|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
19-506 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 789.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 19 SQSDNIITTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLF 98
Cdd:COG0753 5 DDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 99 TEAGKKTDVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPN 178
Cdd:COG0753 85 QEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 179 RYFDFFSNVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQH 258
Cdd:COG0753 165 TFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 259 ATVSLRKAIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALI 338
Cdd:COG0753 245 HRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 339 PGIEPSEDKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGwisAGNKRFENPDVNYQPSTKASLTEDPQYK 418
Cdd:COG0753 325 PGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDG---AMRYDINGGRVNYEPNSLGGPREDPGFK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 419 QSETTLKNvTITQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLGQVTDKNIQKTMIGYFYRADRDYGMRIAKALG 498
Cdd:COG0753 402 EPPLKVDG-DKVRYRSESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAEALG 480
|
....*...
gi 503317087 499 FSQKDFMN 506
Cdd:COG0753 481 LDLPEAKA 488
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
26-497 |
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: 772.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 26 TTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKT 105
Cdd:cd08154 3 TTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFS 185
Cdd:cd08154 83 PVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 186 NVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRK 265
Cdd:cd08154 163 HVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 266 AIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSE 345
Cdd:cd08154 243 AIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPSD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 346 DKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGwisAGNKRFENPDVNYQPSTKASLTEDPQYKQSETTLK 425
Cdd:cd08154 323 DKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDG---QMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLS 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503317087 426 NVTiTQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLGQVtDKNIQKTMIGYFYRADRDYGMRIAKAL 497
Cdd:cd08154 400 GTT-QQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSDV-NEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| Catalase |
pfam00199 |
Catalase; |
26-407 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 658.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 26 TTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKT 105
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFS 185
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 186 NVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRK 265
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 266 AIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSE 345
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503317087 346 DKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGwisAGNKRFENP-DVNYQPST 407
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDG---AMRFDINQGsRPNYEPNS 380
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
30-403 |
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: 626.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 30 GVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKTDVAV 109
Cdd:smart01060 2 GAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 110 RLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFSNVPE 189
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 190 ATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRKAIAD 269
Cdd:smart01060 162 SLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 270 GNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLL 349
Cdd:smart01060 242 GDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKML 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 503317087 350 QGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGWISAGNKRfeNPDVNY 403
Cdd:smart01060 322 QGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDGNQ--GGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
26-498 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 591.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 26 TTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKT 105
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFS 185
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 186 NVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRK 265
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 266 AIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSE 345
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 346 DKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGWIsagNKRFENPDVNYQPSTKASLTEDPQYKQSETTLK 425
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFM---NFMHRDEEVNYFPSRFDPVRHAERVPIPHPPLS 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503317087 426 NVTiTQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLG--QVTDKnIQKTMIGYFYRADRDYGMRIAKALG 498
Cdd:PLN02609 415 GRR-EKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSdpRVTHE-IRSIWISYWSQCDKSLGQKLASRLN 487
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
19-506 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 789.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 19 SQSDNIITTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLF 98
Cdd:COG0753 5 DDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 99 TEAGKKTDVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPN 178
Cdd:COG0753 85 QEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 179 RYFDFFSNVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQH 258
Cdd:COG0753 165 TFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 259 ATVSLRKAIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALI 338
Cdd:COG0753 245 HRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 339 PGIEPSEDKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGwisAGNKRFENPDVNYQPSTKASLTEDPQYK 418
Cdd:COG0753 325 PGIDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDG---AMRYDINGGRVNYEPNSLGGPREDPGFK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 419 QSETTLKNvTITQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLGQVTDKNIQKTMIGYFYRADRDYGMRIAKALG 498
Cdd:COG0753 402 EPPLKVDG-DKVRYRSESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELGARVAEALG 480
|
....*...
gi 503317087 499 FSQKDFMN 506
Cdd:COG0753 481 LDLPEAKA 488
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
26-497 |
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: 772.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 26 TTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKT 105
Cdd:cd08154 3 TTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFS 185
Cdd:cd08154 83 PVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDFFS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 186 NVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRK 265
Cdd:cd08154 163 HVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDLYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 266 AIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSE 345
Cdd:cd08154 243 AIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEPSD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 346 DKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGwisAGNKRFENPDVNYQPSTKASLTEDPQYKQSETTLK 425
Cdd:cd08154 323 DKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDG---QMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQPPLS 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503317087 426 NVTiTQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLGQVtDKNIQKTMIGYFYRADRDYGMRIAKAL 497
Cdd:cd08154 400 GTT-QQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLSDV-NEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| Catalase |
pfam00199 |
Catalase; |
26-407 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 658.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 26 TTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKT 105
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFS 185
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 186 NVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRK 265
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 266 AIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSE 345
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503317087 346 DKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGwisAGNKRFENP-DVNYQPST 407
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDG---AMRFDINQGsRPNYEPNS 380
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
30-403 |
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: 626.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 30 GVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKTDVAV 109
Cdd:smart01060 2 GAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 110 RLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFSNVPE 189
Cdd:smart01060 82 RFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 190 ATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRKAIAD 269
Cdd:smart01060 162 SLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 270 GNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLL 349
Cdd:smart01060 242 GDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKML 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 503317087 350 QGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGWISAGNKRfeNPDVNY 403
Cdd:smart01060 322 QGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDGNQ--GGDPNY 373
|
|
| PLN02609 |
PLN02609 |
catalase |
26-498 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 591.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 26 TTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKT 105
Cdd:PLN02609 18 TTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFS 185
Cdd:PLN02609 98 PVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKPNPKTHIQEPWRILDFLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 186 NVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRK 265
Cdd:PLN02609 178 HHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEAVRVGGSNHSHATQDLYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 266 AIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSE 345
Cdd:PLN02609 258 SIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENEQLAFCPAIVVPGIYYSD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 346 DKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNSDGWIsagNKRFENPDVNYQPSTKASLTEDPQYKQSETTLK 425
Cdd:PLN02609 338 DKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFM---NFMHRDEEVNYFPSRFDPVRHAERVPIPHPPLS 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503317087 426 NVTiTQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLG--QVTDKnIQKTMIGYFYRADRDYGMRIAKALG 498
Cdd:PLN02609 415 GRR-EKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSdpRVTHE-IRSIWISYWSQCDKSLGQKLASRLN 487
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
66-497 |
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: 544.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 66 RIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKTDVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVG 145
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 146 NNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFSNVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAG 225
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 226 KVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRKAIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADK 305
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 306 IEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNS 385
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 386 DGWISAGNKRfeNPDVNYQPSTKASLTEDPQYKQSETTLKNVTITQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGD 465
Cdd:cd08156 321 DGAMRVDGNG--GGAPNYEPNSFGGPPEDPEYAEPPLPVSGDADRYNYRDDDDDYTQAGDLYRLVSEDERERLVENIAGH 398
|
410 420 430
....*....|....*....|....*....|..
gi 503317087 466 LGQVTdKNIQKTMIGYFYRADRDYGMRIAKAL 497
Cdd:cd08156 399 LKGAP-EFIQERQVAHFYKADPDYGERVAKAL 429
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
66-497 |
1.71e-174 |
|
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: 498.14 E-value: 1.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 66 RIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKTDVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVG 145
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 146 NNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFSNVPEATHMITRLWTDLGIPKGYQYMNGSSVHGYKWINQAG 225
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 226 KVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRKAIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADK 305
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 306 IEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLLQGRLFSYFDTQRHRLGPNFQQLKINQPLEAPKNYNS 385
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 386 DGwisAGNKRFENPDVNYQPSTK----ASLTEDPQYKQSETTLKNVTITQKKITKTNDFAQAGDFYRSLTKQEQDNLIKN 461
Cdd:cd00328 321 DG---AGNMNDNTGVPNYEPNAKdvryPAQGAPKFDRGHFSHWKSGVNREASTTNDDNFTQARLFYRSLTPGQQKRLVDA 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 503317087 462 LSGDLGQVTDKNIQKTMIGYFYRADRDYGMRIAKAL 497
Cdd:cd00328 398 FRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
50-498 |
3.42e-172 |
|
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: 493.02 E-value: 3.42e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 50 LEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKTDVAVRLSTVIHGKGSPETARDPRG 129
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 130 FAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPETNKQDPNRYFDFFSNVPEATHMITRLWTDLGIPKGYQY 209
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 210 MNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRKAIADGNYPQWDLYVQMIKPEDLHS 289
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 290 FDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLLQGRLFSYFDTQRHRLGPNFQ 369
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 370 QLKINQPLEAPKN--YNSDGWISAGNKRFENPDV--NYQPSTKASLTEDPQyKQSETTLKNVTITQKKITKTnDFAQAGD 445
Cdd:cd08157 321 QLPVNRPKTSPVYnpYQRDGPMSVNGNYGGDPNYvsSILPPTYFKKRVDAD-GHHENWVGEVVAFLTEITDE-DFVQPRA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 503317087 446 FYRSLTKQE-QDNLIKNLSGDLGQVTDKnIQKTMIGYFYRADRDYGMRIAKALG 498
Cdd:cd08157 399 LWEVVGKPGqQERFVKNVAGHLSGAPPE-IRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
25-499 |
3.41e-154 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 457.58 E-value: 3.41e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 25 ITTNGGVPVGDNQNSKTVGEYGPVLLEDIFLVEKLAAFDRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKK 104
Cdd:PRK11249 77 LTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 105 TDVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYDIVGNNLPIFFIRDAIKFPDMVHSLKPSPE----TNKQDPNRY 180
Cdd:PRK11249 157 TPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHneipQGQSAHDTF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 181 FDFFSNVPEATHMItrLWT--DLGIPKGYQYMNGSSVHGYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQH 258
Cdd:PRK11249 237 WDYVSLQPETLHNV--MWAmsDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 259 ATVSLRKAIADGNYPQWDLYVQMIKPEDLHSFDFWPLDATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALI 338
Cdd:PRK11249 315 HRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIV 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 339 PGIEPSEDKLLQGRLFSYFDTQRHRL-GPNFQQLKINQPLEAPKNYNSDGW----ISAGNKRFEnP---DVNYQPSTKAS 410
Cdd:PRK11249 395 PGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDGMhrmtIDTGPANYE-PnsiNGNWPRETPPA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 411 lTEDPQYKQSETTLKNVTITQKKITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLGQVTDKNIQKTMIGYFYRADRDYG 490
Cdd:PRK11249 474 -PKRGGFESYQERVEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAHIDLTLA 552
|
....*....
gi 503317087 491 MRIAKALGF 499
Cdd:PRK11249 553 QAVAENLGI 561
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
63-497 |
1.82e-153 |
|
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: 444.89 E-value: 1.82e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 63 DRERIPERVVHPRGAGASGYFEATKDMSTYTKAVLFTEAGKKTDVAVRLSTVIHGKGSPETARDPRGFAVKFYTEQGNYD 142
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 143 IVGNNLPIFFIRDAIKFPDMVHSLKPSPetNKQDP------NRYFDFFSNVPEATHMITRLWTDLGIPKGYQYMNGSSVH 216
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEP--HNEMPqaqsahDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 217 GYKWINQAGKVTYVKYSWVSKQGEKNLTAEEATIQQGLDWQHATVSLRKAIADGNYPQWDLYVQMIKPEDLHSFDFWPLD 296
Cdd:cd08155 159 TFRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 297 ATKDWPADKIEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLLQGRLFSYFDTQRHRLG-PNFQQLKINQ 375
Cdd:cd08155 239 PTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 376 PLEAPKNYNSDGWIsagnkRFENPD--VNYQPST------KASLTEDPQYKQSETTLKNVTITQKKITKTNDFAQAGDFY 447
Cdd:cd08155 319 PVCPVHNNQRDGHM-----RMTINKgrVNYFPNSlgagppRAASPAEGGFVHYPEKVEGPKIRIRSESFADHYSQARLFW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 503317087 448 RSLTKQEQDNLIKNLSGDLGQVTDKNIQKTMIGYFYRADRDYGMRIAKAL 497
Cdd:cd08155 394 NSMSPVEKEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
68-364 |
1.75e-58 |
|
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: 195.08 E-value: 1.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 68 PERVVHPRGAGASGYFEATKDMSTYTKAVLFTEaGKKTDVAVRLSTvihGKGSPETARDPRGFAVKFYTEQGN--YDIVG 145
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAE-GKVYPAYIRFSN---GAGIDDTKPDIRGFAIKFTGVADAgtLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 146 NNLPIFFIRDAIKFPDMVHSLKPSPeTNKQDPNRYFDFFSNVPEATHMItrLWTDLGIPKGYQYMNGSSVHGYKWINQAG 225
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSA-RGEPPLDFIAWYVEKRPEDLPNL--LGARSQVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 226 KVTYVKYSWVSKQGEKNLTAEEATiQQGLDWqhatvsLRKAIAD---GNYPQWDLYVQMIKPEDlhsfDFWPLDATKDWP 302
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELE-ARPPDY------LREELTErlqRGPVVYDFRIQLNDDTD----ATTIDNPTILWP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503317087 303 ADKiEKIKIGTMTLNQNPVNyfEQVESIAFSPGALIPGIEPSEDK--LLQGRLFSYFDTQRHRL 364
Cdd:cd08150 223 TEH-PVEAVAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDLgpILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
70-352 |
1.36e-44 |
|
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: 158.55 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 70 RVVHPRGAGASGYFEATKDMSTYTKAVLFteAGKKTDVAVRLSTvihGKGSP---ETARDPRGFAVKFYTEQGN-YDIVG 145
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLF--SGGSVPVTGRFSL---GGGNPkapDDAANPRGMALKFRLPDGEqWRMVM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 146 NNLPIFFIRDAIKFPDMVHSLKPSPeTNKQDPNRYFDFFSNVPEATHMITRLWTdLGIPKGYQYMNGSSVHGYKWINQAG 225
Cdd:cd08153 90 NSFPVFPVRTPEEFLALLKAIAPDA-TGKPDPAKLKAFLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNANG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 226 KVTYVKYSWVSKQGEKNLTAEEATiQQGLDWQHATvsLRKAIADGNYpQWDLYVQMIKPEDlhsfdfwPL-DATKDWPAD 304
Cdd:cd08153 168 KRQPVRWRFVPEDGVKYLSDEEAA-KLGPDFLFDE--LAQRLAQGPV-RWDLVLQLAEPGD-------PTdDPTKPWPAD 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 503317087 305 KiEKIKIGTMTLNQNPVNYFEQVESIAFSPGALIPGIEPSEDKLLQGR 352
Cdd:cd08153 237 R-KEVDAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAAR 283
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
434-497 |
1.57e-26 |
|
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: 102.06 E-value: 1.57e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503317087 434 ITKTNDFAQAGDFYRSLTKQEQDNLIKNLSGDLGQVTDKNIQKTMIGYFYRADRDYGMRIAKAL 497
Cdd:pfam06628 2 IDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
106-334 |
4.77e-07 |
|
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: 51.49 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 106 DVAVRLSTViHGKGSPETARDPRGFAVKFY----------TEQGNYDIVGNNLPIFFIRDAikfPDMVHSLKPSPETnKQ 175
Cdd:cd08152 41 PAVIRFSNA-PGDILDDSVPDPRGMAIKVLgvpgekllpeEDATTQDFVLVNHPVFFARDA---KDYLALLKLLART-TS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 176 DPNRYFDFFSNVpeATHMItRLWTDLGIPKGYQYMNGSSVH---GYKWINQA----GKvTYVKYSWVSKQgeknlTAEEA 248
Cdd:cd08152 116 LPDGAKAALSAP--LRGAL-RVLEAAGGESPTLKLGGHPPAhplGETYWSQApyrfGD-YVAKYSVVPAS-----PALPA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503317087 249 TIQQGLDWQHATVSLRKAIAD---GNYPQWDLYVQMIKPEDLHsfdfwPL-DATKDWPADKIEKIKIGTMTLNQ----NP 320
Cdd:cd08152 187 LTGKELDLTDDPDALREALADflaENDAEFEFRIQLCTDLEKM-----PIeDASVEWPEALSPFVPVATITIPPqdfdSP 261
|
250
....*....|....
gi 503317087 321 VNYFEQVESIAFSP 334
Cdd:cd08152 262 ARQRAFDDNLSFNP 275
|
|
| |
