|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
847-1393 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 724.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 847 YRTFNGWCNNLKFPEYANSFAPLRHLLPPQYDDGFDAPRtRAKSGRPLPNPRRVSNLVCE-DKDVSHVKFTHMVMQFGQL 925
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPR-GSSSGSPLPSPRLVSNKLFAgDSGIPDPNLTLLLMQWGQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 926 LDHELTHSPVARGPNDEILNCtkCDSPEKISVHCMPIRVEKDDPFFPTNYPngepRCLPFARSLLGQLNLGYRNQLNQLT 1005
Cdd:pfam03098 80 IDHDLTLTPESTSPNGSSCDC--CCPPENLHPPCFPIPIPPDDPFFSPFGV----RCMPFVRSAPGCGLGNPREQINQVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1006 AYVDGSAIYGSTKCEAKNLRLFTRGLLNFTDFGHGQMMLPQGNQEKDCRStlEKRHMPCFVAGDERNSHQPGLTIMHTFF 1085
Cdd:pfam03098 154 SFLDGSQVYGSSEETARSLRSFSGGLLKVNRSDDGKELLPFDPDGPCCCN--SSGGVPCFLAGDSRANENPGLTALHTLF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1086 VREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLLNAQNLVPKkngYFGGYDNTCDASISQP 1165
Cdd:pfam03098 232 LREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFGLLPL---PYNGYDPNVDPSISNE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1166 FATAAFRFGHTLIRRMFPRMNYNYKNMSEPVDLAQHFGHVGPLYEqekGGMDSMLMGLLGTPSMAFDRHITDAVRNHLFm 1245
Cdd:pfam03098 309 FATAAFRFGHSLIPPFLYRLDENNVPEEPSLRLHDSFFNPDRLYE---GGIDPLLRGLATQPAQAVDNNFTEELTNHLF- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1246 RRGEKTSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLKGEMDQDNINILQSLYESVDDVDLFPGLVSERPLR 1325
Cdd:pfam03098 385 GPPGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAKLRELYGSVDDIDLWVGGLAEKPLP 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536077 1326 GALLGTTMSCIIAEQFGRLKKCDRFYYENDNSAAkFTPGQLNEIRKVKLASIFCSNSKYLKTIQPNVF 1393
Cdd:pfam03098 465 GGLVGPTFACIIGDQFRRLRDGDRFWYENGNQGS-FTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
998-1381 |
0e+00 |
|
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: 590.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 998 RNQLNQLTAYVDGSAIYGSTKCEAKNLRLFTRGLLNFTDFgHGQMMLPQGNQEKDCRsTLEKRHMPCFVAGDERNSHQPG 1077
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRR-NGRELLPFSNNPTDDC-SLSSAGKPCFLAGDGRVNEQPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1078 LTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLLNAQNLVPKKNGYFGGYDNT 1157
Cdd:cd09823 79 LTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNGYDPN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1158 CDASISQPFATAAFRFGHTLIRRMFPRMNYNYkNMSEPVDLAQHFGHVGPLYEQekGGMDSMLMGLLGTPSMAFDRHITD 1237
Cdd:cd09823 159 VDPSILNEFAAAAFRFGHSLVPGTFERLDENY-RPQGSVNLHDLFFNPDRLYEE--GGLDPLLRGLATQPAQKVDRFFTD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1238 AVRNHLFmRRGEKTSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLKGEMDQDNINILQSLYESVDDVDLFPG 1317
Cdd:cd09823 236 ELTTHFF-FRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVG 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17536077 1318 LVSERPLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDNSAAKFTPGQLNEIRKVKLASIFCSN 1381
Cdd:cd09823 315 GLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQPSSFTPAQLNEIRKVSLARIICDN 378
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
160-676 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 569.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 160 YRSFSGICNNVARPEWGASHTPMARIVRPDYADGVSEPRAAAASKPLPSVRSLSLTIFTPRGEV-HSDVTTMMGLWMQLI 238
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSSGSPLPSPRLVSNKLFAGDSGIpDPNLTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 239 ASDMVNIVPFQAVNegTSSALPCCKRGFNHSECDAIDIPAADPAYRTRLN-CIPHARSiiapREACRLG-PREQANFASS 316
Cdd:pfam03098 81 DHDLTLTPESTSPN--GSSCDCCCPPENLHPPCFPIPIPPDDPFFSPFGVrCMPFVRS----APGCGLGnPREQINQVTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 317 YLDASFIYGSNMEKAKQLRTFRNGQLRTAGSIGE---LP--ATDGTLQCQATHSRCALSGTDEVNILPSVAALHTVFIRH 391
Cdd:pfam03098 155 FLDGSQVYGSSEETARSLRSFSGGLLKVNRSDDGkelLPfdPDGPCCCNSSGGVPCFLAGDSRANENPGLTALHTLFLRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 392 HNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRENMRNYGLNLHSAgfdSNYEMNLEGTTFNEFAV 471
Cdd:pfam03098 235 HNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFGLLPLPY---NGYDPNVDPSISNEFAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 472 TITYYFWALLPSEKSFVD---------------FNNPSRLYEQGPVQIIRQVLNTNIYQPTLRANDEVKSG-FLKDNHEF 535
Cdd:pfam03098 312 AAFRFGHSLIPPFLYRLDennvpeepslrlhdsFFNPDRLYEGGIDPLLRGLATQPAQAVDNNFTEELTNHlFGPPGEFS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 536 GLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLREIFLPEVkFEQVSSAYTRVEDVDLLVGVLAEKPLKGSLVGP 615
Cdd:pfam03098 392 GLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEV-IAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGP 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17536077 616 TMACIIGKQMQRTRRADRFWYENYFaQSGFNEAQLSEIRNTKLAEIICSNID-IRRIQRNVF 676
Cdd:pfam03098 471 TFACIIGDQFRRLRDGDRFWYENGN-QGSFTPEQLEEIRKTSLARVICDNTDiIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
308-665 |
5.39e-155 |
|
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: 474.76 E-value: 5.39e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 308 REQANFASSYLDASFIYGSNMEKAKQLRTFRNGQLRTAGSIG--ELPATDGTLQCQ---ATHSRCALSGTDEVNILPSVA 382
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGreLLPFSNNPTDDCslsSAGKPCFLAGDGRVNEQPGLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 383 ALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRENMRNYGLNLHSAGFDSNYEMNLE 462
Cdd:cd09823 81 SMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNGYDPNVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 463 GTTFNEFAVTITYYFWALLPSEKSFVD--------------FNNPSRLYEQGpvqIIRQVLNTNIYQPTLRANDEVKSG- 527
Cdd:cd09823 161 PSILNEFAAAAFRFGHSLVPGTFERLDenyrpqgsvnlhdlFFNPDRLYEEG---GLDPLLRGLATQPAQKVDRFFTDEl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 528 ----FLKDNHEFGLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLREIFLPEVkFEQVSSAYTRVEDVDLLVGVL 603
Cdd:cd09823 238 tthfFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIMSPET-IQKLRRLYKSVDDIDLYVGGL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17536077 604 AEKPLKGSLVGPTMACIIGKQMQRTRRADRFWYENYFAQSGFNEAQLSEIRNTKLAEIICSN 665
Cdd:cd09823 317 SEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQPSSFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
981-1408 |
7.21e-130 |
|
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: 409.77 E-value: 7.21e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 981 RCLPFARS-----------LLGQLNlgYRNQLNQLTAYVDGSAIYGSTKCEAKNLRLFT--RGLLNF-TDFGHGQMMLP- 1045
Cdd:cd09826 11 RCIEFVRSsavcgsgstslLFNSVT--PREQINQLTSYIDASNVYGSSDEEALELRDLAsdRGLLRVgIVSEAGKPLLPf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1046 QGNQEKDCRSTLEKRHMPCFVAGDERNSHQPGLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITF 1125
Cdd:cd09826 89 ERDSPMDCRRDPNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHITY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1126 AEFLPKIIGLDLLnaqnlvpKKNGYFGGYDNTCDASISQPFATAAFRFGHTLIRRMFPRMNYNYKNMSEpvdlaqhfGHV 1205
Cdd:cd09826 169 SHWLPKILGPVGM-------EMLGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPE--------GHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1206 gPLYEQ--------EKGGMDSMLMGLLGTPSMA------FDRHITDavrnHLFMRRGEktSGMDLIVLNILRARDHGVQP 1271
Cdd:cd09826 234 -PLHKAffapyrlvNEGGIDPLLRGLFATAAKDrvpdqlLNTELTE----KLFEMAHE--VALDLAALNIQRGRDHGLPG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1272 YNDLREFCGLRRAVKWDDLKGEMDQDNI-NILQSLYESVDDVDLFPGLVSERPLRGALLGTTMSCIIAEQFGRLKKCDRF 1350
Cdd:cd09826 307 YNDYRKFCNLSVAETFEDLKNEIKNDDVrEKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRF 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 17536077 1351 YYENDNSaakFTPGQLNEIRKVKLASIFCSNSKYLKTIQPNVFDVTdELTNAQVPCTD 1408
Cdd:cd09826 387 WYENPGV---FSPAQLTQIKKTSLARVLCDNGDNITRVQEDVFLVP-GNPHGYVSCES 440
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
865-1419 |
1.90e-115 |
|
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: 375.23 E-value: 1.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 865 SFAPLRHLLPPQYDDGFDAPRTRAKS----GRPLPNPRRVSN---LVCEDKDVSHVKFTHMVMQFGQLLDH--ELTHSPV 935
Cdd:cd09825 3 SNTPLARWLPPIYEDGFSEPVGWNKErlynGFTLPSVREVSNkimRTSSTAVTPDDLYSHMLTVWGQYIDHdiDFTPQSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 936 ARGPndeILNCTKCDSPEKISVHCMPIRVEKDDPffptnyPNGEPRCLPFARS-----------LLGQLNLGY-RNQLNQ 1003
Cdd:cd09825 83 SRTM---FIGSTDCKMTCENQNPCFPIQLPSEDP------RILGRACLPFFRSsavcgtgdtstLFGNLSLANpREQING 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1004 LTAYVDGSAIYGSTKCEAKNLRLFTR--GLLN----FTDFGhgQMMLP-QGNQEKDCRSTL-EKRHMPCFVAGDERNSHQ 1075
Cdd:cd09825 154 LTSFIDASTVYGSTLALARSLRDLSSddGLLRvnskFDDSG--RDYLPfQPEEVSSCNPDPnGGERVPCFLAGDGRASEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1076 PGLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLLnaQNLVpkknGYFGGYD 1155
Cdd:cd09825 232 LTLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAF--DQYG----GYYEGYD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1156 NTCDASISQPFATAAFRFGHTLIRRMFPRMNYNYKNMSEPVDLAQHFGHVGPLYEQEKGGMDSMLMGLLGTPS--MAFDR 1233
Cdd:cd09825 306 PTVNPTVSNVFSTAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAklVTPDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1234 HITDAVRNHLFMRrgEKTSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLKGEM-DQDNINILQSLYESVDDV 1312
Cdd:cd09825 386 LMNEELTEKLFVL--SNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIaDQAVADKILDLYKHPDNI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1313 DLFPGLVSERPLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDNSaakFTPGQLNEIRKVKLASIFCSNSKyLKTIQPNV 1392
Cdd:cd09825 464 DVWLGGLAEDFLPGARTGPLFACLIGKQMKALRDGDRFWWENSNV---FTDAQRRELRKHSLSRVICDNTG-LTRVPPDA 539
|
570 580
....*....|....*....|....*..
gi 17536077 1393 FDVTDELTNAqVPCTDIPQVDLSLWRE 1419
Cdd:cd09825 540 FQLGKFPEDF-VSCDSIPGINLEAWRE 565
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
894-1393 |
1.44e-109 |
|
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: 353.92 E-value: 1.44e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 894 LPNPRRVSNLVCEDKDV--SHVKFTHMVMQFGQLLDHELTHSPvargpndeilnctkcDSPekisvhcmpirvekddpff 971
Cdd:cd09822 2 RPSPREISNAVADQTESipNSRGLSDWFWVWGQFLDHDIDLTP---------------DNP------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 972 ptnypngeprclpfarsllgqlnlgyRNQLNQLTAYVDGSAIYGSTKCEAKNLRLFTRGLLNFTDFGHGQMmLPQGNQEK 1051
Cdd:cd09822 48 --------------------------REQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAGDL-LPFNEAGL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1052 DCRSTLEKRHmPCFVAGDERNSHQPGLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPK 1131
Cdd:cd09822 101 PNDNGGVPAD-DLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1132 IIGLDLLNAQNlvpkkngyfgGYDNTCDASISQPFATAAFRFGHTLIRRMFPRMNYNYKNMsEPVDLAQHFGHVGPLyeq 1211
Cdd:cd09822 180 LLGENALPAYS----------GYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEA-TSLALRDAFFNPDEL--- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1212 EKGGMDSMLMGLLGTPSMAFDRHITDAVRNHLFMRRGEktSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLK 1291
Cdd:cd09822 246 EENGIDPLLRGLASQVAQEIDTFIVDDVRNFLFGPPGA--GGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDIT 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1292 GemDQDNINILQSLYESVDDVDLFPGLVSERPLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDNsaakFTPGQLNEIRK 1371
Cdd:cd09822 324 S--DPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDD----LLLDEIADIEN 397
|
490 500
....*....|....*....|..
gi 17536077 1372 VKLASIFCSNSKYlKTIQPNVF 1393
Cdd:cd09822 398 TTLADVIRRNTDV-DDIQDNVF 418
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
1000-1381 |
1.72e-89 |
|
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: 295.88 E-value: 1.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1000 QLNQLTAYVDGSAIYGSTKCEAKNLRLFTRGLLNF-TDFG--HGQMMLPQGNQEKDCRsTLEKRHMPCFVAGDERNSHQP 1076
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTnEVKGpsYGTELLPFNNPNPSMG-TIGLPPTRCFIAGDPRVNENL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1077 GLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGldllnaQNLVPKKNGYFGGYDN 1156
Cdd:cd05396 80 LLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILG------KFTDPRDDLVLLFPDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1157 TCDASISQPFATAAFRFGHTLIRRMFPRMNYNYKNMSEP-VDLAQHFGHVGpLYEQEKGGMDSMLMGLLGTPSMAFDRHI 1235
Cdd:cd05396 154 DVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQPKEIPdVPLKDFFFNTS-RSILSDTGLDPLLRGFLRQPAGLIDQNV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1236 TDavrnHLFMRRGEKTSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLKGEMDQdnINILQSLYESVDDVDLF 1315
Cdd:cd05396 233 DD----VMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTDPEL--AKKLAELYGDPDDVDLW 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17536077 1316 PGLVSERPLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDNSAAKFTPGQLNEIRkvKLASIFCSN 1381
Cdd:cd05396 307 VGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKLI--SLADIICLN 370
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
277-691 |
7.55e-88 |
|
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: 293.83 E-value: 7.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 277 PAADPAYRTRlNCIPHARSiiapREAC----------RLGPREQANFASSYLDASFIYGSNMEKAKQLR--TFRNGQLR- 343
Cdd:cd09826 1 PPDDPRRRGH-RCIEFVRS----SAVCgsgstsllfnSVTPREQINQLTSYIDASNVYGSSDEEALELRdlASDRGLLRv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 344 ---TAGSIGELP-ATDGTLQCQA----THSRCALSGTDEVNILPSVAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEA 415
Cdd:cd09826 76 givSEAGKPLLPfERDSPMDCRRdpneSPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 416 RKIVAAQVQHITYNEFLPVLLGRENMRnyglnlhSAGFDSNYEMNLEGTTFNEFAVTITYYFWAL--------------- 480
Cdd:cd09826 156 RKIVGAQMQHITYSHWLPKILGPVGME-------MLGEYRGYNPNVNPSIANEFATAAFRFGHTLinpilfrldedfqpi 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 481 ----LPSEKSFvdFNnPSRLYEQGPVQ-IIRQVLNTNIYQPTLRA--NDEVKSGFLKDNHEFGLDLISIALKQGRDHGIP 553
Cdd:cd09826 229 peghLPLHKAF--FA-PYRLVNEGGIDpLLRGLFATAAKDRVPDQllNTELTEKLFEMAHEVALDLAALNIQRGRDHGLP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 554 GYTALRASCGLGRIASFNDLR-EIFLPEVKfEQVSSAYTRVEDVDLLVGVLAEKPLKGSLVGPTMACIIGKQMQRTRRAD 632
Cdd:cd09826 306 GYNDYRKFCNLSVAETFEDLKnEIKNDDVR-EKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGD 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 633 RFWYENyfaQSGFNEAQLSEIRNTKLAEIICSNID-IRRIQRNVFFREDvFDNMAISCNS 691
Cdd:cd09826 385 RFWYEN---PGVFSPAQLTQIKKTSLARVLCDNGDnITRVQEDVFLVPG-NPHGYVSCES 440
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
176-704 |
4.82e-87 |
|
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: 295.88 E-value: 4.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 176 GASHTPMARIVRPDYADGVSEPRAAAASK-----PLPSVRSLSLTIFTPRGEVHSDV---TTMMGLWMQLIASDM----- 242
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERlyngfTLPSVREVSNKIMRTSSTAVTPDdlySHMLTVWGQYIDHDIdftpq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 243 -VNIVPFQavneGTSSALPCCKrgfNHSECDAIDIPAADPAYRTRlNCIPHARSI---------IAPREACRLGPREQAN 312
Cdd:cd09825 81 sVSRTMFI----GSTDCKMTCE---NQNPCFPIQLPSEDPRILGR-ACLPFFRSSavcgtgdtsTLFGNLSLANPREQIN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 313 FASSYLDASFIYGSNMEKAKQLRTF--RNGQLRTAG-----SIGELPATD--GTLQCQATH----SRCALSGTDEVNILP 379
Cdd:cd09825 153 GLTSFIDASTVYGSTLALARSLRDLssDDGLLRVNSkfddsGRDYLPFQPeeVSSCNPDPNggerVPCFLAGDGRASEVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 380 SVAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRENMRNYGLNlhSAGFDSNYem 459
Cdd:cd09825 233 TLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGY--YEGYDPTV-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 460 nlEGTTFNEFAvTITYYFW------------------ALLPSEKSFVDFNNPSRLYEQGPVQ-IIRQVLN--TNIYQPTL 518
Cdd:cd09825 309 --NPTVSNVFS-TAAFRFGhatihptvrrldenfqehPVLPNLALHDAFFSPWRLVREGGLDpVIRGLIGgpAKLVTPDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 519 RANDEVKSGFLKDNHEFGLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLREIFLPEVKFEQVSSAYTRVEDVDL 598
Cdd:cd09825 386 LMNEELTEKLFVLSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 599 LVGVLAEKPLKGSLVGPTMACIIGKQMQRTRRADRFWYENyfaQSGFNEAQLSEIRNTKLAEIICSNIDIRRIQRNVFFR 678
Cdd:cd09825 466 WLGGLAEDFLPGARTGPLFACLIGKQMKALRDGDRFWWEN---SNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQL 542
|
570 580
....*....|....*....|....*.
gi 17536077 679 EDVFDNMaISCNStvLNSPDFNEWRD 704
Cdd:cd09825 543 GKFPEDF-VSCDS--IPGINLEAWRE 565
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
998-1386 |
6.80e-83 |
|
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: 278.53 E-value: 6.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 998 RNQLNQLTAYVDGSAIYGSTKCEAKNLRLFT--RGLL----NFTDfgHGQMMLPQGNQEKD-CRSTLEKRHMPCFVAGDE 1070
Cdd:cd09824 12 REQINALTSFVDASMVYGSEPSLAK*LRNLTnqLGLLavnqRFTD--NGLALLPFENLHNDpCALRNTSANIPCFLAGDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1071 RNSHQPGLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDllnAQNLVPKkngy 1150
Cdd:cd09824 90 RVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGED---AAARLPP---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1151 FGGYDNTCDASISQPFATaAFRFGHTLIRRMFPRMNYNYKNMSEPVDLAQHFGHVGPLYEQEKGGMDSMLMGLLGTPS-- 1228
Cdd:cd09824 163 YRGYNESVDPRIANVFTT-AFRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAkl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1229 MAFDRHITDAVRNHLFmrrgEKTSGM--DLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLKGEMDQDNI-NILQSL 1305
Cdd:cd09824 242 NNQNQMLVDELRERLF----QQTKRMglDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLaRKLLDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1306 YESVDDVDLFPGLVSERPLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDNSaakFTPGQLNEIRKVKLASIFCSNSKYL 1385
Cdd:cd09824 318 YGTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGV---FTEEQRESLRSVSLSRIICDNTGIT 394
|
.
gi 17536077 1386 K 1386
Cdd:cd09824 395 K 395
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
306-677 |
1.08e-81 |
|
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: 275.34 E-value: 1.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 306 GPREQANFASSYLDASFIYGSNMEKAKQLRTFRNGQLRTAGSIGE-LPATDGTLQCQATHSRCA----LSGTDEVNILPS 380
Cdd:cd09822 46 NPREQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAGdLLPFNEAGLPNDNGGVPAddlfLAGDVRANENPG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 381 VAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRENMRNYglnlhsAGFDSnyemN 460
Cdd:cd09822 126 LTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLGENALPAY------SGYDE----T 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 461 LEGTTFNEFAvTITYYF-WALLPSEKSFVD--------------FNNPSRLYEQGPVQIIR-------QVLNTNIYqptl 518
Cdd:cd09822 196 VNPGISNEFS-TAAYRFgHSMLSSELLRGDedgteatslalrdaFFNPDELEENGIDPLLRglasqvaQEIDTFIV---- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 519 ranDEVKSgFLkdnheF------GLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDlreIFLPEVKFEQVSSAYTR 592
Cdd:cd09822 271 ---DDVRN-FL-----FgppgagGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSD---ITSDPDLAARLASVYGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 593 VEDVDLLVGVLAEKPLKGSLVGPTMACIIGKQMQRTRRADRFWYENyfaqSGFNEAQLSEIRNTKLAEIICSNIDIRRIQ 672
Cdd:cd09822 339 VDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEN----DDLLLDEIADIENTTLADVIRRNTDVDDIQ 414
|
....*
gi 17536077 673 RNVFF 677
Cdd:cd09822 415 DNVFL 419
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
850-1413 |
1.81e-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: 262.24 E-value: 1.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 850 FNGWCNNLKFPEYANSFAPLRHLLPPQYDDGFDAPrtrakSGRPLPNPRRVSNLVCEDKD--VSHVKFTHMVMQFGQLld 927
Cdd:cd09820 1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAP-----SGEERPNPRSLSNLLMKGESglPSTRNRTALLVFFGQH-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 928 helthspVArgpnDEILNCTK--CdSPEKISvhcmpIRVEKDDPFFPTNYPNgePRCLPFARSLLgQLNLGY-----RNQ 1000
Cdd:cd09820 74 -------VV----SEILDASRpgC-PPEYFN-----IEIPKGDPVFDPECTG--NIELPFQRSRY-DKNTGYspnnpREQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1001 LNQLTAYVDGSAIYGSTKCEAKNLRLFTRGLLNFTDFGHGQMM----LPQGNQEKDC-RSTLEKRHMpcFVAGDERNSHQ 1075
Cdd:cd09820 134 LNEVTSWIDGSSIYGSSKAWSDALRSFSGGRLASGDDGGFPRRntnrLPLANPPPPSyHGTRGPERL--FKLGNPRGNEN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1076 PGLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLLNaqnlvpkkngyFGGYD 1155
Cdd:cd09820 212 PFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTNVPP-----------YTGYK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1156 NTCDASISQPFATAAFRFGHTLI-----RR--------------MFP--RMNYNYKNMSEPVdlaqhfghvgplyeqEKG 1214
Cdd:cd09820 281 PHVDPGISHEFQAAAFRFGHTLVppgvyRRnrqcnfrevlttsgGSPalRLCNTYWNSQEPL---------------LKS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1215 GMDSMLMGLLGTPSMAFDRHITDAVRNHLF--MRRgektSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLKG 1292
Cdd:cd09820 346 DIDELLLGMASQIAEREDNIIVEDLRDYLFgpLEF----SRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1293 EMDQDNINI---LQSLYE-SVDDVDLFPGLVSErpLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDNSAAkFTPGQLNE 1368
Cdd:cd09820 422 DLFKKDPELlerLAELYGnDLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKNGL-FTAEEIEE 498
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17536077 1369 IRKVKLAS-IFCSNSKYLKTIQPNVFDVTDELtnaqvPCTDIPQVD 1413
Cdd:cd09820 499 IRNTTLRDvILAVTDIDNTDLQKNVFFWKNGD-----PCPQPKQLT 539
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
310-665 |
2.35e-66 |
|
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: 229.62 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 310 QANFASSYLDASFIYGSNMEKAKQLRTFRNGQLRTAGSIGE------LP---ATDGTLQCQATHSRCALSGTDEVNILPS 380
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPsygtelLPfnnPNPSMGTIGLPPTRCFIAGDPRVNENLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 381 VAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRENMRNYGLnlhsagFDSNYEMN 460
Cdd:cd05396 81 LLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDL------VLLFPDPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 461 LEGTTFNEFAvTITYYFW-ALLPSEKSFVDFNNPSRLYEQGPVQiiRQVLNTNIYQPTLRANDEVKSGFLKD-------- 531
Cdd:cd05396 155 VVPYVLSEFF-TAAYRFGhSLVPEGVDRIDENGQPKEIPDVPLK--DFFFNTSRSILSDTGLDPLLRGFLRQpaglidqn 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 532 ----------NHEFGLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLreIFLPEVKfEQVSSAYTRVEDVDLLVG 601
Cdd:cd05396 232 vddvmflfgpLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDI--LTDPELA-KKLAELYGDPDDVDLWVG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17536077 602 VLAEKPLKGSLVGPTMACIIGKQMQRTRRADRFWYENY--FAQSGFNEAqlseIRNTKLAEIICSN 665
Cdd:cd05396 309 GLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYnpFGKSGKEEL----EKLISLADIICLN 370
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
308-678 |
2.43e-62 |
|
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: 219.21 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 308 REQANFASSYLDASFIYGSNMEKAKQLRTFRN--GQLR-----TAGSIGELPATDGTLQ-C----QATHSRCALSGTDEV 375
Cdd:cd09824 12 REQINALTSFVDASMVYGSEPSLAK*LRNLTNqlGLLAvnqrfTDNGLALLPFENLHNDpCalrnTSANIPCFLAGDTRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 376 NILPSVAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRENMRNYGLnlhSAGFDS 455
Cdd:cd09824 92 SENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARLPP---YRGYNE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 456 N---YEMNLEGTTFNEFAVTI---------TYYFWALLPSEKSFVDFNNPSRL-YEQGPVQIIRQVLNTN--IYQPTLRA 520
Cdd:cd09824 169 SvdpRIANVFTTAFRRGHTTVqpfvfrldeNYQPHPPNPQVPLHKAFFASWRIiREGGIDPILRGLMATPakLNNQNQML 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 521 NDEVKSGFLKDNHEFGLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLREIFLPEVKFEQVSSAYTRVEDVDLLV 600
Cdd:cd09824 249 VDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDNIDIWI 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536077 601 GVLAEKPLKGSLVGPTMACIIGKQMQRTRRADRFWYENyfaQSGFNEAQLSEIRNTKLAEIICSNIDIRRIQRNVFFR 678
Cdd:cd09824 329 GGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWEN---PGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQP 403
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
163-677 |
6.56e-62 |
|
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: 222.56 E-value: 6.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 163 FSGICNNVARPEWGASHTPMARIVRPDYADGVSEPraaaASKPLPSVRSLSLTIFtpRGEV----HSDVTTMMGLWMQLI 238
Cdd:cd09820 1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAP----SGEERPNPRSLSNLLM--KGESglpsTRNRTALLVFFGQHV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 239 ASDMVnivpfqavnegtSSALPCCKRGFNHsecdaIDIPAADPAYRTRlnC-----IPHARSiiapREACRLG-----PR 308
Cdd:cd09820 75 VSEIL------------DASRPGCPPEYFN-----IEIPKGDPVFDPE--CtgnieLPFQRS----RYDKNTGyspnnPR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 309 EQANFASSYLDASFIYGSNMEKAKQLRTFRNGQLRTAGSIGEL--------------PATDGTLQCQathsRCALSGTDE 374
Cdd:cd09820 132 EQLNEVTSWIDGSSIYGSSKAWSDALRSFSGGRLASGDDGGFPrrntnrlplanpppPSYHGTRGPE----RLFKLGNPR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 375 VNILPSVAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGrENMRNY-GLNLH---- 449
Cdd:cd09820 208 GNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLG-TNVPPYtGYKPHvdpg 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 450 ------SAGFDSNYEMNLEG----TTFNEF-AVTITYYFWALLPSEKSFVDFNNPsrLYEQGPVQII----RQV--LNTN 512
Cdd:cd09820 287 ishefqAAAFRFGHTLVPPGvyrrNRQCNFrEVLTTSGGSPALRLCNTYWNSQEP--LLKSDIDELLlgmaSQIaeREDN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 513 IYQPTLRandevksGFLKDNHEF-GLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDL--REIFLPEVKFEQVSSA 589
Cdd:cd09820 365 IIVEDLR-------DYLFGPLEFsRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDInpDLFKKDPELLERLAEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 590 YTR-VEDVDLLVGVLAEkpLKGSLVGPTMACIIGKQMQRTRRADRFWYENyfAQSG-FNEAQLSEIRNTKLAEII--CSN 665
Cdd:cd09820 438 YGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFEN--VKNGlFTAEEIEEIRNTTLRDVIlaVTD 513
|
570
....*....|..
gi 17536077 666 IDIRRIQRNVFF 677
Cdd:cd09820 514 IDNTDLQKNVFF 525
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
915-1398 |
1.28e-32 |
|
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: 135.23 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 915 FTHMVMQFGQLLDHELTHspVARGPNDEILnctkcdspekisvhcmpIRVEKDDPFF---PTNYPNGEPRCLPFARS--L 989
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDF--IPKGGNGTVL-----------------IPLPPDDPLYdlgRGTNGMALDRGTNNAGPdgI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 990 LGQLNlGYRNQLNQLTAYVDGSAIYGSTKCEAKNLR------LFTRGLLN------------FTD------------FGH 1039
Cdd:cd09821 74 LGTAD-GEGEHTNVTTPFVDQNQTYGSHASHQVFLReydgdgVATGRLLEgatggsartghaFLDdiahnaapkgglGSL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1040 GQMMLPQGNQEKDCRSTLEKRHMPCFVAGDERNSHQPGLTIMHTFFVREHNRIAMQLSAL----------------NPQW 1103
Cdd:cd09821 153 RDNPTEDPPGPGAPGSYDNELLDAHFVAGDGRVNENIGLTAVHTVFHREHNRLVDQIKDTllqsadlafaneaggnNLAW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1104 NDDTVFEEARRIVTAEMQHITFAEFLPKII-GLDLLNAQNlvpkkngyfgGYDNTCDASISQPFATAAFRFGHTLIRRMF 1182
Cdd:cd09821 233 DGERLFQAARFANEMQYQHLVFEEFARRIQpGIDGFGSFN----------GYNPEINPSISAEFAHAVYRFGHSMLTETV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1183 PRMNYNY-KNMSEPVDLAQHFGHVGPLYEQ---EKGGMDSMLMGLLGTPSMAFDRHITDAVRNHLFmrrgektsGM--DL 1256
Cdd:cd09821 303 TRIGPDAdEGLDNQVGLIDAFLNPVAFLPAtlyAEEGAGAILRGMTRQVGNEIDEFVTDALRNNLV--------GLplDL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1257 IVLNILRARDHGV--------------------QPYNDLREFcGLR---------------------------------- 1282
Cdd:cd09821 375 AALNIARGRDTGLptlnearaqlfaatgdtilkAPYESWNDF-GARlknpeslinfiaaygthltitgattlaakraaaq 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1283 RAVKWDDLKGEMDQDNINILQSLYESV---DDVDLFPGLVSERP-LRGALLGTTMSCIIAEQFGRLKKCDRFYYENDnsa 1358
Cdd:cd09821 454 DLVDGGDGAPADRADFMNAAGAGAGTVkglDNVDLWVGGLAEKQvPFGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR--- 530
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 17536077 1359 akfTPGQ--LNEIRKVKLASIFCSNS--KYLKTiqpNVFDVTDE 1398
Cdd:cd09821 531 ---TAGLdlLNQLENNTFADMIMRNTgaTHLPQ---DIFSVPDY 568
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
1001-1379 |
4.36e-30 |
|
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: 126.25 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1001 LNQLTAYVDGSAIYGSTKCEAKNLRLFTR-GLLNFTDFGHgqmmLPqgnqekdcrsTLEKRHMPcfVAGDERNShQPGLT 1079
Cdd:cd09818 87 INTNTHWWDGSQIYGSTEEAQKRLRTFPPdGKLKLDADGL----LP----------VDEHTGLP--LTGFNDNW-WVGLS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1080 IMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLL------NAQNLVPKKNGYFGG 1153
Cdd:cd09818 150 LLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPTLeiamraNWWGLLGERLKRVLG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1154 YDNTCDA------SISQ----PFA-TAAFrfghTLIRRMFPRM--NYNYKNMS-----EPVDLAQHFGHVGPLYEQEKGG 1215
Cdd:cd09818 230 RDGTSELlsgipgSPPNhhgvPYSlTEEF----VAVYRMHPLIpdDIDFRSADdgatgEEISLTDLAGGKARELLRKLGF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1216 MDSMLMglLGTPSM-AFDRHitdavrNHL-FMR--RGEKTSGMDLIVLNILRARDHGVQPYNDLREFCGLRRAVKWDDLK 1291
Cdd:cd09818 306 ADLLYS--FGITHPgALTLH------NYPrFLRdlHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLT 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1292 GemDQDNINILQSLYE-SVDDVDLFPGLVSERPLRG-ALLGTTMSCIIAEQFGRLKKcDRFyYENDNSAAKFTPGQLNEI 1369
Cdd:cd09818 378 G--DEEVAAELREVYGgDVEKVDLLVGLLAEPLPPGfGFSDTAFRIFILMASRRLKS-DRF-FTNDFRPEVYTPEGMDWV 453
|
410
....*....|
gi 17536077 1370 RKVKLASIFC 1379
Cdd:cd09818 454 NNNTMKSVLL 463
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
1008-1338 |
1.80e-25 |
|
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: 112.36 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1008 VDGSAIYGSTKCEAKNLRLFTRGLLNFTDFGhGQMMLP----QGNQE----------KDCRSTLEKRHMpcFVAGDERNS 1073
Cdd:cd09816 131 IDLSQIYGLTEARTHALRLFKDGKLKSQMIN-GEEYPPylfeDGGVKmefpplvpplGDELTPEREAKL--FAVGHERFN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1074 HQPGLTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGL--DLLNAQNLVPKKNGYf 1151
Cdd:cd09816 208 LTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYhfKLFFDPELAFNEPWQ- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1152 ggYDNtcdaSISQPFATaAFRFgHTLIrrmfP-RMNYNyknmSEPVDLAQHFGHVGPLyeqEKGGMDSMLMGLLGTPSMA 1230
Cdd:cd09816 287 --RQN----RIALEFNL-LYRW-HPLV----PdTFNIG----GQRYPLSDFLFNNDLV---VDHGLGALVDAASRQPAGR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1231 FdrhitdAVRNH-LFMRRGEKTSgmdlivlnILRARDHGVQPYNDLREFCGLRRAVKWDDLKGemDQDNINILQSLYESV 1309
Cdd:cd09816 348 I------GLRNTpPFLLPVEVRS--------IEQGRKLRLASFNDYRKRFGLPPYTSFEELTG--DPEVAAELEELYGDV 411
|
330 340
....*....|....*....|....*....
gi 17536077 1310 DDVDLFPGLVSERPLRGALLGTTMSCIIA 1338
Cdd:cd09816 412 DAVEFYVGLFAEDPRPNSPLPPLMVEMVA 440
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
319-667 |
1.35e-24 |
|
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: 109.66 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 319 DASFIYGSNMEKAKQLRTFRNGQLRT---------------AGSIGELPATDGTLQCQATHSRCAL---SGTDEVNILPS 380
Cdd:cd09816 132 DLSQIYGLTEARTHALRLFKDGKLKSqmingeeyppylfedGGVKMEFPPLVPPLGDELTPEREAKlfaVGHERFNLTPG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 381 VAALHTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQ---------VQHITyneflpvllgrenmrNYGLNL--- 448
Cdd:cd09816 212 LFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGElikiviedyINHLS---------------PYHFKLffd 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 449 ----HSAGFDSNYEMNLEgttFNefavtiTYYFW-ALLPS-------EKSFVDF-NNPSRLYEQGPVQIIRQVLNTNIYQ 515
Cdd:cd09816 277 pelaFNEPWQRQNRIALE---FN------LLYRWhPLVPDtfniggqRYPLSDFlFNNDLVVDHGLGALVDAASRQPAGR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 516 PTLRandevksgflkdNH-EFGLDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLREIflPEVKfEQVSSAYTRVE 594
Cdd:cd09816 348 IGLR------------NTpPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTGD--PEVA-AELEELYGDVD 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 595 DVDLLVGVLAEKPLKGSLVGPTMACIIGkqmqrtrrADRF--------WYENYFAQSGFNEAQLSEIRNTK-LAEIICSN 665
Cdd:cd09816 413 AVEFYVGLFAEDPRPNSPLPPLMVEMVA--------PDAFsgaltnplLSPEVWKPSTFGGEGGFDIVKTAtLQDLVCRN 484
|
..
gi 17536077 666 ID 667
Cdd:cd09816 485 VK 486
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
306-640 |
6.40e-23 |
|
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: 104.29 E-value: 6.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 306 GPREQANFASSYLDASFIYGSNMEKAKQLRTF-RNGQLRTAGSiGELPaTDgtlqcqaTHSRCALSGTDEvNILPSVAAL 384
Cdd:cd09818 82 GPPTYINTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLKLDAD-GLLP-VD-------EHTGLPLTGFND-NWWVGLSLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 385 HTVFIRHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLG----RENMR-N-YGL----NLHSAGFD 454
Cdd:cd09818 152 HTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAhptlEIAMRaNwWGLlgerLKRVLGRD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 455 SNYEM--NLEGTTFNEFAV--------TITYYFWALLPSEKSFvdfnnpsRLYEQGPvqIIRQVLNTNIYQPTLRANDEv 524
Cdd:cd09818 232 GTSELlsGIPGSPPNHHGVpyslteefVAVYRMHPLIPDDIDF-------RSADDGA--TGEEISLTDLAGGKARELLR- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 525 KSGFLKDNHEFG--------------------------LDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDLREIfl 578
Cdd:cd09818 302 KLGFADLLYSFGithpgaltlhnyprflrdlhrpdgrvIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLTGD-- 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17536077 579 PEV--KFEQVssaY-TRVEDVDLLVGVLAEKPLKGSLVGPT-------MAciigkqmqrTRR--ADRFwYENYF 640
Cdd:cd09818 380 EEVaaELREV---YgGDVEKVDLLVGLLAEPLPPGFGFSDTafrifilMA---------SRRlkSDRF-FTNDF 440
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
1001-1357 |
8.49e-15 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 79.42 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1001 LNQLTAYVDGSAIYGSTKCEAKNLRLFTRGLLNFTDFG---HGQMMLPqgnqekdcrstlekrhmpcfVAGDERNShQPG 1077
Cdd:PLN02283 207 LNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKISEDGlllHDEDGIP--------------------ISGDVRNS-WAG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1078 LTIMHTFFVREHNRIAMQLSALNPQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLL------NAQNLVPKK---- 1147
Cdd:PLN02283 266 VSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLKTDTLlagmraNWYGLLGKKfkdt 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1148 NGYFGG------------YDNTCDASISQPFaTAAFRFgH-----TLIRRMFPRMNYNYKN--MSEPVDLAQHFGHVGPl 1208
Cdd:PLN02283 346 FGHIGGpilsglvglkkpNNHGVPYSLTEEF-TSVYRM-HsllpdHLILRDITAAPGENKSppLIEEIPMPELIGLKGE- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1209 YEQEKGGMDSML--MG--------LLGTPSmaFDRHITDAVRNhlfmrrGE-KTSGMDLIVLNILRARDHGVQPYNDLRE 1277
Cdd:PLN02283 423 KKLSKIGFEKLMvsMGhqacgaleLWNYPS--WMRDLVPQDID------GEdRPDHVDMAALEIYRDRERGVARYNEFRR 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1278 FCGLRRAVKWDDLKGemDQDNINILQSLY-ESVDDVDLFPGLVSERPLRGALLGTTMSCIIAEQFGRLKKCDRFYYENDN 1356
Cdd:PLN02283 495 NLLMIPISKWEDLTD--DEEAIEVLREVYgDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRRLEADRFFTSNFN 572
|
.
gi 17536077 1357 S 1357
Cdd:PLN02283 573 E 573
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
312-647 |
4.34e-14 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 77.11 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 312 NFASSYLDASFIYGSNMEKAKQLRTFRNGQLRtagsIGElpatDGTLQcqatHSR--CALSGtDEVNILPSVAALHTVFI 389
Cdd:PLN02283 208 NIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLK----ISE----DGLLL----HDEdgIPISG-DVRNSWAGVSLLQALFV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 390 RHHNRIADNLRSINRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLG----RENMRN--YGL--------------NLH 449
Cdd:PLN02283 275 KEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLKtdtlLAGMRAnwYGLlgkkfkdtfghiggPIL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 450 SaGFDSNYEMNLEGTTFN---EFavTITYYFWALLPSEKSFVDFNNPSRLYEQGPVqiIRQVLNTNIYqpTLRANDEV-K 525
Cdd:PLN02283 355 S-GLVGLKKPNNHGVPYSlteEF--TSVYRMHSLLPDHLILRDITAAPGENKSPPL--IEEIPMPELI--GLKGEKKLsK 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 526 SGFLKDNHEFG--------------------------------LDLISIALKQGRDHGIPGYTALRASCGLGRIASFNDL 573
Cdd:PLN02283 428 IGFEKLMVSMGhqacgalelwnypswmrdlvpqdidgedrpdhVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDL 507
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17536077 574 REiflPEVKFEQVSSAY-TRVEDVDLLVGVLAEKPLKGSLVGPTmACIIGKQMQrTRR--ADRFWYENyfaqsgFNE 647
Cdd:PLN02283 508 TD---DEEAIEVLREVYgDDVEKLDLLVGLMAEKKIKGFAISET-AFFIFLLMA-SRRleADRFFTSN------FNE 573
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
383-676 |
7.71e-14 |
|
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: 76.30 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 383 ALHTVFIRHHNRIADNLRSI----------------NRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGrenmrnyGL 446
Cdd:cd09821 193 AVHTVFHREHNRLVDQIKDTllqsadlafaneaggnNLAWDGERLFQAARFANEMQYQHLVFEEFARRIQP-------GI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 447 NLHSAGFDSNYEMNLEGTTfnEFAVTiTYYF----------------WALLPSEKSFVD------FNNPSRLYEQGPV-Q 503
Cdd:cd09821 266 DGFGSFNGYNPEINPSISA--EFAHA-VYRFghsmltetvtrigpdaDEGLDNQVGLIDaflnpvAFLPATLYAEEGAgA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 504 IIR----QVLNtniyqptlrANDEVKSGFLKDNH-EFGLDLISIALKQGRDHGIPGYTALR----ASCGLGRI----ASF 570
Cdd:cd09821 343 ILRgmtrQVGN---------EIDEFVTDALRNNLvGLPLDLAALNIARGRDTGLPTLNEARaqlfAATGDTILkapyESW 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 571 ND-LREIFLPEVKFEQVSSAYTR----------------------------------------------VEDVDLLVGVL 603
Cdd:cd09821 414 NDfGARLKNPESLINFIAAYGTHltitgattlaakraaaqdlvdggdgapadradfmnaagagagtvkgLDNVDLWVGGL 493
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17536077 604 AEKPLK-GSLVGPTMACIIGKQMQRTRRADRFWYENYFAQSGFneaqLSEIRNTKLAEIICSNIDIRRIQRNVF 676
Cdd:cd09821 494 AEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSRTAGLDL----LNQLENNTFADMIMRNTGATHLPQDIF 563
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
1002-1351 |
1.18e-12 |
|
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: 72.37 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1002 NQLTAYVDGSAIYGSTKCEAKNLRLFTRGLLnftdfghgqmmlpqgnqEKDCRStlEKR--HMPcfvagdernshqPGLT 1079
Cdd:cd09817 118 NNTSSYLDLSPLYGSNQEEQNKVRTMKDGKL-----------------KPDTFS--DKRllGQP------------PGVC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1080 IMHTFFVREHNRIAMQLSALN-----------------PQWNDDTVFEEARRIVTAEMQHITFAEFLPKIIGLDLLNAQ- 1141
Cdd:cd09817 167 ALLVMFNRFHNYVVEQLAQINeggrftppgdkldssakEEKLDEDLFQTARLITCGLYINIVLHDYVRAILNLNRTDSTw 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1142 NLVPKKN------GYFGGYDNTCD----------ASISQpfATAAFRfgHTLIRRMFPRMNYNYKNMSEPVD-LAQHFGH 1204
Cdd:cd09817 247 TLDPRVEigrsltGVPRGTGNQVSvefnllyrwhSAISA--RDEKWT--EDLFESLFGGKSPDEVTLKEFMQaLGRFEAL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1205 VGPLYEQ-EKGGMDSMLMGLLGTPSMAfdRHITDAVRN--HLFMRRGEKTSGMDLIVLNILRARDHGVQPYNDLREFCGL 1281
Cdd:cd09817 323 IPKDPSQrTFGGLKRGPDGRFRDEDLV--RILKDSIEDpaGAFGARNVPASLKVIEILGILQAREWNVATLNEFRKFFGL 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17536077 1282 RRAVKWDDLKgeMDQDNINILQSLYESVDDVDLFPGLVSE----RPLRGALL--GTTMSCIIAEQFGRLKKCDRFY 1351
Cdd:cd09817 401 KPYETFEDIN--SDPEVAEALELLYGHPDNVELYPGLVAEdakpPMPPGSGLcpGYTISRAILSDAVALVRGDRFY 474
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
1066-1363 |
4.33e-11 |
|
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: 66.98 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1066 VAGDERNSHQpgLTI--MHTFFVREHNRIAMQLSALNPQWNDDtvFEEARRIVTAEMQHITFAEFLPKIIG---LDLLNA 1140
Cdd:cd09819 145 LIGDPRNDEN--LIVaqLHLAFLRFHNAVVDALRAHGTPGDEL--FEEARRLVRWHYQWLVLNDFLPRICDpdvVDDVLA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1141 QNLVPKKNGYFGGydntcdasISQP--FATAAFRFGHTLIRrmfPRMNYNYKNMSEPVDLAQHFGHVGPlyeqekggmds 1218
Cdd:cd09819 221 NGRRFYRFFREGK--------PFMPveFSVAAYRFGHSMVR---ASYDYNRNFPDASLELLFTFTGGGE----------- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1219 mlMGLLGTPSMAFDRHI-------TDAVRNHLFMRRgektsgMD-LIVLNILRARDHGVQPYNDLRE--FCGLRRAVKW- 1287
Cdd:cd09819 279 --GDLGGFSPLPENWIIdwrrffdIDGSAPPQFARK------IDtKLAPPLFDLPNGGVGLAPPMKSlaFRNLLRGYRLg 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 1288 ----DDLKGEMDQDN--INILQSLyESVDDVDLFPGLVSERPL------------RGALLGTTMSCIIAEQFGRLKKCDR 1349
Cdd:cd09819 351 lpsgQAVARALGIAPltADELGDG-EDGAPAVAGGGLHEATPLwfyilkeaevrgGGNRLGPVGSRIVAEVFIGLLEGDP 429
|
330
....*....|....
gi 17536077 1350 FYYENDNSAAKFTP 1363
Cdd:cd09819 430 SSYLSLGFNPDWTP 443
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
307-439 |
7.62e-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: 56.58 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536077 307 PREQANFASSYLDASFIYGSNMEKAKQLRTFRN----GQLRTAGsigELPATDGTLQCQATH------SRCALSG---TD 373
Cdd:cd09819 76 PAELRNFRTPALDLDSVYGGGPDGSPYLYDQATpndgAKLRVGR---ESPGGPGGLPGDGARdlprngQGTALIGdprND 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17536077 374 EvNILpsVAALHTVFIRHHNRIADNLRSinRHWTDDKLYEEARKIVAAQVQHITYNEFLPVLLGRE 439
Cdd:cd09819 153 E-NLI--VAQLHLAFLRFHNAVVDALRA--HGTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPD 213
|
|
| |
