFGRLDATEPDlGVPDPEGLLPNETSS-ATELRDKFKRMGLSPSELVALSaGAHTLgGKN----HGDLLNY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 279 TKYTKegpgapggqsWTPEWLKFDNSYFKEIKEK------------RDEDLLVLPTDAAIFEDSSFKVYAEKYAADQDAF 346
Cdd:cd00314 173 EGSGL----------WTSTPFTFDNAYFKNLLDMnwewrvgspdpdGVKGPGLLPSDYALLSDSETRALVERYASDQEKF 242
|
250
....*....|...
gi 42572847 347 FKDYAVAHAKLSN 359
Cdd:cd00314 243 FEDFAKAWIKMVN 255
|
|
| secretory_peroxidase |
cd00693 |
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ... |
160-361 |
1.74e-28 |
|
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: 112.61 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 160 ELKHAANAGLVnALNLIKDIK---EKYSG--ISYADLfqLASAT--AIEEAGGPKIPMKYGRVDaSGPEDCPEEGRLPda 232
Cdd:cd00693 64 EKDAPPNLSLR-GFDVIDDIKaalEAACPgvVSCADI--LALAArdAVVLAGGPSYEVPLGRRD-GRVSSANDVGNLP-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 233 GPPSPATHLREVFYRMGLDDKDIVALSGAHTLGRSR----PER----SGWGKP----ETKYTKE-----GPGAPGGQS-- 293
Cdd:cd00693 138 SPFFSVSQLISLFASKGLTVTDLVALSGAHTIGRAHcssfSDRlynfSGTGDPdptlDPAYAAQlrkkcPAGGDDDTLvp 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42572847 294 ---WTPewLKFDNSYFKEIKEKRDedllVLPTDAAIFEDSSFKVYAEKYAADQDAFFKDYAVAHAKLSNLG 361
Cdd:cd00693 218 ldpGTP--NTFDNSYYKNLLAGRG----LLTSDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
|
|
| catalase_peroxidase_1 |
cd00649 |
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
103-357 |
3.60e-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: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 103 DPDQLKnarEDIKELLSTK-------FCH--PILVRLGWHDAGTYnkniKEWPQRGGAN-GSLRFDIELKHAANAGLVNA 172
Cdd:cd00649 43 DLEALK---EDLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY----RIADGRGGAGtGQQRFAPLNSWPDNVNLDKA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 173 LNLIKDIKEKY-SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDC----PEEGRLPDA--------------- 232
Cdd:cd00649 116 RRLLWPIKQKYgNKISWADLMILAGNVALESMGFKTFGFAGGREDVWEPDEDvywgPEKEWLADKrysgdrdlenplaav 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 233 ----------GP---PSP---ATHLREVFYRMGLDDKDIVAL-SGAHTLGRSR-----------PERS-------GW--- 274
Cdd:cd00649 196 qmgliyvnpeGPdgnPDPlaaAKDIRETFARMAMNDEETVALiAGGHTFGKTHgagpashvgpePEAApieqqglGWkns 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 275 ---GKPETKYTK--EGpgapggqSWTPEWLKFDNSYFKEI-------------------KEKRDEDLLV----------- 319
Cdd:cd00649 276 ygtGKGKDTITSglEG-------AWTPTPTKWDNNYLKNLfgyeweltkspagawqwvpKNAAGENTVPdahdpskkhap 348
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 42572847 320 --LPTDAAIFEDSSFKVYAEKYAADQDAFFKDYAVAHAKL 357
Cdd:cd00649 349 mmLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKL 388
|
|
| ligninase |
cd00692 |
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ... |
128-361 |
5.29e-20 |
|
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.
Pssm-ID: 173826 [Multi-domain] Cd Length: 328 Bit Score: 89.76 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 128 VRLGWHDAGTYNKNIKEWP-QRGGANGSLRF--DIELKHAANAGLVNALNLIKDIKEKYsGISYADLFQLASATAIEE-A 203
Cdd:cd00692 42 LRLTFHDAIGFSPALAAGQfGGGGADGSIVLfdDIETAFHANIGLDEIVEALRPFHQKH-NVSMADFIQFAGAVAVSNcP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 204 GGPKIPMKYGRVDASGPedcPEEGRLPDagPPSPATHLREVFYRMGLDDKDIVALSGAHTLGRSR---------PERSGW 274
Cdd:cd00692 121 GAPRLEFYAGRKDATQP---APDGLVPE--PFDSVDKILARFADAGFSPDELVALLAAHSVAAQDfvdpsiagtPFDSTP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 275 GKPETKYTKE----GPGAPGGQSWTPEWLKFDNSYFKeikekrdedllvLPTDAAIFEDSSFKVYAEKYAADQDAFFKDY 350
Cdd:cd00692 196 GVFDTQFFIEtllkGTAFPGSGGNQGEVESPLPGEFR------------LQSDFLLARDPRTACEWQSFVNNQAKMNAAF 263
|
250
....*....|.
gi 42572847 351 AVAHAKLSNLG 361
Cdd:cd00692 264 AAAMLKLSLLG 274
|
|
| cat_per_HPI |
TIGR00198 |
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ... |
111-359 |
1.42e-16 |
|
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: 81.13 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 111 REDIKELLSTK-------FCH--PILVRLGWHDAGTYnkniKEWPQRGGA-NGSLRFDIELKHAANAGLVNALNLIKDIK 180
Cdd:TIGR00198 58 KQDLKHLMTDSqswwpadWGHygGLFIRMAWHAAGTY----RIADGRGGAaTGNQRFAPLNSWPDNVNLDKARRLLWPIK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 181 EKY-SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDCPEEG---------RLPDA------------------ 232
Cdd:TIGR00198 134 KKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDKDIYWGaekewltssREDREslenplaatemgliyvnp 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 233 ----GPPSP---ATHLREVFYRMGLDDKDIVAL-SGAHTLGRSR-----------PERS-------GWgkpETKYTKeGP 286
Cdd:TIGR00198 214 egpdGHPDPlctAQDIRTTFARMGMNDEETVALiAGGHTVGKCHgagpaeligpdPEGApieeqglGW---HNQYGK-GV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 287 GAPGGQS-----WTPEWLKFDNSYF--------------------------KEIKEKRDEDL----LVLPTDAAIFEDSS 331
Cdd:TIGR00198 290 GRDTMTSglevaWTTTPTQWDNGYFymlfnyewelkkspagawqweavdapEIIPDVEDPNKkhnpIMLDADLALRFDPE 369
|
330 340
....*....|....*....|....*...
gi 42572847 332 FKVYAEKYAADQDAFFKDYAVAHAKLSN 359
Cdd:TIGR00198 370 FRKISRRFLREPDYFAEAFAKAWFKLTH 397
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
103-306 |
1.24e-14 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 75.16 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 103 DPDQLKNareDIKELLSTK-------FCH--PILVRLGWHDAGTYnkniKEWPQRGGAN-GSLRF-------Dielkhaa 165
Cdd:COG0376 61 DLDAVKK---DLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY----RIGDGRGGAGgGQQRFaplnswpD------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 166 NAGLVNALNLIKDIKEKY-SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDC----PEEGRLPDA-------- 232
Cdd:COG0376 127 NANLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDvywgPETEWLGDErysgdrel 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 233 -----------------GP---PSP---ATHLREVFYRMGLDDKDIVAL-SGAHTLGRSR-----------PERS----- 272
Cdd:COG0376 207 enplaavqmgliyvnpeGPngnPDPlaaARDIRETFGRMAMNDEETVALiAGGHTFGKTHgagdaehvgpePEAApieeq 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 42572847 273 --GW------GKPETKYTK--EGpgapggqSWTPEWLKFDNSYF 306
Cdd:COG0376 287 glGWknsfgsGKGEDTITSglEG-------AWTPTPTQWDNGYF 323
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
103-357 |
1.46e-14 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 75.18 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 103 DPDQLKnarEDIKELLSTK-------FCH--PILVRLGWHDAGTYnkNIKEwpQRGGAN-GSLRF-------Dielkhaa 165
Cdd:PRK15061 55 DLEALK---KDLKALMTDSqdwwpadYGHygPLFIRMAWHSAGTY--RIGD--GRGGAGgGQQRFaplnswpD------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 166 NAGLVNALNLIKDIKEKY-SGISYADLFQLASATAIEEAGGPKIPMKYGRVDASGPEDC----PE--------------- 225
Cdd:PRK15061 121 NVNLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDvywgPEkewlggderysgerd 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 226 -----------------EGrlPDaGPPSP---ATHLREVFYRMGLDDKDIVAL-SGAHTLGRSR-----------PERS- 272
Cdd:PRK15061 201 lenplaavqmgliyvnpEG--PN-GNPDPlaaARDIRETFARMAMNDEETVALiAGGHTFGKTHgagdashvgpePEAAp 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 273 ------GW------GKPETKYTK--EGPgapggqsWTPEWLKFDNSYFK-------------------EIKEKRDEDLLV 319
Cdd:PRK15061 278 ieeqglGWknsygsGKGADTITSglEGA-------WTTTPTQWDNGYFEnlfgyeweltkspagawqwVPKDGAAEDTVP 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 42572847 320 -------------LPTDAAIFEDSSFKVYAEKYAADQDAFFKDYAVAHAKL 357
Cdd:PRK15061 351 dahdpskkhaptmLTTDLALRFDPEYEKISRRFLENPEEFADAFARAWFKL 401
|
|
| plant_peroxidase_like_1 |
cd08201 |
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ... |
128-270 |
5.51e-14 |
|
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.
Pssm-ID: 173829 Cd Length: 264 Bit Score: 71.34 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 128 VRLGWHDAGTYNKNIKEwpqrGGANGSLRFdiELKHAAN--AGLVNALNLIKDIKEKYSgiSYADLFQLASATAIEEAGG 205
Cdd:cd08201 46 LRTAFHDMATHNVDDGT----GGLDASIQY--ELDRPENigSGFNTTLNFFVNFYSPRS--SMADLIAMGVVTSVASCGG 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42572847 206 PKIPMKYGRVDASGPedcpeegrlPDAGPPSPATHL---REVFYRMGLDDKDIVALSG-AHTLGRSRPE 270
Cdd:cd08201 118 PVVPFRAGRIDATEA---------GQAGVPEPQTDLgttTESFRRQGFSTSEMIALVAcGHTLGGVHSE 177
|
|
| catalase_peroxidase_2 |
cd08200 |
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ... |
112-218 |
2.56e-06 |
|
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: 48.38 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 112 EDIKEL----LSTKFCHPILVRLGWHDAGTYNKNIKewpqRGGANGS-LRF----DIELKHAANAGLVnaLNLIKDIKEK 182
Cdd:cd08200 14 ADIAALkakiLASGLTVSELVSTAWASASTFRNSDK----RGGANGArIRLapqkDWEVNEPEELAKV--LAVLEGIQKE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 42572847 183 Y-------SGISYADLFQLASATAIEEA---GGPKIPMKY--GRVDAS 218
Cdd:cd08200 88 FnesqsggKKVSLADLIVLGGCAAVEKAakdAGVDIKVPFtpGRTDAT 135
|
|
| PLN03030 |
PLN03030 |
cationic peroxidase; Provisional |
169-363 |
4.99e-05 |
|
cationic peroxidase; Provisional
Pssm-ID: 215545 [Multi-domain] Cd Length: 324 Bit Score: 44.56 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 169 LVNALNLIKDIKEKYSG-----ISYADLFQLASATAIEEAGGPKIPMKYGRVD-----ASGPEDCPeegrlpdaGPPSPA 238
Cdd:PLN03030 92 LLRGYDVIDDAKTQLEAacpgvVSCADILALAARDSVVLTNGLTWPVPTGRRDgrvslASDASNLP--------GFTDSI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 239 THLREVFYRMGLDDKDIVALSGAHTLGRSRPERSGWGKpeTKYTKEGPGA---------PGGQSWTPE------------ 297
Cdd:PLN03030 164 DVQKQKFAAKGLNTQDLVTLVGGHTIGTTACQFFRYRL--YNFTTTGNGAdpsidasfvPQLQALCPQngdgsrrialdt 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42572847 298 --WLKFDNSYFKEIKEKRDedllVLPTDAAIFEDSSFKVYAEKYAADQD----AFFKDYAVAHAKLSNLGAE 363
Cdd:PLN03030 242 gsSNRFDASFFSNLKNGRG----ILESDQKLWTDASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIGVK 309
|
|
| KatG |
COG0376 |
Catalase (peroxidase I) [Inorganic ion transport and metabolism]; |
112-218 |
1.13e-03 |
|
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
Pssm-ID: 440145 [Multi-domain] Cd Length: 731 Bit Score: 40.87 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 112 EDIKEL----LSTKFCHPILVRLGWHDAGTYNKNIKewpqRGGANGS-LRFDIELKHAAN--AGLVNALNLIKDIKEKYS 184
Cdd:COG0376 444 ADIAALkakiLASGLSVSELVSTAWASASTFRGSDK----RGGANGArIRLAPQKDWEVNepEQLAKVLAVLEGIQKDFN 519
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 42572847 185 G-------ISYADLFQLASATAIEEA---GGPKI--PMKYGRVDAS 218
Cdd:COG0376 520 AaqsggkkVSLADLIVLGGCAAVEKAakdAGHDVtvPFTPGRTDAT 565
|
|
| PRK15061 |
PRK15061 |
catalase/peroxidase; |
127-218 |
1.99e-03 |
|
catalase/peroxidase;
Pssm-ID: 237891 [Multi-domain] Cd Length: 726 Bit Score: 40.12 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572847 127 LVRLGWHDAGTYNKNIKewpqRGGANGS-LRFDIELKHAAN--AGLVNALNLIKDIKEKYSG-------ISYADLFQLAS 196
Cdd:PRK15061 458 LVSTAWASASTFRGSDK----RGGANGArIRLAPQKDWEVNepAQLAKVLAVLEGIQAEFNAaqsggkkVSLADLIVLGG 533
|
90 100
....*....|....*....|....*..
gi 42572847 197 ATAIEEA---GGPKI--PMKYGRVDAS 218
Cdd:PRK15061 534 NAAVEQAakaAGHDVtvPFTPGRTDAT 560
|
|
| |
