|
Name |
Accession |
Description |
Interval |
E-value |
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
170-609 |
0e+00 |
|
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: 948.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 170 PNDPRVRSGARCMFFVRSSPVCGSGMTSLLMNSVYPREQINQLTSYIDASNVYGSTDHEARSIRDLASHRGLLRQGIVQR 249
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVTPREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGIVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 250 SGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVG 329
Cdd:cd09826 81 AGKPLLPFERDSPMDCRRDPNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 330 AEIQHITYRHWLPKILGEVGMKMLGEYRGYDPSVNAGIFNAFATAAFRFGHTLINPLLYRLDENFEPIPQGHVPLHKAFF 409
Cdd:cd09826 161 AQMQHITYSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPEGHLPLHKAFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 410 SPFRIVNEGGIDPLLRGLFGVAGKMRIPSQLLNTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAY 489
Cdd:cd09826 241 APYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYNDYRKFCNLSVAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 490 TFEDLKNEIKSPVIREKLQRLYGSTLNIDLFPALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENPGVFSPAQLT 569
Cdd:cd09826 321 TFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQLT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907089070 570 QLKQTSLARILCDNSDNITRVQQDVFRVAEFPHGYSSCED 609
Cdd:cd09826 401 QIKKTSLARVLCDNGDNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
47-595 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 777.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 47 YRTHDGTCNNLQHPMWGASLTAFERLLKAVYENGFNTPRGINsqrqyNGHVLPMPRLVSTTLIGTEVITPDEQFTHMLMQ 126
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFAGDSGIPDPNLTLLLMQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 127 WGQFLDHDLDSTVVALSQARFSDGQHCSsvCSN-DPPCFSVMIPPNDPRV-RSGARCMFFVRSSPVCGSGmtsllmnsvY 204
Cdd:pfam03098 76 WGQFIDHDLTLTPESTSPNGSSCDCCCP--PENlHPPCFPIPIPPDDPFFsPFGVRCMPFVRSAPGCGLG---------N 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 205 PREQINQLTSYIDASNVYGSTDHEARSIRDLasHRGLLRQGIVqRSGKPLLPFATGPPTECMRdenESPIPCFLAGDHRA 284
Cdd:pfam03098 145 PREQINQVTSFLDGSQVYGSSEETARSLRSF--SGGLLKVNRS-DDGKELLPFDPDGPCCCNS---SGGVPCFLAGDSRA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 285 NEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILGEVGMKMLG----EYRGYD 360
Cdd:pfam03098 219 NENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFGllplPYNGYD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 361 PSVNAGIFNAFATAAFRFGHTLINPLLYRLDENFEPIPQgHVPLHKAFFSPFRIVnEGGIDPLLRGLFGVAGKMriPSQL 440
Cdd:pfam03098 299 PNVDPSISNEFATAAFRFGHSLIPPFLYRLDENNVPEEP-SLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQA--VDNN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 441 LNTELTERLFS-MAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEIKSPVIrEKLQRLYGSTLNIDL 519
Cdd:pfam03098 375 FTEELTNHLFGpPGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVI-AKLRELYGSVDDIDL 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089070 520 FPALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENP--GVFSPAQLTQLKQTSLARILCDNSDNITRVQQDVF 595
Cdd:pfam03098 454 WVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTDIIETIQPNVF 531
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
63-620 |
0e+00 |
|
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: 690.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 63 GASLTAFERLLKAVYENGFNTPRGINSQRQYNGHVLPMPRLVSTTLIGT--EVITPDEQFTHMLMQWGQFLDHDLDSTVV 140
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTssTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 141 ALSQARFSDGQHCSSVCSNDPPCFSVMIPPNDPRVRSGArCMFFVRSSPVCGSGMTSLLMNSV---YPREQINQLTSYID 217
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRA-CLPFFRSSAVCGTGDTSTLFGNLslaNPREQINGLTSFID 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 218 ASNVYGSTDHEARSIRDLASHRGLLR-QGIVQRSGKPLLPFATGPPTECMRDENESP-IPCFLAGDHRANEQLGLTSMHT 295
Cdd:cd09825 160 ASTVYGSTLALARSLRDLSSDDGLLRvNSKFDDSGRDYLPFQPEEVSSCNPDPNGGErVPCFLAGDGRASEVLTLTASHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 296 LWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILGEVGMKMLGE-YRGYDPSVNAGIFNAFATA 374
Cdd:cd09825 240 LWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGyYEGYDPTVNPTVSNVFSTA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 375 AFRFGHTLINPLLYRLDENFEPIPQ-GHVPLHKAFFSPFRIVNEGGIDPLLRGLFGVAGKMRIPSQLLNTELTERLFSMA 453
Cdd:cd09825 320 AFRFGHATIHPTVRRLDENFQEHPVlPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFVLS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 454 HTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEIKSPVIREKLQRLYGSTLNIDLFPALMVEDLVPGSR 533
Cdd:cd09825 400 NSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 534 LGPTLMCLLSTQFRRLRDGDRLWYENPGVFSPAQLTQLKQTSLARILCDNSDnITRVQQDVFRVAEFPHGYSSCEDIPRV 613
Cdd:cd09825 480 TGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTG-LTRVPPDAFQLGKFPEDFVSCDSIPGI 558
|
....*..
gi 1907089070 614 DLRVWQD 620
Cdd:cd09825 559 NLEAWRE 565
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
206-583 |
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: 547.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 206 REQINQLTSYIDASNVYGSTDHEARSIRDLasHRGLLRqgIVQRSGKPLLPFATGPPTECMRDENESPipCFLAGDHRAN 285
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTF--KGGLLK--TQRRNGRELLPFSNNPTDDCSLSSAGKP--CFLAGDGRVN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 286 EQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILGEVGMKML-------GEYRG 358
Cdd:cd09823 75 EQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 359 YDPSVNAGIFNAFATAAFRFGHTLINPLLYRLDENFepIPQGHVPLHKAFFSPFRIVNEGGIDPLLRGLfgvagkMRIPS 438
Cdd:cd09823 155 YDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENY--RPQGSVNLHDLFFNPDRLYEEGGLDPLLRGL------ATQPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 439 QLLNTELT-----ERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEIkSPVIREKLQRLYGS 513
Cdd:cd09823 227 QKVDRFFTdelttHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYKS 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907089070 514 TLNIDLFPALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENPGV---FSPAQLTQLKQTSLARILCDN 583
Cdd:cd09823 306 VDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
187-604 |
1.36e-169 |
|
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: 495.02 E-value: 1.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 187 SSPVCGSGMTSllmnsvypREQINQLTSYIDASNVYGSTDHEARSIRDLASHRGLLRqgIVQR---SGKPLLPFATGPPT 263
Cdd:cd09824 1 SCGACTSKRNV--------REQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLA--VNQRftdNGLALLPFENLHND 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 264 ECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPK 343
Cdd:cd09824 71 PCALRNTSANIPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 344 ILGEVGMKMLGEYRGYDPSVNAGIFNAFATAaFRFGHTLINPLLYRLDENFEPIPQ-GHVPLHKAFFSPFRIVNEGGIDP 422
Cdd:cd09824 151 ILGEDAAARLPPYRGYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPnPQVPLHKAFFASWRIIREGGIDP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 423 LLRGLFGVAGKMRIPSQLLNTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEIKSPV 502
Cdd:cd09824 230 ILRGLMATPAKLNNQNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 503 IREKLQRLYGSTLNIDLFPALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENPGVFSPAQLTQLKQTSLARILCD 582
Cdd:cd09824 310 LARKLLDLYGTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICD 389
|
410 420
....*....|....*....|..
gi 1907089070 583 NSdNITRVQQDVFRVAEFPHGY 604
Cdd:cd09824 390 NT-GITKVPRDPFQPNSYPRDF 410
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
97-597 |
1.69e-134 |
|
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: 405.16 E-value: 1.69e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 97 VLPMPRLVSTTLI-GTEVITPDEQFTHMLMQWGQFLDHDLDstvvaLSQARfsdgqhcssvcsndppcfsvmippndprv 175
Cdd:cd09822 1 DRPSPREISNAVAdQTESIPNSRGLSDWFWVWGQFLDHDID-----LTPDN----------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 176 rsgarcmffvrsspvcgsgmtsllmnsvyPREQINQLTSYIDASNVYGSTDHEARSIRDLAShrGLLRqgIVQRSGKPLL 255
Cdd:cd09822 47 -----------------------------PREQINAITAYIDGSNVYGSDEERADALRSFGG--GKLK--TSVANAGDLL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 256 PFATgpPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHI 335
Cdd:cd09822 94 PFNE--AGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAI 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 336 TYRHWLPKILGEvgmKMLGEYRGYDPSVNAGIFNAFATAAFRFGHTLINPLLYRLDENfePIPQGHVPLHKAFFSPFRIV 415
Cdd:cd09822 172 TYNEFLPALLGE---NALPAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDED--GTEATSLALRDAFFNPDELE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 416 nEGGIDPLLRGLfgvagkMRIPSQLLNTELTE--R--LFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTF 491
Cdd:cd09822 247 -ENGIDPLLRGL------ASQVAQEIDTFIVDdvRnfLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 492 EDLkneIKSPVIREKLQRLYGSTLNIDLFPALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENPgVFSPAQLTQL 571
Cdd:cd09822 320 SDI---TSDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-DLLLDEIADI 395
|
490 500
....*....|....*....|....*.
gi 1907089070 572 KQTSLARILCDNSDNITrVQQDVFRV 597
Cdd:cd09822 396 ENTTLADVIRRNTDVDD-IQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
208-583 |
7.72e-104 |
|
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: 323.99 E-value: 7.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 208 QINQLTSYIDASNVYGSTDHEARSIRDLasHRGLLR-QGIVQRS-GKPLLPFATGPPTECMRdeNESPIPCFLAGDHRAN 285
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTF--KGGLLKtNEVKGPSyGTELLPFNNPNPSMGTI--GLPPTRCFIAGDPRVN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 286 EQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILGEVGM-KMLGEYRGYDPSVN 364
Cdd:cd05396 77 ENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDpRDDLVLLFPDPDVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 365 AGIFNAFATAAFRFGHTLINPLLYRLDENFEPIPQGHVPLHKAFFSPFRIVN-EGGIDPLLRGLFGVagkmriPSQLL-- 441
Cdd:cd05396 157 PYVLSEFFTAAYRFGHSLVPEGVDRIDENGQPKEIPDVPLKDFFFNTSRSILsDTGLDPLLRGFLRQ------PAGLIdq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 442 NTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLkneIKSPVIREKLQRLYGSTLNIDLFP 521
Cdd:cd05396 231 NVDDVMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDI---LTDPELAKKLAELYGDPDDVDLWV 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907089070 522 ALMVEDLVPGSRLGPTLMCLLSTQFRRLRDGDRLWYENPGVFSPAQLTQL-KQTSLARILCDN 583
Cdd:cd05396 308 GGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELeKLISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
51-595 |
1.59e-82 |
|
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: 273.79 E-value: 1.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 51 DGTCNNLQHPMWGASLTAFERLLKAVYENGFNTPRGINsqrqynghvLPMPRLVSTTLIGTEVITPDEqfthmlmqwgqf 130
Cdd:cd09820 2 DGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPRSLSNLLMKGESGLPST------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 131 ldhdLDSTVVALSqarFsdGQHCSS--VCSNDPPC----FSVMIPPNDP---RVRSGARCMFFVRSSPVCGSGMTSllmN 201
Cdd:cd09820 61 ----RNRTALLVF---F--GQHVVSeiLDASRPGCppeyFNIEIPKGDPvfdPECTGNIELPFQRSRYDKNTGYSP---N 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 202 SvyPREQINQLTSYIDASNVYGSTDHEARSIRDLasHRGLLRQGivqrSGKPLLPFATG------PPTECMRdENESPIP 275
Cdd:cd09820 129 N--PREQLNEVTSWIDGSSIYGSSKAWSDALRSF--SGGRLASG----DDGGFPRRNTNrlplanPPPPSYH-GTRGPER 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 276 CFLAGDHRANEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILGEvgmkMLGE 355
Cdd:cd09820 200 LFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGT----NVPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 356 YRGYDPSVNAGIFNAFATAAFRFGHTLINPLLYRLDE--NFEPIPQGHVPLHK-----AFFSPFRIVNEGGIDPLlrgLF 428
Cdd:cd09820 276 YTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRqcNFREVLTTSGGSPAlrlcnTYWNSQEPLLKSDIDEL---LL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 429 GVAgkmripSQLLNTE-------LTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEI--K 499
Cdd:cd09820 353 GMA------SQIAEREdniivedLRDYLFGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLfkK 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 500 SPVIREKLQRLYG-STLNIDLFPALMVEDLvpGSRLGPTLMCLLSTQFRRLRDGDRLWYENP--GVFSPAQLTQLKQTSL 576
Cdd:cd09820 427 DPELLERLAELYGnDLSKLDLYVGGMLESK--GGGPGELFRAIILDQFQRLRDGDRFWFENVknGLFTAEEIEEIRNTTL 504
|
570 580
....*....|....*....|
gi 1907089070 577 AR-ILCDNSDNITRVQQDVF 595
Cdd:cd09820 505 RDvILAVTDIDNTDLQKNVF 524
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
115-602 |
2.76e-41 |
|
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: 159.89 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 115 TPDEQ----FTHMLMQWGQFLDHDLDSTvvalsqarfsdgqhcsSVCSNDPpcfsVMIP--PNDPRVRSGARCMFFVRSS 188
Cdd:cd09821 4 APDAGlsapYNSWMTFFGQFFDHGLDFI----------------PKGGNGT----VLIPlpPDDPLYDLGRGTNGMALDR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 189 PVCGSGMTSLLMNSVYPREQINQLTSYIDASNVYGSTdhearsirdlASHRGLLR----------------QGIVQRSGK 252
Cdd:cd09821 64 GTNNAGPDGILGTADGEGEHTNVTTPFVDQNQTYGSH----------ASHQVFLReydgdgvatgrllegaTGGSARTGH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 253 PLL-----PFATGPPTECMRDENESPIPC---------------FLAGDHRANEQLGLTSMHTLWFREHNRI-------- 304
Cdd:cd09821 134 AFLddiahNAAPKGGLGSLRDNPTEDPPGpgapgsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRLvdqikdtl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 305 --AAELLKLNPH------WDGDTVYHETRKIVGAEIQHITYRHWLPKILGevGMKMLGEYRGYDPSVNAGIFNAFATAAF 376
Cdd:cd09821 214 lqSADLAFANEAggnnlaWDGERLFQAARFANEMQYQHLVFEEFARRIQP--GIDGFGSFNGYNPEINPSISAEFAHAVY 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 377 RFGHTLINPLLYRLDENFE-----PIPQGHVPLHKAFFSPFRIVNEGGIDPLLRGLfgvagkMRIPSQLLNTELTERLFS 451
Cdd:cd09821 292 RFGHSMLTETVTRIGPDADegldnQVGLIDAFLNPVAFLPATLYAEEGAGAILRGM------TRQVGNEIDEFVTDALRN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 452 MAHTVALDLAAINIQRGRDHGIP--------------------PY-----------HDYRVYcNLSAAY-------TFED 493
Cdd:cd09821 366 NLVGLPLDLAALNIARGRDTGLPtlnearaqlfaatgdtilkaPYeswndfgarlkNPESLI-NFIAAYgthltitGATT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 494 LKNEI-----------KSPVIREKLQRLYGSTL-------NIDLFPALMVEDLVP-GSRLGPTLMCLLSTQFRRLRDGDR 554
Cdd:cd09821 445 LAAKRaaaqdlvdggdGAPADRADFMNAAGAGAgtvkgldNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDR 524
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907089070 555 LWY--ENPGVfspAQLTQLKQTSLARILCDNSDnITRVQQDVFRVAEFPH 602
Cdd:cd09821 525 FYYlsRTAGL---DLLNQLENNTFADMIMRNTG-ATHLPQDIFSVPDYDT 570
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
48-581 |
3.02e-29 |
|
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: 122.39 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 48 RTHDGTCNNLQHPMWGASLTAFERllkavyengfNTPRGINSQRQYNGHVLPMPRLVSTTLIGTEVITPDEQFTHMLMQW 127
Cdd:cd09818 1 RTADGSYNDLDNPSMGSVGTRFGR----------NVPLDATFPEDKDELLTPNPRVISRRLLARTEFKPATSLNLLAAAW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 128 GQFLDHDldstvvalsqaRFSDGqhcssvcsndPPCFsvmippndprvrsgarcmffvrsspvcgsgmtsllmnsvypre 207
Cdd:cd09818 71 IQFMVHD-----------WFSHG----------PPTY------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 208 qINQLTSYIDASNVYGSTDHEARSIRdLASHRGLLRqgiVQRSGkpLLPfatgpptecmRDENESPIpcfLAGDHRaNEQ 287
Cdd:cd09818 87 -INTNTHWWDGSQIYGSTEEAQKRLR-TFPPDGKLK---LDADG--LLP----------VDEHTGLP---LTGFND-NWW 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 288 LGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKILG----EVGMK-----MLGEY-- 356
Cdd:cd09818 146 VGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAhptlEIAMRanwwgLLGERlk 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 357 ----RGYDPSVNAGIF----NAFA---------TAAFRFgHTLInPLLYRLdENFEPIPQGH-VPLHKAFFspfrivneG 418
Cdd:cd09818 226 rvlgRDGTSELLSGIPgsppNHHGvpyslteefVAVYRM-HPLI-PDDIDF-RSADDGATGEeISLTDLAG--------G 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 419 GIDPLLRGL--------FGVA--GKMRipsqLLNTELTERLFSMAHTVALDLAAINIQRGRDHGIPPYHDYRVYCNLSAA 488
Cdd:cd09818 295 KARELLRKLgfadllysFGIThpGALT----LHNYPRFLRDLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLHLPPA 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 489 YTFEDLKNEiksPVIREKLQRLYGSTLN-IDLFPALMVEDLVPGSRLGPT---LMCLLSTqfRRLRdGDRLW--YENPGV 562
Cdd:cd09818 371 KSFEDLTGD---EEVAAELREVYGGDVEkVDLLVGLLAEPLPPGFGFSDTafrIFILMAS--RRLK-SDRFFtnDFRPEV 444
|
570
....*....|....*....
gi 1907089070 563 FSPAQLTQLKQTSLARILC 581
Cdd:cd09818 445 YTPEGMDWVNNNTMKSVLL 463
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
216-583 |
1.59e-27 |
|
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1.
Pssm-ID: 188648 [Multi-domain] Cd Length: 490 Bit Score: 117.37 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 216 IDASNVYGSTdhEARSiRDLASHRG--LLRQGI--------VQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRAN 285
Cdd:cd09816 131 IDLSQIYGLT--EART-HALRLFKDgkLKSQMIngeeyppyLFEDGGVKMEFPPLVPPLGDELTPEREAKLFAVGHERFN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 286 EQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAE---------IQHITYRHwlpkilgevgMKMLgey 356
Cdd:cd09816 208 LTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGElikiviedyINHLSPYH----------FKLF--- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 357 rgYDPSVnagIFNA------FATAAFRfghtlinpLLYR----LDENFEpIPQGHVPLHKAFFSPfRIVNEGGIDPLLRG 426
Cdd:cd09816 275 --FDPEL---AFNEpwqrqnRIALEFN--------LLYRwhplVPDTFN-IGGQRYPLSDFLFNN-DLVVDHGLGALVDA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 427 LF-GVAGKMripsQLLNTElterlfsmAHTVALDLAAinIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEiksPVIRE 505
Cdd:cd09816 340 ASrQPAGRI----GLRNTP--------PFLLPVEVRS--IEQGRKLRLASFNDYRKRFGLPPYTSFEELTGD---PEVAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 506 KLQRLYGSTLNIDLFPALMVEDLVPGSRLGPTLMC--------------LLSTQFrrlrdgdrlWyeNPGVFSPAQLTQL 571
Cdd:cd09816 403 ELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEmvapdafsgaltnpLLSPEV---------W--KPSTFGGEGGFDI 471
|
410
....*....|...
gi 1907089070 572 KQT-SLARILCDN 583
Cdd:cd09816 472 VKTaTLQDLVCRN 484
|
|
| VWC |
smart00214 |
von Willebrand factor (vWF) type C domain; |
720-775 |
2.70e-13 |
|
von Willebrand factor (vWF) type C domain;
Pssm-ID: 214564 Cd Length: 59 Bit Score: 64.84 E-value: 2.70e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 720 CVDDsGESHGGNTKWKKDPCTVCECKNGQ-ITCFVEACQPA-ACPQP--VKVEGACCPVC 775
Cdd:smart00214 1 CVHN-GRVYNDGETWKPDPCQICTCLDGTtVLCDPVECPPPpDCPNPerVKPPGECCPRC 59
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
47-559 |
8.51e-13 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 71.72 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 47 YRTHDGTCNNLQHPMWGASLTAFERllkavyengfNTPrginSQRQYNGHVLPMPRLVSTTLIG-TEVITPDEQFTHMLM 125
Cdd:PLN02283 85 YRTADGKCNDPFNEGAGSQGTFFGR----------NMP----PVDQKDKLLDPHPSVVATKLLArKKFIDTGKQFNMIAA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 126 QWGQFLDHDLDSTVVALSQARFSDGQHCSSVCsndpPCFSVM------IPPNDPRVRSGArcmffvrsspvcgsgmtsll 199
Cdd:PLN02283 151 SWIQFMIHDWIDHLEDTQQIELTAPKEVASQC----PLKSFKfyktkeVPTGSPDIKTGS-------------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 200 mnsvypreqINQLTSYIDASNVYGSTDHEARSIRDLashrgllRQGIVQRSGKPLLpfatgpptecMRDENESPIpcflA 279
Cdd:PLN02283 207 ---------LNIRTPWWDGSVIYGSNEKGLRRVRTF-------KDGKLKISEDGLL----------LHDEDGIPI----S 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 280 GDHRaNEQLGLTSMHTLWFREHNRIAAELLKLNPHWDGDTVYHETRKIVGAEIQHITYRHWLPKIL-------------- 345
Cdd:PLN02283 257 GDVR-NSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVELLktdtllagmranwy 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 346 -----------GEVGMKMLGEYRGYDPSVNAGIFNAFA---TAAFRFgHTLINPLLYRLDENFEPIPQGHVPLHKAFFSP 411
Cdd:PLN02283 336 gllgkkfkdtfGHIGGPILSGLVGLKKPNNHGVPYSLTeefTSVYRM-HSLLPDHLILRDITAAPGENKSPPLIEEIPMP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 412 FRIVNEGGidpllrglfgvagkmripSQLLNTELTERLFSMAHTVA----------------------------LDLAAI 463
Cdd:PLN02283 415 ELIGLKGE------------------KKLSKIGFEKLMVSMGHQACgalelwnypswmrdlvpqdidgedrpdhVDMAAL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 464 NIQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNEikSPVIrEKLQRLYGSTL-NIDLFPALMVEDLVPGSRLGPT---LM 539
Cdd:PLN02283 477 EIYRDRERGVARYNEFRRNLLMIPISKWEDLTDD--EEAI-EVLREVYGDDVeKLDLLVGLMAEKKIKGFAISETaffIF 553
|
570 580
....*....|....*....|
gi 1907089070 540 CLLSTqfRRLrDGDRLWYEN 559
Cdd:PLN02283 554 LLMAS--RRL-EADRFFTSN 570
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
127-474 |
1.03e-10 |
|
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: 64.67 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 127 WGQFLDHDL--DSTVVALsqarfsdgqhcssvcsndppcfsvmIPPNDPR----VRSGArcmffvrsspvcgsgmtsLLM 200
Cdd:cd09819 53 LGQFIDHDItlDTTSSLA-------------------------PRQIDPAelrnFRTPA------------------LDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 201 NSVYPReqinqltsyidasnvyGSTDHEARSIRDLASHRGLLRQGIVQRSGKPllpfatGPPTECMRDenespIPCF--- 277
Cdd:cd09819 90 DSVYGG----------------GPDGSPYLYDQATPNDGAKLRVGRESPGGPG------GLPGDGARD-----LPRNgqg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 278 --LAGDHRANEQLGLTSMHTLWFREHNRIAAELLKLNPhwDGDTVYHETRKIVGAEIQHITYRHWLPKILGE--VGMKML 353
Cdd:cd09819 143 taLIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAHGT--PGDELFEEARRLVRWHYQWLVLNDFLPRICDPdvVDDVLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 354 GEYRGYDPSVNAGIFNA--FATAAFRFGHTLINPlLYRLDENFEPIPqghvplHKAFFSpfriVNEGGIDPLLRG----- 426
Cdd:cd09819 221 NGRRFYRFFREGKPFMPveFSVAAYRFGHSMVRA-SYDYNRNFPDAS------LELLFT----FTGGGEGDLGGFsplpe 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907089070 427 --------LFGVAGKMRI-PSQLLNTELTERLFSM------AHTVALDLAAINIQRGRDHGIP 474
Cdd:cd09819 290 nwiidwrrFFDIDGSAPPqFARKIDTKLAPPLFDLpnggvgLAPPMKSLAFRNLLRGYRLGLP 352
|
|
| VWC |
pfam00093 |
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ... |
720-775 |
1.26e-10 |
|
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.
Pssm-ID: 278520 Cd Length: 57 Bit Score: 57.43 E-value: 1.26e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907089070 720 CVDDsGESHGGNTKWKKDPCTVCECKNGQITCFVEACQPAACPQP--VKVEGACCPVC 775
Cdd:pfam00093 1 CVQN-GVVYENGETWKPDLCTICTCDDGKVLCDKIICPPLDCPNPrlEIPPGECCPVC 57
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
453-570 |
5.14e-06 |
|
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: 50.03 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 453 AHTVALDLAAIN---IQRGRDHGIPPYHDYRVYCNLSAAYTFEDLKNeikSPVIREKLQRLYGSTLNIDLFPALMVED-- 527
Cdd:cd09817 365 ARNVPASLKVIEilgILQAREWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAEDak 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907089070 528 --LVPGSRLGPTlmclLSTQFRRLRD------GDR-LWYEnpgvFSPAQLTQ 570
Cdd:cd09817 442 ppMPPGSGLCPG----YTISRAILSDavalvrGDRfYTVD----YNPNNLTN 485
|
|
| PSP94 |
pfam05825 |
Beta-microseminoprotein (PSP-94); This family consists of the mammalian specific protein ... |
716-762 |
3.02e-05 |
|
Beta-microseminoprotein (PSP-94); This family consists of the mammalian specific protein beta-microseminoprotein. Prostatic secretory protein of 94 amino acids (PSP94), also called beta-microseminoprotein, is a small, nonglycosylated protein, rich in cysteine residues. It was first isolated as a major protein from human seminal plasma. The exact function of this protein is unknown.
Pssm-ID: 283482 Cd Length: 94 Bit Score: 43.38 E-value: 3.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907089070 716 STTECVDDSGESHGGNTKWKKDPCTVCECKNGQITCfveaCQPAACP 762
Cdd:pfam05825 14 KSDECTDLKGNKHPLNSVWKTKNCEWCTCGKTAITC----CTTAAIP 56
|
|
| Amnionless |
pfam14828 |
Amnionless; The amnionless protein forms a complex with cubilin. This complex is necessary for ... |
690-775 |
1.28e-03 |
|
Amnionless; The amnionless protein forms a complex with cubilin. This complex is necessary for vitamin B12 uptake.
Pssm-ID: 464340 Cd Length: 449 Bit Score: 41.99 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907089070 690 LKEFVLEMQKIITDlrkqiNSLESRLSTtecvdDSGES--HG-GNTKWKKDPC---TVCEC---KNGQITCFV--EACQP 758
Cdd:pfam14828 149 VKSVSLLGQTFTSD-----EDFAEFLSS-----RLGQLqfHGaGALRVGPEACsdpSGCGCgndENLERICANvlQRCPP 218
|
90
....*....|....*..
gi 1907089070 759 AACPQPVKVEGACCPVC 775
Cdd:pfam14828 219 PHCLSPLRPEGHCCDVC 235
|
|
| |
