|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
323-837 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 628.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 323 FRTLDGTCNNMKgEPLRGASYRPYTRLLPTIYDNEVSEPVGSLFTDARPSPREITRRLTSSQASVESPDYNALIMQFGQF 402
Cdd:pfam03098 1 YRTIDGSCNNLK-NPSWGAAGTPFARLLPPAYEDGVSAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPNLTLLLMQWGQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 403 ISHDMAKTTLVPSSK------CNVCQNITSRCMSVPITFDDSNANFRQAQCIRVSRSSPICGSGNlkPRQQLNENTGYID 476
Cdd:pfam03098 80 IDHDLTLTPESTSPNgsscdcCCPPENLHPPCFPIPIPPDDPFFSPFGVRCMPFVRSAPGCGLGN--PREQINQVTSFLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 477 ASPIYGSSVHDSKKFRDGNSGFLKLPMF-NGKAFLPFDQNK--CRNRGQCSVIFTAGDSRVNLFVGLSAWHTIFTEEHNR 553
Cdd:pfam03098 158 GSQVYGSSEETARSLRSFSGGLLKVNRSdDGKELLPFDPDGpcCCNSSGGVPCFLAGDSRANENPGLTALHTLFLREHNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 554 LVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGASFATVVG----DYRGYDSDVDSTVANEFTSAAFRFG 629
Cdd:pfam03098 238 IADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFGllplPYNGYDPNVDPSISNEFATAAFRFG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 630 HGMIQEFYQRLDNSfRNISFGALPFQKGTLHSDVLVnEGGVDPLIRGMFSQNVKRPQR-VTTTVTENMFGS------TDL 702
Cdd:pfam03098 318 HSLIPPFLYRLDEN-NVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQAVDNnFTEELTNHLFGPpgefsgLDL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 703 STINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREIlNTGTRNKLQEIYGSVDKIDLWVGALLEDPIIRGLVGPTVAC 782
Cdd:pfam03098 396 AALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFAC 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 17533607 783 IIGPQFKRTRDGDRFYYENP--GVFSRRQLVEIRKSSLSRIICDNTNTISTIPREAF 837
Cdd:pfam03098 475 IIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
443-847 |
2.88e-170 |
|
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: 500.30 E-value: 2.88e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 443 RQAQCIRVSRSSPICGSG-------NLKPRQQLNENTGYIDASPIYGSSVHDSKKFRDGNS--GFLK--LPMFNGKAFLP 511
Cdd:cd09826 8 RGHRCIEFVRSSAVCGSGstsllfnSVTPREQINQLTSYIDASNVYGSSDEEALELRDLASdrGLLRvgIVSEAGKPLLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 512 FDQN---KCRNRGQCSVI--FTAGDSRVNLFVGLSAWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIV 586
Cdd:cd09826 88 FERDspmDCRRDPNESPIpcFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 587 YREWLPKVLGASFATVVGDYRGYDSDVDSTVANEFTSAAFRFGHGMIQEFYQRLDNSFRNISFGALPFQKGTLHSDVLVN 666
Cdd:cd09826 168 YSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPEGHLPLHKAFFAPYRLVN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 667 EGGVDPLIRGMFSQNVKRP---QRVTTTVTENMFG-----STDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSR 738
Cdd:cd09826 248 EGGIDPLLRGLFATAAKDRvpdQLLNTELTEKLFEmahevALDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 739 EILNTGTRNKLQEIYGSVDKIDLWVGALLEDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYENPGVFSRRQLVEIRKSSL 818
Cdd:cd09826 328 EIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQLTQIKKTSL 407
|
410 420 430
....*....|....*....|....*....|...
gi 17533607 819 SRIICDNTNTISTIPREAFRV----GHMVPCSQ 847
Cdd:cd09826 408 ARVLCDNGDNITRVQEDVFLVpgnpHGYVSCES 440
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
468-801 |
2.18e-13 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 74.03 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 468 LNENTGYIDASPIYGSSVHDSKKFRDGNSGFLKLpmfNGKAFLPFDQNKcrnrgqcsvIFTAGDSRvNLFVGLSAWHTIF 547
Cdd:PLN02283 207 LNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI---SEDGLLLHDEDG---------IPISGDVR-NSWAGVSLLQALF 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 548 TEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVL-----------------------------GAS 598
Cdd:PLN02283 274 VKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLktdtllagmranwygllgkkfkdtfghigGPI 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 599 FATVVGDYRGYDSDVDSTVANEFTSaAFRFgHGMIQEFYQRLDNSFRNISFGALPFQKGTLHSDVLVNEGGVDPLIRGMF 678
Cdd:PLN02283 354 LSGLVGLKKPNNHGVPYSLTEEFTS-VYRM-HSLLPDHLILRDITAAPGENKSPPLIEEIPMPELIGLKGEKKLSKIGFE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 679 SQNVKR-------------PQRVTTTVTENMFGS-----TDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREi 740
Cdd:PLN02283 432 KLMVSMghqacgalelwnyPSWMRDLVPQDIDGEdrpdhVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTDD- 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17533607 741 lnTGTRNKLQEIYGS-VDKIDLWVGALLEDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYEN 801
Cdd:PLN02283 511 --EEAIEVLREVYGDdVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRRLEADRFFTSN 570
|
|
| ShKT |
smart00254 |
ShK toxin domain; ShK toxin domain |
41-75 |
1.66e-05 |
|
ShK toxin domain; ShK toxin domain
Pssm-ID: 214586 [Multi-domain] Cd Length: 33 Bit Score: 42.37 E-value: 1.66e-05
10 20 30
....*....|....*....|....*....|....*
gi 17533607 41 CCDHHEWCRFWASvGECkTNADWMVDNCQLACNTC 75
Cdd:smart00254 1 CVDRHPDCAAWAK-GFC-TNPFYMKSNCPKTCGFC 33
|
|
| ShK |
pfam01549 |
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ... |
40-75 |
3.94e-04 |
|
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: 38.53 E-value: 3.94e-04
10 20 30
....*....|....*....|....*....|....*...
gi 17533607 40 GCCDHHEWCRFWASVGeCKTNA--DWMVDNCQLACNTC 75
Cdd:pfam01549 1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
|
|
| PLN00052 |
PLN00052 |
prolyl 4-hydroxylase; Provisional |
29-75 |
1.01e-03 |
|
prolyl 4-hydroxylase; Provisional
Pssm-ID: 177683 [Multi-domain] Cd Length: 310 Bit Score: 41.96 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 17533607 29 PVTSRfhcLKNGCCDHHEWCRFWASVGECKTNADWMV------DNCQLACNTC 75
Cdd:PLN00052 259 PVVPK---DTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
323-837 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 628.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 323 FRTLDGTCNNMKgEPLRGASYRPYTRLLPTIYDNEVSEPVGSLFTDARPSPREITRRLTSSQASVESPDYNALIMQFGQF 402
Cdd:pfam03098 1 YRTIDGSCNNLK-NPSWGAAGTPFARLLPPAYEDGVSAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPNLTLLLMQWGQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 403 ISHDMAKTTLVPSSK------CNVCQNITSRCMSVPITFDDSNANFRQAQCIRVSRSSPICGSGNlkPRQQLNENTGYID 476
Cdd:pfam03098 80 IDHDLTLTPESTSPNgsscdcCCPPENLHPPCFPIPIPPDDPFFSPFGVRCMPFVRSAPGCGLGN--PREQINQVTSFLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 477 ASPIYGSSVHDSKKFRDGNSGFLKLPMF-NGKAFLPFDQNK--CRNRGQCSVIFTAGDSRVNLFVGLSAWHTIFTEEHNR 553
Cdd:pfam03098 158 GSQVYGSSEETARSLRSFSGGLLKVNRSdDGKELLPFDPDGpcCCNSSGGVPCFLAGDSRANENPGLTALHTLFLREHNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 554 LVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGASFATVVG----DYRGYDSDVDSTVANEFTSAAFRFG 629
Cdd:pfam03098 238 IADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFGllplPYNGYDPNVDPSISNEFATAAFRFG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 630 HGMIQEFYQRLDNSfRNISFGALPFQKGTLHSDVLVnEGGVDPLIRGMFSQNVKRPQR-VTTTVTENMFGS------TDL 702
Cdd:pfam03098 318 HSLIPPFLYRLDEN-NVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQAVDNnFTEELTNHLFGPpgefsgLDL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 703 STINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREIlNTGTRNKLQEIYGSVDKIDLWVGALLEDPIIRGLVGPTVAC 782
Cdd:pfam03098 396 AALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFAC 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 17533607 783 IIGPQFKRTRDGDRFYYENP--GVFSRRQLVEIRKSSLSRIICDNTNTISTIPREAF 837
Cdd:pfam03098 475 IIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
443-847 |
2.88e-170 |
|
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: 500.30 E-value: 2.88e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 443 RQAQCIRVSRSSPICGSG-------NLKPRQQLNENTGYIDASPIYGSSVHDSKKFRDGNS--GFLK--LPMFNGKAFLP 511
Cdd:cd09826 8 RGHRCIEFVRSSAVCGSGstsllfnSVTPREQINQLTSYIDASNVYGSSDEEALELRDLASdrGLLRvgIVSEAGKPLLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 512 FDQN---KCRNRGQCSVI--FTAGDSRVNLFVGLSAWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIV 586
Cdd:cd09826 88 FERDspmDCRRDPNESPIpcFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 587 YREWLPKVLGASFATVVGDYRGYDSDVDSTVANEFTSAAFRFGHGMIQEFYQRLDNSFRNISFGALPFQKGTLHSDVLVN 666
Cdd:cd09826 168 YSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPEGHLPLHKAFFAPYRLVN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 667 EGGVDPLIRGMFSQNVKRP---QRVTTTVTENMFG-----STDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSR 738
Cdd:cd09826 248 EGGIDPLLRGLFATAAKDRvpdQLLNTELTEKLFEmahevALDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 739 EILNTGTRNKLQEIYGSVDKIDLWVGALLEDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYENPGVFSRRQLVEIRKSSL 818
Cdd:cd09826 328 EIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQLTQIKKTSL 407
|
410 420 430
....*....|....*....|....*....|...
gi 17533607 819 SRIICDNTNTISTIPREAFRV----GHMVPCSQ 847
Cdd:cd09826 408 ARVLCDNGDNITRVQEDVFLVpgnpHGYVSCES 440
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
465-825 |
2.04e-168 |
|
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: 493.25 E-value: 2.04e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 465 RQQLNENTGYIDASPIYGSSVHDSKKFRDGNSGFLKLPMFNGKAFLPFDQNK---CRNRGQCSVIFTAGDSRVNLFVGLS 541
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPtddCSLSSAGKPCFLAGDGRVNEQPGLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 542 AWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGASFATVV-------GDYRGYDSDVD 614
Cdd:cd09823 81 SMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFNGYDPNVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 615 STVANEFTSAAFRFGHGMIQEFYQRLDNSFRniSFGALPFQKGTLHSDVLVNEGGVDPLIRGMFSQNVKRPQR-VTTTVT 693
Cdd:cd09823 161 PSILNEFAAAAFRFGHSLVPGTFERLDENYR--PQGSVNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQKVDRfFTDELT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 694 ------ENMFGSTDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREIlNTGTRNKLQEIYGSVDKIDLWVGALL 767
Cdd:cd09823 239 thfffrGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYKSVDDIDLYVGGLS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533607 768 EDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYENPGV---FSRRQLVEIRKSSLSRIICDN 825
Cdd:cd09823 318 EKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
340-858 |
5.86e-148 |
|
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: 447.65 E-value: 5.86e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 340 GASYRPYTRLLPTIYDNEVSEPVG-------SLFTdaRPSPREITRRL--TSSQASVESPDYNALIMQFGQFISHDM--- 407
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGwnkerlyNGFT--LPSVREVSNKImrTSSTAVTPDDLYSHMLTVWGQYIDHDIdft 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 408 ----AKTTLVPSSKCNV-CQNITSrCMsvPITFDDSNANFRQAQCIRVSRSSPICGSGN----------LKPRQQLNENT 472
Cdd:cd09825 79 pqsvSRTMFIGSTDCKMtCENQNP-CF--PIQLPSEDPRILGRACLPFFRSSAVCGTGDtstlfgnlslANPREQINGLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 473 GYIDASPIYGSSVHDSKKFRD--GNSGFLKL-PMFN--GKAFLPFDQNKC------RNRGQCSVIFTAGDSRVNLFVGLS 541
Cdd:cd09825 156 SFIDASTVYGSTLALARSLRDlsSDDGLLRVnSKFDdsGRDYLPFQPEEVsscnpdPNGGERVPCFLAGDGRASEVLTLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 542 AWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLG-ASFATVVGDYRGYDSDVDSTVANE 620
Cdd:cd09825 236 ASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGpEAFDQYGGYYEGYDPTVNPTVSNV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 621 FTSAAFRFGHGMIQEFYQRLDNSFRN-ISFGALPFQKGTLHSDVLVNEGGVDPLIRGMFSQNVKRP---QRVTTTVTENM 696
Cdd:cd09825 316 FSTAAFRFGHATIHPTVRRLDENFQEhPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVtpdDLMNEELTEKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 697 F-----GSTDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREILNTGTRNKLQEIYGSVDKIDLWVGALLEDPI 771
Cdd:cd09825 396 FvlsnsSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 772 IRGLVGPTVACIIGPQFKRTRDGDRFYYENPGVFSRRQLVEIRKSSLSRIICDNTNtISTIPREAFRVG----HMVPCSQ 847
Cdd:cd09825 476 PGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTG-LTRVPPDAFQLGkfpeDFVSCDS 554
|
570
....*....|.
gi 17533607 848 IPSMDLNQWRD 858
Cdd:cd09825 555 IPGINLEAWRE 565
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
453-850 |
1.50e-125 |
|
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: 384.08 E-value: 1.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 453 SSPICGSGNlKPRQQLNENTGYIDASPIYGSSVHDSKKFRDGNS--GFLKL-PMF--NGKAFLPFDQ---NKC--RNRGQ 522
Cdd:cd09824 1 SCGACTSKR-NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNqlGLLAVnQRFtdNGLALLPFENlhnDPCalRNTSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 523 CSVIFTAGDSRVNLFVGLSAWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGASFATV 602
Cdd:cd09824 80 NIPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 603 VGDYRGYDSDVDSTVANEFTSAaFRFGHGMIQEFYQRLDNSFRNI-SFGALPFQKGTLHSDVLVNEGGVDPLIRGMFSQN 681
Cdd:cd09824 160 LPPYRGYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHpPNPQVPLHKAFFASWRIIREGGIDPILRGLMATP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 682 VK--RPQR-VTTTVTENMFGST-----DLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREILNTGTRNKLQEIY 753
Cdd:cd09824 239 AKlnNQNQmLVDELRERLFQQTkrmglDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 754 GSVDKIDLWVGALLEDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYENPGVFSRRQLVEIRKSSLSRIICDNTNtISTIP 833
Cdd:cd09824 319 GTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTG-ITKVP 397
|
410
....*....|....*..
gi 17533607 834 REAFRvghmvPCSQIPS 850
Cdd:cd09824 398 RDPFQ-----PNSYPRD 409
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
370-839 |
1.20e-116 |
|
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: 361.24 E-value: 1.20e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 370 RPSPREITRRLTSSQASVESPDY-NALIMQFGQFISHDMAkttLVPSSkcnvcqnitsrcmsvpitfddsnanfrqaqci 448
Cdd:cd09822 2 RPSPREISNAVADQTESIPNSRGlSDWFWVWGQFLDHDID---LTPDN-------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 449 rvsrsspicgsgnlkPRQQLNENTGYIDASPIYGSSVHDSKKFRDGNSGFLKLPMFNGKAFLPFDQNKCRNRGQCSVI-- 526
Cdd:cd09822 47 ---------------PREQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAGDLLPFNEAGLPNDNGGVPAdd 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 527 -FTAGDSRVNLFVGLSAWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGasfATVVGD 605
Cdd:cd09822 112 lFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLG---ENALPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 606 YRGYDSDVDSTVANEFTSAAFRFGHGMIQEFYQRLDNSFRNIsfGALPFQKGTLHSDvLVNEGGVDPLIRGMFSQnvkRP 685
Cdd:cd09822 189 YSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEA--TSLALRDAFFNPD-ELEENGIDPLLRGLASQ---VA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 686 QRVTTTVTENM----FGST-----DLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHL-SREILntgtRNKLQEIYGS 755
Cdd:cd09822 263 QEIDTFIVDDVrnflFGPPgaggfDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDItSDPDL----AARLASVYGD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 756 VDKIDLWVGALLEDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYENPgVFSRRQLVEIRKSSLSRIICDNTNtISTIPRE 835
Cdd:cd09822 339 VDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-DLLLDEIADIENTTLADVIRRNTD-VDDIQDN 416
|
....
gi 17533607 836 AFRV 839
Cdd:cd09822 417 VFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
467-825 |
8.60e-95 |
|
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: 302.04 E-value: 8.60e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 467 QLNENTGYIDASPIYGSSVHDSKKFRDGNSGFLK----LPMFNGKAFLPFD--QNKCRNRGQCSVI-FTAGDSRVNLFVG 539
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKtnevKGPSYGTELLPFNnpNPSMGTIGLPPTRcFIAGDPRVNENLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 540 LSAWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGASFATVVGD-YRGYDSDVDSTVA 618
Cdd:cd05396 81 LLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLvLLFPDPDVVPYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 619 NEFTSAAFRFGHGMIQEFYQRLDNSFRNISFGALPFQKGTLHSDVLVN-EGGVDPLIRGMFSQnvkRPQRVTTTVTENMF 697
Cdd:cd05396 161 SEFFTAAYRFGHSLVPEGVDRIDENGQPKEIPDVPLKDFFFNTSRSILsDTGLDPLLRGFLRQ---PAGLIDQNVDDVMF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 698 GST-------DLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSR--EILntgtrNKLQEIYGSVDKIDLWVGALLE 768
Cdd:cd05396 238 LFGplegvglDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTdpELA-----KKLAELYGDPDDVDLWVGGLLE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17533607 769 DPIIRGLVGPTVACIIGPQFKRTRDGDRFYYENPGVFSRRQLVEIRKS-SLSRIICDN 825
Cdd:cd05396 313 KKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKLiSLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
327-848 |
1.89e-75 |
|
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: 256.46 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 327 DGTCNNMkGEPLRGASYRPYTRLLPTIYDNEVSEPVGSlftdARPSPREITRRLTSSQASVESPD-YNALIMQFGQFISH 405
Cdd:cd09820 2 DGWYNNL-AHPEWGAADSRLTRRLPAHYSDGVYAPSGE----ERPNPRSLSNLLMKGESGLPSTRnRTALLVFFGQHVVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 406 DMakttlVPSSKcNVCQ----NI-TSRCMSVpitFDDSNANFRQAQCIRvSRSSPICGSGNLKPRQQLNENTGYIDASPI 480
Cdd:cd09820 77 EI-----LDASR-PGCPpeyfNIeIPKGDPV---FDPECTGNIELPFQR-SRYDKNTGYSPNNPREQLNEVTSWIDGSSI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 481 YGSSVHDSKKFR---------DGNSGFL-----KLPMFNgkaflPFDQNKCRNRGqCSVIFTAGDSRVNLFVGLSAWHTI 546
Cdd:cd09820 147 YGSSKAWSDALRsfsggrlasGDDGGFPrrntnRLPLAN-----PPPPSYHGTRG-PERLFKLGNPRGNENPFLLTFGIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 547 FTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGasfaTVVGDYRGYDSDVDSTVANEFTSAAF 626
Cdd:cd09820 221 WFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLG----TNVPPYTGYKPHVDPGISHEFQAAAF 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 627 RFGHGMIQE-FYQR-LDNSFRNISFGALPFQKGTL-----HSDVLVNEGGVDPLIRGMFSQNVKRP-QRVTTTVTENMFG 698
Cdd:cd09820 297 RFGHTLVPPgVYRRnRQCNFREVLTTSGGSPALRLcntywNSQEPLLKSDIDELLLGMASQIAEREdNIIVEDLRDYLFG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 699 S-----TDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREILNTGTR--NKLQEIYG-SVDKIDLWVGALLEDP 770
Cdd:cd09820 377 PlefsrRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLFKKDPEllERLAELYGnDLSKLDLYVGGMLESK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 771 iiRGLVGPTVACIIGPQFKRTRDGDRFYYENP--GVFSRRQLVEIRKSSLSRIICDNTNTI-STIPREAFRVGHMVPCSQ 847
Cdd:cd09820 457 --GGGPGELFRAIILDQFQRLRDGDRFWFENVknGLFTAEEIEEIRNTTLRDVILAVTDIDnTDLQKNVFFWKNGDPCPQ 534
|
.
gi 17533607 848 I 848
Cdd:cd09820 535 P 535
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
388-839 |
6.31e-38 |
|
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: 150.26 E-value: 6.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 388 ESPDYNALIMQFGQFISHDmakTTLVPSSKCNVcqnitsrcMSVPITFDD------SNANFRQAQCIRVSRSSPICGSGN 461
Cdd:cd09821 9 LSAPYNSWMTFFGQFFDHG---LDFIPKGGNGT--------VLIPLPPDDplydlgRGTNGMALDRGTNNAGPDGILGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 462 LKPRQQLNENTGYIDASPIYGSsvHDSKKF----RDGNSGFL-------KLPM-FNGKAFL------------------- 510
Cdd:cd09821 78 DGEGEHTNVTTPFVDQNQTYGS--HASHQVflreYDGDGVATgrllegaTGGSaRTGHAFLddiahnaapkgglgslrdn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 511 --PFDQNKCRNR----GQCSVIFTAGDSRVNLFVGLSAWHTIFTEEHNRLVTAFKRL----------------NPHWDGE 568
Cdd:cd09821 156 ptEDPPGPGAPGsydnELLDAHFVAGDGRVNENIGLTAVHTVFHREHNRLVDQIKDTllqsadlafaneaggnNLAWDGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 569 RLYQEARKMIGAQVQAIVYREWLPKVLG--ASFatvvGDYRGYDSDVDSTVANEFTSAAFRFGHGMIQEFYQRLDNSFRN 646
Cdd:cd09821 236 RLFQAARFANEMQYQHLVFEEFARRIQPgiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRIGPDADE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 647 ISFGALPFQKGTLH-----SDVLVNEGGVDPLIRGMFSQnvkRPQRVTTTVTE----NMFG-STDLSTINIQRGRDHGHP 716
Cdd:cd09821 312 GLDNQVGLIDAFLNpvaflPATLYAEEGAGAILRGMTRQ---VGNEIDEFVTDalrnNLVGlPLDLAALNIARGRDTGLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 717 AYVKYRE------------------------LCGMGTAFNF-----EHLS----REILNTGTRNKLQEIYGS-------- 755
Cdd:cd09821 389 TLNEARAqlfaatgdtilkapyeswndfgarLKNPESLINFiaaygTHLTitgaTTLAAKRAAAQDLVDGGDgapadrad 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 756 --------------VDKIDLWVGALLEDPII-RGLVGPTVACIIGPQFKRTRDGDRFYYenpgvFSRRQ----LVEIRKS 816
Cdd:cd09821 469 fmnaagagagtvkgLDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYY-----LSRTAgldlLNQLENN 543
|
570 580
....*....|....*....|...
gi 17533607 817 SLSRIICDNTNtISTIPREAFRV 839
Cdd:cd09821 544 TFADMIMRNTG-ATHLPQDIFSV 565
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
324-771 |
2.85e-27 |
|
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: 116.62 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 324 RTLDGTCNNMKgEPLRGASYRPYTRLLPtiYDNEVSEPVGSLFTdarPSPREITRRLTSSQASVESPDYNALIMQFGQFI 403
Cdd:cd09818 1 RTADGSYNDLD-NPSMGSVGTRFGRNVP--LDATFPEDKDELLT---PNPRVISRRLLARTEFKPATSLNLLAAAWIQFM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 404 SHDmakttlvpsskcnvcqnitsRCMSVPITFddsnanfrqaqcirvsrsspicgsgnlkprqqLNENTGYIDASPIYGS 483
Cdd:cd09818 75 VHD--------------------WFSHGPPTY--------------------------------INTNTHWWDGSQIYGS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 484 SVHDSKKFRDGNS-GFLKLpmfNGKAFLPFDQNKCrnrgqcsvIFTAGDSRvNLFVGLSAWHTIFTEEHNRLVTAFKRLN 562
Cdd:cd09818 103 TEEAQKRLRTFPPdGKLKL---DADGLLPVDEHTG--------LPLTGFND-NWWVGLSLLHTLFVREHNAICDALRKEY 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 563 PHWDGERLYQEARKMIGAQVQAIVYREWLPKVL-----------------GASFATVVGdyRGYDSDVDS----TVAN-- 619
Cdd:cd09818 171 PDWSDEQLFDKARLVNAALMAKIHTVEWTPAILahptleiamranwwgllGERLKRVLG--RDGTSELLSgipgSPPNhh 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 620 --------EFTsAAFRFgHGMIQEFYQrldnsFRNISFGA----LPFQK--GTLHSDVLVNEGGVDPLIRGM-------- 677
Cdd:cd09818 249 gvpyslteEFV-AVYRM-HPLIPDDID-----FRSADDGAtgeeISLTDlaGGKARELLRKLGFADLLYSFGithpgalt 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 678 ------FSQNVKRPQRvtttvtenmfGSTDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSReilNTGTRNKLQE 751
Cdd:cd09818 322 lhnyprFLRDLHRPDG----------RVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLTG---DEEVAAELRE 388
|
490 500
....*....|....*....|.
gi 17533607 752 IYG-SVDKIDLWVGALLEDPI 771
Cdd:cd09818 389 VYGgDVEKVDLLVGLLAEPLP 409
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
469-826 |
5.50e-27 |
|
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: 115.82 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 469 NENTGYIDASPIYGSSVHDSKKFRDGNSGFLKLPMFNGKAFLPF----------------DQNKCRNRGQCSVIFTAGDS 532
Cdd:cd09816 125 NTSNHGIDLSQIYGLTEARTHALRLFKDGKLKSQMINGEEYPPYlfedggvkmefpplvpPLGDELTPEREAKLFAVGHE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 533 RVNLFVGLSAWHTIFTEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVLGASFatvvgdYRGYDSD 612
Cdd:cd09816 205 RFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHF------KLFFDPE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 613 V--------DSTVANEFtSAAFRFgHGMIQEFYqrldnsfrNISFGALPFqKGTLHSDVLVNEGGVDPLIRGMFSQnvkR 684
Cdd:cd09816 279 LafnepwqrQNRIALEF-NLLYRW-HPLVPDTF--------NIGGQRYPL-SDFLFNNDLVVDHGLGALVDAASRQ---P 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 685 PQRVTTTVTENMFGSTDLSTinIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREilnTGTRNKLQEIYGSVDKIDLWVG 764
Cdd:cd09816 345 AGRIGLRNTPPFLLPVEVRS--IEQGRKLRLASFNDYRKRFGLPPYTSFEELTGD---PEVAAELEELYGDVDAVEFYVG 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533607 765 ALLEDPIIRGLVGPTVACIIGPqfkrtrdgDRF-----------YYENPGVFSRRQLVEIRK-SSLSRIICDNT 826
Cdd:cd09816 420 LFAEDPRPNSPLPPLMVEMVAP--------DAFsgaltnpllspEVWKPSTFGGEGGFDIVKtATLQDLVCRNV 485
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
468-801 |
2.18e-13 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 74.03 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 468 LNENTGYIDASPIYGSSVHDSKKFRDGNSGFLKLpmfNGKAFLPFDQNKcrnrgqcsvIFTAGDSRvNLFVGLSAWHTIF 547
Cdd:PLN02283 207 LNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI---SEDGLLLHDEDG---------IPISGDVR-NSWAGVSLLQALF 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 548 TEEHNRLVTAFKRLNPHWDGERLYQEARKMIGAQVQAIVYREWLPKVL-----------------------------GAS 598
Cdd:PLN02283 274 VKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLktdtllagmranwygllgkkfkdtfghigGPI 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 599 FATVVGDYRGYDSDVDSTVANEFTSaAFRFgHGMIQEFYQRLDNSFRNISFGALPFQKGTLHSDVLVNEGGVDPLIRGMF 678
Cdd:PLN02283 354 LSGLVGLKKPNNHGVPYSLTEEFTS-VYRM-HSLLPDHLILRDITAAPGENKSPPLIEEIPMPELIGLKGEKKLSKIGFE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 679 SQNVKR-------------PQRVTTTVTENMFGS-----TDLSTINIQRGRDHGHPAYVKYRELCGMGTAFNFEHLSREi 740
Cdd:PLN02283 432 KLMVSMghqacgalelwnyPSWMRDLVPQDIDGEdrpdhVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTDD- 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17533607 741 lnTGTRNKLQEIYGS-VDKIDLWVGALLEDPIIRGLVGPTVACIIGPQFKRTRDGDRFYYEN 801
Cdd:PLN02283 511 --EEAIEVLREVYGDdVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRRLEADRFFTSN 570
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
399-652 |
1.81e-08 |
|
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: 57.74 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 399 FGQFISHDmakttlvpsskcnvcqnitsrcmsvpITFD-DSNANFRQAQcirvsrsspicgsgnlkPRQQLNENTGYIDA 477
Cdd:cd09819 53 LGQFIDHD--------------------------ITLDtTSSLAPRQID-----------------PAELRNFRTPALDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 478 SPIYGSSVHDSK------------KFRDG-NSGFLKLPMFNGKAF-LPfdqnkcRNRGQCSVIftaGDSR--VNLFVglS 541
Cdd:cd09819 90 DSVYGGGPDGSPylydqatpndgaKLRVGrESPGGPGGLPGDGARdLP------RNGQGTALI---GDPRndENLIV--A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533607 542 AWHTIFTEEHNRLVTAfkrLNPH-WDGERLYQEARKMIGAQVQAIVYREWLPKVLGASfatVVGDY-----RGYDSDVDS 615
Cdd:cd09819 159 QLHLAFLRFHNAVVDA---LRAHgTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPD---VVDDVlangrRFYRFFREG 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 17533607 616 TVAN--EFTSAAFRFGHGMIQEFYQrLDNSFRNISFGAL 652
Cdd:cd09819 233 KPFMpvEFSVAAYRFGHSMVRASYD-YNRNFPDASLELL 270
|
|
| ShKT |
smart00254 |
ShK toxin domain; ShK toxin domain |
41-75 |
1.66e-05 |
|
ShK toxin domain; ShK toxin domain
Pssm-ID: 214586 [Multi-domain] Cd Length: 33 Bit Score: 42.37 E-value: 1.66e-05
10 20 30
....*....|....*....|....*....|....*
gi 17533607 41 CCDHHEWCRFWASvGECkTNADWMVDNCQLACNTC 75
Cdd:smart00254 1 CVDRHPDCAAWAK-GFC-TNPFYMKSNCPKTCGFC 33
|
|
| ShK |
pfam01549 |
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ... |
40-75 |
3.94e-04 |
|
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: 38.53 E-value: 3.94e-04
10 20 30
....*....|....*....|....*....|....*...
gi 17533607 40 GCCDHHEWCRFWASVGeCKTNA--DWMVDNCQLACNTC 75
Cdd:pfam01549 1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
|
|
| PLN00052 |
PLN00052 |
prolyl 4-hydroxylase; Provisional |
29-75 |
1.01e-03 |
|
prolyl 4-hydroxylase; Provisional
Pssm-ID: 177683 [Multi-domain] Cd Length: 310 Bit Score: 41.96 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 17533607 29 PVTSRfhcLKNGCCDHHEWCRFWASVGECKTNADWMV------DNCQLACNTC 75
Cdd:PLN00052 259 PVVPK---DTEGCADKSAHCAEWAAAGECEKNPVYMVgaegapGNCRKSCGVC 308
|
|
| |
