|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
191-700 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 644.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 191 YRTLDGTCNNLEKPMQGAAFRRFNRHFPAQYDDGKGEP-ISSLNQSRPSAREANRVMLSSAQSVVHDKFNNMMMQWGQFM 269
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPrGSSSGSPLPSPRLVSNKLFAGDSGIPDPNLTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 270 SHDMSKTTLQPSAN------CKTCDPVPSKCMPIPIGEKDPNLGFKSKQCLKVSRSAPICRV-EPREQLNENTAYIDGSM 342
Cdd:pfam03098 81 DHDLTLTPESTSPNgsscdcCCPPENLHPPCFPIPIPPDDPFFSPFGVRCMPFVRSAPGCGLgNPREQINQVTSFLDGSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 343 IYGSSLKDLHKFRDGRTGFLRVTRF-NNQNVLPF--DQSKCANKDKCTASFTAGDIRANLFIGLSSLHIMFAREHNRIAQ 419
Cdd:pfam03098 161 VYGSSEETARSLRSFSGGLLKVNRSdDGKELLPFdpDGPCCCNSSGGVPCFLAGDSRANENPGLTALHTLFLREHNRIAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 420 KLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLG----VSFDKVIGPYKGYDTNVDATIANEFTTSAFRFGHGM 495
Cdd:pfam03098 241 ELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGednmNWFGLLPLPYNGYDPNVDPSISNEFATAAFRFGHSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 496 IEEFYKRVDlsGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVKRP-HRMTPAITEKMFGS------TDLGSL 568
Cdd:pfam03098 321 IPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLYEGGIDPLLRGLATQPAQAVdNNFTEELTNHLFGPpgefsgLDLAAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 569 NIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMILDRNLRAgLARNYNTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIG 648
Cdd:pfam03098 399 NIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAK-LRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17537877 649 EQFKRARDGDRFYFENP--GIFTRSQMEEIKKSSLSRIICDNADNFELVSQDAF 700
Cdd:pfam03098 478 DQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
328-688 |
3.21e-177 |
|
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: 510.96 E-value: 3.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 328 REQLNENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNVLPFDQSK---CANKDKCTASFTAGDIRANLFIGLS 404
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPtddCSLSSAGKPCFLAGDGRVNEQPGLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 405 SLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSFDKVI-------GPYKGYDTNVD 477
Cdd:cd09823 81 SMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFNGYDPNVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 478 ATIANEFTTSAFRFGHGMIEEFYKRVDLSGNNITHggFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVKRPHRM-TPAIT 556
Cdd:cd09823 161 PSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGS--VNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQKVDRFfTDELT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 557 EKMF------GSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmILDRNLRAGLARNYNTTNDVDFYVGSML 630
Cdd:cd09823 239 THFFfrggnpFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLG-IMSPETIQKLRRLYKSVDDIDLYVGGLS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537877 631 EDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGI---FTRSQMEEIKKSSLSRIICDN 688
Cdd:cd09823 318 EKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
191-685 |
1.63e-14 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 77.11 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 191 YRTLDGTCNNLEKPMQGAAFRRFNRHFPaqyddgkgePISS---LNQSRPSArEANRVMLSSAQSVVHDKFNNMMMQWGQ 267
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGRNMP---------PVDQkdkLLDPHPSV-VATKLLARKKFIDTGKQFNMIAASWIQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 268 FMSHD----MSKTTLQ----PSANCKTCdPVPS----KCMPIPIGEKDPNLGFkskqclkvsrsapicrvepreqLNENT 335
Cdd:PLN02283 155 FMIHDwidhLEDTQQIeltaPKEVASQC-PLKSfkfyKTKEVPTGSPDIKTGS----------------------LNIRT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 336 AYIDGSMIYGSSLKDLHKFRDGRTGFLRVTrfnNQNVLPFDQSKCAnkdkctasfTAGDIRaNLFIGLSSLHIMFAREHN 415
Cdd:PLN02283 212 PWWDGSVIYGSNEKGLRRVRTFKDGKLKIS---EDGLLLHDEDGIP---------ISGDVR-NSWAGVSLLQALFVKEHN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 416 RIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLL-----------------------------GVSFDKVI 466
Cdd:PLN02283 279 AVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLktdtllagmranwygllgkkfkdtfghigGPILSGLV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 467 GPYKGYDTNVDATIANEFtTSAFRFgHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVK 546
Cdd:PLN02283 359 GLKKPNNHGVPYSLTEEF-TSVYRM-HSLLPDHLILRDITAAPGENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVS 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 547 RPHRMTPAIT------------------EKMFGSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmilDRNL 608
Cdd:PLN02283 437 MGHQACGALElwnypswmrdlvpqdidgEDRPDHVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTD---DEEA 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 609 RAGLARNYNttNDV---DFYVGSMLEDPVIGglvgttlsCAIGEQ-F-------KRARDGDRFYFE--NPGIFTRSQMEE 675
Cdd:PLN02283 514 IEVLREVYG--DDVeklDLLVGLMAEKKIKG--------FAISETaFfifllmaSRRLEADRFFTSnfNEKTYTKKGLEW 583
|
570
....*....|.
gi 17537877 676 IKKS-SLSRII 685
Cdd:PLN02283 584 VNTTeSLKDVI 594
|
|
| ShK |
pfam01549 |
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ... |
41-76 |
5.73e-07 |
|
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.
Pssm-ID: 426319 Cd Length: 37 Bit Score: 46.23 E-value: 5.73e-07
10 20 30
....*....|....*....|....*....|....*...
gi 17537877 41 GCCDHHEWCRFWASIGeCNANK--DWMTENCQLACGTC 76
Cdd:pfam01549 1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
|
|
| ShKT |
smart00254 |
ShK toxin domain; ShK toxin domain |
42-76 |
2.06e-06 |
|
ShK toxin domain; ShK toxin domain
Pssm-ID: 214586 [Multi-domain] Cd Length: 33 Bit Score: 44.68 E-value: 2.06e-06
10 20 30
....*....|....*....|....*....|....*
gi 17537877 42 CCDHHEWCRFWAsIGECNaNKDWMTENCQLACGTC 76
Cdd:smart00254 1 CVDRHPDCAAWA-KGFCT-NPFYMKSNCPKTCGFC 33
|
|
| PLN00052 |
PLN00052 |
prolyl 4-hydroxylase; Provisional |
29-76 |
5.24e-04 |
|
prolyl 4-hydroxylase; Provisional
Pssm-ID: 177683 [Multi-domain] Cd Length: 310 Bit Score: 42.73 E-value: 5.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17537877 29 PPITDRfkcLTNGCCDHHEWCRFWASIGECNANKDWMT------ENCQLACGTC 76
Cdd:PLN00052 258 PPVVPK---DTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
191-700 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 644.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 191 YRTLDGTCNNLEKPMQGAAFRRFNRHFPAQYDDGKGEP-ISSLNQSRPSAREANRVMLSSAQSVVHDKFNNMMMQWGQFM 269
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPrGSSSGSPLPSPRLVSNKLFAGDSGIPDPNLTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 270 SHDMSKTTLQPSAN------CKTCDPVPSKCMPIPIGEKDPNLGFKSKQCLKVSRSAPICRV-EPREQLNENTAYIDGSM 342
Cdd:pfam03098 81 DHDLTLTPESTSPNgsscdcCCPPENLHPPCFPIPIPPDDPFFSPFGVRCMPFVRSAPGCGLgNPREQINQVTSFLDGSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 343 IYGSSLKDLHKFRDGRTGFLRVTRF-NNQNVLPF--DQSKCANKDKCTASFTAGDIRANLFIGLSSLHIMFAREHNRIAQ 419
Cdd:pfam03098 161 VYGSSEETARSLRSFSGGLLKVNRSdDGKELLPFdpDGPCCCNSSGGVPCFLAGDSRANENPGLTALHTLFLREHNRIAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 420 KLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLG----VSFDKVIGPYKGYDTNVDATIANEFTTSAFRFGHGM 495
Cdd:pfam03098 241 ELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGednmNWFGLLPLPYNGYDPNVDPSISNEFATAAFRFGHSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 496 IEEFYKRVDlsGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVKRP-HRMTPAITEKMFGS------TDLGSL 568
Cdd:pfam03098 321 IPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLYEGGIDPLLRGLATQPAQAVdNNFTEELTNHLFGPpgefsgLDLAAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 569 NIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMILDRNLRAgLARNYNTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIG 648
Cdd:pfam03098 399 NIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAK-LRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17537877 649 EQFKRARDGDRFYFENP--GIFTRSQMEEIKKSSLSRIICDNADNFELVSQDAF 700
Cdd:pfam03098 478 DQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
328-688 |
3.21e-177 |
|
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: 510.96 E-value: 3.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 328 REQLNENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNVLPFDQSK---CANKDKCTASFTAGDIRANLFIGLS 404
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPtddCSLSSAGKPCFLAGDGRVNEQPGLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 405 SLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSFDKVI-------GPYKGYDTNVD 477
Cdd:cd09823 81 SMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFNGYDPNVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 478 ATIANEFTTSAFRFGHGMIEEFYKRVDLSGNNITHggFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVKRPHRM-TPAIT 556
Cdd:cd09823 161 PSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGS--VNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQKVDRFfTDELT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 557 EKMF------GSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmILDRNLRAGLARNYNTTNDVDFYVGSML 630
Cdd:cd09823 239 THFFfrggnpFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLG-IMSPETIQKLRRLYKSVDDIDLYVGGLS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17537877 631 EDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGI---FTRSQMEEIKKSSLSRIICDN 688
Cdd:cd09823 318 EKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
312-712 |
1.81e-155 |
|
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: 457.92 E-value: 1.81e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 312 QCLKVSRSAPIC----------RVEPREQLNENTAYIDGSMIYGSSLKDLHKFRD--GRTGFLRV--TRFNNQNVLPFD- 376
Cdd:cd09826 11 RCIEFVRSSAVCgsgstsllfnSVTPREQINQLTSYIDASNVYGSSDEEALELRDlaSDRGLLRVgiVSEAGKPLLPFEr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 377 --QSKCANKDK-----CtasFTAGDIRANLFIGLSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVL 449
Cdd:cd09826 91 dsPMDCRRDPNespipC---FLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 450 YKEYLPKLLGVSFDKVIGPYKGYDTNVDATIANEFTTSAFRFGHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSGKILF 529
Cdd:cd09826 168 YSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPEGHLPLHKAFFAPYRLVN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 530 EGGVDPIIRGFMTTAVKRPHR---MTPAITEKMFG-----STDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFAD 601
Cdd:cd09826 248 EGGIDPLLRGLFATAAKDRVPdqlLNTELTEKLFEmahevALDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 602 MILDRNLRAGLARNYNTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGIFTRSQMEEIKKSSL 681
Cdd:cd09826 328 EIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQLTQIKKTSL 407
|
410 420 430
....*....|....*....|....*....|...
gi 17537877 682 SRIICDNADNFELVSQDAFLLPG--SNLTPCSK 712
Cdd:cd09826 408 ARVLCDNGDNITRVQEDVFLVPGnpHGYVSCES 440
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
207-722 |
6.63e-146 |
|
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: 438.02 E-value: 6.63e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 207 GAAFRRFNRHFPAQYDDGKGEPISsLNQSR-------PSAREANRVMLSSAQSVVH--DKFNNMMMQWGQFMSHDM---- 273
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVG-WNKERlyngftlPSVREVSNKIMRTSSTAVTpdDLYSHMLTVWGQYIDHDIdftp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 274 ---SKTTLQPSANCK-TCDPVpSKCMPIPIGEKDPNLgfKSKQCLKVSRSAPIC-------------RVEPREQLNENTA 336
Cdd:cd09825 80 qsvSRTMFIGSTDCKmTCENQ-NPCFPIQLPSEDPRI--LGRACLPFFRSSAVCgtgdtstlfgnlsLANPREQINGLTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 337 YIDGSMIYGSSLKDLHKFRD--GRTGFLRV-TRFN--NQNVLPFDQSKCANKDKCTAS------FTAGDIRANLFIGLSS 405
Cdd:cd09825 157 FIDASTVYGSTLALARSLRDlsSDDGLLRVnSKFDdsGRDYLPFQPEEVSSCNPDPNGgervpcFLAGDGRASEVLTLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 406 LHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLG-VSFDKVIGPYKGYDTNVDATIANEF 484
Cdd:cd09825 237 SHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGpEAFDQYGGYYEGYDPTVNPTVSNVF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 485 TTSAFRFGHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSG-KILFEGGVDPIIRGFmttaVKRPHRM-TPA------IT 556
Cdd:cd09825 317 STAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPwRLVREGGLDPVIRGL----IGGPAKLvTPDdlmneeLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 557 EKMF-----GSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMILDRNLRAGLARNYNTTNDVDFYVGSMLE 631
Cdd:cd09825 393 EKLFvlsnsSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 632 DPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGIFTRSQMEEIKKSSLSRIICDNADnFELVSQDAFLLP--GSNLTP 709
Cdd:cd09825 473 DFLPGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTG-LTRVPPDAFQLGkfPEDFVS 551
|
570
....*....|...
gi 17537877 710 CSKIPKMDLSKWR 722
Cdd:cd09825 552 CDSIPGINLEAWR 564
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
235-701 |
1.84e-119 |
|
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: 364.32 E-value: 1.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 235 SRPSARE-ANRVMlssAQSVvhDKFNN-----MMMQWGQFMSHDMSKTtlqpsancktcdpvpskcmpipigekdPNlgf 308
Cdd:cd09822 1 DRPSPREiSNAVA---DQTE--SIPNSrglsdWFWVWGQFLDHDIDLT---------------------------PD--- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 309 kskqclkvsrsapicrvEPREQLNENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNVLPFDQSKCANKDKCTA 388
Cdd:cd09822 46 -----------------NPREQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAGDLLPFNEAGLPNDNGGVP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 389 S---FTAGDIRANLFIGLSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGvsfDKV 465
Cdd:cd09822 109 AddlFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLG---ENA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 466 IGPYKGYDTNVDATIANEFTTSAFRFGHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSgkiLFEGGVDPIIRGfmtTAV 545
Cdd:cd09822 186 LPAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLALRDAFFNPDE---LEENGIDPLLRG---LAS 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 546 KRPHRMTPAITEKM----FGST-----DLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmilDRNLRAGLARNY 616
Cdd:cd09822 260 QVAQEIDTFIVDDVrnflFGPPgaggfDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDITS---DPDLAARLASVY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 617 NTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGiFTRSQMEEIKKSSLSRIICDNADnFELVS 696
Cdd:cd09822 337 GDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDD-LLLDEIADIENTTLADVIRRNTD-VDDIQ 414
|
....*
gi 17537877 697 QDAFL 701
Cdd:cd09822 415 DNVFL 419
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
317-714 |
2.59e-115 |
|
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: 353.65 E-value: 2.59e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 317 SRSAPICRVEPREQLNENTAYIDGSMIYGSS------LKDLHKFRdgrtGFLRV-TRF--NNQNVLPFDQSK---CA--N 382
Cdd:cd09824 1 SCGACTSKRNVREQINALTSFVDASMVYGSEpslak*LRNLTNQL----GLLAVnQRFtdNGLALLPFENLHndpCAlrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 383 KDKCTASFTAGDIRANLFIGLSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSF 462
Cdd:cd09824 77 TSANIPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 463 DKVIGPYKGYDTNVDATIANEFTTsAFRFGHGMIEEFYKRVDLSGNNI-THGGFFFGDGVFKSGKILFEGGVDPIIRGFM 541
Cdd:cd09824 157 AARLPPYRGYNESVDPRIANVFTT-AFRRGHTTVQPFVFRLDENYQPHpPNPQVPLHKAFFASWRIIREGGIDPILRGLM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 542 TTAVK--RP-HRMTPAITEKMFGST-----DLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMILDRNLRAGLA 613
Cdd:cd09824 236 ATPAKlnNQnQMLVDELRERLFQQTkrmglDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 614 RNYNTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGIFTRSQMEEIKKSSLSRIICDNAdNFE 693
Cdd:cd09824 316 DLYGTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNT-GIT 394
|
410 420
....*....|....*....|.
gi 17537877 694 LVSQDAFLlpgsnltPCSKIP 714
Cdd:cd09824 395 KVPRDPFQ-------PNSYPR 408
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
330-688 |
6.88e-94 |
|
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: 296.26 E-value: 6.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 330 QLNENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNV----LPFD---QSKCANKDKCTASFTAGDIRANLFIG 402
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYgtelLPFNnpnPSMGTIGLPPTRCFIAGDPRVNENLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 403 LSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSFDKVIGPYK-GYDTNVDATIA 481
Cdd:cd05396 81 LLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLlFPDPDVVPYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 482 NEFTTSAFRFGHGMIEEFYKRVDLSGNNITHGGFFFGDG-VFKSGKILFEGGVDPIIRGFMTTAVKrphRMTPAITEKMF 560
Cdd:cd05396 161 SEFFTAAYRFGHSLVPEGVDRIDENGQPKEIPDVPLKDFfFNTSRSILSDTGLDPLLRGFLRQPAG---LIDQNVDDVMF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 561 GST-------DLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmilDRNLRAGLARNYNTTNDVDFYVGSMLEDP 633
Cdd:cd05396 238 LFGplegvglDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDDVDLWVGGLLEKK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17537877 634 VIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGIFTRSQMEEIKKS-SLSRIICDN 688
Cdd:cd05396 315 VPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKLiSLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
195-717 |
1.94e-80 |
|
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: 266.86 E-value: 1.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 195 DGTCNNLEKPMQGAAFRRFNRHFPAQYDDGKGEPissLNQSRPSAREANRVmLSSAQSVVHDKFNN--MMMQWGQFMSHD 272
Cdd:cd09820 2 DGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAP---SGEERPNPRSLSNL-LMKGESGLPSTRNRtaLLVFFGQHVVSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 273 MSkttlqpSANCKTCdpvPSKCMPIPIGEKDPNLGFK--SKQCLKVSRSAPICRV-----EPREQLNENTAYIDGSMIYG 345
Cdd:cd09820 78 IL------DASRPGC---PPEYFNIEIPKGDPVFDPEctGNIELPFQRSRYDKNTgyspnNPREQLNEVTSWIDGSSIYG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 346 SS---LKDLHKFRDGRT---GFLRVTRFNNQNVL---PFDQSKCANKdKCTASFTAGDIRANLFIGLSSLHIMFAREHNR 416
Cdd:cd09820 149 SSkawSDALRSFSGGRLasgDDGGFPRRNTNRLPlanPPPPSYHGTR-GPERLFKLGNPRGNENPFLLTFGILWFRYHNY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 417 IAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSfdkvIGPYKGYDTNVDATIANEFTTSAFRFGHGMI 496
Cdd:cd09820 228 LAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN----VPPYTGYKPHVDPGISHEFQAAAFRFGHTLV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 497 EE-FYKRvDLSGNNITHGGFFFGDGVF-------KSGKILFEGGVDPIIRGfMTT--AVKRPHRMTPAITEKMFGS---- 562
Cdd:cd09820 304 PPgVYRR-NRQCNFREVLTTSGGSPALrlcntywNSQEPLLKSDIDELLLG-MASqiAEREDNIIVEDLRDYLFGPlefs 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 563 -TDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMI--LDRNLRAGLARNY-NTTNDVDFYVGSMLEDPviGGL 638
Cdd:cd09820 382 rRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLfkKDPELLERLAELYgNDLSKLDLYVGGMLESK--GGG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 639 VGTTLSCAIGEQFKRARDGDRFYFENP--GIFTRSQMEEIKKSSLSRII--CDNADNFELVSQDAFLLPGS--------- 705
Cdd:cd09820 460 PGELFRAIILDQFQRLRDGDRFWFENVknGLFTAEEIEEIRNTTLRDVIlaVTDIDNTDLQKNVFFWKNGDpcpqpkqlt 539
|
570
....*....|....
gi 17537877 706 --NLTPCSKIPKMD 717
Cdd:cd09820 540 enMLEPCTPLTVYD 553
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
258-707 |
1.96e-36 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188653 [Multi-domain] Cd Length: 570 Bit Score: 144.86 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 258 FNNMMMQWGQFMSHDMSKTTLQPSANcktcdpvpskcMPIPIGEKDP-------NLGFKSKQCLKVSRSAPICRVEP--R 328
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGNGT-----------VLIPLPPDDPlydlgrgTNGMALDRGTNNAGPDGILGTADgeG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 329 EQLNENTAYIDGSMIYGSS------LKD-----------LHKFRDG--RTG--FLRVTRFN----------NQNVLPFDQ 377
Cdd:cd09821 82 EHTNVTTPFVDQNQTYGSHashqvfLREydgdgvatgrlLEGATGGsaRTGhaFLDDIAHNaapkgglgslRDNPTEDPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 378 SKCANKDKCT----ASFTAGDIRANLFIGLSSLHIMFAREHNRIAQKLTEL----------------NPTWSGDRVFQEA 437
Cdd:cd09821 162 GPGAPGSYDNelldAHFVAGDGRVNENIGLTAVHTVFHREHNRLVDQIKDTllqsadlafaneaggnNLAWDGERLFQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 438 RKIVGAQIQNVLYKEYLPKLL-GVSFDkviGPYKGYDTNVDATIANEFTTSAFRFGHGMIEEfykRVDLSGNNITHGGFF 516
Cdd:cd09821 242 RFANEMQYQHLVFEEFARRIQpGIDGF---GSFNGYNPEINPSISAEFAHAVYRFGHSMLTE---TVTRIGPDADEGLDN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 517 FGDGVFKSGKILF--------EGGVDPIIRGfMTTAVKRP--HRMTPAITEKMFG-STDLGSLNIQRGRDHGIPSYNKMR 585
Cdd:cd09821 316 QVGLIDAFLNPVAflpatlyaEEGAGAILRG-MTRQVGNEidEFVTDALRNNLVGlPLDLAALNIARGRDTGLPTLNEAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 586 -QFcglkSANTFD-----------DFA------------------DMIL-------------------DRNLRAGLARNY 616
Cdd:cd09821 395 aQL----FAATGDtilkapyeswnDFGarlknpeslinfiaaygtHLTItgattlaakraaaqdlvdgGDGAPADRADFM 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 617 NTT----------NDVDFYVGSMLEDPVI-GGLVGTTLSCAIGEQFKRARDGDRFYF--ENPGIFTRSQMEEikkSSLSR 683
Cdd:cd09821 471 NAAgagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYlsRTAGLDLLNQLEN---NTFAD 547
|
570 580
....*....|....*....|....
gi 17537877 684 IICDNADNFELvSQDAFLLPGSNL 707
Cdd:cd09821 548 MIMRNTGATHL-PQDIFSVPDYDT 570
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
338-690 |
1.64e-30 |
|
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: 125.84 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 338 IDGSMIYGSSLKDLHKFRDGRTGFLRvTRFNNQNVLP---FDQSKCA---------NKDKCTAS-----FTAGDIRANLF 400
Cdd:cd09816 131 IDLSQIYGLTEARTHALRLFKDGKLK-SQMINGEEYPpylFEDGGVKmefpplvppLGDELTPEreaklFAVGHERFNLT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 401 IGLSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSFDKVIGPYKGYDTNVDAT- 479
Cdd:cd09816 210 PGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQn 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 480 -IANEFTTsAFRFgHGMIEEFY----KRVDLSG---NNithggfffgdgvfksgKILFEGGVDPIIRGFMTTavkRPHRM 551
Cdd:cd09816 290 rIALEFNL-LYRW-HPLVPDTFniggQRYPLSDflfNN----------------DLVVDHGLGALVDAASRQ---PAGRI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 552 TPAITEKMFGSTDLGSlnIQRGRDHGIPSYNKMRQFCGLKSantFDDFADMILDRNLRAGLARNYNTTNDVDFYVGSMLE 631
Cdd:cd09816 349 GLRNTPPFLLPVEVRS--IEQGRKLRLASFNDYRKRFGLPP---YTSFEELTGDPEVAAELEELYGDVDAVEFYVGLFAE 423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537877 632 DPVIGGLVGTTLSCAIG-EQFKRARD---GDRFYFeNPGIFTRSQMEEI-KKSSLSRIICDNAD 690
Cdd:cd09816 424 DPRPNSPLPPLMVEMVApDAFSGALTnplLSPEVW-KPSTFGGEGGFDIvKTATLQDLVCRNVK 486
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
192-686 |
1.06e-28 |
|
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: 120.47 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 192 RTLDGTCNNLEKPMQGAAFRRFNRHFPaqYDDGKGEPISSLnqSRPSAREANRVMLSSAQSVVHDKFNNMMMQWGQFMSH 271
Cdd:cd09818 1 RTADGSYNDLDNPSMGSVGTRFGRNVP--LDATFPEDKDEL--LTPNPRVISRRLLARTEFKPATSLNLLAAAWIQFMVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 272 DMskttlqpsancktcdpvpskCMPIPIGekdpnlgfkskqclkvsrsapicrvepreQLNENTAYIDGSMIYGSSLKDL 351
Cdd:cd09818 77 DW--------------------FSHGPPT-----------------------------YINTNTHWWDGSQIYGSTEEAQ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 352 HKFR-DGRTGFLRVTRfnnQNVLPFDQSKCANKdkctasftAGDIRaNLFIGLSSLHIMFAREHNRIAQKLTELNPTWSG 430
Cdd:cd09818 108 KRLRtFPPDGKLKLDA---DGLLPVDEHTGLPL--------TGFND-NWWVGLSLLHTLFVREHNAICDALRKEYPDWSD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 431 DRVFQEARKIVGAQIQNVLYKEYLPKLLG--------------------------VSFDKVIGPYKGYDTN---VDATIA 481
Cdd:cd09818 176 EQLFDKARLVNAALMAKIHTVEWTPAILAhptleiamranwwgllgerlkrvlgrDGTSELLSGIPGSPPNhhgVPYSLT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 482 NEFtTSAFRFgHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAV------KRPHRMTPAI 555
Cdd:cd09818 256 EEF-VAVYRM-HPLIPDDIDFRSADDGATGEEISLTDLAGGKARELLRKLGFADLLYSFGITHPgaltlhNYPRFLRDLH 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 556 TEKMfGSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmilDRNLRAGLARNY-NTTNDVDFYVGsMLEDPV 634
Cdd:cd09818 334 RPDG-RVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLTG---DEEVAAELREVYgGDVEKVDLLVG-LLAEPL 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17537877 635 IGGLvgttlscAIGE-QFK-------RARDGDRFYFE--NPGIFTRSQMEEIKKSSLSRIIC 686
Cdd:cd09818 409 PPGF-------GFSDtAFRifilmasRRLKSDRFFTNdfRPEVYTPEGMDWVNNNTMKSVLL 463
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
191-685 |
1.63e-14 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 77.11 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 191 YRTLDGTCNNLEKPMQGAAFRRFNRHFPaqyddgkgePISS---LNQSRPSArEANRVMLSSAQSVVHDKFNNMMMQWGQ 267
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGRNMP---------PVDQkdkLLDPHPSV-VATKLLARKKFIDTGKQFNMIAASWIQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 268 FMSHD----MSKTTLQ----PSANCKTCdPVPS----KCMPIPIGEKDPNLGFkskqclkvsrsapicrvepreqLNENT 335
Cdd:PLN02283 155 FMIHDwidhLEDTQQIeltaPKEVASQC-PLKSfkfyKTKEVPTGSPDIKTGS----------------------LNIRT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 336 AYIDGSMIYGSSLKDLHKFRDGRTGFLRVTrfnNQNVLPFDQSKCAnkdkctasfTAGDIRaNLFIGLSSLHIMFAREHN 415
Cdd:PLN02283 212 PWWDGSVIYGSNEKGLRRVRTFKDGKLKIS---EDGLLLHDEDGIP---------ISGDVR-NSWAGVSLLQALFVKEHN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 416 RIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLL-----------------------------GVSFDKVI 466
Cdd:PLN02283 279 AVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLktdtllagmranwygllgkkfkdtfghigGPILSGLV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 467 GPYKGYDTNVDATIANEFtTSAFRFgHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVK 546
Cdd:PLN02283 359 GLKKPNNHGVPYSLTEEF-TSVYRM-HSLLPDHLILRDITAAPGENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVS 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 547 RPHRMTPAIT------------------EKMFGSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADmilDRNL 608
Cdd:PLN02283 437 MGHQACGALElwnypswmrdlvpqdidgEDRPDHVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTD---DEEA 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 609 RAGLARNYNttNDV---DFYVGSMLEDPVIGglvgttlsCAIGEQ-F-------KRARDGDRFYFE--NPGIFTRSQMEE 675
Cdd:PLN02283 514 IEVLREVYG--DDVeklDLLVGLMAEKKIKG--------FAISETaFfifllmaSRRLEADRFFTSnfNEKTYTKKGLEW 583
|
570
....*....|.
gi 17537877 676 IKKS-SLSRII 685
Cdd:PLN02283 584 VNTTeSLKDVI 594
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
393-500 |
1.08e-12 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188651 Cd Length: 465 Bit Score: 70.83 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 393 GDIR--ANLFIglSSLHIMFAREHNRIAQKLTELNPTWsgDRVFQEARKIVGAQIQNVLYKEYLPKLLGVS-FDKVI--- 466
Cdd:cd09819 147 GDPRndENLIV--AQLHLAFLRFHNAVVDALRAHGTPG--DELFEEARRLVRWHYQWLVLNDFLPRICDPDvVDDVLang 222
|
90 100 110
....*....|....*....|....*....|....*
gi 17537877 467 -GPYKGYDTNVdATIANEFTTSAFRFGHGMIEEFY 500
Cdd:cd09819 223 rRFYRFFREGK-PFMPVEFSVAAYRFGHSMVRASY 256
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
332-661 |
7.95e-10 |
|
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: 61.97 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 332 NENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNVLPFDQSKCAnkdkctasftagdiranlfiglssLHIMFA 411
Cdd:cd09817 118 NNTSSYLDLSPLYGSNQEEQNKVRTMKDGKLKPDTFSDKRLLGQPPGVCA------------------------LLVMFN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 412 REHNRIAQKLTELN-----PTWSGDR------------VFQEARKIVGAQIQNVLYKEYLPKLLGV---SFDKVIGPYKG 471
Cdd:cd09817 174 RFHNYVVEQLAQINeggrfTPPGDKLdssakeekldedLFQTARLITCGLYINIVLHDYVRAILNLnrtDSTWTLDPRVE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 472 YDTNVDAT---IANeFTTSAF----RFgHGMI--------EEFYKRVDLSGNNITHGGFFFGDGVFKsgkilFEGGV--D 534
Cdd:cd09817 254 IGRSLTGVprgTGN-QVSVEFnllyRW-HSAIsardekwtEDLFESLFGGKSPDEVTLKEFMQALGR-----FEALIpkD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537877 535 PIIRGF-------------------MTTAVKRP-----HRMTPAItekmFGSTDLgsLNIQRGRDHGIPSYNKMRQFCGL 590
Cdd:cd09817 327 PSQRTFgglkrgpdgrfrdedlvriLKDSIEDPagafgARNVPAS----LKVIEI--LGILQAREWNVATLNEFRKFFGL 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17537877 591 KsanTFDDFADMILDRNLRAGLARNYNTTNDVDFYVGSMLED---PVIGGL---VGTTLSCAIGEQFKRARDGDRFY 661
Cdd:cd09817 401 K---PYETFEDINSDPEVAEALELLYGHPDNVELYPGLVAEDakpPMPPGSglcPGYTISRAILSDAVALVRGDRFY 474
|
|
| ShK |
pfam01549 |
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ... |
41-76 |
5.73e-07 |
|
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.
Pssm-ID: 426319 Cd Length: 37 Bit Score: 46.23 E-value: 5.73e-07
10 20 30
....*....|....*....|....*....|....*...
gi 17537877 41 GCCDHHEWCRFWASIGeCNANK--DWMTENCQLACGTC 76
Cdd:pfam01549 1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
|
|
| ShKT |
smart00254 |
ShK toxin domain; ShK toxin domain |
42-76 |
2.06e-06 |
|
ShK toxin domain; ShK toxin domain
Pssm-ID: 214586 [Multi-domain] Cd Length: 33 Bit Score: 44.68 E-value: 2.06e-06
10 20 30
....*....|....*....|....*....|....*
gi 17537877 42 CCDHHEWCRFWAsIGECNaNKDWMTENCQLACGTC 76
Cdd:smart00254 1 CVDRHPDCAAWA-KGFCT-NPFYMKSNCPKTCGFC 33
|
|
| PLN00052 |
PLN00052 |
prolyl 4-hydroxylase; Provisional |
29-76 |
5.24e-04 |
|
prolyl 4-hydroxylase; Provisional
Pssm-ID: 177683 [Multi-domain] Cd Length: 310 Bit Score: 42.73 E-value: 5.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17537877 29 PPITDRfkcLTNGCCDHHEWCRFWASIGECNANKDWMT------ENCQLACGTC 76
Cdd:PLN00052 258 PPVVPK---DTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
|
|
| |
