|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
1-634 |
0e+00 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 1302.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 1 MAFSKSSSSFIHPQLLHIVAKMTLFDTFLFYIVHFVDKLGVWHRLPVLLGLAYLGIRRHLHQRYNLLHVGGV-NGGRYDT 79
Cdd:PLN02283 1 MLFSASLSWFIHPDLHEVVSKMSLFDRFLFLIVHFVDKLGLWHRLPVFLGLAYLALRRHLHQRYNLLNVGQTpNGQRYDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 80 EEFCYRTADGKCNHPIDDQIGSQGTLFGRNMPPSTSSYRLLEPHPTVVATKLLARKKFIDNGKQFNLIACSWVQFMIHDW 159
Cdd:PLN02283 81 AEYPYRTADGKCNDPFNEGAGSQGTFFGRNMPPVDQKDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 160 IDHMEDTQQIEIKAPSDIASGCPLKSFKFFKSKSIPTGSPHMEDGFLNTRTPWWDGSVIYGNNDDGMRRVRTFKDGKLKI 239
Cdd:PLN02283 161 IDHLEDTQQIELTAPKEVASQCPLKSFKFYKTKEVPTGSPDIKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 240 SNDGLLEHDGKGIPISGDVRNCWAGFSLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVEL 319
Cdd:PLN02283 241 SEDGLLLHDEDGIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 320 LKTDTLLAGMRINWYGFMGKKFKDSFGHILGPILSGLVGLKKPRDHGVPYSLTEEFVSVYRMHALLPDELHIRDTNSsnT 399
Cdd:PLN02283 321 LKTDTLLAGMRANWYGLLGKKFKDTFGHIGGPILSGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLLPDHLILRDITA--A 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 400 ASEGECPPLIEEVPMREMVGLEGEKRLSKIGMEKMMVSMGHQASGAMALWNYPSWMRNLVAHDVNGEDRPDLVDMAALEI 479
Cdd:PLN02283 399 PGENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVSMGHQACGALELWNYPSWMRDLVPQDIDGEDRPDHVDMAALEI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 480 YRDRERGVARYNEFRRNLLMIPISKWEDLTDDEKVVEALCEVYGDDVEKLDLLVGLHAEKKIKGFAICETAFFIFLLIAS 559
Cdd:PLN02283 479 YRDRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMAS 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225456100 560 RRLEADRFFTTNFNSQTYTRSGLDWVNKTETLQDVLDRHFPDMTKKWMRCSSAFSVWDSTPTPTNYIPLYLRPAP 634
Cdd:PLN02283 559 RRLEADRFFTSNFNEKTYTKKGLEWVNTTESLKDVIDRHYPEMTDKWMNSSSAFSVWDSPPNPHNWIPLYLRPPP 633
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
85-617 |
0e+00 |
|
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death.
Pssm-ID: 188650 [Multi-domain] Cd Length: 484 Bit Score: 645.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 85 RTADGKCNHPIDDQIGSQGTLFGRNMPPST----SSYRLLEPHPTVVATKLLARKKFIdNGKQFNLIACSWVQFMIHDWI 160
Cdd:cd09818 1 RTADGSYNDLDNPSMGSVGTRFGRNVPLDAtfpeDKDELLTPNPRVISRRLLARTEFK-PATSLNLLAAAWIQFMVHDWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 161 DHmedtqqieikapsdiasGCPlksfkffksksiptgsphmedGFLNTRTPWWDGSVIYGNNDDGMRRVRTF-KDGKLKI 239
Cdd:cd09818 80 SH-----------------GPP---------------------TYINTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLKL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 240 SNDGLLEHD-GKGIPISGDVRNCWAGFSLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVE 318
Cdd:cd09818 122 DADGLLPVDeHTGLPLTGFNDNWWVGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 319 LLKTDTLLAGMRINWYGFMGKKFKDSFGHILG-PILSGLVGLKkPRDHGVPYSLTEEFVSVYRMHALLPDELHIRDTNSS 397
Cdd:cd09818 202 ILAHPTLEIAMRANWWGLLGERLKRVLGRDGTsELLSGIPGSP-PNHHGVPYSLTEEFVAVYRMHPLIPDDIDFRSADDG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 398 ntasegecpPLIEEVPMREMVGLEGEKRLSKIGMEKMMVSMGHQASGAMALWNYPSWMRNLVAHDvngedrPDLVDMAAL 477
Cdd:cd09818 281 ---------ATGEEISLTDLAGGKARELLRKLGFADLLYSFGITHPGALTLHNYPRFLRDLHRPD------GRVIDLAAI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 478 EIYRDRERGVARYNEFRRNLLMIPISKWEDLTDDEKVVEALCEVYGDDVEKLDLLVGLHAEKKIKGFAICETAFFIFLLI 557
Cdd:cd09818 346 DILRDRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGGDVEKVDLLVGLLAEPLPPGFGFSDTAFRIFILM 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225456100 558 ASRRLEADRFFTTNFNSQTYTRSGLDWVNKTeTLQDVLDRHFPDMtKKWMR-CSSAFSVWD 617
Cdd:cd09818 426 ASRRLKSDRFFTNDFRPEVYTPEGMDWVNNN-TMKSVLLRHFPEL-APALRgVENAFAPWR 484
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
84-604 |
1.20e-127 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 386.53 E-value: 1.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 84 YRTADGKCNHPIDDQIGSQGTLFGRNMP---------PSTSSYRLLEPHPTVVATKLLARKKFIDNgKQFNLIACSWVQF 154
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPpayedgvsaPRGSSSGSPLPSPRLVSNKLFAGDSGIPD-PNLTLLLMQWGQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 155 MIHDWIDHMEDTQQIEI-----KAPSDIASGC-PLKsfkffksksIPTGSPHMED---------------------GFLN 207
Cdd:pfam03098 80 IDHDLTLTPESTSPNGSscdccCPPENLHPPCfPIP---------IPPDDPFFSPfgvrcmpfvrsapgcglgnprEQIN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 208 TRTPWWDGSVIYGNNDDGMRRVRTFKDGKLKIS----NDGLLEHDGKGIP-----------ISGDVR-NCWAGFSLLQAL 271
Cdd:pfam03098 151 QVTSFLDGSQVYGSSEETARSLRSFSGGLLKVNrsddGKELLPFDPDGPCccnssggvpcfLAGDSRaNENPGLTALHTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 272 FVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVELLKTdtllagMRINWYGFMGKKFKDsfghilgp 351
Cdd:pfam03098 231 FLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGE------DNMNWFGLLPLPYNG-------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 352 ilsglvglkkpRDHGVPYSLTEEFVS-VYRM-HALLPDELHIRDTNSSNTasegecpplIEEVPMREMvgLEGEKRLSKI 429
Cdd:pfam03098 297 -----------YDPNVDPSISNEFATaAFRFgHSLIPPFLYRLDENNVPE---------EPSLRLHDS--FFNPDRLYEG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 430 GMEKMMVSMGHQASGAMaLWNYPSWMRNlvaHDVNGEDRPDLVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLT 509
Cdd:pfam03098 355 GIDPLLRGLATQPAQAV-DNNFTEELTN---HLFGPPGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 510 D--DEKVVEALCEVYGdDVEKLDLLVGLHAEKKIKGFAIcETAFFIFLLIASRRLE-ADRFFTTNFNSQTYTRSGLDWVN 586
Cdd:pfam03098 431 DviPNEVIAKLRELYG-SVDDIDLWVGGLAEKPLPGGLV-GPTFACIIGDQFRRLRdGDRFWYENGNQGSFTPEQLEEIR 508
|
570
....*....|....*...
gi 225456100 587 KTeTLQDVLDRHFPDMTK 604
Cdd:pfam03098 509 KT-SLARVICDNTDIIET 525
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
206-598 |
8.34e-84 |
|
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.
Pssm-ID: 188647 [Multi-domain] Cd Length: 370 Bit Score: 267.76 E-value: 8.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 206 LNTRTPWWDGSVIYGNNDDGMRRVRTFKDGKLKIS-------NDGLLE----HDGKGIPIS--------GDVR-NCWAGF 265
Cdd:cd05396 2 LNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNevkgpsyGTELLPfnnpNPSMGTIGLpptrcfiaGDPRvNENLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 266 SLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVELLKTDTLLAGMRINWYgfmgkkfkdsf 345
Cdd:cd05396 82 LAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLF----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 346 ghilgpilsglvglkkPRDHGVPYSLTEEFVSVYRM-HALLPDELHIRDTNSSntasegecPPLIEEVPMREMVGLEGEK 424
Cdd:cd05396 151 ----------------PDPDVVPYVLSEFFTAAYRFgHSLVPEGVDRIDENGQ--------PKEIPDVPLKDFFFNTSRS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 425 RLSKIGMEKMMVSMGHQASGAMALWNYPSwmrnlvaHDVNGEDRPDLVDMAALEIYRDRERGVARYNEFRRNLLMIPISK 504
Cdd:cd05396 207 ILSDTGLDPLLRGFLRQPAGLIDQNVDDV-------MFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 505 WEDLTDDEKVVEALCEVYGdDVEKLDLLVGLHAEKKIKGFAICETAFFIFLLIASRRLEADRFFTTNFNsqTYTRSGLDW 584
Cdd:cd05396 280 FQDILTDPELAKKLAELYG-DPDDVDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYN--PFGKSGKEE 356
|
410
....*....|....
gi 225456100 585 VNKTETLQDVLDRH 598
Cdd:cd05396 357 LEKLISLADIICLN 370
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
104-602 |
5.20e-34 |
|
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1.
Pssm-ID: 188648 [Multi-domain] Cd Length: 490 Bit Score: 135.86 E-value: 5.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 104 TLFGRNMPPSTSSYRLLEPHPTVVATKLLARKKFIDNGKQFNLIACSWVQFMIHDWI--DHMedtqqieikapsdiasgc 181
Cdd:cd09816 59 TYYGRHLPPVPRDCPTELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLrtDPG------------------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 182 plksfkffksksiptgsphmeDGFLNTRTPWWDGSVIYGNNDDGMRRVRTFKDGKLK--ISNDG----LLEHDGK----- 250
Cdd:cd09816 121 ---------------------DPRRNTSNHGIDLSQIYGLTEARTHALRLFKDGKLKsqMINGEeyppYLFEDGGvkmef 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 251 --GIPISGDV------RNCWA----------GFSLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTsaviakiht 312
Cdd:cd09816 180 ppLVPPLGDEltpereAKLFAvgherfnltpGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNIL--------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 313 idwTVELLKtdtllagMRINWY--GFMGKKFKDSFghilgpilsglvglkKPRD-HGVPYS----LTEEFVSVYRMHALL 385
Cdd:cd09816 251 ---IGELIK-------IVIEDYinHLSPYHFKLFF---------------DPELaFNEPWQrqnrIALEFNLLYRWHPLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 386 PDELHIRDtnssntasegecppliEEVPMREMvgLEGEKRLSKIGMEKMMVSMGHQASGAMALWNYPSWMRNlvahdvng 465
Cdd:cd09816 306 PDTFNIGG----------------QRYPLSDF--LFNNDLVVDHGLGALVDAASRQPAGRIGLRNTPPFLLP-------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 466 edrpdlVDMAALEIyrDRERGVARYNEFRRNLLMIPISKWEDLTDDEKVVEALCEVYGdDVEKLDLLVGLHAEKKIKGFA 545
Cdd:cd09816 360 ------VEVRSIEQ--GRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELYG-DVDAVEFYVGLFAEDPRPNSP 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225456100 546 ICETaffIFLLIASrrlEADRFFTTN-------FNSQTYTRSGLDWVNKTETLQDVLDRHFPDM 602
Cdd:cd09816 431 LPPL---MVEMVAP---DAFSGALTNpllspevWKPSTFGGEGGFDIVKTATLQDLVCRNVKGG 488
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
151-597 |
8.56e-33 |
|
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.
Pssm-ID: 188654 [Multi-domain] Cd Length: 420 Bit Score: 130.89 E-value: 8.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 151 WVQFMIHDwIDHMEDT--QQIeikapsdiasgcplksfkffksksiptgsphmedgflNTRTPWWDGSVIYGNNDDGMRR 228
Cdd:cd09822 32 WGQFLDHD-IDLTPDNprEQI-------------------------------------NAITAYIDGSNVYGSDEERADA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 229 VRTFKDGKLKISN---DGLLEHDGKGIP------------ISGDVR-NCWAGFSLLQALFVKEHNAVCDMLKVHHPEFDD 292
Cdd:cd09822 74 LRSFGGGKLKTSVanaGDLLPFNEAGLPndnggvpaddlfLAGDVRaNENPGLTALHTLFVREHNRLADELARRNPSLSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 293 ERLYRHARLVTSAVIAKIhTIDwtvELLktdtllagmrinwygfmgkkfkdsfghilgPILsgLVGLKKPRDHG----VP 368
Cdd:cd09822 154 EEIYQAARAIVIAEIQAI-TYN---EFL------------------------------PAL--LGENALPAYSGydetVN 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 369 YSLTEEFVSV-YRM-HALLPDELHIRDTNSSNtasegECPPLIEEVPMRemvglegEKRLSKIGMEKMMvsMGhQASG-A 445
Cdd:cd09822 198 PGISNEFSTAaYRFgHSMLSSELLRGDEDGTE-----ATSLALRDAFFN-------PDELEENGIDPLL--RG-LASQvA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 446 MALWNY-PSWMRNLvahdVNGEDRPDLVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTDDEKVVEALCEVYGd 524
Cdd:cd09822 263 QEIDTFiVDDVRNF----LFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDITSDPDLAARLASVYG- 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225456100 525 DVEKLDLLVGLHAEKKIKGFAICETAFFIFLLIASRRLEADRFFTTNFNSqtyTRSGLDWVNKTeTLQDVLDR 597
Cdd:cd09822 338 DVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDDL---LLDEIADIENT-TLADVIRR 406
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
206-576 |
1.74e-29 |
|
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.
Pssm-ID: 188655 [Multi-domain] Cd Length: 378 Bit Score: 120.37 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 206 LNTRTPWWDGSVIYGNNDDGMRRVRTFKDGKLKISNDGLLE-------HDGKGIP--------ISGDVRNCW-AGFSLLQ 269
Cdd:cd09823 4 LNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGREllpfsnnPTDDCSLssagkpcfLAGDGRVNEqPGLTSMH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 270 ALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVELLktdtllagmrinwygfmGKKFKDSFghil 349
Cdd:cd09823 84 TLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILL-----------------GRELMEKF---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 350 gpilsGLVGLKKPRDHG----VPYSLTEEF-VSVYRM-HALLPDELHIRDTNSsntasegecpPLIEEVPMREMVG---- 419
Cdd:cd09823 143 -----GLYLLTSGYFNGydpnVDPSILNEFaAAAFRFgHSLVPGTFERLDENY----------RPQGSVNLHDLFFnpdr 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 420 LEGEKrlskiGMEKMMVSMGHQASGAMAlwnyPSWMRNLVAHDVNGEDRPDLVDMAALEIYRDRERGVARYNEFRRNLLM 499
Cdd:cd09823 208 LYEEG-----GLDPLLRGLATQPAQKVD----RFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 500 IPISKWEDLTD--DEKVVEALCEVYGdDVEKLDLLVGLHAEKKIKG------FAiCetaffiflLIAS--RRL-EADRFF 568
Cdd:cd09823 279 PRATTFDDLLGimSPETIQKLRRLYK-SVDDIDLYVGGLSEKPVPGglvgptFA-C--------IIGEqfRRLrRGDRFW 348
|
....*...
gi 225456100 569 TTNFNSQT 576
Cdd:cd09823 349 YENGGQPS 356
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
206-595 |
7.03e-18 |
|
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.
Pssm-ID: 188652 [Multi-domain] Cd Length: 558 Bit Score: 87.35 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 206 LNTRTPWWDGSVIYGNNDDGMRRVRTFKDGKLKISNDGLLEHDGKG--------IPISGDVRNCWAGFSL---------- 267
Cdd:cd09820 134 LNEVTSWIDGSSIYGSSKAWSDALRSFSGGRLASGDDGGFPRRNTNrlplanppPPSYHGTRGPERLFKLgnprgnenpf 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 268 LQA---LFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVELLKTDtllagmRINWYGFMGkkfkds 344
Cdd:cd09820 214 LLTfgiLWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN------VPPYTGYKP------ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 345 fghilgpilsglvglkkprdhGVPYSLTEEFVS-VYRM-HALLPDELHIRDTNSSNTAsegecpplieevpmremvgleg 422
Cdd:cd09820 282 ---------------------HVDPGISHEFQAaAFRFgHTLVPPGVYRRNRQCNFRE---------------------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 423 ekrlskigmekmmVSMGHQASGAMALWN-YpsWMRN--LVAHDVNG------------EDR---PDL------------V 472
Cdd:cd09820 319 -------------VLTTSGGSPALRLCNtY--WNSQepLLKSDIDElllgmasqiaerEDNiivEDLrdylfgplefsrR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 473 DMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTD-----DEKVVEALCEVYGDDVEKLDLLVGLHAEKKIKG---- 543
Cdd:cd09820 384 DLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPdlfkkDPELLERLAELYGNDLSKLDLYVGGMLESKGGGpgel 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 225456100 544 F-AICETAFfiflliasRRL-EADRFFTTNFNSQTYTRSGLDWVNKTeTLQDVL 595
Cdd:cd09820 464 FrAIILDQF--------QRLrDGDRFWFENVKNGLFTAEEIEEIRNT-TLRDVI 508
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
80-601 |
5.15e-17 |
|
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme peroxidases, catalyze the oxygenation of linoleate and similar targets. Linoleate (8R)-dioxygenase, also called linoleate:oxygen 7S,8S-oxidoreductase, generates (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate as a product. Other members are 5,8-linoleate dioxygenase (LDS, ppoA) and linoleate 10R-dioxygenase (ppoC), involved in the biosynthesis of oxylipins.
Pssm-ID: 188649 [Multi-domain] Cd Length: 550 Bit Score: 84.70 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 80 EEFCYRTADGKCNHPIDDQIGSQGTLFGRNMPPSTSSYRLLePHPTVVATKLLARKKFIDNGKQFNLIACSWVQFMIHD- 158
Cdd:cd09817 29 DNYKYRKADGSNNNILNPRLGAAGSPYARSVPPKHDQPGVL-PDPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 159 -WIDHmedtqqieikapsdiasgcplksfkffksksiptgsphmEDGFLNTRTPWWDGSVIYGNNDDGMRRVRTFKDGKL 237
Cdd:cd09817 108 fRTDH---------------------------------------RDMNINNTSSYLDLSPLYGSNQEEQNKVRTMKDGKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 238 K---ISNDGLLehdgkGIPisgdvrncwAGFSLLQALFVKEHNAVCDML-----------------KVHHPEFDDERLYR 297
Cdd:cd09817 149 KpdtFSDKRLL-----GQP---------PGVCALLVMFNRFHNYVVEQLaqineggrftppgdkldSSAKEEKLDEDLFQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 298 HARLVTSAVIAKIHTIDWTVELL---KTDTllagmriNWYGFMGKKFKDSFGHIlgpilsglvglkkPRDHGVPYSLteE 374
Cdd:cd09817 215 TARLITCGLYINIVLHDYVRAILnlnRTDS-------TWTLDPRVEIGRSLTGV-------------PRGTGNQVSV--E 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 375 FVSVYRMHALLPD------ELHIRDTNSSNTASEGECPPLIEEVPM-----------REMVGLEGEK--RLSKIGMEKMM 435
Cdd:cd09817 273 FNLLYRWHSAISArdekwtEDLFESLFGGKSPDEVTLKEFMQALGRfealipkdpsqRTFGGLKRGPdgRFRDEDLVRIL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 436 VSMGHQASGAMALWNYPSWMRNlvahdvngedrpdlVDMaaLEIYRDRERGVARYNEFRRNLLMIPISKWEDLTDDEKVV 515
Cdd:cd09817 353 KDSIEDPAGAFGARNVPASLKV--------------IEI--LGILQAREWNVATLNEFRKFFGLKPYETFEDINSDPEVA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 516 EALCEVYG--DDVEkldLLVGLHAE--KKIK----GFAICETAFFIFLLIASRRLEADRFFTTNFNSQTYTRSGLD---- 583
Cdd:cd09817 417 EALELLYGhpDNVE---LYPGLVAEdaKPPMppgsGLCPGYTISRAILSDAVALVRGDRFYTVDYNPNNLTNWGYAevsp 493
|
570 580
....*....|....*....|
gi 225456100 584 --WVNKTETLQDVLDRHFPD 601
Cdd:cd09817 494 dpDVAFGGVFYKLLLRALPN 513
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
206-571 |
6.89e-13 |
|
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix.
Pssm-ID: 188658 Cd Length: 440 Bit Score: 71.18 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 206 LNTRTPWWDGSVIYGNNDDGMRRVRTFKD--GKLKI-----SNDGLLEHDGKG------------IP--ISGDVR-NCWA 263
Cdd:cd09826 40 INQLTSYIDASNVYGSSDEEALELRDLASdrGLLRVgivseAGKPLLPFERDSpmdcrrdpnespIPcfLAGDHRaNEQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 264 GFSLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVELLKTDtllaGMRI--NWYG------ 335
Cdd:cd09826 120 GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHITYSHWLPKILGPV----GMEMlgEYRGynpnvn 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 336 ------FMGKKFKdsFGH-ILGPILSGLVGLKKPRDHGvPYSLTEEFVSVYRMhallpdelhirdtnssntASEGECPPL 408
Cdd:cd09826 196 psianeFATAAFR--FGHtLINPILFRLDEDFQPIPEG-HLPLHKAFFAPYRL------------------VNEGGIDPL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 409 ieevpMREMVGLEGEKRLSKIGM-----EKMMvSMGHqasgAMALwnypswmrnlvahdvngedrpdlvDMAALEIYRDR 483
Cdd:cd09826 255 -----LRGLFATAAKDRVPDQLLnteltEKLF-EMAH----EVAL------------------------DLAALNIQRGR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 484 ERGVARYNEFRRNLLMIPISKWEDLTD---DEKVVEALCEVYGdDVEKLDLLVGLHAEKKIKGFAICETaFFIFLLIASR 560
Cdd:cd09826 301 DHGLPGYNDYRKFCNLSVAETFEDLKNeikNDDVREKLKRLYG-HPGNIDLFVGGILEDLLPGARVGPT-LACLLAEQFR 378
|
410
....*....|..
gi 225456100 561 RL-EADRFFTTN 571
Cdd:cd09826 379 RLrDGDRFWYEN 390
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
206-324 |
7.25e-06 |
|
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of animal heme peroxidases contains members with somewhat diverse functions. Myeloperoxidases are lysosomal proteins found in azurophilic granules of neutrophils and the lysosomes of monocytes. They are involved in the formation of microbicidal agents upon activation of activated neutrophils (neutrophils undergoing respiratory bursts as a result of phagocytosis), by catalyzing the conversion of hydrogen peroxide to hypochlorous acid. As a heme protein, myeloperoxidase is responsible for the greenish tint of pus, which is rich in neutrophils. Eosinophil peroxidases are haloperoxidases as well, preferring bromide over chloride. Expressed by eosinophil granulocytes, they are involved in attacking multicellular parasites and play roles in various inflammatory diseases such as asthma. The haloperoxidase lactoperoxidase is secreted from mucosal glands and provides antibacterial activity by oxidizing a variety of substrates such as bromide or chloride in the presence of hydrogen peroxide.
Pssm-ID: 188656 [Multi-domain] Cd Length: 411 Bit Score: 48.57 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 206 LNTRTPWWDGSVIYGN------------NDDGMRRVRT-FKDGKL------KISND--GLLEHdGKGIP--ISGDVR-NC 261
Cdd:cd09824 15 INALTSFVDASMVYGSepslak*lrnltNQLGLLAVNQrFTDNGLallpfeNLHNDpcALRNT-SANIPcfLAGDTRvSE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225456100 262 WAGFSLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDWTVELLKTDT 324
Cdd:cd09824 94 NPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA 156
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
206-315 |
6.13e-04 |
|
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is expressed in the thyroid and involved in the processing of iodine and iodine compounds. Specifically, TPO oxidizes iodide via hydrogen peroxide to form active iodine, which is then, for example, incorporated into the tyrosine residues of thyroglobulin to yield mono- and di-iodotyrosines.
Pssm-ID: 188657 [Multi-domain] Cd Length: 565 Bit Score: 42.81 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225456100 206 LNTRTPWWDGSVIYGNNDDGMRRVRTF--KDGKLKIsNDGlleHDGKG----------------IPISGDVRNCW-AG-- 264
Cdd:cd09825 151 INGLTSFIDASTVYGSTLALARSLRDLssDDGLLRV-NSK---FDDSGrdylpfqpeevsscnpDPNGGERVPCFlAGdg 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 225456100 265 -------FSLLQALFVKEHNAVCDMLKVHHPEFDDERLYRHARLVTSAVIAKIHTIDW 315
Cdd:cd09825 227 rasevltLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDY 284
|
|
| |
