|
Name |
Accession |
Description |
Interval |
E-value |
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
237-781 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 701.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 237 YRSMDGTCNNPepQRSLWGAAGQPMERMLPPAYEDGIWTPRAhSSDGTPLLGARKISRTLLS-DVDRPHPKYNLMVMQFG 315
Cdd:pfam03098 1 YRTIDGSCNNL--KNPSWGAAGTPFARLLPPAYEDGVSAPRG-SSSGSPLPSPRLVSNKLFAgDSGIPDPNLTLLLMQWG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 316 QVLAHDISQTSSIRLEDGSLVQCCSPegkvalsPQQSHFACMPIHVEPDDEFFSAFGVRCLNFVRlslvPSPDCQL-SYG 394
Cdd:pfam03098 78 QFIDHDLTLTPESTSPNGSSCDCCCP-------PENLHPPCFPIPIPPDDPFFSPFGVRCMPFVR----SAPGCGLgNPR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 395 KQLTKVTHFVDASPVYGSSDEASRSLRAFRGGRLRM-MNDFGRDLLPLTNDKKACPSEEAGKSCFHSGDGRTNQIISLIT 473
Cdd:pfam03098 147 EQINQVTSFLDGSQVYGSSEETARSLRSFSGGLLKVnRSDDGKELLPFDPDGPCCCNSSGGVPCFLAGDSRANENPGLTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 474 LQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRFRLVPLhqgYSHDYNVNVNP 553
Cdd:pfam03098 227 LHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFGLLPL---PYNGYDPNVDP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 554 AITNEFSGAAYRMGHSSVDGKFQiRQEHGRIDEVVNIP--DVMFNPSRMRKREFyDDMLRTLYSQPMQQVDSSISQGLSR 631
Cdd:pfam03098 304 SISNEFATAAFRFGHSLIPPFLY-RLDENNVPEEPSLRlhDSFFNPDRLYEGGI-DPLLRGLATQPAQAVDNNFTEELTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 632 FLFRGDNPF-GLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQF----PIEIAQKLSRVYRTPDDIDLWVGGLLEK 706
Cdd:pfam03098 382 HLFGPPGEFsGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLtdviPNEVIAKLRELYGSVDDIDLWVGGLAEK 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571758 707 AVEGGVVGVTFAEIIADQFARFKQGDRYYYEYDngiNPGAFNPLQLQEIRKVTLARLLCDNSDrlTLQAVPLAAF 781
Cdd:pfam03098 462 PLPGGLVGPTFACIIGDQFRRLRDGDRFWYENG---NQGSFTPEQLEEIRKTSLARVICDNTD--IIETIQPNVF 531
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
396-767 |
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: 573.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 396 QLTKVTHFVDASPVYGSSDEASRSLRAFRGGRLRMMNDFGRDLLPLTNDKKA-CPSEEAGKSCFHSGDGRTNQIISLITL 474
Cdd:cd09823 3 QLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPTDdCSLSSAGKPCFLAGDGRVNEQPGLTSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 475 QILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRFRLVPLHQGYSHDYNVNVNPA 554
Cdd:cd09823 83 HTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNGYDPNVDPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 555 ITNEFSGAAYRMGHSSVDGKFQIRQEHGRIDEVVNIPDVMFNPSRMRKREFYDDMLRTLYSQPMQQVDSSISQGLSR-FL 633
Cdd:cd09823 163 ILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQKVDRFFTDELTThFF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 634 FRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFE----QFPIEIAQKLSRVYRTPDDIDLWVGGLLEKAVE 709
Cdd:cd09823 243 FRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDdllgIMSPETIQKLRRLYKSVDDIDLYVGGLSEKPVP 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 28571758 710 GGVVGVTFAEIIADQFARFKQGDRYYYEYDNGinPGAFNPLQLQEIRKVTLARLLCDN 767
Cdd:cd09823 323 GGLVGPTFACIIGEQFRRLRRGDRFWYENGGQ--PSSFTPAQLNEIRKVSLARIICDN 378
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
255-808 |
2.94e-122 |
|
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: 379.47 E-value: 2.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 255 GAAGQPMERMLPPAYEDGIWTPRAHSS----DGTPLLGARKISRTLL---SDVDRPHPKYNLMVMQFGQVLAHDISQT-- 325
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKerlyNGFTLPSVREVSNKIMrtsSTAVTPDDLYSHMLTVWGQYIDHDIDFTpq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 326 SSIRLEDGSLVQCcspegKVALSPQQShfaCMPIHVEPDDEFFSAFGvrCLNFVRLS----------LVPSPDCQLSYgK 395
Cdd:cd09825 81 SVSRTMFIGSTDC-----KMTCENQNP---CFPIQLPSEDPRILGRA--CLPFFRSSavcgtgdtstLFGNLSLANPR-E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 396 QLTKVTHFVDASPVYGSSDEASRSLRAFRG--GRLR---MMNDFGRDLLPLTNDKKAC----PSEEAGKSCFHSGDGRTN 466
Cdd:cd09825 150 QINGLTSFIDASTVYGSTLALARSLRDLSSddGLLRvnsKFDDSGRDYLPFQPEEVSScnpdPNGGERVPCFLAGDGRAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 467 QIISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRfrlvplHQGYSHD 546
Cdd:cd09825 230 EVLTLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQ------YGGYYEG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 547 YNVNVNPAITNEFSGAAYRMGHSSV-------DGKFqirQEHgriDEVVNIP--DVMFNPSRMRKREFYDDMLRTLYSQP 617
Cdd:cd09825 304 YDPTVNPTVSNVFSTAAFRFGHATIhptvrrlDENF---QEH---PVLPNLAlhDAFFSPWRLVREGGLDPVIRGLIGGP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 618 --MQQVDSSISQGLSRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQFPIEI-----AQKLSRVY 690
Cdd:cd09825 378 akLVTPDDLMNEELTEKLFVLSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIadqavADKILDLY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 691 RTPDDIDLWVGGLLEKAVEGGVVGVTFAEIIADQFARFKQGDRYYYEydngiNPGAFNPLQLQEIRKVTLARLLCDNSDr 770
Cdd:cd09825 458 KHPDNIDVWLGGLAEDFLPGARTGPLFACLIGKQMKALRDGDRFWWE-----NSNVFTDAQRRELRKHSLSRVICDNTG- 531
|
570 580 590
....*....|....*....|....*....|....*...
gi 28571758 771 ltLQAVPLAAFVRADHPgNQMIGCDDpnLPSVNLEAWR 808
Cdd:cd09825 532 --LTRVPPDAFQLGKFP-EDFVSCDS--IPGINLEAWR 564
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
372-796 |
1.99e-118 |
|
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: 365.09 E-value: 1.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 372 GVRCLNFVRLSLVpspdC----------QLSYGKQLTKVTHFVDASPVYGSSDEASRSLRAFRG--GRLR--MMNDFGRD 437
Cdd:cd09826 9 GHRCIEFVRSSAV----CgsgstsllfnSVTPREQINQLTSYIDASNVYGSSDEEALELRDLASdrGLLRvgIVSEAGKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 438 LLPLTNDKK-ACPSEEAGK--SCFHSGDGRTNQIISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQ 514
Cdd:cd09826 85 LLPFERDSPmDCRRDPNESpiPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 515 HITYNEFLPIIIGPQQMKrfrLVPLHQGyshdYNVNVNPAITNEFSGAAYRMGHSSV-------DGKFQ-IRQEHgride 586
Cdd:cd09826 165 HITYSHWLPKILGPVGME---MLGEYRG----YNPNVNPSIANEFATAAFRFGHTLInpilfrlDEDFQpIPEGH----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 587 vVNIPDVMFNPSRMRKREFYDDMLRTLYSQPMQQV--DSSISQGLSRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYL 664
Cdd:cd09826 233 -LPLHKAFFAPYRLVNEGGIDPLLRGLFATAAKDRvpDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYNDYR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 665 ELMGAPKLHSFEQFPIEIA-----QKLSRVYRTPDDIDLWVGGLLEKAVEGGVVGVTFAEIIADQFARFKQGDRYYYEyd 739
Cdd:cd09826 312 KFCNLSVAETFEDLKNEIKnddvrEKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYE-- 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571758 740 ngiNPGAFNPLQLQEIRKVTLARLLCDNSDRLTLqaVPLAAFVRADHPGNQmIGCDD 796
Cdd:cd09826 390 ---NPGVFSPAQLTQIKKTSLARVLCDNGDNITR--VQEDVFLVPGNPHGY-VSCES 440
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
394-774 |
6.30e-111 |
|
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: 344.68 E-value: 6.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 394 GKQLTKVTHFVDASPVYGSSDEASRSLRAFRGGRLRMMNDFGRDLLP-----LTNDKKACPSEeagkSCFHSGDGRTNQI 468
Cdd:cd09822 48 REQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAGDLLPfneagLPNDNGGVPAD----DLFLAGDVRANEN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 469 ISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMkrfrlvPLHQGyshdYN 548
Cdd:cd09822 124 PGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLGENAL------PAYSG----YD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 549 VNVNPAITNEFSGAAYRMGHSSVDGKFQIRQEHGRIDEVVNIPDVMFNPSRMRKREFyDDMLRTLYSQPMQQVDSSISQG 628
Cdd:cd09822 194 ETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLALRDAFFNPDELEENGI-DPLLRGLASQVAQEIDTFIVDD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 629 LSRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQ--FPIEIAQKLSRVYRTPDDIDLWVGGLLEK 706
Cdd:cd09822 273 VRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDitSDPDLAARLASVYGDVDQIDLWVGGLAED 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571758 707 AVEGGVVGVTFAEIIADQFARFKQGDRYYYEYDNginpgaFNPLQLQEIRKVTLARLLCDNSDRLTLQ 774
Cdd:cd09822 353 HVNGGLVGETFSTIIADQFTRLRDGDRFFYENDD------LLLDEIADIENTTLADVIRRNTDVDDIQ 414
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
396-767 |
4.54e-106 |
|
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: 330.54 E-value: 4.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 396 QLTKVTHFVDASPVYGSSDEASRSLRAFRGGRLRM----MNDFGRDLLPLTNDKKACPSEEAGKS-CFHSGDGRTNQIIS 470
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTnevkGPSYGTELLPFNNPNPSMGTIGLPPTrCFIAGDPRVNENLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 471 LITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRFRLVPLHqgyshdYNVN 550
Cdd:cd05396 81 LLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLF------PDPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 551 VNPAITNEFSGAAYRMGHSSVDGKFQIRQEHGRIDEVVNIP--DVMFNPSR-MRKREFYDDMLRTLYSQPMQQVDSSISQ 627
Cdd:cd05396 155 VVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQPKEIPDVPlkDFFFNTSRsILSDTGLDPLLRGFLRQPAGLIDQNVDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 628 GlsRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQ--FPIEIAQKLSRVYRTPDDIDLWVGGLLE 705
Cdd:cd05396 235 V--MFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDilTDPELAKKLAELYGDPDDVDLWVGGLLE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571758 706 KAVEGGVVGVTFAEIIADQFARFKQGDRYYYEydngiNPGAFNPLQLQEIRKV-TLARLLCDN 767
Cdd:cd05396 313 KKVPPARLGELLATIILEQFKRLVDGDRFYYV-----NYNPFGKSGKEELEKLiSLADIICLN 370
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
396-787 |
3.29e-82 |
|
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: 268.90 E-value: 3.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 396 QLTKVTHFVDASPVYGSSDEASRSLR--AFRGGRLRMMNDF---GRDLLPLTN-DKKACPSEE--AGKSCFHSGDGRTNQ 467
Cdd:cd09824 14 QINALTSFVDASMVYGSEPSLAK*LRnlTNQLGLLAVNQRFtdnGLALLPFENlHNDPCALRNtsANIPCFLAGDTRVSE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 468 IISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRfrlVPLHQGyshdY 547
Cdd:cd09824 94 NPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAAR---LPPYRG----Y 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 548 NVNVNPAITNEFSGAAyRMGHSSVDgKFQIR-----QEHGRIDEvVNIPDVMFNPSRMRKREFYDDMLRTLYSQP---MQ 619
Cdd:cd09824 167 NESVDPRIANVFTTAF-RRGHTTVQ-PFVFRldenyQPHPPNPQ-VPLHKAFFASWRIIREGGIDPILRGLMATPaklNN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 620 QVDSSISQgLSRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQFP-----IEIAQKLSRVYRTPD 694
Cdd:cd09824 244 QNQMLVDE-LRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAavlnnTVLARKLLDLYGTPD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 695 DIDLWVGGLLEKAVEGGVVGVTFAEIIADQFARFKQGDRYYYEydngiNPGAFNPLQLQEIRKVTLARLLCDNSDRLTlq 774
Cdd:cd09824 323 NIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWE-----NPGVFTEEQRESLRSVSLSRIICDNTGITK-- 395
|
410
....*....|...
gi 28571758 775 aVPLAAFVRADHP 787
Cdd:cd09824 396 -VPRDPFQPNSYP 407
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
240-798 |
2.66e-74 |
|
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: 252.22 E-value: 2.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 240 MDGTCNN---PEpqrslWGAAGQPMERMLPPAYEDGIWTPrahSSDGTPllGARKISRTLLSDVDRPHPKYNLMVMQ--F 314
Cdd:cd09820 1 YDGWYNNlahPE-----WGAADSRLTRRLPAHYSDGVYAP---SGEERP--NPRSLSNLLMKGESGLPSTRNRTALLvfF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 315 GQVLAHDISQTSSirledgslvQCCSPEgkvalspqqshfaCMPIHVEPDDEFF--SAFGVRCLNFVRLSLVP----SPD 388
Cdd:cd09820 71 GQHVVSEILDASR---------PGCPPE-------------YFNIEIPKGDPVFdpECTGNIELPFQRSRYDKntgySPN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 389 cqlSYGKQLTKVTHFVDASPVYGSSDEASRSLRAFRGGRLRMMNDFG-----RDLLPLTNDKKACPSEEAGKSCFHS-GD 462
Cdd:cd09820 129 ---NPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSGGRLASGDDGGfprrnTNRLPLANPPPPSYHGTRGPERLFKlGN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 463 GRTNQIISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGpqqmkrfRLVPLHQG 542
Cdd:cd09820 206 PRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLG-------TNVPPYTG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 543 YSHDynvnVNPAITNEFSGAAYRMGHSSVDGKFQIRQEHGRIDEVVNIPDVMF---------NPSRMRKREFYDDMLRTL 613
Cdd:cd09820 279 YKPH----VDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNFREVLTTSGGSPalrlcntywNSQEPLLKSDIDELLLGM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 614 YSQPMQQVDSSISQGLSRFLFrGDNPF-GLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQF-------PIEIAQK 685
Cdd:cd09820 355 ASQIAEREDNIIVEDLRDYLF-GPLEFsRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDInpdlfkkDPELLER 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 686 LSRVY-RTPDDIDLWVGGLLEKAveGGVVGVTFAEIIADQFARFKQGDRYYYEydNGINpGAFNPLQLQEIRKVTLARLL 764
Cdd:cd09820 434 LAELYgNDLSKLDLYVGGMLESK--GGGPGELFRAIILDQFQRLRDGDRFWFE--NVKN-GLFTAEEIEEIRNTTLRDVI 508
|
570 580 590
....*....|....*....|....*....|....*.
gi 28571758 765 --CDNSDRLTLQAVPLaaFVRADHPgnqmigCDDPN 798
Cdd:cd09820 509 laVTDIDNTDLQKNVF--FWKNGDP------CPQPK 536
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
394-736 |
4.41e-37 |
|
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: 147.18 E-value: 4.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 394 GKQLTKVTHFVDASPVYGSSDEASRSLRAFRG-----GRLRM-------------MNDFGRDLLP-------LTNDKKAC 448
Cdd:cd09821 81 GEHTNVTTPFVDQNQTYGSHASHQVFLREYDGdgvatGRLLEgatggsartghafLDDIAHNAAPkgglgslRDNPTEDP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 449 PSEEAGKSCF------H--SGDGRTNQIISLITLQILLAREHNRV----------AGALHELNPSASD------ETLFQE 504
Cdd:cd09821 161 PGPGAPGSYDnelldaHfvAGDGRVNENIGLTAVHTVFHREHNRLvdqikdtllqSADLAFANEAGGNnlawdgERLFQA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 505 ARRIVIAEMQHITYNEFLPIIIGpqQMKRFrlvplhqGYSHDYNVNVNPAITNEFSGAAYRMGHS---------SVDGKF 575
Cdd:cd09821 241 ARFANEMQYQHLVFEEFARRIQP--GIDGF-------GSFNGYNPEINPSISAEFAHAVYRFGHSmltetvtriGPDADE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 576 QIRQEHGRIDEVVNipDVMFNPSRMRKREFYDDMLRTLYSQPMQQVDSSISQGLSRFLFRgdnpFGLDLAAINIQRGRDQ 655
Cdd:cd09821 312 GLDNQVGLIDAFLN--PVAFLPATLYAEEGAGAILRGMTRQVGNEIDEFVTDALRNNLVG----LPLDLAALNIARGRDT 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 656 GL-----------------------RSYNDYLELMGAPKlhSFEQF------------PIEIAQKlsRVYRTP------- 693
Cdd:cd09821 386 GLptlnearaqlfaatgdtilkapyESWNDFGARLKNPE--SLINFiaaygthltitgATTLAAK--RAAAQDlvdggdg 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571758 694 ----------------------DDIDLWVGGLLEKAVE-GGVVGVTFAEIIADQFARFKQGDRYYY 736
Cdd:cd09821 462 apadradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYY 527
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
400-765 |
1.52e-32 |
|
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: 132.41 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 400 VTHFVDASPVYGSSDEASRSLRAF-RGGRLRMMNDfgrDLLPLTndkkacpsEEAGKScfHSGDGRtNQIISLITLQILL 478
Cdd:cd09818 90 NTHWWDGSQIYGSTEEAQKRLRTFpPDGKLKLDAD---GLLPVD--------EHTGLP--LTGFND-NWWVGLSLLHTLF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 479 AREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIII--------------GPQQmKRFRLVPLHQGYS 544
Cdd:cd09818 156 VREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILahptleiamranwwGLLG-ERLKRVLGRDGTS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 545 H-----------DYNVNVnpAITNEFSgAAYRMgHSSVDGKFQIRQEH-GRIDEVVNIPDVMFNPSRMRKREFydDMLRT 612
Cdd:cd09818 235 EllsgipgsppnHHGVPY--SLTEEFV-AVYRM-HPLIPDDIDFRSADdGATGEEISLTDLAGGKARELLRKL--GFADL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 613 LYSQPMQQVDSSISQGLSRFL--FRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQFP--IEIAQKLSR 688
Cdd:cd09818 309 LYSFGITHPGALTLHNYPRFLrdLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLTgdEEVAAELRE 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28571758 689 VYR-TPDDIDLWVGGLLEKAVEG-GVVGVTFAEIIADQFARFKQgDRYYYEYdngINPGAFNPLQLQEIRKVTLARLLC 765
Cdd:cd09818 389 VYGgDVEKVDLLVGLLAEPLPPGfGFSDTAFRIFILMASRRLKS-DRFFTND---FRPEVYTPEGMDWVNNNTMKSVLL 463
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
394-767 |
4.56e-32 |
|
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: 130.85 E-value: 4.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 394 GKQLTKVTHFVDASPVYGSSDEASRSLRAFRGGRL--RMMND--FGRDLLPLTNDK----------KACPSEEAGKSCFH 459
Cdd:cd09816 121 DPRRNTSNHGIDLSQIYGLTEARTHALRLFKDGKLksQMINGeeYPPYLFEDGGVKmefpplvpplGDELTPEREAKLFA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 460 SGDGRTNQIISLITLQILLAREHNRVAGALHELNPSASDETLFQEARRIVIAEMQHITYNEFLPIIIGpqqmKRFRLVPl 539
Cdd:cd09816 201 VGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSP----YHFKLFF- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 540 HQGYSHDYNVNVNPAITNEFSgAAYRMgHSSVDGKFQIRqehgriDEVVNIPDVMFNPSRMrkrefYDDMLRTLysqpmq 619
Cdd:cd09816 276 DPELAFNEPWQRQNRIALEFN-LLYRW-HPLVPDTFNIG------GQRYPLSDFLFNNDLV-----VDHGLGAL------ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 620 qVDSSISQGLSRFLFRGDNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHSFEQFP--IEIAQKLSRVYRTPDDID 697
Cdd:cd09816 337 -VDAASRQPAGRIGLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTgdPEVAAELEELYGDVDAVE 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571758 698 LWVGGLLEKAVEGGVVGVTFAEIIAdQFArFKQ------GDRYYYeydngiNPGAFNPLQLQEIRKV-TLARLLCDN 767
Cdd:cd09816 416 FYVGLFAEDPRPNSPLPPLMVEMVA-PDA-FSGaltnplLSPEVW------KPSTFGGEGGFDIVKTaTLQDLVCRN 484
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
461-764 |
1.10e-18 |
|
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: 89.71 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 461 GDGRT--NQIISLITLQILlaREHNRVAGALHELNPSASDetLFQEARRIVIAEMQHITYNEFLPIIIGPQQMKRFrlvp 538
Cdd:cd09819 147 GDPRNdeNLIVAQLHLAFL--RFHNAVVDALRAHGTPGDE--LFEEARRLVRWHYQWLVLNDFLPRICDPDVVDDV---- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 539 LHQGYSH--DYNVNVnPAITNEFSGAAYRMGHSSVDGKFQIRQEHGRidevvNIPDVMFNPSRMRK-------------- 602
Cdd:cd09819 219 LANGRRFyrFFREGK-PFMPVEFSVAAYRFGHSMVRASYDYNRNFPD-----ASLELLFTFTGGGEgdlggfsplpenwi 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 603 ---REFY--DDMLRTlysQPMQQVDSSISQGLSRfLFRG---DNPFGLDLAAINIQRGRDQGLRSYNDYLELMGAPKLHs 674
Cdd:cd09819 293 idwRRFFdiDGSAPP---QFARKIDTKLAPPLFD-LPNGgvgLAPPMKSLAFRNLLRGYRLGLPSGQAVARALGIAPLT- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 675 feqfPIEIAQKLSRV---------YRTPddidLWVGGLLEKAVEG-----GVVGvtfAEIIADQFARFKQGDRYYYEyDN 740
Cdd:cd09819 368 ----ADELGDGEDGApavaggglhEATP----LWFYILKEAEVRGggnrlGPVG---SRIVAEVFIGLLEGDPSSYL-SL 435
|
330 340
....*....|....*....|....*.
gi 28571758 741 GINPG--AFNPLQLQEIrkVTLARLL 764
Cdd:cd09819 436 GFNPDwtPTLPSATPGI--FTMADLL 459
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
237-710 |
7.09e-15 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 78.65 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 237 YRSMDGTCNNPE-----PQRSLWGaagqpmERMLPPAYEDGIWTPRahssdgtPLLGARK-ISRTLLSDVDRphpKYNLM 310
Cdd:PLN02283 85 YRTADGKCNDPFnegagSQGTFFG------RNMPPVDQKDKLLDPH-------PSVVATKlLARKKFIDTGK---QFNMI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 311 VMQFGQVLAHDISQtssiRLEDGSLVQCCSPEGKVALSPQQShfacmpihvepddeffsafgvrcLNFVRLSLVPSPDCQ 390
Cdd:PLN02283 149 AASWIQFMIHDWID----HLEDTQQIELTAPKEVASQCPLKS-----------------------FKFYKTKEVPTGSPD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 391 LSYGKQLTKvTHFVDASPVYGSSDEASRSLRAFRGGRLRMMNDfGRdllpLTNDKKACPSeeagkscfhSGDGRtNQIIS 470
Cdd:PLN02283 202 IKTGSLNIR-TPWWDGSVIYGSNEKGLRRVRTFKDGKLKISED-GL----LLHDEDGIPI---------SGDVR-NSWAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 471 LITLQILLAREHNRVAGALHELNPSASDETLFQEARRI---VIAEMQHITYN-EFLPIIIGPQQM---------KRFR-- 535
Cdd:PLN02283 266 VSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVtsaVIAKIHTIDWTvELLKTDTLLAGMranwygllgKKFKdt 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 536 -----------LVPLHQGYSHdynvNVNPAITNEFSgAAYRMgHSSVDGKFQIRQEHGRIDEVVNIPDVMFNP------- 597
Cdd:PLN02283 346 fghiggpilsgLVGLKKPNNH----GVPYSLTEEFT-SVYRM-HSLLPDHLILRDITAAPGENKSPPLIEEIPmpeligl 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 598 ---SRMRKREFYDDMLR---------TLYSQPM-------QQVDSSisqglsrflfrgDNPFGLDLAAINIQRGRDQGLR 658
Cdd:PLN02283 420 kgeKKLSKIGFEKLMVSmghqacgalELWNYPSwmrdlvpQDIDGE------------DRPDHVDMAALEIYRDRERGVA 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 28571758 659 SYNDYLELMGAPKLHSFEQFP--IEIAQKLSRVYrtPDDI---DLWVGGLLEKAVEG 710
Cdd:PLN02283 488 RYNEFRRNLLMIPISKWEDLTddEEAIEVLREVY--GDDVeklDLLVGLMAEKKIKG 542
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
649-739 |
2.74e-04 |
|
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: 44.25 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571758 649 IQRGRDQGLRSYNDYLELMGAPKLHSFEQF---PiEIAQKLSRVYRTPDDIDLWVGGLLEKAVEGGVVGV-------TFA 718
Cdd:cd09817 380 ILQAREWNVATLNEFRKFFGLKPYETFEDInsdP-EVAEALELLYGHPDNVELYPGLVAEDAKPPMPPGSglcpgytISR 458
|
90 100
....*....|....*....|..
gi 28571758 719 EIIADQFArFKQGDRYY-YEYD 739
Cdd:cd09817 459 AILSDAVA-LVRGDRFYtVDYN 479
|
|
| |
