|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
47-678 |
0e+00 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 1324.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 47 MGFSLLSSPFVHPQLSEIVSKMTLFDTIFFYAIHFVDKMELWHRLPVILGIIYLAIRRHLHQRYNLLNVGGI-NGQKYDT 125
Cdd:PLN02283 1 MLFSASLSWFIHPDLHEVVSKMSLFDRFLFLIVHFVDKLGLWHRLPVFLGLAYLALRRHLHQRYNLLNVGQTpNGQRYDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 126 NEFSHRTADGKCNHPSDHIIGSQGTFFGRNMPPSSSPYWLLDPHPTVVANKLLARKKFIDNGKQFNMIACSWIQFMIHDW 205
Cdd:PLN02283 81 AEYPYRTADGKCNDPFNEGAGSQGTFFGRNMPPVDQKDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 206 IDHMEDTQQVEIRAPDEIADGCPLKSFKFYKTKKVHTGSPDFRTGCVNTRTPWWDGSVIYGNNEDGMRRVRTFRDGKLKI 285
Cdd:PLN02283 161 IDHLEDTQQIELTAPKEVASQCPLKSFKFYKTKEVPTGSPDIKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 286 AEDGLLEHDEKGIPISGDVRNCWAGFSLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDWTVEL 365
Cdd:PLN02283 241 SEDGLLLHDEDGIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 366 LKTNTLLAGMRINWYGFFGKKVKDLFGHFAGPLFSGLVGLRKPRDHGVPYSLTEEFTSVYRMHSLLPDQLIIRDIRSTTS 445
Cdd:PLN02283 321 LKTDTLLAGMRANWYGLLGKKFKDTFGHIGGPILSGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLLPDHLILRDITAAPG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 446 ESGCPPVLEEVPMKEMAGKEGEKKMSEIGMELMLVSMGHQACGAVTLWNYPSWMRNLVAHDINGEDRPDPVDMAAIEIYR 525
Cdd:PLN02283 401 ENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVSMGHQACGALELWNYPSWMRDLVPQDIDGEDRPDHVDMAALEIYR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 526 DRERGVARYNEFRRNLLMIPIRKWEDLTDEQEVVEALHEVYGDDVEKLDLLIGLHAEKKMKGFAISETAFFIFLLIASRR 605
Cdd:PLN02283 481 DRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRR 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2241025354 606 LEADRFFTTNFNSKSYTEKGLEWVNKTETLKDVIDRNFPGMTKKWMRCSSAFSVWDSEPDQMSYVPLYLRPAA 678
Cdd:PLN02283 561 LEADRFFTSNFNEKTYTKKGLEWVNTTESLKDVIDRHYPEMTDKWMNSSSAFSVWDSPPNPHNWIPLYLRPPP 633
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
131-661 |
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: 667.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 131 RTADGKCNHPSDHIIGSQGTFFGRNMPPSS----SPYWLLDPHPTVVANKLLARKKFIdNGKQFNMIACSWIQFMIHDWI 206
Cdd:cd09818 1 RTADGSYNDLDNPSMGSVGTRFGRNVPLDAtfpeDKDELLTPNPRVISRRLLARTEFK-PATSLNLLAAAWIQFMVHDWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 207 DHmedtqqveirapdeiadgcplksfkfyktkkvhtGSPDFRtgcvNTRTPWWDGSVIYGNNEDGMRRVRTF-RDGKLKI 285
Cdd:cd09818 80 SH----------------------------------GPPTYI----NTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLKL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 286 AEDGLLEHDEK-GIPISGDVRNCWAGFSLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDWTVE 364
Cdd:cd09818 122 DADGLLPVDEHtGLPLTGFNDNWWVGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 365 LLKTNTLLAGMRINWYGFFGKKVKDLFGHFAG-PLFSGLVGLrKPRDHGVPYSLTEEFTSVYRMHSLLPDQLIIRDIRST 443
Cdd:cd09818 202 ILAHPTLEIAMRANWWGLLGERLKRVLGRDGTsELLSGIPGS-PPNHHGVPYSLTEEFVAVYRMHPLIPDDIDFRSADDG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 444 tsesgcpPVLEEVPMKEMAGKEGEKKMSEIGMELMLVSMGHQACGAVTLWNYPSWMRNLVahdingedRPDP--VDMAAI 521
Cdd:cd09818 281 -------ATGEEISLTDLAGGKARELLRKLGFADLLYSFGITHPGALTLHNYPRFLRDLH--------RPDGrvIDLAAI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 522 EIYRDRERGVARYNEFRRNLLMIPIRKWEDLTDEQEVVEALHEVYGDDVEKLDLLIGLHAEKKMKGFAISETAFFIFLLI 601
Cdd:cd09818 346 DILRDRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGGDVEKVDLLVGLLAEPLPPGFGFSDTAFRIFILM 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2241025354 602 ASRRLEADRFFTTNFNSKSYTEKGLEWVNKTeTLKDVIDRNFPGMtKKWMR-CSSAFSVWD 661
Cdd:cd09818 426 ASRRLKSDRFFTNDFRPEVYTPEGMDWVNNN-TMKSVLLRHFPEL-APALRgVENAFAPWR 484
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
131-648 |
8.27e-135 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 406.56 E-value: 8.27e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 131 RTADGKCNHPSDHIIGSQGTFFGRNMPPS-----SSPYWLLD----PHPTVVANKLLARKKFIDNgKQFNMIACSWIQFM 201
Cdd:pfam03098 2 RTIDGSCNNLKNPSWGAAGTPFARLLPPAyedgvSAPRGSSSgsplPSPRLVSNKLFAGDSGIPD-PNLTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 202 IHDWIDHMEDTQQVE------------------IRAP--DEIADGCPLKSFKFYKTKKV-HTGSPdfrTGCVNTRTPWWD 260
Cdd:pfam03098 81 DHDLTLTPESTSPNGsscdcccppenlhppcfpIPIPpdDPFFSPFGVRCMPFVRSAPGcGLGNP---REQINQVTSFLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 261 GSVIYGNNEDGMRRVRTFRDGKLKIAED----GLLEHDEKGIP-----------ISGDVR-NCWAGFSLLQALFVKEHNA 324
Cdd:pfam03098 158 GSQVYGSSEETARSLRSFSGGLLKVNRSddgkELLPFDPDGPCccnssggvpcfLAGDSRaNENPGLTALHTLFLREHNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 325 VCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDWTVELLKTntllagMRINWYGFFGKKVKDLfghfagplfsglvg 404
Cdd:pfam03098 238 IADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGE------DNMNWFGLLPLPYNGY-------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 405 lrkprDHGVPYSLTEEFTS-VYRM-HSLLPDQLIIRDIRSTTSESgcppvleEVPMKEMAGKEGEkkMSEIGMELMLVSM 482
Cdd:pfam03098 298 -----DPNVDPSISNEFATaAFRFgHSLIPPFLYRLDENNVPEEP-------SLRLHDSFFNPDR--LYEGGIDPLLRGL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 483 GHQACGAVtLWNYPSWMRNLVAHDINGEDRpdpVDMAAIEIYRDRERGVARYNEFRRNLLMIPIRKWEDLTDE--QEVVE 560
Cdd:pfam03098 364 ATQPAQAV-DNNFTEELTNHLFGPPGEFSG---LDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVipNEVIA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 561 ALHEVYGdDVEKLDLLIGLHAEKKMKGfAISETAFFIFLLIASRRLE-ADRFFTTNFNSKSYTEKGLEWVNKTeTLKDVI 639
Cdd:pfam03098 440 KLRELYG-SVDDIDLWVGGLAEKPLPG-GLVGPTFACIIGDQFRRLRdGDRFWYENGNQGSFTPEQLEEIRKT-SLARVI 516
|
....*....
gi 2241025354 640 DRNFPGMTK 648
Cdd:pfam03098 517 CDNTDIIET 525
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
252-642 |
2.96e-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: 270.07 E-value: 2.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 252 VNTRTPWWDGSVIYGNNEDGMRRVRTFRDGKLKIAEDGLLEHDEKGIPIS-------------------GDVR-NCWAGF 311
Cdd:cd05396 2 LNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYGTELLPFNnpnpsmgtiglpptrcfiaGDPRvNENLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 312 SLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDWTVELLKTNTLLAGMRINWYGFFGKkvkdlf 391
Cdd:cd05396 82 LAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDV------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 392 ghfagplfsglvglrkprdhgVPYSLTEEFTSVYRM-HSLLPDQLIIRDIRsttsesGCPPVLEEVPMKEMAGKEGEKKM 470
Cdd:cd05396 156 ---------------------VPYVLSEFFTAAYRFgHSLVPEGVDRIDEN------GQPKEIPDVPLKDFFFNTSRSIL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 471 SEIGMELMLVSMGHQACGAVTLWNYPSwmrnlvaHDINGEDRPDPVDMAAIEIYRDRERGVARYNEFRRNLLMIPIRKWE 550
Cdd:cd05396 209 SDTGLDPLLRGFLRQPAGLIDQNVDDV-------MFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 551 DLTDEQEVVEALHEVYGdDVEKLDLLIGLHAEKKMKGFAISETAFFIFLLIASRRLEADRFFTTNFNskSYTEKGLEWVN 630
Cdd:cd05396 282 DILTDPELAKKLAELYG-DPDDVDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYN--PFGKSGKEELE 358
|
410
....*....|..
gi 2241025354 631 KTETLKDVIDRN 642
Cdd:cd05396 359 KLISLADIICLN 370
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
150-646 |
6.07e-38 |
|
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: 147.80 E-value: 6.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 150 TFFGRNMPPSSSPYWLLDPHPTVVANKLLARKKFIDNGKQFNMIACSWIQfmihdWIDHMedtqqveirapdeiadgcpl 229
Cdd:cd09816 59 TYYGRHLPPVPRDCPTELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQ-----WFTDQ-------------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 230 ksfkFYKTkkvHTGSPDFRTGCVNTrtpwwDGSVIYGNNEDGMRRVRTFRDGKLK------------IAEDGLLEHD-EK 296
Cdd:cd09816 114 ----FLRT---DPGDPRRNTSNHGI-----DLSQIYGLTEARTHALRLFKDGKLKsqmingeeyppyLFEDGGVKMEfPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 297 GIPISGDV------RNCWA----------GFSLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTsaviakihtid 360
Cdd:cd09816 182 LVPPLGDEltpereAKLFAvgherfnltpGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNIL----------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 361 wTVELLKTntllagmrinwygffgkKVKDLFGHFAGPLFSGLVglrKPRD-HGVPYS----LTEEFTSVYRMHSLLPDQL 435
Cdd:cd09816 251 -IGELIKI-----------------VIEDYINHLSPYHFKLFF---DPELaFNEPWQrqnrIALEFNLLYRWHPLVPDTF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 436 IIRDirsttsesgcppvlEEVPMKEMAgkEGEKKMSEIGMELMLVSMGHQACGAVTLWNYPSWMRnlvahdingedrpdP 515
Cdd:cd09816 310 NIGG--------------QRYPLSDFL--FNNDLVVDHGLGALVDAASRQPAGRIGLRNTPPFLL--------------P 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 516 VDMAAIEIyrDRERGVARYNEFRRNLLMIPIRKWEDLTDEQEVVEALHEVYGdDVEKLDLLIGLHAEKKMKGFAISETaf 595
Cdd:cd09816 360 VEVRSIEQ--GRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELYG-DVDAVEFYVGLFAEDPRPNSPLPPL-- 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2241025354 596 fIFLLIASrrlEADRFFTTN-------FNSKSYTEKGLEWVNKTETLKDVIDRNFPGM 646
Cdd:cd09816 435 -MVEMVAP---DAFSGALTNpllspevWKPSTFGGEGGFDIVKTATLQDLVCRNVKGG 488
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
252-642 |
1.22e-36 |
|
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: 142.45 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 252 VNTRTPWWDGSVIYGNNEDGMRRVRTFRDGKLKI---AEDGLLEHDEKGIP------------ISGDVR-NCWAGFSLLQ 315
Cdd:cd09822 51 INAITAYIDGSNVYGSDEERADALRSFGGGKLKTsvaNAGDLLPFNEAGLPndnggvpaddlfLAGDVRaNENPGLTALH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 316 ALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIhTIDwtvELLKTntllagmrinwygffgkkvkdLFGHFA 395
Cdd:cd09822 131 TLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAI-TYN---EFLPA---------------------LLGENA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 396 GPLFSGLvglrkprDHGVPYSLTEEF-TSVYRM-HSLLPDQLIIRDIRSTTSEsgcPPVLEEVPMKEMAGKEGekkmsei 473
Cdd:cd09822 186 LPAYSGY-------DETVNPGISNEFsTAAYRFgHSMLSSELLRGDEDGTEAT---SLALRDAFFNPDELEEN------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 474 GMELMLVSMGHQACGAVTLWnYPSWMRNLVahdingEDRPDP--VDMAAIEIYRDRERGVARYNEFRRNLLMIPIRKWED 551
Cdd:cd09822 249 GIDPLLRGLASQVAQEIDTF-IVDDVRNFL------FGPPGAggFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 552 LTDEQEVVEALHEVYGdDVEKLDLLIGLHAEKKMKGFAISETAFFIFLLIASRRLEADRFFTTNFNSksyTEKGLEWVNK 631
Cdd:cd09822 322 ITSDPDLAARLASVYG-DVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDDL---LLDEIADIEN 397
|
410
....*....|.
gi 2241025354 632 TeTLKDVIDRN 642
Cdd:cd09822 398 T-TLADVIRRN 407
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
252-642 |
2.11e-28 |
|
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: 117.68 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 252 VNTRTPWWDGSVIYGNNEDGMRRVRTFRDGKLK---------------IAEDGLLEHDEKGIPISGDVRNCW-AGFSLLQ 315
Cdd:cd09823 4 LNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKtqrrngrellpfsnnPTDDCSLSSAGKPCFLAGDGRVNEqPGLTSMH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 316 ALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIhtidwtvellktnTLlagmriNWY--GFFGKKVKDLFgh 393
Cdd:cd09823 84 TLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHI-------------TY------NEFlpILLGRELMEKF-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 394 fagplfsGLVGLRKPRDHG----VPYSLTEEF-TSVYRM-HSLLPDQLIIRDIRSttsesgcpPVLEEVPMKEM---AGK 464
Cdd:cd09823 143 -------GLYLLTSGYFNGydpnVDPSILNEFaAAAFRFgHSLVPGTFERLDENY--------RPQGSVNLHDLffnPDR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 465 EGEKKmseiGMELMLVSMGHQACGAVTlwnyPSWMRNLVAHDINGEDRPDPVDMAAIEIYRDRERGVARYNEFRRNLLMI 544
Cdd:cd09823 208 LYEEG----GLDPLLRGLATQPAQKVD----RFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 545 PIRKWEDLTDE--QEVVEALHEVYGdDVEKLDLLIGLHAEKKMKGFAISETAFFIfllIAS--RRL-EADRFFTTNFNS- 618
Cdd:cd09823 280 RATTFDDLLGImsPETIQKLRRLYK-SVDDIDLYVGGLSEKPVPGGLVGPTFACI---IGEqfRRLrRGDRFWYENGGQp 355
|
410 420
....*....|....*....|....
gi 2241025354 619 KSYTEKGLEWVNKTeTLKDVIDRN 642
Cdd:cd09823 356 SSFTPAQLNEIRKV-SLARIICDN 378
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
221-639 |
1.07e-17 |
|
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: 86.97 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 221 DEIAD----GCPLKSFK---------FYKTKKVHTGSP------DFRTGC--------VNTRTPWWDGSVIYGNNEDGMR 273
Cdd:cd09820 76 SEILDasrpGCPPEYFNieipkgdpvFDPECTGNIELPfqrsryDKNTGYspnnpreqLNEVTSWIDGSSIYGSSKAWSD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 274 RVRTFRDGKLKIAEDGLLEHDEKG--------IPISGDVRNCWAGFSL----------LQA---LFVKEHNAVCDMLREH 332
Cdd:cd09820 156 ALRSFSGGRLASGDDGGFPRRNTNrlplanppPPSYHGTRGPERLFKLgnprgnenpfLLTfgiLWFRYHNYLAQRIARE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 333 YPDSDDDKLYQHARLVTSAVIAKIHTIDWTVELLKTNtllagmRINWYGFfgkkvkdlfghfagplfsglvglrKPrdhG 412
Cdd:cd09820 236 HPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN------VPPYTGY------------------------KP---H 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 413 VPYSLTEEFTS-VYRM-HSLLPDQLIIRD-----IRSTTSESGCPPV--------LEEVPMKemagkegekkmseIGMEL 477
Cdd:cd09820 283 VDPGISHEFQAaAFRFgHTLVPPGVYRRNrqcnfREVLTTSGGSPALrlcntywnSQEPLLK-------------SDIDE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 478 MLVSMGHQACgavtlwnypswMR--NLVAHDIN----GEDRPDPVDMAAIEIYRDRERGVARYNEFRRNLLMIPIRKWED 551
Cdd:cd09820 350 LLLGMASQIA-----------ERedNIIVEDLRdylfGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 552 LTDEQ-----EVVEALHEVYGDDVEKLDLLIGLHAEkkMKGFAISETAFFIFLLIASRRLEADRFFTTNFNSKSYTEKGL 626
Cdd:cd09820 419 INPDLfkkdpELLERLAELYGNDLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKNGLFTAEEI 496
|
490
....*....|...
gi 2241025354 627 EWVNKTeTLKDVI 639
Cdd:cd09820 497 EEIRNT-TLRDVI 508
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
126-622 |
2.24e-16 |
|
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: 82.77 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 126 NEFSHRTADGKCNHPSDHIIGSQGTFFGRNMPPSSSPYWLLdPHPTVVANKLLARKKFIDNGKQFNMIACSWIQFMIHDw 205
Cdd:cd09817 29 DNYKYRKADGSNNNILNPRLGAAGSPYARSVPPKHDQPGVL-PDPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 206 idhmedtqqveirapdeiadgcplkSFKFyktkkvhtgspDFRTGCVNTRTPWWDGSVIYGNNEDGMRRVRTFRDGKLK- 284
Cdd:cd09817 107 -------------------------IFRT-----------DHRDMNINNTSSYLDLSPLYGSNQEEQNKVRTMKDGKLKp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 285 --IAEDGLLehdekGIPisgdvrncwAGFSLLQALFVKEHNAVCDML-------REHYPDSDDDK----------LYQHA 345
Cdd:cd09817 151 dtFSDKRLL-----GQP---------PGVCALLVMFNRFHNYVVEQLaqineggRFTPPGDKLDSsakeekldedLFQTA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 346 RLVTSAVIAKIHTIDWTVELLKTN------TLLAGMRInwygffgkkvkdlfghfagplfsGLVGLRKPRDHGVPYSLte 419
Cdd:cd09817 217 RLITCGLYINIVLHDYVRAILNLNrtdstwTLDPRVEI-----------------------GRSLTGVPRGTGNQVSV-- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 420 EFTSVYRMHSLLPDqliiRDIRSTtsESGCPPVLEEVPMKEMAGKEGekkMSEIG-MELMLVSMGHQacgavtlWNYPSW 498
Cdd:cd09817 272 EFNLLYRWHSAISA----RDEKWT--EDLFESLFGGKSPDEVTLKEF---MQALGrFEALIPKDPSQ-------RTFGGL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 499 MRN---------LVAHDING-ED-------RPDPVDMAAIE---IYRDRERGVARYNEFRRNLLMIPIRKWEDLTDEQEV 558
Cdd:cd09817 336 KRGpdgrfrdedLVRILKDSiEDpagafgaRNVPASLKVIEilgILQAREWNVATLNEFRKFFGLKPYETFEDINSDPEV 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241025354 559 VEALHEVYG--DDVEkldLLIGLHAEKKMK------GFAISETAFFIFLL--IASRRleADRFFTTNFNSKSYT 622
Cdd:cd09817 416 AEALELLYGhpDNVE---LYPGLVAEDAKPpmppgsGLCPGYTISRAILSdaVALVR--GDRFYTVDYNPNNLT 484
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
252-615 |
2.72e-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: 72.34 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 252 VNTRTPWWDGSVIYGNNED------------GMRRVRT-FRDGK--LKIAEDGLLE--HDEKGIPIS----GDVR-NCWA 309
Cdd:cd09826 40 INQLTSYIDASNVYGSSDEealelrdlasdrGLLRVGIvSEAGKplLPFERDSPMDcrRDPNESPIPcflaGDHRaNEQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 310 GFSLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDWTVELL--KTNTLL--------------- 372
Cdd:cd09826 120 GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHITYSHWLPKILgpVGMEMLgeyrgynpnvnpsia 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 373 -----AGMRinwygffgkkvkdlFGHFagplfsglvgLRKPrdhgVPYSLTEEFTSVYRMHSLL------PDQLIirdir 441
Cdd:cd09826 200 nefatAAFR--------------FGHT----------LINP----ILFRLDEDFQPIPEGHLPLhkaffaPYRLV----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 442 sttSESGCPPVLE---EVPMKemagkegeKKMSE--IGMELM--LVSMGHqacgAVTLwnypswmrnlvahdingedrpd 514
Cdd:cd09826 247 ---NEGGIDPLLRglfATAAK--------DRVPDqlLNTELTekLFEMAH----EVAL---------------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 515 pvDMAAIEIYRDRERGVARYNEFRRNLLMIPIRKWEDLTDE---QEVVEALHEVYGdDVEKLDLLIGLHAEKKMKGFAIS 591
Cdd:cd09826 290 --DLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEiknDDVREKLKRLYG-HPGNIDLFVGGILEDLLPGARVG 366
|
410 420
....*....|....*....|....*
gi 2241025354 592 ETaFFIFLLIASRRL-EADRFFTTN 615
Cdd:cd09826 367 PT-LACLLAEQFRRLrDGDRFWYEN 390
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
252-370 |
8.57e-05 |
|
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: 45.49 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 252 VNTRTPWWDGSVIYGNNEDGMRRVR--TFRDGKLKI---AEDGLLE-------HDE--------KGIP--ISGDVR-NCW 308
Cdd:cd09824 15 INALTSFVDASMVYGSEPSLAK*LRnlTNQLGLLAVnqrFTDNGLAllpfenlHNDpcalrntsANIPcfLAGDTRvSEN 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241025354 309 AGFSLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDWTVELLKTNT 370
Cdd:cd09824 95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA 156
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
252-361 |
4.18e-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: 43.58 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241025354 252 VNTRTPWWDGSVIYGNNEDGMRRVRTF--RDGKLKIAE-------DGLLEHDEK-----GIPISGDVRNCW-AG------ 310
Cdd:cd09825 151 INGLTSFIDASTVYGSTLALARSLRDLssDDGLLRVNSkfddsgrDYLPFQPEEvsscnPDPNGGERVPCFlAGdgrase 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2241025354 311 ---FSLLQALFVKEHNAVCDMLREHYPDSDDDKLYQHARLVTSAVIAKIHTIDW 361
Cdd:cd09825 231 vltLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDY 284
|
|
| |
