|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02609 |
PLN02609 |
catalase |
1-496 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 986.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 1 MDPCKYRPSSSFDKKTTTTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHD 80
Cdd:PLN02609 1 MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 81 VTDLTCADFLRAPGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKP 160
Cdd:PLN02609 81 ISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 161 NPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEA 240
Cdd:PLN02609 161 NPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 241 TLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENE 320
Cdd:PLN02609 241 VRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 321 QLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYYPSRHAPL 400
Cdd:PLN02609 321 QLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 401 KQAEPapacFPVPVRTVVGKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGHPKVSHELRAIWVNFLSQCDK 480
Cdd:PLN02609 401 RHAER----VPIPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDK 476
|
490
....*....|....*.
gi 357144297 481 SCGMKVANRLNVKPSM 496
Cdd:PLN02609 477 SLGQKLASRLNVKPSM 492
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
16-490 |
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: 803.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 16 TTTTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGA 95
Cdd:cd08154 1 TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 96 RTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDF 175
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 176 LSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDL 255
Cdd:cd08154 161 FSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 256 YDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYY 335
Cdd:cd08154 241 YDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 336 SDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYYPSRHAPLKQAEPAPACFPvPVR 415
Cdd:cd08154 321 SDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQP-PLS 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357144297 416 tvvGKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGhpKVSHELRAIWVNFLSQCDKSCGMKVANRL 490
Cdd:cd08154 400 ---GTTQQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLS--DVNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
13-495 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 730.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 13 DKKTTTTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRA 92
Cdd:COG0753 7 EGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 93 PGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRV 172
Cdd:COG0753 87 PGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 173 FDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHAT 252
Cdd:COG0753 167 WDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 253 QDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPG 332
Cdd:COG0753 247 RDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 333 IYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYYPSRHAPLKQAePAPACFPV 412
Cdd:COG0753 327 IDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPRED-PGFKEPPL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 413 PVRtvvGKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGhpKVSHE-LRAIWVNFLSQCDKSCGMKVANRLN 491
Cdd:COG0753 406 KVD---GDKVRYRSESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELG--KVESEeIRERMVAHFYNVDPELGARVAEALG 480
|
....
gi 357144297 492 VKPS 495
Cdd:COG0753 481 LDLP 484
|
|
| Catalase |
pfam00199 |
Catalase; |
18-399 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 707.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 18 TTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGART 97
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 98 PVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLS 177
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 178 HLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYD 257
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 258 SIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSD 337
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357144297 338 DKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRD-EEVDYYPSRHAP 399
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFDINQgSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
21-393 |
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: 644.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 21 AGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGARTPVI 100
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 101 VRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLP 180
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 181 ESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSID 260
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 261 AGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKM 340
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 357144297 341 LQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYY 393
Cdd:smart01060 321 LQGRLFSYPDTQRYRLGPNYHQLPVNRPRCPVHNYQRDGAMRVDGNQGGDPNY 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02609 |
PLN02609 |
catalase |
1-496 |
0e+00 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 986.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 1 MDPCKYRPSSSFDKKTTTTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHD 80
Cdd:PLN02609 1 MDPYKYRPSSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 81 VTDLTCADFLRAPGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKP 160
Cdd:PLN02609 81 ISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 161 NPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEA 240
Cdd:PLN02609 161 NPKTHIQEPWRILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLDEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 241 TLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENE 320
Cdd:PLN02609 241 VRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFAENE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 321 QLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYYPSRHAPL 400
Cdd:PLN02609 321 QLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRLGPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRFDPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 401 KQAEPapacFPVPVRTVVGKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGHPKVSHELRAIWVNFLSQCDK 480
Cdd:PLN02609 401 RHAER----VPIPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPRVTHEIRSIWISYWSQCDK 476
|
490
....*....|....*.
gi 357144297 481 SCGMKVANRLNVKPSM 496
Cdd:PLN02609 477 SLGQKLASRLNVKPSM 492
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
16-490 |
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: 803.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 16 TTTTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGA 95
Cdd:cd08154 1 TLTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 96 RTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDF 175
Cdd:cd08154 81 KTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKPSPVTNIQDPNRIFDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 176 LSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDL 255
Cdd:cd08154 161 FSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQGKNFNHATQDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 256 YDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYY 335
Cdd:cd08154 241 YDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFSPGNLVPGIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 336 SDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYYPSRHAPLKQAEPAPACFPvPVR 415
Cdd:cd08154 321 SDDKMLQGRLFSYSDTQRYRLGPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLDGLPEAPKYPYSQP-PLS 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357144297 416 tvvGKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGhpKVSHELRAIWVNFLSQCDKSCGMKVANRL 490
Cdd:cd08154 400 ---GTTQQAPIAKTNNFKQAGERYRSFSEEEQENLIKNLVVDLS--DVNEEIKLRMLSYFSQADPDYGERVAEGL 469
|
|
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
13-495 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 730.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 13 DKKTTTTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRA 92
Cdd:COG0753 7 EGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKAKFFQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 93 PGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRV 172
Cdd:COG0753 87 PGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLPQHDTF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 173 FDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHAT 252
Cdd:COG0753 167 WDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKIAGKDPDFHR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 253 QDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPG 332
Cdd:COG0753 247 RDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAAFSPGNLVPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 333 IYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYYPSRHAPLKQAePAPACFPV 412
Cdd:COG0753 327 IDFSPDKMLQGRLFSYADTQRYRLGPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLGGPRED-PGFKEPPL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 413 PVRtvvGKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGhpKVSHE-LRAIWVNFLSQCDKSCGMKVANRLN 491
Cdd:COG0753 406 KVD---GDKVRYRSESDDHFSQAGLLYRSMSDEEKQHLIDNIAFELG--KVESEeIRERMVAHFYNVDPELGARVAEALG 480
|
....
gi 357144297 492 VKPS 495
Cdd:COG0753 481 LDLP 484
|
|
| Catalase |
pfam00199 |
Catalase; |
18-399 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 707.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 18 TTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGART 97
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 98 PVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLS 177
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDPAMFWDFWS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 178 HLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYD 257
Cdd:pfam00199 161 LNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTRDLYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 258 SIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSD 337
Cdd:pfam00199 241 AIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGIEPSP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357144297 338 DKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRD-EEVDYYPSRHAP 399
Cdd:pfam00199 321 DPMLQGRLFSYPDTQRYRLGPNYQQLPVNRPPCPVHNYQRDGAMRFDINQgSRPNYEPNSFGG 383
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
21-393 |
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: 644.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 21 AGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGARTPVI 100
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 101 VRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLP 180
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPDHDMFWDFWSLNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 181 ESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSID 260
Cdd:smart01060 161 ESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLYEAIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 261 AGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKM 340
Cdd:smart01060 241 RGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFSPDKM 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 357144297 341 LQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHFDGAMNFMHRDEEVDYY 393
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 ... |
58-490 |
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: 522.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 58 RIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLG 137
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 138 NNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREG 217
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKDPDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLVNAKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 218 KSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDL 297
Cdd:cd08156 161 ERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVWPHKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 298 LPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHF 377
Cdd:cd08156 241 YPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRLGVNYHQLPVNRPKCPVNNYQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 378 DGAMNFMH-RDEEVDYYP-SRHAPLKQAEPAPACFPVPVRTVvgkREKTRiKKENDFQQSGERYRSWAPDRQDRFVKRFA 455
Cdd:cd08156 321 DGAMRVDGnGGGAPNYEPnSFGGPPEDPEYAEPPLPVSGDAD---RYNYR-DDDDDYTQAGDLYRLVSEDERERLVENIA 396
|
410 420 430
....*....|....*....|....*....|....*
gi 357144297 456 DALGHPKVSHELRAIwVNFlSQCDKSCGMKVANRL 490
Cdd:cd08156 397 GHLKGAPEFIQERQV-AHF-YKADPDYGERVAKAL 429
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
58-487 |
9.20e-176 |
|
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: 500.84 E-value: 9.20e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 58 RIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLG 137
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 138 NNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREG 217
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPDADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLVNANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 218 KSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDL 297
Cdd:cd00328 161 KVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVWPEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 298 LPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCGHRNAHF 377
Cdd:cd00328 241 VPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRLGPNFQQLPVNRPYAPVHNNQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 378 DGAMNFMHRDEEVDYYPSRHAPLKQAEPAPACFPVPVRTVV-GKREKTRIKKENDFQQSGERYRSWAPDRQDRFVKRFAD 456
Cdd:cd00328 321 DGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDRGHFSHWKsGVNREASTTNDDNFTQARLFYRSLTPGQQKRLVDAFRF 400
|
410 420 430
....*....|....*....|....*....|.
gi 357144297 457 ALGHpKVSHELRAIWVNFLSQCDKSCGMKVA 487
Cdd:cd00328 401 ELAD-AVSPQIQQRVLDQFAKVDAAAAKRVA 430
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
18-490 |
4.74e-169 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 495.33 E-value: 4.74e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 18 TTNAGAPVWNDNEALTVGHRGPILLEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGART 97
Cdd:PRK11249 78 TTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKIT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 98 PVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQE-------YW 170
Cdd:PRK11249 158 PVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQgqsahdtFW 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 171 rvfDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSH 250
Cdd:PRK11249 238 ---DYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRDPDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 251 ATQDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIV 330
Cdd:PRK11249 315 HRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPGHIV 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 331 PGIYYSDDKMLQCRVFAYADTQRYRL-GPNYLMLPVNAPKCGHRNAHFDGamnfMHRdEEVDYYPSRHAP-------LKQ 402
Cdd:PRK11249 395 PGIDFTNDPLLQGRLFSYTDTQISRLgGPNFHEIPINRPTCPYHNFQRDG----MHR-MTIDTGPANYEPnsingnwPRE 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 403 AEPAPA-----CFPVPVrtvvgkrEKTRIKKEND-----FQQSGERYRSWAPDRQDRFVKRFADALGhpKVSHE-LRAIW 471
Cdd:PRK11249 470 TPPAPKrggfeSYQERV-------EGNKVRERSPsfgdyYSQPRLFWLSQTPIEQRHIIDAFSFELG--KVVRPyIRERV 540
|
490
....*....|....*....
gi 357144297 472 VNFLSQCDKSCGMKVANRL 490
Cdd:PRK11249 541 VDQLAHIDLTLAQAVAENL 559
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
42-490 |
3.84e-166 |
|
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: 477.22 E-value: 3.84e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 42 LEDYHLLEKVAHFARERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGARTPVIVRFSTVIHERGSPETIRDPRG 121
Cdd:cd08157 1 LQDFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 122 FAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGIPTDYRH 201
Cdd:cd08157 81 FAVKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDSTMFWDYLSQNPESIHQVMILFSDRGTPASYRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 202 MEGFGVNTYTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVMDPDEEDK 281
Cdd:cd08157 161 MNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 282 YDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYL 361
Cdd:cd08157 241 LRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRLGPNYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 362 MLPVNAPK--CGHRNAHFDGAMNFMHRDEEVDYYPSRHAPL---KQAEPAPACFPVPVRTVVGKREKTRikkENDFQQSG 436
Cdd:cd08157 321 QLPVNRPKtsPVYNPYQRDGPMSVNGNYGGDPNYVSSILPPtyfKKRVDADGHHENWVGEVVAFLTEIT---DEDFVQPR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 357144297 437 ERY-RSWAPDRQDRFVKRFADALGhpKVSHELRAIWVNFLSQCDKSCGMKVANRL 490
Cdd:cd08157 398 ALWeVVGKPGQQERFVKNVAGHLS--GAPPEIRKRVYEIFARVNPDLGKRIEKAT 450
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
57-490 |
5.94e-165 |
|
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: 473.78 E-value: 5.94e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 57 ERIPERVVHARGASAKGFFECTHDVTDLTCADFLRAPGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLL 136
Cdd:cd08155 3 ERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 137 GNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQE-------YWrvfDFLSHLPESLHTFFFLFDDVGIPTDYRHMEGFGVNT 209
Cdd:cd08155 83 GNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQaqsahdtFW---DFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 210 YTFVTREGKSKYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIDAGNFPEWKLFVQVMDPDEEDKYDFDPLDD 289
Cdd:cd08155 160 FRLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 290 TKTWPEDLLPLRPVGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRLG-PNYLMLPVNAP 368
Cdd:cd08155 240 TKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGgPNFHELPINRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 369 KCGHRNAHFDGAMNFMHRDEEVDYYPSRHA--PLKQAEPAPACFPVPVRTVVGKREKTRIKKEND-FQQSGERYRSWAPD 445
Cdd:cd08155 320 VCPVHNNQRDGHMRMTINKGRVNYFPNSLGagPPRAASPAEGGFVHYPEKVEGPKIRIRSESFADhYSQARLFWNSMSPV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 357144297 446 RQDRFVKRFADALGHPKVSHeLRAIWVNFLSQCDKSCGMKVANRL 490
Cdd:cd08155 400 EKEHIISAFTFELSKVETPE-IRERVVDHLANIDEDLAKKVAKGL 443
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
60-356 |
2.05e-52 |
|
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.
Pssm-ID: 163706 Cd Length: 283 Bit Score: 178.91 E-value: 2.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 60 PERVVHARGASAKGFFECTHDVTDLTCADFLrAPGARTPVIVRFSTViheRGSPETIRDPRGFAVKFYT--REGNWDLLG 137
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLF-AEGKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGvaDAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 138 NNFPVFFIRDGIKFPDVIHAFKPNPRSHvQEYWRVFDFLSHLPESLHTFFFLFDdvGIPTDYRHMEGFGVNTYTFVTREG 217
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSARGE-PPLDFIAWYVEKRPEDLPNLLGARS--QVPDSYAAARYFSQVTFAFINGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 218 KSKYVKFHWKPTCGVSCLMDDEATlvgGKNHSHATQDLYDSIDAGnFPEWKLFVQVMDPDEedkyDFDPLDDTKTWPEDl 297
Cdd:cd08150 154 KYRVVRSKDNPVDGIPSLEDHELE---ARPPDYLREELTERLQRG-PVVYDFRIQLNDDTD----ATTIDNPTILWPTE- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357144297 298 LPLRPVGRLVLDRNVDNffNENEQLAFGPGLIVPGIYYSDDK--MLQCRVFAYADTQRYRL 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 |
8.18e-34 |
|
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: 129.27 E-value: 8.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 62 RVVHARGASAKGFFECTHDVTDLTCADFLRapGARTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGN-WDLLGNNF 140
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 141 PVFFIRDGIKFPDVIHAF------KPNPRshvqeywRVFDFLSHLPESLHtFFFLFDDVGIPTDYRHMEGFGVNTYTFVT 214
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIapdatgKPDPA-------KLKAFLAAHPEAAA-FLAWIKTAPPPASFANTTYYGVNAFYFTN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 215 REGKSKYVKFHWKPTCGVSCLMDDEAtlvGGKNHSHATQDLYDSIDAGNFpEWKLFVQVMDPDeedkydfDPLDD-TKTW 293
Cdd:cd08153 165 ANGKRQPVRWRFVPEDGVKYLSDEEA---AKLGPDFLFDELAQRLAQGPV-RWDLVLQLAEPG-------DPTDDpTKPW 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357144297 294 PEDllplRP---VGRLVLDRNVDNFFNENEQLAFGPGLIVPGIYYSDDKMLQCRVFAYADTQRYRL 356
Cdd:cd08153 234 PAD----RKevdAGTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
425-490 |
1.10e-12 |
|
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: 62.77 E-value: 1.10e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357144297 425 RIKKENDFQQSGERYRSWAPDRQDRFVKRFADALGHPKvSHELRAIWVNFLSQCDKSCGMKVANRL 490
Cdd:pfam06628 1 SIDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKVT-DPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
92-328 |
4.72e-06 |
|
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: 48.41 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 92 APGARTPVIVRFST---VIHergsPETIRDPRGFAVKFYTREG----------NWDLLGNNFPVFFIRDgikfpdvihaf 158
Cdd:cd08152 35 AEPGTYPAVIRFSNapgDIL----DDSVPDPRGMAIKVLGVPGekllpeedatTQDFVLVNHPVFFARD----------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 159 kpnprshVQEYWRVFDFL---SHLPESLHTFFF--------LFDDVGIPTDYRHMEGFGVN---TYTFVT----REGKSk 220
Cdd:cd08152 100 -------AKDYLALLKLLartTSLPDGAKAALSaplrgalrVLEAAGGESPTLKLGGHPPAhplGETYWSqapyRFGDY- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357144297 221 YVKFHWKPtcgvscLMDDEATLVGGKNHSHATQD-----LYDSIdAGNFPEWKLFVQVMDPDEEdkydfDPLDD-TKTWP 294
Cdd:cd08152 172 VAKYSVVP------ASPALPALTGKELDLTDDPDalreaLADFL-AENDAEFEFRIQLCTDLEK-----MPIEDaSVEWP 239
|
250 260 270
....*....|....*....|....*....|....
gi 357144297 295 EDLLPLRPVGRLVLDRNvdNFFNENEQLAFGPGL 328
Cdd:cd08152 240 EALSPFVPVATITIPPQ--DFDSPARQRAFDDNL 271
|
|
| |
