|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
143-631 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 564.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 143 YRSMDGTCNNLQNPVKGAAFTAFTRLMPAAYDDGFNTLVSASR-RNRPNPREVSVFLLSSERSLP-GHVNSLLMLFGQFV 220
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSSgSPLPSPRLVSNKLFAGDSGIPdPNLTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 221 SHDITS---------NAAQNFCGCQNSGPMCASIFAPPSD-----RSRRCIPFTRSFPICGtgqFGRVREQLNMNTAAID 286
Cdd:pfam03098 81 DHDLTLtpestspngSSCDCCCPPENLHPPCFPIPIPPDDpffspFGVRCMPFVRSAPGCG---LGNPREQINQVTSFLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 287 ASLIYGSEAITARSLR-FA-AMLRTSM-IGGRMFPPNTNPGSL-----------TAGDGRAILFVGLAALHTSFLRLHNN 352
Cdd:pfam03098 158 GSQVYGSSEETARSLRsFSgGLLKVNRsDDGKELLPFDPDGPCccnssggvpcfLAGDSRANENPGLTALHTLFLREHNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 353 VAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGD----ASKTILGAYNGYNPNVEIGVLNEFAAGAYRL- 427
Cdd:pfam03098 238 IADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEdnmnWFGLLPLPYNGYDPNVDPSISNEFATAAFRFg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 428 HGMIQETYPLVNSQ-FQEVNRYRFIDGVNNINHVL-NNIDAIYRGMMTVPVRSPQR-LTTSVTERLFGGS-----VDMAA 499
Cdd:pfam03098 318 HSLIPPFLYRLDENnVPEEPSLRLHDSFFNPDRLYeGGIDPLLRGLATQPAQAVDNnFTEELTNHLFGPPgefsgLDLAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 500 VNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEVPDENVRQRIGQLYRTPDDLDFYVGGILEQPAAGSLLGATFACVIG 579
Cdd:pfam03098 398 LNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17534209 580 KQFERLRDGDRFYYENP--GVFTSPQLAELKRTTLSWVLCQTGDNMVRVGRRAF 631
Cdd:pfam03098 478 DQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
275-619 |
1.14e-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: 453.57 E-value: 1.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 275 REQLNMNTAAIDASLIYGSEAITARSLRF--AAMLRTSMIGGRMFPPNTNPGS------------LTAGDGRAILFVGLA 340
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTfkGGLLKTQRRNGRELLPFSNNPTddcslssagkpcFLAGDGRVNEQPGLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 341 ALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGDASKTIL-------GAYNGYNPNVE 413
Cdd:cd09823 81 SMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFNGYDPNVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 414 IGVLNEFAAGAYRL-HGMIQETYPLVNSQFQEVNRYRFIDGVNNINHVL--NNIDAIYRGMMTVPVRSPQRLTTSVTERL 490
Cdd:cd09823 161 PSILNEFAAAAFRFgHSLVPGTFERLDENYRPQGSVNLHDLFFNPDRLYeeGGLDPLLRGLATQPAQKVDRFFTDELTTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 491 F------GGSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEVPDENVRQRIGQLYRTPDDLDFYVGGILEQP 564
Cdd:cd09823 241 FffrggnPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVGGLSEKP 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17534209 565 AAGSLLGATFACVIGKQFERLRDGDRFYYENPGV---FTSPQLAELKRTTLSWVLCQT 619
Cdd:cd09823 321 VPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
143-595 |
2.89e-11 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 66.71 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 143 YRSMDGTCNNLQNPVKGAAFTAFTRLMPAAyddgfntlVSASRRNRPNPREVSVFLLSSERSLPG--HVNSLLMLFGQFV 220
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGRNMPPV--------DQKDKLLDPHPSVVATKLLARKKFIDTgkQFNMIAASWIQFM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 221 SHDITSNAaqnfcgcQNSGPMcaSIFAPPSDRSRrCiPF-------TRSFPicgTGQFGRVREQLNMNTAAIDASLIYGS 293
Cdd:PLN02283 157 IHDWIDHL-------EDTQQI--ELTAPKEVASQ-C-PLksfkfykTKEVP---TGSPDIKTGSLNIRTPWWDGSVIYGS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 294 EAITARSLR-FA-AMLRTSMIGGRMFPPNTNPGSltaGDGRAiLFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQ 371
Cdd:PLN02283 223 NEKGLRRVRtFKdGKLKISEDGLLLHDEDGIPIS---GDVRN-SWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 372 ESRKIVGGIVQVITYQEFVPEL-------------------------IGDASKTILGAYNGYNPNVEIGV---LNEFAAG 423
Cdd:PLN02283 299 HARLVTSAVIAKIHTIDWTVELlktdtllagmranwygllgkkfkdtFGHIGGPILSGLVGLKKPNNHGVpysLTEEFTS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 424 AYRLHGMIQETYPLvnsqfqevnryRFIDGVNNINHVLNNIDAI------------------YRGMMT----------VP 475
Cdd:PLN02283 379 VYRMHSLLPDHLIL-----------RDITAAPGENKSPPLIEEIpmpeliglkgekklskigFEKLMVsmghqacgalEL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 476 VRSPQRLTTSVTERLFGGS----VDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEvpDENVRQRIGQLYrtPD 551
Cdd:PLN02283 448 WNYPSWMRDLVPQDIDGEDrpdhVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTD--DEEAIEVLREVY--GD 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17534209 552 D---LDFYVGGILEQPAAGSLLGAT-FACVIGKQFERLrDGDRFYYEN 595
Cdd:PLN02283 524 DvekLDLLVGLMAEKKIKGFAISETaFFIFLLMASRRL-EADRFFTSN 570
|
|
| ShKT |
smart00254 |
ShK toxin domain; ShK toxin domain |
22-56 |
8.93e-08 |
|
ShK toxin domain; ShK toxin domain
Pssm-ID: 214586 [Multi-domain] Cd Length: 33 Bit Score: 48.53 E-value: 8.93e-08
10 20 30
....*....|....*....|....*....|....*
gi 17534209 22 CTDKHIHCFFWSQeGECeVNPRWMKKHCQKACGTC 56
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 ... |
21-56 |
7.76e-07 |
|
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.
Pssm-ID: 426319 Cd Length: 37 Bit Score: 45.85 E-value: 7.76e-07
10 20 30
....*....|....*....|....*....|....*...
gi 17534209 21 ECTDKHIHCFFWSQEGeCEVNP--RWMKKHCQKACGTC 56
Cdd:pfam01549 1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
|
|
| PLN00052 |
PLN00052 |
prolyl 4-hydroxylase; Provisional |
19-56 |
4.13e-05 |
|
prolyl 4-hydroxylase; Provisional
Pssm-ID: 177683 [Multi-domain] Cd Length: 310 Bit Score: 46.20 E-value: 4.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 17534209 19 SEECTDKHIHCFFWSQEGECEVNPRWM------KKHCQKACGTC 56
Cdd:PLN00052 265 TEGCADKSAHCAEWAAAGECEKNPVYMvgaegaPGNCRKSCGVC 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
143-631 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 564.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 143 YRSMDGTCNNLQNPVKGAAFTAFTRLMPAAYDDGFNTLVSASR-RNRPNPREVSVFLLSSERSLP-GHVNSLLMLFGQFV 220
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSSgSPLPSPRLVSNKLFAGDSGIPdPNLTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 221 SHDITS---------NAAQNFCGCQNSGPMCASIFAPPSD-----RSRRCIPFTRSFPICGtgqFGRVREQLNMNTAAID 286
Cdd:pfam03098 81 DHDLTLtpestspngSSCDCCCPPENLHPPCFPIPIPPDDpffspFGVRCMPFVRSAPGCG---LGNPREQINQVTSFLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 287 ASLIYGSEAITARSLR-FA-AMLRTSM-IGGRMFPPNTNPGSL-----------TAGDGRAILFVGLAALHTSFLRLHNN 352
Cdd:pfam03098 158 GSQVYGSSEETARSLRsFSgGLLKVNRsDDGKELLPFDPDGPCccnssggvpcfLAGDSRANENPGLTALHTLFLREHNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 353 VAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGD----ASKTILGAYNGYNPNVEIGVLNEFAAGAYRL- 427
Cdd:pfam03098 238 IADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEdnmnWFGLLPLPYNGYDPNVDPSISNEFATAAFRFg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 428 HGMIQETYPLVNSQ-FQEVNRYRFIDGVNNINHVL-NNIDAIYRGMMTVPVRSPQR-LTTSVTERLFGGS-----VDMAA 499
Cdd:pfam03098 318 HSLIPPFLYRLDENnVPEEPSLRLHDSFFNPDRLYeGGIDPLLRGLATQPAQAVDNnFTEELTNHLFGPPgefsgLDLAA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 500 VNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEVPDENVRQRIGQLYRTPDDLDFYVGGILEQPAAGSLLGATFACVIG 579
Cdd:pfam03098 398 LNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17534209 580 KQFERLRDGDRFYYENP--GVFTSPQLAELKRTTLSWVLCQTGDNMVRVGRRAF 631
Cdd:pfam03098 478 DQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
275-619 |
1.14e-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: 453.57 E-value: 1.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 275 REQLNMNTAAIDASLIYGSEAITARSLRF--AAMLRTSMIGGRMFPPNTNPGS------------LTAGDGRAILFVGLA 340
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTfkGGLLKTQRRNGRELLPFSNNPTddcslssagkpcFLAGDGRVNEQPGLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 341 ALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGDASKTIL-------GAYNGYNPNVE 413
Cdd:cd09823 81 SMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFNGYDPNVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 414 IGVLNEFAAGAYRL-HGMIQETYPLVNSQFQEVNRYRFIDGVNNINHVL--NNIDAIYRGMMTVPVRSPQRLTTSVTERL 490
Cdd:cd09823 161 PSILNEFAAAAFRFgHSLVPGTFERLDENYRPQGSVNLHDLFFNPDRLYeeGGLDPLLRGLATQPAQKVDRFFTDELTTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 491 F------GGSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEVPDENVRQRIGQLYRTPDDLDFYVGGILEQP 564
Cdd:cd09823 241 FffrggnPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIMSPETIQKLRRLYKSVDDIDLYVGGLSEKP 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17534209 565 AAGSLLGATFACVIGKQFERLRDGDRFYYENPGV---FTSPQLAELKRTTLSWVLCQT 619
Cdd:cd09823 321 VPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
248-644 |
3.61e-131 |
|
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: 393.21 E-value: 3.61e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 248 PPSDRSR---RCIPFTRSFPICGTGQ----FGRV--REQLNMNTAAIDASLIYGSEAITARSLRFAA----MLRTSMI-- 312
Cdd:cd09826 1 PPDDPRRrghRCIEFVRSSAVCGSGStsllFNSVtpREQINQLTSYIDASNVYGSSDEEALELRDLAsdrgLLRVGIVse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 313 -GGRMFPPNTNPGS-------------LTAGDGRAILFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVG 378
Cdd:cd09826 81 aGKPLLPFERDSPMdcrrdpnespipcFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 379 GIVQVITYQEFVPELIGDASKTILGAYNGYNPNVEIGVLNEFAAGAYRL-HGMIQetyPLV---NSQFQEV--------- 445
Cdd:cd09826 161 AQMQHITYSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFATAAFRFgHTLIN---PILfrlDEDFQPIpeghlplhk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 446 ---NRYRFI-DGvnninhvlnNIDAIYRGMMTVPVRSP---QRLTTSVTERLFGGS----VDMAAVNIQRGRDHGLRSYN 514
Cdd:cd09826 238 affAPYRLVnEG---------GIDPLLRGLFATAAKDRvpdQLLNTELTEKLFEMAhevaLDLAALNIQRGRDHGLPGYN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 515 DYRRFCNLRPITSFNDWP-EVPDENVRQRIGQLYRTPDDLDFYVGGILEQPAAGSLLGATFACVIGKQFERLRDGDRFYY 593
Cdd:cd09826 309 DYRKFCNLSVAETFEDLKnEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 17534209 594 ENPGVFTSPQLAELKRTTLSWVLCQTGDNMVRVGRRAFDIENGSRA-VPCSS 644
Cdd:cd09826 389 ENPGVFSPAQLTQIKKTSLARVLCDNGDNITRVQEDVFLVPGNPHGyVSCES 440
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
159-655 |
8.85e-118 |
|
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: 362.91 E-value: 8.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 159 GAAFTAFTRLMPAAYDDGFNTLVS--ASRR----NRPNPREVS--VFLLSSERSLPGHVNS-LLMLFGQFVSHDI----T 225
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGwnKERLyngfTLPSVREVSnkIMRTSSTAVTPDDLYShMLTVWGQYIDHDIdftpQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 226 SNAAQNFCG-------CQNSGPmCASIFAP---PSDRSRRCIPFTRSFPICGTGQ----FGRV-----REQLNMNTAAID 286
Cdd:cd09825 81 SVSRTMFIGstdckmtCENQNP-CFPIQLPsedPRILGRACLPFFRSSAVCGTGDtstlFGNLslanpREQINGLTSFID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 287 ASLIYGSEAITARSLR----FAAMLRTSM---IGGRMFPPNTNPGSLT---------------AGDGRAILFVGLAALHT 344
Cdd:cd09825 160 ASTVYGSTLALARSLRdlssDDGLLRVNSkfdDSGRDYLPFQPEEVSScnpdpnggervpcflAGDGRASEVLTLTASHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 345 SFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIG-DASKTILGAYNGYNPNVEIGVLNEFAAG 423
Cdd:cd09825 240 LWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGpEAFDQYGGYYEGYDPTVNPTVSNVFSTA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 424 AYRL-HGMIQETYPLVNSQFQE-------------VNRYRFIDGVNninhvlnnIDAIYRGMMTVPVRSP---QRLTTSV 486
Cdd:cd09825 320 AFRFgHATIHPTVRRLDENFQEhpvlpnlalhdafFSPWRLVREGG--------LDPVIRGLIGGPAKLVtpdDLMNEEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 487 TERLF----GGSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDW-PEVPDENVRQRIGQLYRTPDDLDFYVGGIL 561
Cdd:cd09825 392 TEKLFvlsnSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLaTAIADQAVADKILDLYKHPDNIDVWLGGLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 562 EQPAAGSLLGATFACVIGKQFERLRDGDRFYYENPGVFTSPQLAELKRTTLSWVLCQTGDnMVRVGRRAFDIEN-GSRAV 640
Cdd:cd09825 472 EDFLPGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTG-LTRVPPDAFQLGKfPEDFV 550
|
570
....*....|....*
gi 17534209 641 PCSSITGLNLEAWRE 655
Cdd:cd09825 551 SCDSIPGINLEAWRE 565
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
187-613 |
5.11e-92 |
|
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: 291.14 E-value: 5.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 187 NRPNPREVSVFLLSSERSLPG--HVNSLLMLFGQFVSHDITsnaaqnfcgcqnsgpmcasiFAPpsdrsrrcipftrsfp 264
Cdd:cd09822 1 DRPSPREISNAVADQTESIPNsrGLSDWFWVWGQFLDHDID--------------------LTP---------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 265 icgtgqfGRVREQLNMNTAAIDASLIYGSEAITARSLR-FA-AMLRTSMI-GGRMFP------PNTNPGS-----LTAGD 330
Cdd:cd09822 45 -------DNPREQINAITAYIDGSNVYGSDEERADALRsFGgGKLKTSVAnAGDLLPfneaglPNDNGGVpaddlFLAGD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 331 GRAILFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGDaskTILGAYNGYNP 410
Cdd:cd09822 118 VRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLGE---NALPAYSGYDE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 411 NVEIGVLNEFAAGAYRL-HGMIQETYPLVNSQFQEVNRYRFIDGVNNINHVLNN-IDAIYRGMMTVPVrspQRLTTSVTE 488
Cdd:cd09822 195 TVNPGISNEFSTAAYRFgHSMLSSELLRGDEDGTEATSLALRDAFFNPDELEENgIDPLLRGLASQVA---QEIDTFIVD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 489 --R--LFG----GSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEvpDENVRQRIGQLYRTPDDLDFYVGGI 560
Cdd:cd09822 272 dvRnfLFGppgaGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDITS--DPDLAARLASVYGDVDQIDLWVGGL 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 17534209 561 LEQPAAGSLLGATFACVIGKQFERLRDGDRFYYENPgVFTSPQLAELKRTTLS 613
Cdd:cd09822 350 AEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-DLLLDEIADIENTTLA 401
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
273-649 |
2.67e-88 |
|
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: 281.23 E-value: 2.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 273 RVREQLNMNTAAIDASLIYGSEAITARSLR----FAAMLRTS---MIGGRMFPP----NTNPGSLT----------AGDG 331
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRnltnQLGLLAVNqrfTDNGLALLPfenlHNDPCALRntsanipcflAGDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 332 RAILFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGDASKTILGAYNGYNPN 411
Cdd:cd09824 90 RVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARLPPYRGYNES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 412 VEIGVLNEFAAGAYRLHGMIQETYPLVNSQFQE-------------VNRYRFI-DGvnninhvlnNIDAIYRGMMTVPV- 476
Cdd:cd09824 170 VDPRIANVFTTAFRRGHTTVQPFVFRLDENYQPhppnpqvplhkafFASWRIIrEG---------GIDPILRGLMATPAk 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 477 --RSPQRLTTSVTERLF----GGSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEV-PDENVRQRIGQLYRT 549
Cdd:cd09824 241 lnNQNQMLVDELRERLFqqtkRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVlNNTVLARKLLDLYGT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 550 PDDLDFYVGGILEQPAAGSLLGATFACVIGKQFERLRDGDRFYYENPGVFTSPQLAELKRTTLSWVLCqtgDN--MVRVG 627
Cdd:cd09824 321 PDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIIC---DNtgITKVP 397
|
410 420
....*....|....*....|..
gi 17534209 628 RRAFDiengsravPCSSITGLN 649
Cdd:cd09824 398 RDPFQ--------PNSYPRDFV 411
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
277-618 |
2.42e-81 |
|
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: 261.59 E-value: 2.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 277 QLNMNTAAIDASLIYGSEAITARSLRfaamlrtSMIGGRM-------------FPPNTNP------------GSLTAGDG 331
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR-------TFKGGLLktnevkgpsygteLLPFNNPnpsmgtiglpptRCFIAGDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 332 RAILFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIG-DASKTILGAYNGYNP 410
Cdd:cd05396 74 RVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGkFTDPRDDLVLLFPDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 411 NVEIGVLNEFAAGAYRL-HGMIQETYP--LVNSQFQEVNRYRFIDGVNN---INHVLNNIDAIYRGMMTVPVRSPqRLTT 484
Cdd:cd05396 154 DVVPYVLSEFFTAAYRFgHSLVPEGVDriDENGQPKEIPDVPLKDFFFNtsrSILSDTGLDPLLRGFLRQPAGLI-DQNV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 485 SVTERLFGGSV----DMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDwpEVPDENVRQRIGQLYRTPDDLDFYVGGI 560
Cdd:cd05396 233 DDVMFLFGPLEgvglDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQD--ILTDPELAKKLAELYGDPDDVDLWVGGL 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17534209 561 LEQPAAGSLLGATFACVIGKQFERLRDGDRFYYENPGVFTSPQLAELKRT-TLSWVLCQ 618
Cdd:cd05396 311 LEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKLiSLADIICL 369
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
146-612 |
1.39e-76 |
|
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: 254.92 E-value: 1.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 146 MDGTCNNLQNPVKGAAFTAFTRLMPAAYDDGFNtlvSASRRNRPNPREVSVFLLSSERSLPGHVNS--LLMLFGQFVSHD 223
Cdd:cd09820 1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVY---APSGEERPNPRSLSNLLMKGESGLPSTRNRtaLLVFFGQHVVSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 224 ITSNaaqnfcgcQNSG----------PMCASIFAPPSdRSRRCIPFTRSFPICGTGQFGRV-REQLNMNTAAIDASLIYG 292
Cdd:cd09820 78 ILDA--------SRPGcppeyfnieiPKGDPVFDPEC-TGNIELPFQRSRYDKNTGYSPNNpREQLNEVTSWIDGSSIYG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 293 SEAITARSLRFAAMLRTSMIGGRMFPPNTNPGSLTA-------------------GDGRAILFVGLAALHTSFLRLHNNV 353
Cdd:cd09820 149 SSKAWSDALRSFSGGRLASGDDGGFPRRNTNRLPLAnppppsyhgtrgperlfklGNPRGNENPFLLTFGILWFRYHNYL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 354 AARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIGdaskTILGAYNGYNPNVEIGVLNEFAAGAYR-LHGMI- 431
Cdd:cd09820 229 AQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLG----TNVPPYTGYKPHVDPGISHEFQAAAFRfGHTLVp 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 432 --------QETYPLVNSQFQEVNRYRFIDGVNNINHVLNN--IDAIYRGMMT-VPVRSPQRLTTSVTERLFG----GSVD 496
Cdd:cd09820 305 pgvyrrnrQCNFREVLTTSGGSPALRLCNTYWNSQEPLLKsdIDELLLGMASqIAEREDNIIVEDLRDYLFGplefSRRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 497 MAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEVP---DENVRQRIGQLY-RTPDDLDFYVGGILEQPAAGSllGA 572
Cdd:cd09820 385 LMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLfkkDPELLERLAELYgNDLSKLDLYVGGMLESKGGGP--GE 462
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17534209 573 TFACVIGKQFERLRDGDRFYYENP--GVFTSPQLAELKRTTL 612
Cdd:cd09820 463 LFRAIILDQFQRLRDGDRFWFENVknGLFTAEEIEEIRNTTL 504
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
210-593 |
1.47e-31 |
|
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: 129.84 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 210 NSLLMLFGQFVSHDITsnaaqnFCGCQNSGPMcaSIFAPPSDRsrrciPFTRSFPICG---------------TGQFGRV 274
Cdd:cd09821 14 NSWMTFFGQFFDHGLD------FIPKGGNGTV--LIPLPPDDP-----LYDLGRGTNGmaldrgtnnagpdgiLGTADGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 275 REQLNMNTAAIDASLIYGSEAITARSLR-------FAAMLRTSMIGG-----------------------------RMFP 318
Cdd:cd09821 81 GEHTNVTTPFVDQNQTYGSHASHQVFLReydgdgvATGRLLEGATGGsartghaflddiahnaapkgglgslrdnpTEDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 319 PNTNPGSL----------TAGDGRAILFVGLAALHTSFLRLHNNVAARLQNM----------------NRHWNADRIFQE 372
Cdd:cd09821 161 PGPGAPGSydnelldahfVAGDGRVNENIGLTAVHTVFHREHNRLVDQIKDTllqsadlafaneaggnNLAWDGERLFQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 373 SRKIVGGIVQVITYQEFVPELIG--DASktilGAYNGYNPNVEIGVLNEFAAGAYRL-HGMIQETYPLVNSQFQE--VNR 447
Cdd:cd09821 241 ARFANEMQYQHLVFEEFARRIQPgiDGF----GSFNGYNPEINPSISAEFAHAVYRFgHSMLTETVTRIGPDADEglDNQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 448 YRFIDG----VNNINHVLNN---IDAIYRGMMTvpvRSPQRLTTSVTE----RLFGGSVDMAAVNIQRGRDHGLRSYNDY 516
Cdd:cd09821 317 VGLIDAflnpVAFLPATLYAeegAGAILRGMTR---QVGNEIDEFVTDalrnNLVGLPLDLAALNIARGRDTGLPTLNEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 517 RR--------FCNLRPITSFNDWPE--VPDENVRQRIGQLYRTP------------------------------------ 550
Cdd:cd09821 394 RAqlfaatgdTILKAPYESWNDFGArlKNPESLINFIAAYGTHLtitgattlaakraaaqdlvdggdgapadradfmnaa 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17534209 551 ----------DDLDFYVGGILEQPAA-GSLLGATFACVIGKQFERLRDGDRFYY 593
Cdd:cd09821 474 gagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYY 527
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
144-620 |
3.51e-31 |
|
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: 127.40 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 144 RSMDGTCNNLQNPVKGAAFTAFTRLMPaaYDDGFNTlvSASRRNRPNPREVSVFLLSSERSLPG-HVNSLLMLFGQFVSH 222
Cdd:cd09818 1 RTADGSYNDLDNPSMGSVGTRFGRNVP--LDATFPE--DKDELLTPNPRVISRRLLARTEFKPAtSLNLLAAAWIQFMVH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 223 DITSNaaqnfcgcqnsgpmcasifappsdrsrrcipftrsfpicGTGQFgrvreqLNMNTAAIDASLIYGSEAITARslr 302
Cdd:cd09818 77 DWFSH---------------------------------------GPPTY------INTNTHWWDGSQIYGSTEEAQK--- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 303 faaMLRTSMIGGR-------MFPPNTNPGSLTAGDGRAiLFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRK 375
Cdd:cd09818 109 ---RLRTFPPDGKlkldadgLLPVDEHTGLPLTGFNDN-WWVGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 376 IVGGIVQVITYQEFVPELI-----------------GDASKTILGAYN---------GYNPN---VEIGVLNEFAAgAYR 426
Cdd:cd09818 185 VNAALMAKIHTVEWTPAILahptleiamranwwgllGERLKRVLGRDGtsellsgipGSPPNhhgVPYSLTEEFVA-VYR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 427 LH--------------GMIQETYPLVNSQFQEVNRYRFIDGVNN------INH----VLNNidaiyrgmmtvpvrSPQRL 482
Cdd:cd09818 264 MHplipddidfrsaddGATGEEISLTDLAGGKARELLRKLGFADllysfgITHpgalTLHN--------------YPRFL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 483 TTSVTERlfGGSVDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEvpDENVRQRIGQLYR-TPDDLDFYVGGIL 561
Cdd:cd09818 330 RDLHRPD--GRVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLTG--DEEVAAELREVYGgDVEKVDLLVGLLA 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17534209 562 EQPAAGSLLGAT-FACVIGKQFERLRdGDRFY--YENPGVFTSPQLAELKRTTLSWVLCQTG 620
Cdd:cd09818 406 EPLPPGFGFSDTaFRIFILMASRRLK-SDRFFtnDFRPEVYTPEGMDWVNNNTMKSVLLRHF 466
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
285-617 |
5.07e-26 |
|
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: 111.97 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 285 IDASLIYG-SEAITArSLRFA--AMLRTSMIGGRMFPP----------------NTNPGSLT---------AGDGRAILF 336
Cdd:cd09816 131 IDLSQIYGlTEARTH-ALRLFkdGKLKSQMINGEEYPPylfedggvkmefpplvPPLGDELTpereaklfaVGHERFNLT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 337 VGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQESRKIVGGIVQVITYQEFV-------------PELIGDAsktilg 403
Cdd:cd09816 210 PGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYInhlspyhfklffdPELAFNE------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 404 ayNGYNPN---VEIGVLnefaagaYRLHGMIQETYpLVNSQFQEVNRYRFidgvNN---INHVLNN-IDAIyrgmmtvpv 476
Cdd:cd09816 284 --PWQRQNriaLEFNLL-------YRWHPLVPDTF-NIGGQRYPLSDFLF----NNdlvVDHGLGAlVDAA--------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 477 rSPQRLTTsVTERLFG---GSVDMAAvnIQRGRDHGLRSYNDYRRFCNLRPITSFNDWpeVPDENVRQRIGQLYRTPDDL 553
Cdd:cd09816 341 -SRQPAGR-IGLRNTPpflLPVEVRS--IEQGRKLRLASFNDYRKRFGLPPYTSFEEL--TGDPEVAAELEELYGDVDAV 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17534209 554 DFYVGGILEQPAAGSLLGATFACVIGKqferlrdgDRF-----------YYENPGVFTSPQLAELKRT-TLSWVLC 617
Cdd:cd09816 415 EFYVGLFAEDPRPNSPLPPLMVEMVAP--------DAFsgaltnpllspEVWKPSTFGGEGGFDIVKTaTLQDLVC 482
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
216-445 |
5.06e-12 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188651 Cd Length: 465 Bit Score: 68.52 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 216 FGQFVSHDITSNAAqnfcgcqnsgpmcaSIFAPPSDRsrrcipftrsfpicgtgqfgrVREQLNMNTAAIDASLIYGSEA 295
Cdd:cd09819 53 LGQFIDHDITLDTT--------------SSLAPRQID---------------------PAELRNFRTPALDLDSVYGGGP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 296 ITARslrFAAMLRTSMIGGRMFPPNTNPGSLT------------AGDGRAI---------LFVglAALHTSFLRLHNNVA 354
Cdd:cd09819 98 DGSP---YLYDQATPNDGAKLRVGRESPGGPGglpgdgardlprNGQGTALigdprndenLIV--AQLHLAFLRFHNAVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 355 ARLQnmNRHWNADRIFQESRKIVGGIVQVITYQEFVPELIG-DASKTILGA----YNGYNPNVEIGVLnEFAAGAYRL-H 428
Cdd:cd09819 173 DALR--AHGTPGDELFEEARRLVRWHYQWLVLNDFLPRICDpDVVDDVLANgrrfYRFFREGKPFMPV-EFSVAAYRFgH 249
|
250
....*....|....*..
gi 17534209 429 GMIQETYpLVNSQFQEV 445
Cdd:cd09819 250 SMVRASY-DYNRNFPDA 265
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
131-592 |
9.67e-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: 67.75 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 131 PDCSINQCFhkKYRSMDGTCNNLQNPVKGAAFTAFTRLMPAAYDDGfntlvsasrRNRPNPREVSVFLLSSE--RSLPGH 208
Cdd:cd09817 23 PDSYLGDNY--KYRKADGSNNNILNPRLGAAGSPYARSVPPKHDQP---------GVLPDPGLIFDTLLARDtgKFHPNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 209 VNSLLMLFGQFVSHDItsnaaqnfcgcqnsgpmcasifaPPSDRSRRCIpftrsfpicgtgqfgrvreqlNMNTAAIDAS 288
Cdd:cd09817 92 ISSMLFYLATIIIHDI-----------------------FRTDHRDMNI---------------------NNTSSYLDLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 289 LIYGSEAITARSLRfaamlrtSMIGGRMFPPntnpgslTAGDGRAILFV-GLAALHTSFLRLHNNVAARLQNMN-----R 362
Cdd:cd09817 128 PLYGSNQEEQNKVR-------TMKDGKLKPD-------TFSDKRLLGQPpGVCALLVMFNRFHNYVVEQLAQINeggrfT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 363 HWNADR------------IFQESRKIVGGI-VQVITYqefvpeligDASKTILGaYNGYN------PNVEIG-------- 415
Cdd:cd09817 194 PPGDKLdssakeekldedLFQTARLITCGLyINIVLH---------DYVRAILN-LNRTDstwtldPRVEIGrsltgvpr 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 416 -----VLNEFAaGAYRLHGMI--QETYPLvnsqfQEVNRYRFIDGVNNINHVLNNIDAIYRGMMTVPVRSPQR------- 481
Cdd:cd09817 264 gtgnqVSVEFN-LLYRWHSAIsaRDEKWT-----EDLFESLFGGKSPDEVTLKEFMQALGRFEALIPKDPSQRtfgglkr 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 482 --------------LTTSVTERL--FGG---SVDMAAVN---IQRGRDHGLRSYNDYRRFCNLRPITSFNDWpeVPDENV 539
Cdd:cd09817 338 gpdgrfrdedlvriLKDSIEDPAgaFGArnvPASLKVIEilgILQAREWNVATLNEFRKFFGLKPYETFEDI--NSDPEV 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 17534209 540 RQRIGQLYRTPDDLDFYVGGILEQ------PAAGSLLGATFACVIGKQFERLRDGDRFY 592
Cdd:cd09817 416 AEALELLYGHPDNVELYPGLVAEDakppmpPGSGLCPGYTISRAILSDAVALVRGDRFY 474
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
143-595 |
2.89e-11 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 66.71 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 143 YRSMDGTCNNLQNPVKGAAFTAFTRLMPAAyddgfntlVSASRRNRPNPREVSVFLLSSERSLPG--HVNSLLMLFGQFV 220
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGRNMPPV--------DQKDKLLDPHPSVVATKLLARKKFIDTgkQFNMIAASWIQFM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 221 SHDITSNAaqnfcgcQNSGPMcaSIFAPPSDRSRrCiPF-------TRSFPicgTGQFGRVREQLNMNTAAIDASLIYGS 293
Cdd:PLN02283 157 IHDWIDHL-------EDTQQI--ELTAPKEVASQ-C-PLksfkfykTKEVP---TGSPDIKTGSLNIRTPWWDGSVIYGS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 294 EAITARSLR-FA-AMLRTSMIGGRMFPPNTNPGSltaGDGRAiLFVGLAALHTSFLRLHNNVAARLQNMNRHWNADRIFQ 371
Cdd:PLN02283 223 NEKGLRRVRtFKdGKLKISEDGLLLHDEDGIPIS---GDVRN-SWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 372 ESRKIVGGIVQVITYQEFVPEL-------------------------IGDASKTILGAYNGYNPNVEIGV---LNEFAAG 423
Cdd:PLN02283 299 HARLVTSAVIAKIHTIDWTVELlktdtllagmranwygllgkkfkdtFGHIGGPILSGLVGLKKPNNHGVpysLTEEFTS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 424 AYRLHGMIQETYPLvnsqfqevnryRFIDGVNNINHVLNNIDAI------------------YRGMMT----------VP 475
Cdd:PLN02283 379 VYRMHSLLPDHLIL-----------RDITAAPGENKSPPLIEEIpmpeliglkgekklskigFEKLMVsmghqacgalEL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534209 476 VRSPQRLTTSVTERLFGGS----VDMAAVNIQRGRDHGLRSYNDYRRFCNLRPITSFNDWPEvpDENVRQRIGQLYrtPD 551
Cdd:PLN02283 448 WNYPSWMRDLVPQDIDGEDrpdhVDMAALEIYRDRERGVARYNEFRRNLLMIPISKWEDLTD--DEEAIEVLREVY--GD 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17534209 552 D---LDFYVGGILEQPAAGSLLGAT-FACVIGKQFERLrDGDRFYYEN 595
Cdd:PLN02283 524 DvekLDLLVGLMAEKKIKGFAISETaFFIFLLMASRRL-EADRFFTSN 570
|
|
| ShKT |
smart00254 |
ShK toxin domain; ShK toxin domain |
22-56 |
8.93e-08 |
|
ShK toxin domain; ShK toxin domain
Pssm-ID: 214586 [Multi-domain] Cd Length: 33 Bit Score: 48.53 E-value: 8.93e-08
10 20 30
....*....|....*....|....*....|....*
gi 17534209 22 CTDKHIHCFFWSQeGECeVNPRWMKKHCQKACGTC 56
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 ... |
21-56 |
7.76e-07 |
|
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.
Pssm-ID: 426319 Cd Length: 37 Bit Score: 45.85 E-value: 7.76e-07
10 20 30
....*....|....*....|....*....|....*...
gi 17534209 21 ECTDKHIHCFFWSQEGeCEVNP--RWMKKHCQKACGTC 56
Cdd:pfam01549 1 SCVDPHSDCASWAALG-CTSPFyqDFMKENCPKTCGFC 37
|
|
| PLN00052 |
PLN00052 |
prolyl 4-hydroxylase; Provisional |
19-56 |
4.13e-05 |
|
prolyl 4-hydroxylase; Provisional
Pssm-ID: 177683 [Multi-domain] Cd Length: 310 Bit Score: 46.20 E-value: 4.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 17534209 19 SEECTDKHIHCFFWSQEGECEVNPRWM------KKHCQKACGTC 56
Cdd:PLN00052 265 TEGCADKSAHCAEWAAAGECEKNPVYMvgaegaPGNCRKSCGVC 308
|
|
| |
