|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
31-528 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 937.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 31 QTAAGDDPVLTTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSA 110
Cdd:COG0753 2 QYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 111 DLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFP 190
Cdd:COG0753 82 KFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 191 QaqtaHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKI 270
Cdd:COG0753 162 Q----HDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 271 NGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVA 350
Cdd:COG0753 238 AGKDPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 351 FMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTGRANYQPNSFGeGPR 430
Cdd:COG0753 318 FSPGNLVPGIDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLG-GPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 431 ESPtrGFQHFPAEEQGAKARLRPESfADHYSQARQFYISQTPSEQRHIASALTFELSKVETPVIRERMVSHLLNIDEALA 510
Cdd:COG0753 396 EDP--GFKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELG 472
|
490
....*....|....*...
gi 1610781719 511 ATVAQKLGFqTMPKPADA 528
Cdd:COG0753 473 ARVAEALGL-DLPEAKAL 489
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
35-700 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 934.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 35 GDDPVLTTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQ 114
Cdd:PRK11249 72 SEGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 115 RAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAQT 194
Cdd:PRK11249 152 DPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 195 AHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGAD 274
Cdd:PRK11249 232 AHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 275 PDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQ 354
Cdd:PRK11249 312 PDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 355 NVPPGIDFSNDPLLQGRNFSYLDTQLKRLGGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTGRANYQPNSFGEG-PRESP 433
Cdd:PRK11249 392 HIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSINGNwPRETP 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 434 TR----GFQHFPAEEQGAKARLRPESFADHYSQARQFYISQTPSEQRHIASALTFELSKVETPVIRERMVSHLLNIDEAL 509
Cdd:PRK11249 472 PApkrgGFESYQERVEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAHIDLTL 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 510 AATVAQKLGFQTMPKPADAAMPTRQD-LEPSPALSIVQRGPKRFEGRKLGILITDGVDAKLLKGLTKAVEAEKAVFEFIA 588
Cdd:PRK11249 552 AQAVAENLGIPLTDEQLNITPPPDVNgLKKDPALSLYAIPDGDIKGRKVAILLNDGVDAADLLAILKALKAKGVHAKLLY 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 589 PKVGGVTASDGTFIEAHHMIDGGPSVLFDAVALLTSAAAIDELIKEATARDFVADAFQHCKFIGYDQSALPLLEKAGIAD 668
Cdd:PRK11249 632 PRMGEVTADDGTVLPIAATFAGAPSLTFDAVIVPGGKANIADLADNGDARYYLLEAYKHLKPIALAGDARKLKAALKLPD 711
|
650 660 670
....*....|....*....|....*....|....
gi 1610781719 669 VMDEGMLPLPGEGG--LAAFVSELGKLRVWAREP 700
Cdd:PRK11249 712 QGEEGLVEADSADGsfMDELLTAMAAHRVWSREP 745
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
78-517 |
0e+00 |
|
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: 870.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 78 DHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWD 157
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 158 LVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAQTAHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTF 237
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 238 RFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPT 317
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 318 KIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLGGPNFTHLPINAPK 397
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 398 CPFAHFQQDGHMAMRNPTGRANYQPNSFGEGPRESPTR---GFQHFPAEEQGAKARLRPESFADHYSQARQFYISQTPSE 474
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPaegGFVHYPEKVEGPKIRIRSESFADHYSQARLFWNSMSPVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1610781719 475 QRHIASALTFELSKVETPVIRERMVSHLLNIDEALAATVAQKL 517
Cdd:cd08155 401 KEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
41-426 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 723.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 41 TTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKT 120
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 121 PAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAqtahDTFW 200
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDP----AMFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 201 DFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRR 280
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 281 DLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGI 360
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610781719 361 DFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTG-RANYQPNSFG 426
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGsRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
44-420 |
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: 698.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 44 QGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAF 123
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 124 VRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQaqtaHDTFWDFI 203
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 204 SLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLW 283
Cdd:smart01060 157 SLNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 284 TAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFS 363
Cdd:smart01060 237 EAIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610781719 364 NDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAM-RNPTGRANY 420
Cdd:smart01060 317 PDKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVdGNQGGDPNY 373
|
|
| GATase1_catalase |
cd03132 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ... |
554-694 |
1.12e-37 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.
Pssm-ID: 153226 Cd Length: 142 Bit Score: 137.01 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 554 GRKLGILITDGVDAKLLKGLTKAVEAEKAVFEFIAPKVGGVTASDGTFIEAHHMIDGGPSVLFDAVALLTSAAAIDELIK 633
Cdd:cd03132 1 GRKVGILVADGVDAAELSALKAALKAAGANVKVVAPTLGGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPGGAEAAFALAP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610781719 634 EATARDFVADAFQHCKFIGYDQSALPLLEKAGIAdVMDEGMLPLPGEGGLAA--FVSELGKLR 694
Cdd:cd03132 81 SGRALHFVTEAFKHGKPIGAVGEGSDLLEAAGIP-LEDPGVVTADDVKDVFTdrFIDALALHR 142
|
|
| Catalase_C |
pfam18011 |
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety ... |
553-700 |
1.67e-07 |
|
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain.
Pssm-ID: 436209 Cd Length: 150 Bit Score: 51.12 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 553 EGRKLGILITDGVDAKL--LKGLTKAVEAEKAVFEFIAPKVG-GVtasDGTFIEAHhmidggpSVLFDAVALLTSAAAID 629
Cdd:pfam18011 1 DGLTVGILASNDSDASLaqAKALAAALAAAGVDVLVVAETLAdGV---NRTYSTAD-------ATLFDAIVVADGAEGLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 630 ELIKEAT--------ARDFVADAFQHCKFIGYDQSALPLLEKAGIaDVMDEGML--PLPGEGGLAAFVSELGKLRVWARE 699
Cdd:pfam18011 71 SAKATAAsslypagrPLQILLDAYRHGKPIGALGSGSSALSGAGI-SAEGPGVYvgDSADDALVEDVEEGLATFRFWDRF 149
|
.
gi 1610781719 700 P 700
Cdd:pfam18011 150 P 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KatE |
COG0753 |
Catalase [Inorganic ion transport and metabolism]; |
31-528 |
0e+00 |
|
Catalase [Inorganic ion transport and metabolism];
Pssm-ID: 440516 [Multi-domain] Cd Length: 489 Bit Score: 937.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 31 QTAAGDDPVLTTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSA 110
Cdd:COG0753 2 QYADDEGKTLTTNQGAPVADNQNSLTAGPRGPTLLEDFHLREKLAHFDRERIPERVVHARGSGAHGTFEVTEDISKYTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 111 DLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFP 190
Cdd:COG0753 82 KFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHAQKRDPDTNLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 191 QaqtaHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKI 270
Cdd:COG0753 162 Q----HDTFWDFWSLSPESLHQVTWLMSDRGIPRSYRHMEGFGSHTFRLVNAEGERFWVKFHWKPKQGIHSLTWDEAQKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 271 NGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVA 350
Cdd:COG0753 238 AGKDPDFHRRDLYEAIERGDFPEWELGVQVMPEEDADKFDFDPLDLTKVWPEEDYPLIEVGKMTLNRNPDNFFAETEQAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 351 FMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTGRANYQPNSFGeGPR 430
Cdd:COG0753 318 FSPGNLVPGIDFSPDKMLQGRLFSYADTQRYRL-GPNFHQLPVNRPKCPVHNYQRDGAMRYDINGGRVNYEPNSLG-GPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 431 ESPtrGFQHFPAEEQGAKARLRPESfADHYSQARQFYISQTPSEQRHIASALTFELSKVETPVIRERMVSHLLNIDEALA 510
Cdd:COG0753 396 EDP--GFKEPPLKVDGDKVRYRSES-DDHFSQAGLLYRSMSDEEKQHLIDNIAFELGKVESEEIRERMVAHFYNVDPELG 472
|
490
....*....|....*...
gi 1610781719 511 ATVAQKLGFqTMPKPADA 528
Cdd:COG0753 473 ARVAEALGL-DLPEAKAL 489
|
|
| katE |
PRK11249 |
hydroperoxidase II; Provisional |
35-700 |
0e+00 |
|
hydroperoxidase II; Provisional
Pssm-ID: 236886 [Multi-domain] Cd Length: 752 Bit Score: 934.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 35 GDDPVLTTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQ 114
Cdd:PRK11249 72 SEGYALTTNQGVRIADDQNSLRAGSRGPSLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKAAFLQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 115 RAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAQT 194
Cdd:PRK11249 152 DPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 195 AHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGAD 274
Cdd:PRK11249 232 AHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPVAGKASLVWDEAQKLTGRD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 275 PDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQ 354
Cdd:PRK11249 312 PDFHRRDLWEAIEAGDYPEYELGVQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFHPG 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 355 NVPPGIDFSNDPLLQGRNFSYLDTQLKRLGGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTGRANYQPNSFGEG-PRESP 433
Cdd:PRK11249 392 HIVPGIDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMTIDTGPANYEPNSINGNwPRETP 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 434 TR----GFQHFPAEEQGAKARLRPESFADHYSQARQFYISQTPSEQRHIASALTFELSKVETPVIRERMVSHLLNIDEAL 509
Cdd:PRK11249 472 PApkrgGFESYQERVEGNKVRERSPSFGDYYSQPRLFWLSQTPIEQRHIIDAFSFELGKVVRPYIRERVVDQLAHIDLTL 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 510 AATVAQKLGFQTMPKPADAAMPTRQD-LEPSPALSIVQRGPKRFEGRKLGILITDGVDAKLLKGLTKAVEAEKAVFEFIA 588
Cdd:PRK11249 552 AQAVAENLGIPLTDEQLNITPPPDVNgLKKDPALSLYAIPDGDIKGRKVAILLNDGVDAADLLAILKALKAKGVHAKLLY 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 589 PKVGGVTASDGTFIEAHHMIDGGPSVLFDAVALLTSAAAIDELIKEATARDFVADAFQHCKFIGYDQSALPLLEKAGIAD 668
Cdd:PRK11249 632 PRMGEVTADDGTVLPIAATFAGAPSLTFDAVIVPGGKANIADLADNGDARYYLLEAYKHLKPIALAGDARKLKAALKLPD 711
|
650 660 670
....*....|....*....|....*....|....
gi 1610781719 669 VMDEGMLPLPGEGG--LAAFVSELGKLRVWAREP 700
Cdd:PRK11249 712 QGEEGLVEADSADGsfMDELLTAMAAHRVWSREP 745
|
|
| catalase_clade_2 |
cd08155 |
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
78-517 |
0e+00 |
|
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: 870.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 78 DHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWD 157
Cdd:cd08155 1 DHERIPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 158 LVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAQTAHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTF 237
Cdd:cd08155 81 LVGNNIPVFFIQDAIKFPDLIHAVKPEPHNEMPQAQSAHDTFWDFVSLQPESAHMVMWAMSDRAIPRSYRMMEGFGVHTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 238 RFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPT 317
Cdd:cd08155 161 RLVNAQGKSTFVKFHWKPVLGVHSLVWDEAQKIAGKDPDFHRRDLWEAIESGDYPEWELGVQLIDEEDEFKFDFDILDPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 318 KIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLGGPNFTHLPINAPK 397
Cdd:cd08155 241 KLIPEELVPVQRVGKMVLNRNPDNFFAETEQVAFCPANVVPGIDFSNDPLLQGRLFSYLDTQLSRLGGPNFHELPINRPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 398 CPFAHFQQDGHMAMRNPTGRANYQPNSFGEGPRESPTR---GFQHFPAEEQGAKARLRPESFADHYSQARQFYISQTPSE 474
Cdd:cd08155 321 CPVHNNQRDGHMRMTINKGRVNYFPNSLGAGPPRAASPaegGFVHYPEKVEGPKIRIRSESFADHYSQARLFWNSMSPVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1610781719 475 QRHIASALTFELSKVETPVIRERMVSHLLNIDEALAATVAQKL 517
Cdd:cd08155 401 KEHIISAFTFELSKVETPEIRERVVDHLANIDEDLAKKVAKGL 443
|
|
| Catalase |
pfam00199 |
Catalase; |
41-426 |
0e+00 |
|
Catalase;
Pssm-ID: 459708 Cd Length: 383 Bit Score: 723.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 41 TTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKT 120
Cdd:pfam00199 1 TTSNGAPVPDNQNSLTAGPRGPLLLQDFHLIEKLAHFDRERIPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 121 PAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAqtahDTFW 200
Cdd:pfam00199 81 PVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHSQKRDPQTNLPDP----AMFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 201 DFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRR 280
Cdd:pfam00199 157 DFWSLNPESLHQVTWLFSDRGIPRSYRHMNGFGVHTFKLVNADGERVYVKFHFKTDQGIKNLTWEEAQKLAGKDPDYHTR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 281 DLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGI 360
Cdd:pfam00199 237 DLYEAIERGDYPSWTLYVQVMTEEDAEKFRFNPFDLTKVWPHKDYPLIEVGKMVLNRNPDNYFAEVEQAAFSPSNLVPGI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610781719 361 DFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTG-RANYQPNSFG 426
Cdd:pfam00199 317 EPSPDPMLQGRLFSYPDTQRYRL-GPNYQQLPVNRPPCPVHNYQRDGAMRFDINQGsRPNYEPNSFG 382
|
|
| Catalase |
smart01060 |
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ... |
44-420 |
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: 698.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 44 QGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAF 123
Cdd:smart01060 1 QGAPVADNQNSLTAGPRGPVLLQDFHLIEKLAHFDRERIPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 124 VRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQaqtaHDTFWDFI 203
Cdd:smart01060 81 VRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGNNTPVFFIRDPIKFPDFIHAQKRDPRTNLPD----HDMFWDFW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 204 SLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLW 283
Cdd:smart01060 157 SLNPESLHQVTWLMSDRGIPASYRHMNGFGVHTFKLVNAEGERFYVKFHFKPDQGIKNLTWEEAAKLAGKDPDYHRRDLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 284 TAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFS 363
Cdd:smart01060 237 EAIERGDYPEWTLYVQVMPEEDAEKFRFDPFDLTKVWPHKDYPLIEVGKMTLNRNPDNYFAEVEQAAFSPSNLVPGIEFS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610781719 364 NDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAM-RNPTGRANY 420
Cdd:smart01060 317 PDKMLQGRLFSYPDTQRYRL-GPNYHQLPVNRPRCPVHNYQRDGAMRVdGNQGGDPNY 373
|
|
| catalase_clade_1 |
cd08154 |
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
40-517 |
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: 611.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 40 LTTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEK 119
Cdd:cd08154 2 LTTNQGAPVGDNQNSQTVGPRGPVLLEDYHLIEKLAHFDRERIPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 120 TPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAK-------QEPDRafpqa 192
Cdd:cd08154 82 TPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGNNLPVFFIRDAIKFPDMIHALKpspvtniQDPNR----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 193 qtahdtFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKING 272
Cdd:cd08154 157 ------IFDFFSHVPESTHMLTFLYSDWGTPASYRHMDGSGVHTYKWVNAEGKVVYVKYHWKPKQGVKNLTAEEAAEVQG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 273 ADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFM 352
Cdd:cd08154 231 KNFNHATQDLYDAIAAGNYPEWELYVQIMDPKDLDKLDFDPLDDTKIWPEDQFPLKPVGKMTLNKNPDNFFAEVEQVAFS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 353 TQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTGRANYQPNSFGeGPRES 432
Cdd:cd08154 311 PGNLVPGIEPSDDKMLQGRLFSYSDTQRYRL-GPNYLQLPINAPKAAVHNNQRDGQMNYGHDTSDVNYEPSRLD-GLPEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 433 PTRGFQHFPAEEQGAKARLRPESFadhYSQARQFYISQTPSEQRHIASALTFELSKVETPvIRERMVSHLLNIDEALAAT 512
Cdd:cd08154 389 PKYPYSQPPLSGTTQQAPIAKTNN---FKQAGERYRSFSEEEQENLIKNLVVDLSDVNEE-IKLRMLSYFSQADPDYGER 464
|
....*
gi 1610781719 513 VAQKL 517
Cdd:cd08154 465 VAEGL 469
|
|
| catalase |
cd00328 |
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ... |
81-517 |
0e+00 |
|
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Most catalases exist as tetramers of 65KD subunits containing a protoheme IX group buried deep inside the structure. In eukaryotic cells, catalases are located in peroxisomes.
Pssm-ID: 163705 [Multi-domain] Cd Length: 433 Bit Score: 553.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 81 RIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVG 160
Cdd:cd00328 1 RIPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 161 NNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQaqtaHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFI 240
Cdd:cd00328 81 NNTPIFFIRDAIKFPDFIHAQKPNPQTALPD----ADRFWDFLSLRPESLHQVSFLFSDRGIPAAYRHMNGYGSHTFKLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 241 NAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKII 320
Cdd:cd00328 157 NANGKVHYVKFHWKTDQGIANLVWEEAARLAGEDPDYHRQDLFEAIEAGDYPSWELYIQVMTFNDAEKFPFNPLDPTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 321 PEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPF 400
Cdd:cd00328 237 PEELVPLIVVGKLVLNRNPLNFFAEVEQAAFDPGHIVPGVEFSEDPLLQGRLFSYADTQLYRL-GPNFQQLPVNRPYAPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 401 AHFQQDGHMAMRNPTGRANYQPNSFGEGPRESPTRGFQHFPAEEQ-GAKARLRPESFADHYSQARQFYISQTPSEQRHIA 479
Cdd:cd00328 316 HNNQRDGAGNMNDNTGVPNYEPNAKDVRYPAQGAPKFDRGHFSHWkSGVNREASTTNDDNFTQARLFYRSLTPGQQKRLV 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 1610781719 480 SALTFELSKVETPVIRERMVSHLLNIDEALAATVAQKL 517
Cdd:cd00328 396 DAFRFELADAVSPQIQQRVLDQFAKVDAAAAKRVAKAL 433
|
|
| catalase_clade_3 |
cd08156 |
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ... |
81-517 |
6.99e-180 |
|
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: 519.40 E-value: 6.99e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 81 RIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVG 160
Cdd:cd08156 1 RIPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 161 NNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQaqtaHDTFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFI 240
Cdd:cd08156 81 NNTPVFFIRDPIKFPDFIHTQKRNPQTNLKD----PDMFWDFWSLSPESLHQVTILFSDRGIPDGYRHMNGYGSHTFSLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 241 NAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKII 320
Cdd:cd08156 157 NAKGERFWVKFHFKTDQGIKNLTNEEAAELAGEDPDYAQRDLFEAIERGDFPSWTLYVQVMPEEDAEKYRFNPFDLTKVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 321 PEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPF 400
Cdd:cd08156 237 PHKDYPLIEVGKLELNRNPENYFAEVEQAAFSPSNLVPGIGFSPDKMLQGRLFSYADAHRYRL-GVNYHQLPVNRPKCPV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 401 AHFQQDGHMAMRNPTGRA-NYQPNSFGeGPRESPTRGFQHFPAeeQGAKARLRPESFADHYSQARQFYISQTPSEQRHIA 479
Cdd:cd08156 316 NNYQRDGAMRVDGNGGGApNYEPNSFG-GPPEDPEYAEPPLPV--SGDADRYNYRDDDDDYTQAGDLYRLVSEDERERLV 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 1610781719 480 SALTFELSKVETPvIRERMVSHLLNIDEALAATVAQKL 517
Cdd:cd08156 393 ENIAGHLKGAPEF-IQERQVAHFYKADPDYGERVAKAL 429
|
|
| PLN02609 |
PLN02609 |
catalase |
32-518 |
1.28e-178 |
|
catalase
Pssm-ID: 215328 [Multi-domain] Cd Length: 492 Bit Score: 518.53 E-value: 1.28e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 32 TAAGDDPVLTTAQGGPVADDQNSLRVGPRGPLVVDDFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSAD 111
Cdd:PLN02609 9 SSAYNSPFFTTNSGAPVWNNNSSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISNLTCAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 112 LFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAK-------QE 184
Cdd:PLN02609 89 FLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGNNFPVFFIRDGMKFPDMVHALKpnpkthiQE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 185 PDRafpqaqtahdtFWDFISLTPESMNMVMWIMSDRTIPRSFRFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAW 264
Cdd:PLN02609 169 PWR-----------ILDFLSHHPESLHMFTFLFDDRGIPQDYRHMEGFGVHTYKLINKAGKAHYVKFHWKPTCGVKNLLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 265 NEAVKINGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFADSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFA 344
Cdd:PLN02609 238 EEAVRVGGSNHSHATQDLYDSIAAGNYPEWKLFIQTMDPEDEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNRNIDNFFA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 345 ETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGPNFTHLPINAPKCPFAHFQQDGHMAMRNPTGRANYQPNS 424
Cdd:PLN02609 318 ENEQLAFCPAIVVPGIYYSDDKLLQTRIFAYADTQRHRL-GPNYLQLPVNAPKCAHHNNHHEGFMNFMHRDEEVNYFPSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 425 FGEGPRESPTRgfqhFPAEEQGAKARLRPESFADHYSQARQFYISQTPSEQRHIASALTFELSKV-ETPVIRERMVSHLL 503
Cdd:PLN02609 397 FDPVRHAERVP----IPHPPLSGRREKCKIEKENNFKQPGERYRSWSPDRQERFIKRWVDALSDPrVTHEIRSIWISYWS 472
|
490
....*....|....*
gi 1610781719 504 NIDEALAATVAQKLG 518
Cdd:PLN02609 473 QCDKSLGQKLASRLN 487
|
|
| catalase_fungal |
cd08157 |
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ... |
67-518 |
6.31e-148 |
|
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: 438.70 E-value: 6.31e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 67 DFHFREKIFHFDHERIPERVVHARGYGAHGYFETYESLAAHTSADLFQRAGEKTPAFVRFSTVAGNKGSADLARDVRGFA 146
Cdd:cd08157 3 DFHLIDTLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRGFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 147 VKLYTKEGNWDLVGNNIPVFFIQDAIKFPDLIHAAKQEPDRAFPQAqtahDTFWDFISLTPESMNMVMWIMSDRTIPRSF 226
Cdd:cd08157 83 VKFYTEEGNWDWVFNNTPVFFIRDPIKFPHFIHSQKRDPQTNLKDS----TMFWDYLSQNPESIHQVMILFSDRGTPASY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 227 RFMEGFGVHTFRFINAKGQSTFVKFHWKPKLGLQSVAWNEAVKINGADPDFHRRDLWTAIQSGNFPEWELQVQLFDQDFA 306
Cdd:cd08157 159 RSMNGYSGHTYKWVNPDGSFKYVQFHLKSDQGPKFLTGEEAARLAGSNPDYATKDLFEAIERGDYPSWTVYVQVMTPEQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 307 DSFDFDVLDPTKIIPEEILAPKPVGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRLgGP 386
Cdd:cd08157 239 EKLRFNIFDLTKVWPHKDFPLRPVGKLTLNENPKNYFAEIEQAAFSPSHMVPGIEPSADPVLQARLFSYPDAHRHRL-GP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 387 NFTHLPINAPK-CPFAHF-QQDGHMAMRNPTG-RANYqPNSFgegprESPTRGFQHFPAEEQGAKARLRPESFADH---- 459
Cdd:cd08157 318 NYQQLPVNRPKtSPVYNPyQRDGPMSVNGNYGgDPNY-VSSI-----LPPTYFKKRVDADGHHENWVGEVVAFLTEitde 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610781719 460 -YSQARQFY-ISQTPSEQRHIASALTFELSKVeTPVIRERMVSHLLNIDEALAATVAQKLG 518
Cdd:cd08157 392 dFVQPRALWeVVGKPGQQERFVKNVAGHLSGA-PPEIRKRVYEIFARVNPDLGKRIEKATE 451
|
|
| catalase_like |
cd08150 |
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ... |
83-383 |
4.04e-75 |
|
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: 243.62 E-value: 4.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 83 PERVVHARGYGAHGYFETYESLAAHTSADLFQrAGEKTPAFVRFSTVagnKGSADLARDVRGFAVKLYT--KEGNWDLVG 160
Cdd:cd08150 1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFA-EGKVYPAYIRFSNG---AGIDDTKPDIRGFAIKFTGvaDAGTLDFVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 161 NNIPVFFIQDAIKFPDLIHAAKQEPdrafpQAQTAHDTFWDFISLTPESMNMVMWIMSDrtIPRSFRFMEGFGVHTFRFI 240
Cdd:cd08150 77 NNTPVFFIRNTSDYEDFVAEFARSA-----RGEPPLDFIAWYVEKRPEDLPNLLGARSQ--VPDSYAAARYFSQVTFAFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 241 NAKGQSTFVKFHWKPKLGLQSVAWNEavkINGADPDFHRRDLWTAIQSGnFPEWELQVQLFDqdfaDSFDFDVLDPTKII 320
Cdd:cd08150 150 NGAGKYRVVRSKDNPVDGIPSLEDHE---LEARPPDYLREELTERLQRG-PVVYDFRIQLND----DTDATTIDNPTILW 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610781719 321 PEEILAPKpVGRLVLDRMPDNffAETEQVAFMTQNVPPGIDFSND--PLLQGRNFSYLDTQLKRL 383
Cdd:cd08150 222 PTEHPVEA-VAKITIPPPTFT--AAQEAFAFNPFTPWHGLLETNDlgPILEVRRRVYTSSQGLRH 283
|
|
| srpA_like |
cd08153 |
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ... |
85-383 |
6.83e-39 |
|
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: 145.84 E-value: 6.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 85 RVVHARGYGAHGYFETYESLAAHTSADLFQRAgeKTPAFVRFSTVAGNKGSADLARDVRGFAVKLYTKEGN-WDLVGNNI 163
Cdd:cd08153 15 RRNHAKGICVSGTFTPSGAAASLSRAPLFSGG--SVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 164 PVFFIQDAIKFPDLIHAAK-QEPDRAFPQAQTAhdtfwdFISLTPESMNMVMWIMSdRTIPRSFRFMEGFGVHTFRFINA 242
Cdd:cd08153 93 PVFPVRTPEEFLALLKAIApDATGKPDPAKLKA------FLAAHPEAAAFLAWIKT-APPPASFANTTYYGVNAFYFTNA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 243 KGQSTFVKFHWKPKLGLQSVAWNEAVKingADPDFHRRDLWTAIQSGNFpEWELQVQLfdqdfADSFDfDVLDPTKIIPE 322
Cdd:cd08153 166 NGKRQPVRWRFVPEDGVKYLSDEEAAK---LGPDFLFDELAQRLAQGPV-RWDLVLQL-----AEPGD-PTDDPTKPWPA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610781719 323 ---EILApkpvGRLVLDRMPDNFFAETEQVAFMTQNVPPGIDFSNDPLLQGRNFSYLDTQLKRL 383
Cdd:cd08153 236 drkEVDA----GTLTITKVAPDQGGACRDINFDPLVLPDGIEPSDDPLLAARSAAYAVSFSRRQ 295
|
|
| GATase1_catalase |
cd03132 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ... |
554-694 |
1.12e-37 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.
Pssm-ID: 153226 Cd Length: 142 Bit Score: 137.01 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 554 GRKLGILITDGVDAKLLKGLTKAVEAEKAVFEFIAPKVGGVTASDGTFIEAHHMIDGGPSVLFDAVALLTSAAAIDELIK 633
Cdd:cd03132 1 GRKVGILVADGVDAAELSALKAALKAAGANVKVVAPTLGGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPGGAEAAFALAP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610781719 634 EATARDFVADAFQHCKFIGYDQSALPLLEKAGIAdVMDEGMLPLPGEGGLAA--FVSELGKLR 694
Cdd:cd03132 81 SGRALHFVTEAFKHGKPIGAVGEGSDLLEAAGIP-LEDPGVVTADDVKDVFTdrFIDALALHR 142
|
|
| Catalase-rel |
pfam06628 |
Catalase-related immune-responsive; This family represents a small conserved region within ... |
453-517 |
1.89e-25 |
|
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: 99.75 E-value: 1.89e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610781719 453 PESFADHYSQARQFYISQTPSEQRHIASALTFELSKVETPVIRERMVSHLLNIDEALAATVAQKL 517
Cdd:pfam06628 1 SIDFDDHFSQAGLFYRSMSEEERQRLVDNIAFELSKVTDPEIQERMVAHFYKVDPDLGQRVAEAL 65
|
|
| y4iL_like |
cd08152 |
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ... |
85-352 |
7.66e-12 |
|
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: 66.90 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 85 RVVHARGYGA-HGYFETYESLAAHTSADLFQRAGEKtPAFVRFSTVAGNkGSADLARDVRGFAVKLYTKEG--------- 154
Cdd:cd08152 5 RDAHAKSHGClKAEFTVLDDLPPELAQGLFAEPGTY-PAVIRFSNAPGD-ILDDSVPDPRGMAIKVLGVPGekllpeeda 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 155 -NWDLVGNNIPVFFIQDAIKF-------------PDLIHAAKQEP---DRAFPQAQTAHDTFWDFISLTPESM-NMVMWI 216
Cdd:cd08152 83 tTQDFVLVNHPVFFARDAKDYlallkllarttslPDGAKAALSAPlrgALRVLEAAGGESPTLKLGGHPPAHPlGETYWS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 217 MSdrtiprSFRFmeGFGVHTFRFINAkgqstfvkfhwKPKLglqsVAWNEAVKINGADPDFHRRDLWTAIQSGNFpEWEL 296
Cdd:cd08152 163 QA------PYRF--GDYVAKYSVVPA-----------SPAL----PALTGKELDLTDDPDALREALADFLAENDA-EFEF 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610781719 297 QVQLFDqdfaDSFDFDVLDPTKIIPEEILAPKPVGRLVLDrmPDNFFAETEQVAFM 352
Cdd:cd08152 219 RIQLCT----DLEKMPIEDASVEWPEALSPFVPVATITIP--PQDFDSPARQRAFD 268
|
|
| Catalase_C |
pfam18011 |
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety ... |
553-700 |
1.67e-07 |
|
C-terminal domain found in long catalases; This domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain.
Pssm-ID: 436209 Cd Length: 150 Bit Score: 51.12 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 553 EGRKLGILITDGVDAKL--LKGLTKAVEAEKAVFEFIAPKVG-GVtasDGTFIEAHhmidggpSVLFDAVALLTSAAAID 629
Cdd:pfam18011 1 DGLTVGILASNDSDASLaqAKALAAALAAAGVDVLVVAETLAdGV---NRTYSTAD-------ATLFDAIVVADGAEGLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610781719 630 ELIKEAT--------ARDFVADAFQHCKFIGYDQSALPLLEKAGIaDVMDEGML--PLPGEGGLAAFVSELGKLRVWARE 699
Cdd:pfam18011 71 SAKATAAsslypagrPLQILLDAYRHGKPIGALGSGSSALSGAGI-SAEGPGVYvgDSADDALVEDVEEGLATFRFWDRF 149
|
.
gi 1610781719 700 P 700
Cdd:pfam18011 150 P 150
|
|
| |
