|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02609 |
PLN02609 |
catalase |
1-492 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 1059.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 1 MDPYKHRPSSSFNGPMWSTNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHD 80
Cdd:PLN02609 1 MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 81 ISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKP 160
Cdd:PLN02609 81 ISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 161 NPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEA 240
Cdd:PLN02609 161 NPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 241 VTVGGTNHSHATKDLYDSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENE 320
Cdd:PLN02609 241 VRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 321 QLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRDEEVDYFPSRFDPA 400
Cdd:PLN02609 321 QLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 401 KHAPRYPIPSSTCNGRREKMVIEKENNFKQPGERYRSMDPARQERFINRWIDALSDPRLTHEIKSIWLSYWSQADRSLGQ 480
Cdd:PLN02609 401 RHAERVPIPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDKSLGQ 480
|
490
....*....|..
gi 357114208 481 KLASRLSAKPSM 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 ... |
17-486 |
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: 888.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 17 WSTNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQ 96
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 97 TPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFF 176
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 177 SHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLY 256
Cdd:cd08154 162 SHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 257 DSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYS 336
Cdd:cd08154 242 DAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 337 DDKLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRDEEVDYFPSRFDPAKHAPRYPIPSSTCNGR 416
Cdd:cd08154 322 DDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLSGT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 417 REKMVIEKENNFKQPGERYRSMDPARQERFINRWIDALSDPrlTHEIKSIWLSYWSQADRSLGQKLASRL 486
Cdd:cd08154 402 TQQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSDV--NEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
19-491 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 769.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 19 TNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:COG0753 13 TNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 99 VIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSH 178
Cdd:COG0753 93 VFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTFWDFWSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 179 HPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDS 258
Cdd:COG0753 173 SPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHRRDLYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 259 IAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDD 338
Cdd:COG0753 253 IERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPGIDFSPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 339 KLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRDEEVDYFPSRFDPAKHAPRYPIPSSTCNGRRE 418
Cdd:COG0753 333 KMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDPGFKEPPLKVDGDKV 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357114208 419 KMVIEKENNFKQPGERYRSMDPARQERFINRWIDALSDPRlTHEIKSIWLSYWSQADRSLGQKLASRLSAKPS 491
Cdd:COG0753 413 RYRSESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVE-SEEIRERMVAHFYNVDPELGARVAEALGLDLP 484
|
|
| Catalase |
pfam00199 |
Catalase; |
19-399 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 714.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 19 TNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 99 VIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSH 178
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 179 HPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDS 258
Cdd:pfam00199 162 NPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 259 IAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDD 338
Cdd:pfam00199 242 IERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357114208 339 KLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRD-EEVDYFPSRFDP 399
Cdd:pfam00199 322 PMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFDINQgSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
21-384 |
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: 666.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 21 SGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVI 100
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 101 VRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSHHP 180
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 181 ESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDSIA 260
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 261 AGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKL 340
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 357114208 341 LQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFM 384
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVD 364
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02609 |
PLN02609 |
catalase |
1-492 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 1059.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 1 MDPYKHRPSSSFNGPMWSTNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHD 80
Cdd:PLN02609 1 MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 81 ISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKP 160
Cdd:PLN02609 81 ISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 161 NPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEA 240
Cdd:PLN02609 161 NPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 241 VTVGGTNHSHATKDLYDSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENE 320
Cdd:PLN02609 241 VRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 321 QLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRDEEVDYFPSRFDPA 400
Cdd:PLN02609 321 QLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 401 KHAPRYPIPSSTCNGRREKMVIEKENNFKQPGERYRSMDPARQERFINRWIDALSDPRLTHEIKSIWLSYWSQADRSLGQ 480
Cdd:PLN02609 401 RHAERVPIPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDKSLGQ 480
|
490
....*....|..
gi 357114208 481 KLASRLSAKPSM 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 ... |
17-486 |
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: 888.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 17 WSTNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQ 96
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 97 TPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFF 176
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 177 SHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLY 256
Cdd:cd08154 162 SHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 257 DSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYS 336
Cdd:cd08154 242 DAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 337 DDKLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRDEEVDYFPSRFDPAKHAPRYPIPSSTCNGR 416
Cdd:cd08154 322 DDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLSGT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 417 REKMVIEKENNFKQPGERYRSMDPARQERFINRWIDALSDPrlTHEIKSIWLSYWSQADRSLGQKLASRL 486
Cdd:cd08154 402 TQQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSDV--NEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
19-491 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 769.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 19 TNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:COG0753 13 TNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 99 VIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSH 178
Cdd:COG0753 93 VFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTFWDFWSL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 179 HPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDS 258
Cdd:COG0753 173 SPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHRRDLYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 259 IAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDD 338
Cdd:COG0753 253 IERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPGIDFSPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 339 KLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRDEEVDYFPSRFDPAKHAPRYPIPSSTCNGRRE 418
Cdd:COG0753 333 KMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPREDPGFKEPPLKVDGDKV 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357114208 419 KMVIEKENNFKQPGERYRSMDPARQERFINRWIDALSDPRlTHEIKSIWLSYWSQADRSLGQKLASRLSAKPS 491
Cdd:COG0753 413 RYRSESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVE-SEEIRERMVAHFYNVDPELGARVAEALGLDLP 484
|
|
| Catalase |
pfam00199 |
Catalase; |
19-399 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 714.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 19 TNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTP 98
Cdd:pfam00199 2 TSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 99 VIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSH 178
Cdd:pfam00199 82 VFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 179 HPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDS 258
Cdd:pfam00199 162 NPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 259 IAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDD 338
Cdd:pfam00199 242 IERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSPD 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357114208 339 KLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFMHRD-EEVDYFPSRFDP 399
Cdd:pfam00199 322 PMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFDINQgSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
21-384 |
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: 666.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 21 SGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVI 100
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 101 VRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSHHP 180
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 181 ESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDSIA 260
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 261 AGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKL 340
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 357114208 341 LQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHYDGTMNFM 384
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVD 364
|
|
| 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: 539.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 58 RIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVG 137
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 138 NNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAG 217
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 218 KSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDI 297
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 298 IPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHY 377
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 378 DGTMNFMH-RDEEVDYFPSRFDPAKHAPRYPIPSSTCNG---RREKMviEKENNFKQPGERYRSMDPARQERFINRWIDA 453
Cdd:cd08156 321 DGAMRVDGnGGGAPNYEPNSFGGPPEDPEYAEPPLPVSGdadRYNYR--DDDDDYTQAGDLYRLVSEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|...
gi 357114208 454 LSDPRLthEIKSIWLSYWSQADRSLGQKLASRL 486
Cdd:cd08156 399 LKGAPE--FIQERQVAHFYKADPDYGERVAKAL 429
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
58-483 |
2.59e-179 |
|
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: 509.70 E-value: 2.59e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 58 RIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVG 137
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 138 NNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAG 217
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 218 KSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDI 297
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 298 IPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLLLPANAPKCAHHNNHY 377
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 378 DGTMNFMHRDEEVDYFPSRFDPAKHAPRYPIPSSTCNGRREKMV-----IEKENNFKQPGERYRSMDPARQERFINRWID 452
Cdd:cd00328 321 DGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDRGHFSHWKSGVnreasTTNDDNFTQARLFYRSLTPGQQKRLVDAFRF 400
|
410 420 430
....*....|....*....|....*....|.
gi 357114208 453 ALSDPRLThEIKSIWLSYWSQADRSLGQKLA 483
Cdd:cd00328 401 ELADAVSP-QIQQRVLDQFAKVDAAAAKRVA 430
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
18-399 |
1.21e-177 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 516.90 E-value: 1.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 18 STNSGAPVWNNDNSLTVGPRGPILLEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQT 97
Cdd:PRK11249 78 TTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKIT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 98 PVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQEN-------W 170
Cdd:PRK11249 158 PVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGqsahdtfW 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 171 rilDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSH 250
Cdd:PRK11249 238 ---DYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 251 ATKDLYDSIAAGNYPEWKFYIQIIDPDHEGRFDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIV 330
Cdd:PRK11249 315 HRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIV 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 331 PGIYYSDDKLLQTRIFSYSDTQRHRL-GPNYLLLPANAPKCAHHNNHYDGtmnfMHRdEEVDYFPSRFDP 399
Cdd:PRK11249 395 PGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDG----MHR-MTIDTGPANYEP 459
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
55-486 |
1.73e-171 |
|
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: 490.34 E-value: 1.73e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 55 DRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWD 134
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 135 LVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQEN-------WrilDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGV 207
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAqsahdtfW---DFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 208 NTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDSIAAGNYPEWKFYIQIIDPDHEGRFDFDPL 287
Cdd:cd08155 158 HTFRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 288 DVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLG-PNYLLLPAN 366
Cdd:cd08155 238 DPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPIN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 367 APKCAHHNNHYDGTMNFMHRDEEVDYFPSRFD---PAKHAPR------YPipsSTCNGRREKMVIEK-ENNFKQPGERYR 436
Cdd:cd08155 318 RPVCPVHNNQRDGHMRMTINKGRVNYFPNSLGagpPRAASPAeggfvhYP---EKVEGPKIRIRSESfADHYSQARLFWN 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 357114208 437 SMDPARQERFINRW---IDALSDPrlthEIKSIWLSYWSQADRSLGQKLASRL 486
Cdd:cd08155 395 SMSPVEKEHIISAFtfeLSKVETP----EIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
42-486 |
1.08e-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: 470.68 E-value: 1.08e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 42 LEDYHLVEKIANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRG 121
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 122 FAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRH 201
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 202 MDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATKDLYDSIAAGNYPEWKFYIQIIDPDHEGR 281
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 282 FDFDPLDVTKTWPEDIIPLQPVGRLVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYL 361
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 362 LLPANAPK--CAHHNNHYDGTMNFM-HRDEEVDYFPSRFDPAKHAPRYPIPSSTCNGRREKMVIEKENN---FKQPGERY 435
Cdd:cd08157 321 QLPVNRPKtsPVYNPYQRDGPMSVNgNYGGDPNYVSSILPPTYFKKRVDADGHHENWVGEVVAFLTEITdedFVQPRALW 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 357114208 436 -RSMDPARQERFINRWIDALSDPRltHEIKSIWLSYWSQADRSLGQKLASRL 486
Cdd:cd08157 401 eVVGKPGQQERFVKNVAGHLSGAP--PEIRKRVYEIFARVNPDLGKRIEKAT 450
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
60-356 |
2.00e-53 |
|
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: 181.60 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 60 PERVVHARGASAKGFFEVTHDISHLTCADFLrAPGVQTPVIVRFSTViheRGSPETLRDPRGFAIKFYT--REGNWDLVG 137
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLF-AEGKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGvaDAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 138 NNFPVFFIRDGMKFPDMVHSLKPNPKSHiQENWRILDFFSHHPESLHMFTFLFDdiGIPADYRHMDGSGVNTYTLVNRAG 217
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGE-PPLDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 218 KSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHShatKDLYDSIAAGnYPEWKFYIQIIDPDHegrfDFDPLDVTKTWPEDi 297
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELEARPPDYLR---EELTERLQRG-PVVYDFRIQLNDDTD----ATTIDNPTILWPTE- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357114208 298 IPLQPVGRLVLNRNIDNffSENEQLAFCPGIIVPGIYYSDDK--LLQTRIFSYSDTQRHRL 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 |
9.48e-36 |
|
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: 134.67 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 62 RVVHARGASAKGFFEVTHDISHLTCADFLRapGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGN-WDLVGNNF 140
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 141 PVFFIRDGMKFPDMVHSL------KPNPKshiqenwRILDFFSHHPESLHMFTFLfDDIGIPADYRHMDGSGVNTYTLVN 214
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIapdatgKPDPA-------KLKAFLAAHPEAAAFLAWI-KTAPPPASFANTTYYGVNAFYFTN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 215 RAGKSHYVKFHWKPTCGVKSLLDDEAVTVGgtnHSHATKDLYDSIAAGNYpEWKFYIQIIDPDhegrfdfDPL-DVTKTW 293
Cdd:cd08153 165 ANGKRQPVRWRFVPEDGVKYLSDEEAAKLG---PDFLFDELAQRLAQGPV-RWDLVLQLAEPG-------DPTdDPTKPW 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 294 PED---IIplqpVGRLVlnrnIDNFFSENE----QLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRL 356
Cdd:cd08153 234 PADrkeVD----AGTLT----ITKVAPDQGgacrDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
422-486 |
5.14e-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: 75.09 E-value: 5.14e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357114208 422 IEKENNFKQPGERYRSMDPARQERFINRWIDALSDPRlTHEIKSIWLSYWSQADRSLGQKLASRL 486
Cdd:pfam06628 2 IDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKVT-DPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
62-325 |
3.97e-13 |
|
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: 69.98 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 62 RVVHARG-ASAKGFFEVTHDISHlTCADFLRAPGVQTPVIVRFST---VIHergsPETLRDPRGFAIKFYTREG------ 131
Cdd:cd08152 5 RDAHAKShGCLKAEFTVLDDLPP-ELAQGLFAEPGTYPAVIRFSNapgDIL----DDSVPDPRGMAIKVLGVPGekllpe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 132 ----NWDLVGNNFPVFFIRDGMKF-------------PDMVHSLKPNPKSHIQE-------NWRILDFFSHHPESLhmft 187
Cdd:cd08152 80 edatTQDFVLVNHPVFFARDAKDYlallkllarttslPDGAKAALSAPLRGALRvleaaggESPTLKLGGHPPAHP---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357114208 188 fLFDDIGIPADYRHMDgsgvntytlvnragksHYVKFHWKPTCGVKSLLDDEAVTVGGTnHSHATKDLYDSIAAGNYpEW 267
Cdd:cd08152 156 -LGETYWSQAPYRFGD----------------YVAKYSVVPASPALPALTGKELDLTDD-PDALREALADFLAENDA-EF 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 357114208 268 KFYIQIIDPDHEGrfdfdPL-DVTKTWPEDIIPLQPVGRLVLNRNidNFFSENEQLAFC 325
Cdd:cd08152 217 EFRIQLCTDLEKM-----PIeDASVEWPEALSPFVPVATITIPPQ--DFDSPARQRAFD 268
|
|
| |
