|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02609 |
PLN02609 |
catalase |
1-492 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 1057.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 1 MDPYKHRPSSGANAGFWSTNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHD 80
Cdd:PLN02609 1 MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 81 ISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKP 160
Cdd:PLN02609 81 ISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 161 SPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEA 240
Cdd:PLN02609 161 NPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 241 VTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENE 320
Cdd:PLN02609 241 VRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 321 QIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNFIHRDEEVNYFPSRFDPT 400
Cdd:PLN02609 321 QLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 401 RHAQKYPIPTRVLTGCREKCIIEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDARVTHEIQGIWISYWSQCDTSLGQ 480
Cdd:PLN02609 401 RHAERVPIPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDKSLGQ 480
|
490
....*....|..
gi 357123085 481 KLGSRLKAKPNM 492
Cdd:PLN02609 481 KLASRLNVKPSM 492
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
16-486 |
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: 885.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 16 FWSTNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGV 95
Cdd:cd08154 1 TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 96 QTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDF 175
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 176 FSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDL 255
Cdd:cd08154 161 FSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 256 TDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHY 335
Cdd:cd08154 241 YDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 336 SDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNFIHRDEEVNYFPSRFDPTRHAQKYPIPTRVLTG 415
Cdd:cd08154 321 SDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLSG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357123085 416 CREKCIIEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDarVTHEIQGIWISYWSQCDTSLGQKLGSRL 486
Cdd:cd08154 401 TTQQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSD--VNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
19-490 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 756.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 19 TNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:COG0753 13 TNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 99 VIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSH 178
Cdd:COG0753 93 VFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTFWDFWSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 179 HPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDS 258
Cdd:COG0753 173 SPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHRRDLYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 259 IAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDD 338
Cdd:COG0753 253 IERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPGIDFSPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 339 KLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNFIHRDEEVNYFPSRFDPTRHAQKYPIPTRVLTG--C 416
Cdd:COG0753 333 KMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDPGFKEPPLKVDGdkV 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357123085 417 REKciIEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDARvTHEIQGIWISYWSQCDTSLGQKLGSRLKAKP 490
Cdd:COG0753 413 RYR--SESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVE-SEEIRERMVAHFYNVDPELGARVAEALGLDL 483
|
|
| Catalase |
pfam00199 |
Catalase; |
19-399 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 707.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 19 TNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 99 VIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSH 178
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 179 HPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDS 258
Cdd:pfam00199 162 NPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 259 IAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDD 338
Cdd:pfam00199 242 IERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357123085 339 KLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNF-IHRDEEVNYFPSRFDP 399
Cdd:pfam00199 322 PMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFdINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
21-392 |
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: 658.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 21 SGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVI 100
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 101 VRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHP 180
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 181 ESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIA 260
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 261 AGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKL 340
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 357123085 341 LQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNF-IHRDEEVNY 392
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVdGNQGGDPNY 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02609 |
PLN02609 |
catalase |
1-492 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 1057.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 1 MDPYKHRPSSGANAGFWSTNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHD 80
Cdd:PLN02609 1 MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 81 ISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKP 160
Cdd:PLN02609 81 ISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 161 SPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEA 240
Cdd:PLN02609 161 NPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 241 VTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENE 320
Cdd:PLN02609 241 VRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 321 QIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNFIHRDEEVNYFPSRFDPT 400
Cdd:PLN02609 321 QLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 401 RHAQKYPIPTRVLTGCREKCIIEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDARVTHEIQGIWISYWSQCDTSLGQ 480
Cdd:PLN02609 401 RHAERVPIPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDKSLGQ 480
|
490
....*....|..
gi 357123085 481 KLGSRLKAKPNM 492
Cdd:PLN02609 481 KLASRLNVKPSM 492
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
16-486 |
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: 885.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 16 FWSTNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGV 95
Cdd:cd08154 1 TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 96 QTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDF 175
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 176 FSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDL 255
Cdd:cd08154 161 FSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 256 TDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHY 335
Cdd:cd08154 241 YDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 336 SDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNFIHRDEEVNYFPSRFDPTRHAQKYPIPTRVLTG 415
Cdd:cd08154 321 SDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLSG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357123085 416 CREKCIIEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDarVTHEIQGIWISYWSQCDTSLGQKLGSRL 486
Cdd:cd08154 401 TTQQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSD--VNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
19-490 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 756.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 19 TNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:COG0753 13 TNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 99 VIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSH 178
Cdd:COG0753 93 VFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTFWDFWSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 179 HPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDS 258
Cdd:COG0753 173 SPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHRRDLYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 259 IAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDD 338
Cdd:COG0753 253 IERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPGIDFSPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 339 KLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNFIHRDEEVNYFPSRFDPTRHAQKYPIPTRVLTG--C 416
Cdd:COG0753 333 KMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDPGFKEPPLKVDGdkV 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357123085 417 REKciIEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDARvTHEIQGIWISYWSQCDTSLGQKLGSRLKAKP 490
Cdd:COG0753 413 RYR--SESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVE-SEEIRERMVAHFYNVDPELGARVAEALGLDL 483
|
|
| Catalase |
pfam00199 |
Catalase; |
19-399 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 707.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 19 TNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 99 VIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSH 178
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 179 HPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDS 258
Cdd:pfam00199 162 NPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 259 IAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDD 338
Cdd:pfam00199 242 IERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357123085 339 KLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNF-IHRDEEVNYFPSRFDP 399
Cdd:pfam00199 322 PMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFdINQGSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
21-392 |
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: 658.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 21 SGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVI 100
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 101 VRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHP 180
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 181 ESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIA 260
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 261 AGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKL 340
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 357123085 341 LQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHEGFMNF-IHRDEEVNY 392
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVdGNQGGDPNY 373
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
58-486 |
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: 525.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 58 RIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVG 137
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 138 NNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDG 217
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 218 KVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDI 297
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 298 IPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHH 377
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 378 EGFMNFIH-RDEEVNYFPSRFDPTRHAQKYPIPTRVLTG--CREKCIIEkENNFKQAGERYRSFDPARQDRFIQRWVDAL 454
Cdd:cd08156 321 DGAMRVDGnGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGdaDRYNYRDD-DDDYTQAGDLYRLVSEDERERLVENIAGHL 399
|
410 420 430
....*....|....*....|....*....|..
gi 357123085 455 SDARvtHEIQGIWISYWSQCDTSLGQKLGSRL 486
Cdd:cd08156 400 KGAP--EFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
58-482 |
0e+00 |
|
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: 515.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 58 RIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVG 137
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 138 NNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDG 217
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 218 KVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDI 297
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 298 IPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHH 377
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 378 EGFMNFIHRDEEVNYFPSRFDPTRHAQKYPIPTR-----VLTGCREKCIIEKENNFKQAGERYRSFDPARQDRFIQRWVD 452
Cdd:cd00328 321 DGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDRghfshWKSGVNREASTTNDDNFTQARLFYRSLTPGQQKRLVDAFRF 400
|
410 420 430
....*....|....*....|....*....|
gi 357123085 453 ALSDArVTHEIQGIWISYWSQCDTSLGQKL 482
Cdd:cd00328 401 ELADA-VSPQIQQRVLDQFAKVDAAAAKRV 429
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
18-386 |
1.54e-178 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 519.22 E-value: 1.54e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 18 STNSGAPVWNNNNALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQT 97
Cdd:PRK11249 78 TTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKIT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 98 PVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQEN-------W 170
Cdd:PRK11249 158 PVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGqsahdtfW 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 171 rivDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTH 250
Cdd:PRK11249 238 ---DYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 251 ATKDLTDSIAAGNYPEWKLFIQTIDADHEDKFDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIV 330
Cdd:PRK11249 315 HRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIV 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 357123085 331 PGIHYSDDKLLQTRIFSYADTQRHRL-GPNYLMLPVNAPKCAHHNNHHEGFmnfiHR 386
Cdd:PRK11249 395 PGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGM----HR 447
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
55-398 |
4.96e-173 |
|
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: 494.19 E-value: 4.96e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 55 DRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFD 134
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 135 LVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQEN-------WrivDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGV 207
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAqsahdtfW---DFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 208 NTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDKFDFDPL 287
Cdd:cd08155 158 HTFRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 288 DVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLG-PNYLMLPVN 366
Cdd:cd08155 238 DPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPIN 317
|
330 340 350
....*....|....*....|....*....|..
gi 357123085 367 APKCAHHNNHHEGFMNFIHRDEEVNYFPSRFD 398
Cdd:cd08155 318 RPVCPVHNNQRDGHMRMTINKGRVNYFPNSLG 349
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
42-487 |
7.21e-163 |
|
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: 468.75 E-value: 7.21e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 42 LEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRG 121
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 122 FAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRH 201
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 202 MEGFGVNTYTLINKDGKVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHTHATKDLTDSIAAGNYPEWKLFIQTIDADHEDK 281
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 282 FDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYL 361
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 362 MLPVNAPKC------------AHHNNHHEGFMNFIHRDEEVNYFPSRFDPTRHAQKYPI-PTRVLTGCREKciiekenNF 428
Cdd:cd08157 321 QLPVNRPKTspvynpyqrdgpMSVNGNYGGDPNYVSSILPPTYFKKRVDADGHHENWVGeVVAFLTEITDE-------DF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 429 KQAGERY-RSFDPARQDRFIQRWVDALSDARVthEIQGIWISYWSQCDTSLGQKLGSRLK 487
Cdd:cd08157 394 VQPRALWeVVGKPGQQERFVKNVAGHLSGAPP--EIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
60-356 |
1.85e-59 |
|
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: 197.40 E-value: 1.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 60 PERVVHARGASAKGFFEVTHDISHLTCADFLrAPGVQTPVIVRFSTVvheRGSPETLRDPRGFAVKFYT--REGNFDLVG 137
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLF-AEGKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGvaDAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 138 NNMPVFFIRDGMKFPDMVHAFKPSPkTNMQENWRIVDFFSHHPESLHMFSFLFDdvGIPLNYRHMEGFGVNTYTLINKDG 217
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSA-RGEPPLDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 218 KVHLVKFHWKPTCGVKCLLDDEAVTVGGTCHthaTKDLTDSIAAGnYPEWKLFIQTidadHEDKFDFDPLDVTKTWPEDi 297
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELEARPPDYL---REELTERLQRG-PVVYDFRIQL----NDDTDATTIDNPTILWPTE- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357123085 298 IPLQPVGRMILNKNIDNffAENEQIAFCPAIIVPGIHYSDDK--LLQTRIFSYADTQRHRL 356
Cdd:cd08150 225 HPVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
62-356 |
4.26e-35 |
|
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: 132.74 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 62 RVVHARGASAKGFFEVTHDISHLTCADFLRapGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNF-DLVGNNM 140
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEQwRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 141 PVFFIRDGMKFPDMVHAFKPSP--KTNMQenwRIVDFFSHHPESLHMFSFLfDDVGIPLNYRHMEGFGVNTYTLINKDGK 218
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIAPDAtgKPDPA---KLKAFLAAHPEAAAFLAWI-KTAPPPASFANTTYYGVNAFYFTNANGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 219 VHLVKFHWKPTCGVKCLLDDEAVTVGgtcHTHATKDLTDSIAAGNYpEWKLFIQTIDADhedkfdfDPL-DVTKTWPED- 296
Cdd:cd08153 169 RQPVRWRFVPEDGVKYLSDEEAAKLG---PDFLFDELAQRLAQGPV-RWDLVLQLAEPG-------DPTdDPTKPWPADr 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357123085 297 --IIplqpVGRMILNKNIDNFFAENEQIAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRL 356
Cdd:cd08153 238 keVD----AGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
422-486 |
9.25e-17 |
|
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: 74.32 E-value: 9.25e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357123085 422 IEKENNFKQAGERYRSFDPARQDRFIQRWVDALSDArVTHEIQGIWISYWSQCDTSLGQKLGSRL 486
Cdd:pfam06628 2 IDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKV-TDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
62-325 |
1.20e-09 |
|
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: 59.58 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 62 RVVHARG-ASAKGFFEVTHDISHlTCADFLRAPGVQTPVIVRFSTvvherGSPE----TLRDPRGFAVKFYTREG----- 131
Cdd:cd08152 5 RDAHAKShGCLKAEFTVLDDLPP-ELAQGLFAEPGTYPAVIRFSN-----APGDilddSVPDPRGMAIKVLGVPGekllp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 132 -----NFDLVGNNMPVFFIRDGMKF-------------PDMVHAFKPSPKTNMQENWRIV-------DFFSHHPES-LHM 185
Cdd:cd08152 79 eedatTQDFVLVNHPVFFARDAKDYlallkllarttslPDGAKAALSAPLRGALRVLEAAggesptlKLGGHPPAHpLGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 186 --FS---FLFDDvgiplnyrhmegfgvntytlinkdgkvHLVKFHWKPTCGVKCLLDDEAVTVGGTcHTHATKDLTDSIA 260
Cdd:cd08152 159 tyWSqapYRFGD---------------------------YVAKYSVVPASPALPALTGKELDLTDD-PDALREALADFLA 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357123085 261 AGNYpEWKLFIQ--TiDADHEdkfdfdPL-DVTKTWPEDIIPLQPVGRMILNKNidNFFAENEQIAFC 325
Cdd:cd08152 211 ENDA-EFEFRIQlcT-DLEKM------PIeDASVEWPEALSPFVPVATITIPPQ--DFDSPARQRAFD 268
|
|
| AOS |
cd08151 |
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ... |
62-327 |
4.91e-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: 48.57 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 62 RVVHARGASAKGFFEVTHDI---SHltcaDFLRaPGVQTPVIVRFSTVVherGSPETLR-DPRGFAVKFYT----REGNF 133
Cdd:cd08151 28 RGTHTIGVGAKGVLTVLAESdfpEH----AFFT-AGKRFPVILRHANIV---GGDDDASlDGRGAALRFLNagddDAGPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 134 DLVGNNMPVFFIRDGMKFPDMVHAFKPSpktnmqeNWRiVDFFSHHPESLHMFSFLFDDvgiPLNYRHMEGFGVNTYTLI 213
Cdd:cd08151 100 DLVMNTGESFGFWTAASFADFAGAGLPF-------REK-AAKLRGPLARYAVWASLRRA---PDSYTDLHYYSQICYEFV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357123085 214 NKDGKVHLVKFHWKP-TCGVKCLLDDEAVTVGGTCHTHATKDLTDSIAAGNY-----------PEWKLFIQTIDADHEDK 281
Cdd:cd08151 169 ALDGKSRYARFRLLPpDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYlrnefrqrlqsPGVRYRLQIQLREVSDD 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 357123085 282 FDFDPLDVTKTWPEDIIPLQPVGRMILNKNIDNffAENEQIAFCPA 327
Cdd:cd08151 249 ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPN--DELEKLAFNPG 292
|
|
| |
