|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
2-487 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 889.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 2 SNKSKLTGLFGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFS 81
Cdd:COG0753 6 DEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 82 EIGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQS 161
Cdd:COG0753 86 EPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 162 NWDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESS 241
Cdd:COG0753 166 FWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 242 QRDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIP 321
Cdd:COG0753 246 RRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 322 GIDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNVcpFSRDGQMRIDGNqGGGINYYPNSYEAHQSQPEYKK 401
Cdd:COG0753 326 GIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHN--YQRDGAMRYDIN-GGRVNYEPNSLGGPREDPGFKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 402 PSLELEGELYEHDFREDDDnyYEQPGKLFRLQSPEQQQRIFQNTANEMQG-TTDEVKHRHIRNCYKADPDYGKGVADALG 480
Cdd:COG0753 403 PPLKVDGDKVRYRSESDDH--FSQAGLLYRSMSDEEKQHLIDNIAFELGKvESEEIRERMVAHFYNVDPELGARVAEALG 480
|
....*..
gi 969850678 481 IDINSVD 487
Cdd:COG0753 481 LDLPEAK 487
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
48-479 |
0e+00 |
|
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163712 [Multi-domain] Cd Length: 429 Bit Score: 816.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 48 VIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVG 127
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 128 NNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAG 207
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 208 ERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDE 287
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 288 YPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNVcpF 367
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNN--Y 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 368 SRDGQMRIDGNQGGGINYYPNSYEAHQSQPEYKKPSLELEGELYEHDFREDDDnYYEQPGKLFRLQSPEQQQRIFQNTAN 447
Cdd:cd08156 319 QRDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRDDDD-DYTQAGDLYRLVSEDERERLVENIAG 397
|
410 420 430
....*....|....*....|....*....|..
gi 969850678 448 EMQGTTDEVKHRHIRNCYKADPDYGKGVADAL 479
Cdd:cd08156 398 HLKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
11-391 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 752.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 11 FGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMF 90
Cdd:pfam00199 4 NGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTPVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 91 ARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLP 170
Cdd:pfam00199 84 VRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSLNP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 171 EALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIE 250
Cdd:pfam00199 164 ESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEAIE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 251 EGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKM 330
Cdd:pfam00199 244 RGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPDPM 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 969850678 331 LQGRLFSYGDAQRYRLGVNHWQIPVNSPKAAtnVCPFSRDGQMRIDGNQGGGINYYPNSYE 391
Cdd:pfam00199 324 LQGRLFSYPDTQRYRLGPNYQQLPVNRPPCP--VHNYQRDGAMRFDINQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
11-385 |
0e+00 |
|
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.
Pssm-ID: 215003 Cd Length: 373 Bit Score: 721.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 11 FGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMF 90
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 91 ARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLP 170
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 171 EALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIE 250
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 251 EGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKM 330
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 969850678 331 LQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNvcPFSRDGQMRIDGNQGGGINY 385
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVH--NYQRDGAMRVDGNQGGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
3-481 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 532.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 3 NKSKLTGLFGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSE 82
Cdd:PLN02609 13 NSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 83 IGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSN 162
Cdd:PLN02609 93 PGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 163 WDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQ 242
Cdd:PLN02609 173 LDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHAT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 243 RDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPG 322
Cdd:PLN02609 253 QDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 323 IDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAAtnVCPFSRDGQMRIDGNqGGGINYYPNSYEAHQSQPEYKKP 402
Cdd:PLN02609 333 IYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCA--HHNNHHEGFMNFMHR-DEEVNYFPSRFDPVRHAERVPIP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 403 SLELEGELYEHDFREDDDnyYEQPGKLFRLQSPEQQQRIFQNTANEMQGTTDEVKHRHIRNCY--KADPDYGKGVADALG 480
Cdd:PLN02609 410 HPPLSGRREKCKIEKENN--FKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYwsQCDKSLGQKLASRLN 487
|
.
gi 969850678 481 I 481
Cdd:PLN02609 488 V 488
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
2-487 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 889.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 2 SNKSKLTGLFGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFS 81
Cdd:COG0753 6 DEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 82 EIGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQS 161
Cdd:COG0753 86 EPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 162 NWDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESS 241
Cdd:COG0753 166 FWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 242 QRDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIP 321
Cdd:COG0753 246 RRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 322 GIDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNVcpFSRDGQMRIDGNqGGGINYYPNSYEAHQSQPEYKK 401
Cdd:COG0753 326 GIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHN--YQRDGAMRYDIN-GGRVNYEPNSLGGPREDPGFKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 402 PSLELEGELYEHDFREDDDnyYEQPGKLFRLQSPEQQQRIFQNTANEMQG-TTDEVKHRHIRNCYKADPDYGKGVADALG 480
Cdd:COG0753 403 PPLKVDGDKVRYRSESDDH--FSQAGLLYRSMSDEEKQHLIDNIAFELGKvESEEIRERMVAHFYNVDPELGARVAEALG 480
|
....*..
gi 969850678 481 IDINSVD 487
Cdd:COG0753 481 LDLPEAK 487
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
48-479 |
0e+00 |
|
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163712 [Multi-domain] Cd Length: 429 Bit Score: 816.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 48 VIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVG 127
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 128 NNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAG 207
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 208 ERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDE 287
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 288 YPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNVcpF 367
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNN--Y 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 368 SRDGQMRIDGNQGGGINYYPNSYEAHQSQPEYKKPSLELEGELYEHDFREDDDnYYEQPGKLFRLQSPEQQQRIFQNTAN 447
Cdd:cd08156 319 QRDGAMRVDGNGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRDDDD-DYTQAGDLYRLVSEDERERLVENIAG 397
|
410 420 430
....*....|....*....|....*....|..
gi 969850678 448 EMQGTTDEVKHRHIRNCYKADPDYGKGVADAL 479
Cdd:cd08156 398 HLKGAPEFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| Catalase |
pfam00199 |
Catalase; |
11-391 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 752.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 11 FGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMF 90
Cdd:pfam00199 4 NGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTPVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 91 ARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLP 170
Cdd:pfam00199 84 VRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSLNP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 171 EALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIE 250
Cdd:pfam00199 164 ESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEAIE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 251 EGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKM 330
Cdd:pfam00199 244 RGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPDPM 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 969850678 331 LQGRLFSYGDAQRYRLGVNHWQIPVNSPKAAtnVCPFSRDGQMRIDGNQGGGINYYPNSYE 391
Cdd:pfam00199 324 LQGRLFSYPDTQRYRLGPNYQQLPVNRPPCP--VHNYQRDGAMRFDINQGSRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
11-385 |
0e+00 |
|
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.
Pssm-ID: 215003 Cd Length: 373 Bit Score: 721.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 11 FGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMF 90
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 91 ARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLP 170
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 171 EALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIE 250
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 251 EGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKM 330
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 969850678 331 LQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNvcPFSRDGQMRIDGNQGGGINY 385
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVH--NYQRDGAMRVDGNQGGDPNY 373
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
12-479 |
0e+00 |
|
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 1 catalases are found in bacteria, algae, and plants; they have a relatively small subunit size of 55 to 69 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163710 [Multi-domain] Cd Length: 469 Bit Score: 582.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 12 GAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFA 91
Cdd:cd08154 7 GAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKKTPVFV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 92 RFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLPE 171
Cdd:cd08154 87 RFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFFSHVPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 172 ALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIEE 251
Cdd:cd08154 167 STHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLYDAIAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 252 GNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKML 331
Cdd:cd08154 247 GNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPSDDKML 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 332 QGRLFSYGDAQRYRLGVNHWQIPVNSPKAA--TNVcpfsRDGQMRIdGNQGGGINYYPNSYEAHQSQPEYKKPSLELEGE 409
Cdd:cd08154 327 QGRLFSYSDTQRYRLGPNYLQLPINAPKAAvhNNQ----RDGQMNY-GHDTSDVNYEPSRLDGLPEAPKYPYSQPPLSGT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 410 LYEHdfREDDDNYYEQPGKLFRLQSPEQQQRIFQNTANEMQGTTDEVKHRHIRNCYKADPDYGKGVADAL 479
Cdd:cd08154 402 TQQA--PIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSDVNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
32-480 |
0e+00 |
|
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though.
Pssm-ID: 163713 [Multi-domain] Cd Length: 451 Bit Score: 546.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 32 MQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFARFSTVAGERGAAEAERDIRG 111
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 112 FALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLPEALHQVTILMTDRGIPKGFRN 191
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 192 MHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIEEGNFPKWKMYIQVMTEEQARN 271
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 272 HKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKMLQGRLFSYGDAQRYRLGVNHW 351
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 352 QIPVNSPKAATNVCPFSRDGQMRIDGNQGGGINY----YPNSYEAHQSQPEYKKPSLELEGELYEHDFREDDdnyYEQPG 427
Cdd:cd08157 321 QLPVNRPKTSPVYNPYQRDGPMSVNGNYGGDPNYvssiLPPTYFKKRVDADGHHENWVGEVVAFLTEITDED---FVQPR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 969850678 428 KL-FRLQSPEQQQRIFQNTANEMQGTTDEVKHRHIRNCYKADPDYGKGVADALG 480
Cdd:cd08157 398 ALwEVVGKPGQQERFVKNVAGHLSGAPPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| PLN02609 |
PLN02609 |
catalase |
3-481 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 532.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 3 NKSKLTGLFGAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSE 82
Cdd:PLN02609 13 NSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 83 IGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSN 162
Cdd:PLN02609 93 PGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 163 WDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQ 242
Cdd:PLN02609 173 LDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHAT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 243 RDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPG 322
Cdd:PLN02609 253 QDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 323 IDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAAtnVCPFSRDGQMRIDGNqGGGINYYPNSYEAHQSQPEYKKP 402
Cdd:PLN02609 333 IYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCA--HHNNHHEGFMNFMHR-DEEVNYFPSRFDPVRHAERVPIP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 403 SLELEGELYEHDFREDDDnyYEQPGKLFRLQSPEQQQRIFQNTANEMQGTTDEVKHRHIRNCY--KADPDYGKGVADALG 480
Cdd:PLN02609 410 HPPLSGRREKCKIEKENN--FKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYwsQCDKSLGQKLASRLN 487
|
.
gi 969850678 481 I 481
Cdd:PLN02609 488 V 488
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
49-479 |
5.89e-178 |
|
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Most catalases exist as tetramers of 65KD subunits containing a protoheme IX group buried deep inside the structure. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163705 [Multi-domain] Cd Length: 433 Bit Score: 506.23 E-value: 5.89e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 49 IPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGN 128
Cdd:cd00328 2 IPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 129 NTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSNWDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGE 208
Cdd:cd00328 82 NTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 209 RVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLTKVWFKDEY 288
Cdd:cd00328 162 VHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEELV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 289 PLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKMLQGRLFSYGDAQRYRLGVNHWQIPVNSPKAATNvcPFS 368
Cdd:cd00328 242 PLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVH--NNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 369 RDGQMRIDGNQgGGINYYPNSYEAHQSQPEYKKPSLELEGELYEHDFRED---DDNYYEQPGKLFRLQSPEQQQRIFQNT 445
Cdd:cd00328 320 RDGAGNMNDNT-GVPNYEPNAKDVRYPAQGAPKFDRGHFSHWKSGVNREAsttNDDNFTQARLFYRSLTPGQQKRLVDAF 398
|
410 420 430
....*....|....*....|....*....|....*
gi 969850678 446 ANEMQGTTD-EVKHRHIRNCYKADPDYGKGVADAL 479
Cdd:cd00328 399 RFELADAVSpQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
45-479 |
8.72e-142 |
|
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163711 Cd Length: 443 Bit Score: 414.46 E-value: 8.72e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 45 DREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGNWD 124
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 125 LVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSN----WDFWTLLPEALHQVTILMTDRGIPKGFRNMHGFGSHTY 200
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAhdtfWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 201 SMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFNAIEEGNFPKWKMYIQVMTEEQARNHKDNPFDLT 280
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 281 KVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKMLQGRLFSYGDAQRYRLG-VNHWQIPVNSPk 359
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINRP- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 360 aatnVCPFS---RDGQMRIDGNQgGGINYYPNSYEAhqSQPEYKKPslelEGELYEHDFREDD-----------DNYYEQ 425
Cdd:cd08155 320 ----VCPVHnnqRDGHMRMTINK-GRVNYFPNSLGA--GPPRAASP----AEGGFVHYPEKVEgpkirirsesfADHYSQ 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 969850678 426 PGKLFRLQSPEQQQRIFQNTANEMqgttDEVKHRHIRNCY-----KADPDYGKGVADAL 479
Cdd:cd08155 389 ARLFWNSMSPVEKEHIISAFTFEL----SKVETPEIRERVvdhlaNIDEDLAKKVAKGL 443
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
12-482 |
4.15e-140 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 420.60 E-value: 4.15e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 12 GAPVSDRENSLTAGKRGPLAMQDIYFLEQMAHFDREVIPERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEIGKQTEMFA 91
Cdd:PRK11249 82 GVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKITPVFV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 92 RFSTVAGERGAAEAERDIRGFALKFYTEEGNWDLVGNNTPVFFFRDPKLFASLNHVVKRDPKTNMHNPQSN----WDFWT 167
Cdd:PRK11249 162 RFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQSAhdtfWDYVS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 168 LLPEALHQVTILMTDRGIPKGFRNMHGFGSHTYSMYNDAGERVWVKFHFRTQQGIENYTAEEAEQVIAKDRESSQRDLFN 247
Cdd:PRK11249 242 LQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDFHRRDLWE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 248 AIEEGNFPKWKMYIQVMTEEQArnHKDNpFDL---TKVWFKDEYPLIPVGEFELNRNPENYFQDVEQAAFAPTNIIPGID 324
Cdd:PRK11249 322 AIEAGDYPEYELGVQLIPEEDE--FKFD-FDLldpTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIVPGID 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 325 FSPDKMLQGRLFSYGDAQRYRL-GVNHWQIPVNSPkaatnVCPF---SRDGQMR--IDGNQGggiNYYPNSYEA---HQS 395
Cdd:PRK11249 399 FTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRP-----TCPYhnfQRDGMHRmtIDTGPA---NYEPNSINGnwpRET 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 396 QPEYKKPSLELEGELYE-HDFREDDD---NYYEQPGKLFRLQSPEQQQRIFQNTANEMQGTT-DEVKHRHIRNCYKADPD 470
Cdd:PRK11249 471 PPAPKRGGFESYQERVEgNKVRERSPsfgDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVrPYIRERVVDQLAHIDLT 550
|
490
....*....|..
gi 969850678 471 YGKGVADALGID 482
Cdd:PRK11249 551 LAQAVAENLGIP 562
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
50-346 |
4.64e-52 |
|
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.
Pssm-ID: 163706 Cd Length: 283 Bit Score: 177.75 E-value: 4.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 50 PERRMHAKGSGAFGTFTVTHDITQYTNAKIFSEiGKQTEMFARFSTVAgerGAAEAERDIRGFALKFYTE--EGNWDLVG 127
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAE-GKVYPAYIRFSNGA---GIDDTKPDIRGFAIKFTGVadAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 128 NNTPVFFFRDPKLFASLNHVVKRDPkTNMHNPQSNWDFWTLLPEALHQVTILMtdRGIPKGFRNMHGFGSHTYSMYNDAG 207
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSA-RGEPPLDFIAWYVEKRPEDLPNLLGAR--SQVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 208 ERVWVKFHFRTQQGIENYTAEEAEqviAKDRESSQRDLFNAIEEGnFPKWKMYIQVMTEEQARNhKDNPfdlTKVWFKdE 287
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRG-PVVYDFRIQLNDDTDATT-IDNP---TILWPT-E 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 969850678 288 YPLIPVGEFELNRNPENYFQdvEQAAFAPTNIIPGIDFSPDK--MLQGRLFSYGDAQRYRL 346
Cdd:cd08150 225 HPVEAVAKITIPPPTFTAAQ--EAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
52-334 |
1.01e-29 |
|
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism.
Pssm-ID: 163709 Cd Length: 295 Bit Score: 117.72 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 52 RRMHAKGSGAFGTFTVTHDITQYTNAKIFSeiGKQTEMFARFSTVAGERGAAEAERDIRGFALKFYTEEGN-WDLVGNNT 130
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 131 PVFFFRDPKLFASLNHVVKRDPkTNMHNPQSNWDFWTLLPEALHQVTILMTdRGIPKGFRNMHGFGSHTYSMYNDAGERV 210
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIAPDA-TGKPDPAKLKAFLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNANGKRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 211 WVKFHFRTQQGIENYTAEEAEQviaKDRESSQRDLFNAIEEGNFpKWKMYIQVMteeqarNHKDNPFDLTKVWfKDEYPL 290
Cdd:cd08153 171 PVRWRFVPEDGVKYLSDEEAAK---LGPDFLFDELAQRLAQGPV-RWDLVLQLA------EPGDPTDDPTKPW-PADRKE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 969850678 291 IPVGEFELNRNPENYFQDVEQAAFAPTNIIPGIDFSPDKMLQGR 334
Cdd:cd08153 240 VDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAAR 283
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
416-479 |
8.01e-23 |
|
Catalase-related immune-responsive; This family represents a small conserved region within catalase enzymes (EC:1.11.1.6). All members also contain the Catalase family, pfam00199 domain. Catalase decomposes hydrogen peroxide into water and oxygen, serving to protect cells from its toxic effects. This domain carries the immune-responsive amphipathic octa-peptide that is recognized by T cells.
Pssm-ID: 461967 [Multi-domain] Cd Length: 65 Bit Score: 91.66 E-value: 8.01e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 969850678 416 REDDDNYYEQPGKLFRLQSPEQQQRIFQNTANEMQG-TTDEVKHRHIRNCYKADPDYGKGVADAL 479
Cdd:pfam06628 1 SIDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKvTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
52-144 |
6.39e-08 |
|
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.
Pssm-ID: 163708 Cd Length: 305 Bit Score: 54.19 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 52 RRMHAKGSGAF-GTFTVTHDITQYTNAKIFSEiGKQTEMFARFSTVAGERgAAEAERDIRGFALKFY----------TEE 120
Cdd:cd08152 5 RDAHAKSHGCLkAEFTVLDDLPPELAQGLFAE-PGTYPAVIRFSNAPGDI-LDDSVPDPRGMAIKVLgvpgekllpeEDA 82
|
90 100
....*....|....*....|....
gi 969850678 121 GNWDLVGNNTPVFFFRDPKLFASL 144
Cdd:cd08152 83 TTQDFVLVNHPVFFARDAKDYLAL 106
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
52-318 |
3.39e-06 |
|
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.
Pssm-ID: 163707 Cd Length: 328 Bit Score: 48.96 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 52 RRMHAKGSGAFGTFTVTHDItQYTNAKIFSEiGKQTEMFARFSTVAGERGAAEAerDIRGFALKFYT----EEGNWDLVG 127
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAES-DFPEHAFFTA-GKRFPVILRHANIVGGDDDASL--DGRGAALRFLNagddDAGPLDLVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 128 NNTPVFFFRDPKLFASLnhVVKRDPKTNMHNPQSNWDFWTLLPEALhqvtilmtdRGIPKGFRNMHGFGSHTYSMYNDAG 207
Cdd:cd08151 104 NTGESFGFWTAASFADF--AGAGLPFREKAAKLRGPLARYAVWASL---------RRAPDSYTDLHYYSQICYEFVALDG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 969850678 208 ERVWVKFHFR-----TQQGIENYTAEEAEQ----VIAKDRESSQRDLFNA---IEEGNFPKWKMYIQVMTEEQARNHKDN 275
Cdd:cd08151 173 KSRYARFRLLppdadTEWDLGEDVLETIFQrprlYLPRLPGDTRPKDYLRnefRQRLQSPGVRYRLQIQLREVSDDATAV 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 969850678 276 PFDLTKVWFKDEYPLIPVGEFELNRNPENyfQDVEQAAFAPTN 318
Cdd:cd08151 253 ALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPGN 293
|
|
| |
