|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
179-746 |
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: 1075.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 179 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 258
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 259 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 338
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 339 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACApepGIPGETRGPCFLAGDGRASEVPSLTAL 418
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP---DPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 419 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 498
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 499 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFV 578
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 579 LSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 658
Cdd:cd09825 398 LSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 659 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 738
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 1370478767 739 MNLEAWRE 746
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
163-721 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 699.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 163 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 242
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 243 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 319
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 320 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 399
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 400 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 478
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 479 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTLLrGGGLDPLIRGLLA 556
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLAT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 557 RPAKLqvQDQLMNEELTERLFVLSNSST-LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKIL 635
Cdd:pfam03098 366 QPAQA--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 636 DLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-G 712
Cdd:pfam03098 443 ELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdI 522
|
....*....
gi 1370478767 713 LTRVPMDAF 721
Cdd:pfam03098 523 IETIQPNVF 531
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
754-807 |
6.89e-09 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 52.85 E-value: 6.89e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478767 754 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 807
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
754-806 |
5.49e-08 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 50.22 E-value: 5.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478767 754 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 806
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
754-806 |
6.91e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.03 E-value: 6.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478767 754 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 806
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
701-807 |
4.12e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 40.42 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 701 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 761
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370478767 762 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCK 807
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICK 145
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
179-746 |
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: 1075.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 179 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 258
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 259 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 338
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 339 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACApepGIPGETRGPCFLAGDGRASEVPSLTAL 418
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP---DPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 419 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 498
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 499 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFV 578
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 579 LSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 658
Cdd:cd09825 398 LSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 659 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 738
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 1370478767 739 MNLEAWRE 746
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
163-721 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 699.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 163 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 242
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 243 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 319
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 320 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 399
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 400 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 478
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 479 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTLLrGGGLDPLIRGLLA 556
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLAT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 557 RPAKLqvQDQLMNEELTERLFVLSNSST-LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKIL 635
Cdd:pfam03098 366 QPAQA--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 636 DLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-G 712
Cdd:pfam03098 443 ELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdI 522
|
....*....
gi 1370478767 713 LTRVPMDAF 721
Cdd:pfam03098 523 IETIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
287-735 |
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: 558.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 287 PEEARPAAGTACLPFYRSSAACGTGDQGALFGNLStanPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHA 366
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVT---PREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 367 RLRdSGRAYLPFVPPRAPAACAPepgiPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVY 446
Cdd:cd09826 78 VSE-AGKPLLPFERDSPMDCRRD----PNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 447 QEARKVVGALHQIITLRDYIPRILGPEAFQQyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHP-- 524
Cdd:cd09826 153 HETRKIVGAQMQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPeg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 525 DLPglwLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYN 604
Cdd:cd09826 232 HLP---LHKAFFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 605 EWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWW 684
Cdd:cd09826 309 DYRKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1370478767 685 ENSHVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAFQVGKFPEDFESCDS 735
Cdd:cd09826 389 ENPGVFSPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
324-730 |
0e+00 |
|
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: 534.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 324 NPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGipgeTRGPCFL 403
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTS----ANIPCFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 404 AGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAfQQYVGPYE 483
Cdd:cd09824 86 AGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA-AARLPPYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 484 GYDSTANPTVSNVFSTAaFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQV 563
Cdd:cd09824 165 GYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAKLNN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 564 QDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDN 643
Cdd:cd09824 244 QNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 644 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 723
Cdd:cd09824 324 IDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQP 403
|
....*..
gi 1370478767 724 GKFPEDF 730
Cdd:cd09824 404 NSYPRDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
326-710 |
1.78e-168 |
|
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.
Pssm-ID: 188655 [Multi-domain] Cd Length: 378 Bit Score: 495.94 E-value: 1.78e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 326 RQQMNGLTSFLDASTVYGSSPALERQLRNWTsaEGLLRVHarlRDSGRAYLPFVPPRAPAacapepGIPGETRGPCFLAG 405
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFK--GGLLKTQ---RRNGRELLPFSNNPTDD------CSLSSAGKPCFLAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 406 DGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY------V 479
Cdd:cd09823 70 DGRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 480 GPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglwLHQAFFSPWTLLRGGGLDPLIRGLLARPA 559
Cdd:cd09823 150 GYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVN---LHDLFFNPDRLYEEGGLDPLLRGLATQPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 560 KlQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYK 639
Cdd:cd09823 227 Q-KVDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYK 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370478767 640 HPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHV---FTDAQRRELEKHSLSRVICDN 710
Cdd:cd09823 305 SVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
214-723 |
3.40e-112 |
|
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: 351.61 E-value: 3.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 214 LPPVREVtrhviqvSNEVVTDD-----DRY-SDLLMAWGQYIDHDIAFTPQstskaafgggadcqmtcenqnpcfpiqlp 287
Cdd:cd09822 2 RPSPREI-------SNAVADQTesipnSRGlSDWFWVWGQFLDHDIDLTPD----------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 288 eearpaagtaclpfyrssaacgtgdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHar 367
Cdd:cd09822 46 ------------------------------------NPREQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTS-- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 368 lRDSGRAYLPFvpprapAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQ 447
Cdd:cd09822 86 -VANAGDLLPF------NEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 448 EARKVVGALHQIITLRDYIPRILGPEAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLP 527
Cdd:cd09822 159 AARAIVIAEIQAITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 528 glwLHQAFFSPwTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWR 607
Cdd:cd09822 235 ---LRDAFFNP-DELEENGIDPLLRGLASQVA--QEIDTFIVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 608 EFCGLPRLETPADlstaIASR-SVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWEN 686
Cdd:cd09822 309 EALGLPAVTSFSD----ITSDpDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEN 384
|
490 500 510
....*....|....*....|....*....|....*..
gi 1370478767 687 ShVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 723
Cdd:cd09822 385 D-DLLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
328-710 |
9.51e-99 |
|
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: 314.36 E-value: 9.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 328 QMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHARLRDS-GRAYLPFVPPRAPAacapepGIPGETRGPCFLAGD 406
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR--TFKGGLLKTNEVKGPSyGTELLPFNNPNPSM------GTIGLPPTRCFIAGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 407 GRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYD 486
Cdd:cd05396 73 PRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 487 STANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEhPDLPGLWLHQAFFSPW-TLLRGGGLDPLIRGLLARPAklqvqd 565
Cdd:cd05396 153 PDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQP-KEIPDVPLKDFFFNTSrSILSDTGLDPLLRGFLRQPA------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 566 QLMNEELTERLFVLSNSST--LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDN 643
Cdd:cd05396 226 GLIDQNVDDVMFLFGPLEGvgLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDD 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370478767 644 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEK-HSLSRVICDN 710
Cdd:cd05396 303 VDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
171-740 |
2.80e-70 |
|
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: 243.75 E-value: 2.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 171 NNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyngfpLPPVRevtrhviQVSNEVVTDDD------RYSDLLMA 244
Cdd:cd09820 6 NNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPR-------SLSNLLMKGESglpstrNRTALLVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 245 WGQYIDHDIAftpqstskaafgggadcqmtcENQNP-C----FPIQLPEE----ARPAAGTACLPFYRSSAACGTGDqga 315
Cdd:cd09820 70 FGQHVVSEIL---------------------DASRPgCppeyFNIEIPKGdpvfDPECTGNIELPFQRSRYDKNTGY--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 316 lfgnlSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAegllrvhaRLRDSGRAYLPFVPPRAPAACAPEPGIPG 395
Cdd:cd09820 126 -----SPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSGG--------RLASGDDGGFPRRNTNRLPLANPPPPSYH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 396 ETRGP--CFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPE 473
Cdd:cd09820 193 GTRGPerLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 474 afqqyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHP--LVRRLDASFQEHPDL----PGLWLHQAFFSPWTLLRGGGL 547
Cdd:cd09820 273 -----VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPgvYRRNRQCNFREVLTTsggsPALRLCNTYWNSQEPLLKSDI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 548 DPLIRGLLARPAKLqvQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIAS 627
Cdd:cd09820 348 DELLLGMASQIAER--EDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLFK 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 628 R--SVADKILDLYKH-PDNIDVWLGGLAEnfLPRARTGPLFACLIGKQMKALRDGDWFWWENSH--VFTDAQRRELEKHS 702
Cdd:cd09820 426 KdpELLERLAELYGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKngLFTAEEIEEIRNTT 503
|
570 580 590
....*....|....*....|....*....|....*....
gi 1370478767 703 LSRVIcdnTGLTRVPMDAFQVGKFPEDFES-CDSITGMN 740
Cdd:cd09820 504 LRDVI---LAVTDIDNTDLQKNVFFWKNGDpCPQPKQLT 539
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
238-727 |
9.23e-40 |
|
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: 156.04 E-value: 9.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 238 YSDLLMAWGQYIDHDIAFTPQSTSKAAFgggadcqmtcenqnpcfpIQLPEEARPA-AGTACLPFYRSSAACGTGDQGAL 316
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGNGTVL------------------IPLPPDDPLYdLGRGTNGMALDRGTNNAGPDGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 317 fgNLSTANPRQQmNGLTSFLDASTVYGSSPALERQLRNWT-----------SAEGLLRV--HARLRDSGRAYLPFVPPRA 383
Cdd:cd09821 75 --GTADGEGEHT-NVTTPFVDQNQTYGSHASHQVFLREYDgdgvatgrlleGATGGSARtgHAFLDDIAHNAAPKGGLGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 384 PAACAPepGIPGETRGPC----------FLAGDGRASEVPSLTALHTLWLREHNR----------------LAAALKALN 437
Cdd:cd09821 152 LRDNPT--EDPPGPGAPGsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRlvdqikdtllqsadlaFANEAGGNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 438 AHWSADAVYQEARKVVGALHQIITLRDYIPRILGP-EAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRL 516
Cdd:cd09821 230 LAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 517 DASFQEHPDLP-GL---WLHQAFFSPWTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSnsstLDLASINL 592
Cdd:cd09821 306 GPDADEGLDNQvGLidaFLNPVAFLPATLYAEEGAGAILRGMTRQVG--NEIDEFVTDALRNNLVGLP----LDLAALNI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 593 QRGRDHGLPGYNE--------------------WREFcgLPRLETPADLSTAIAS----------RSVADKI-----LDL 637
Cdd:cd09821 380 ARGRDTGLPTLNEaraqlfaatgdtilkapyesWNDF--GARLKNPESLINFIAAygthltitgaTTLAAKRaaaqdLVD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 638 YKHP----------------------DNIDVWLGGLAENFLP-RARTGPLFACLIGKQMKALRDGDWFWWENShvfTDAQ 694
Cdd:cd09821 458 GGDGapadradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR---TAGL 534
|
570 580 590
....*....|....*....|....*....|....*
gi 1370478767 695 --RRELEKHSLSRVICDNTGLTRVPMDAFQVGKFP 727
Cdd:cd09821 535 dlLNQLENNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
328-711 |
1.18e-18 |
|
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: 90.40 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 328 QMNGLTSFLDASTVYGSSPALERQLRnwtsaeglLRVHARLRDS---GRAYLPFVPPRA-------PAACAPEPGIPGET 397
Cdd:cd09816 123 RRNTSNHGIDLSQIYGLTEARTHALR--------LFKDGKLKSQminGEEYPPYLFEDGgvkmefpPLVPPLGDELTPER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 398 RGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIprilgpeafqQ 477
Cdd:cd09816 195 EAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYI----------N 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 478 YVGPYeGYDSTANPTVsnVFST-------AAFRFGHA-TIHPLV-RRLDASFQEHPdlpglwLHQAFFSPwTLLRGGGLD 548
Cdd:cd09816 265 HLSPY-HFKLFFDPEL--AFNEpwqrqnrIALEFNLLyRWHPLVpDTFNIGGQRYP------LSDFLFNN-DLVVDHGLG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 549 PLIRGLLARPAKlqvqdqlmneELTER---LFVLsnssTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLStai 625
Cdd:cd09816 335 ALVDAASRQPAG----------RIGLRntpPFLL----PVEVRSI--EQGRKLRLASFNDYRKRFGLPPYTSFEELT--- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 626 ASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIG----KQmkALRD--GDWFWWeNSHVFTDAQRRELE 699
Cdd:cd09816 396 GDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIV 472
|
410
....*....|...
gi 1370478767 700 K-HSLSRVICDNT 711
Cdd:cd09816 473 KtATLQDLVCRNV 485
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
330-657 |
6.03e-13 |
|
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: 72.32 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 330 NGLTSFLDASTVYGSSPALERQLRnwTSAEGllrvhARLRDSGRAYLPfvpprapaaCAPEPGIPgetrgpcfLAGDGRA 409
Cdd:cd09818 88 NTNTHWWDGSQIYGSTEEAQKRLR--TFPPD-----GKLKLDADGLLP---------VDEHTGLP--------LTGFNDN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 410 SEVpSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQqyVGPYEGYDSTA 489
Cdd:cd09818 144 WWV-GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPTLE--IAMRANWWGLL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 490 NPTVSNVfstaafrFGHATIHPLVRRLDASFQE------------------HPDLPGLWlhqAFFS----------PWTL 541
Cdd:cd09818 221 GERLKRV-------LGRDGTSELLSGIPGSPPNhhgvpyslteefvavyrmHPLIPDDI---DFRSaddgatgeeiSLTD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 542 LRGGGLDPLIRGL----------LARPAKLqvqdQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCG 611
Cdd:cd09818 291 LAGGKARELLRKLgfadllysfgITHPGAL----TLHNYPRFLRDLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLH 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1370478767 612 LPRLETPADLSTAiasRSVADKILDLY-KHPDNIDVWLGGLAENFLP 657
Cdd:cd09818 367 LPPAKSFEDLTGD---EEVAAELREVYgGDVEKVDLLVGLLAEPLPP 410
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
323-601 |
2.03e-11 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188651 Cd Length: 465 Bit Score: 67.37 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 323 ANPRQQMNGLTSFLDASTVYGSSPALERQLRnwtsaegllrVHARLRDSGRAYLPFVPPRAPAACAPEPG--IP--GETR 398
Cdd:cd09819 74 IDPAELRNFRTPALDLDSVYGGGPDGSPYLY----------DQATPNDGAKLRVGRESPGGPGGLPGDGArdLPrnGQGT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 399 GpcfLAGDGRASEVPSLTALHTLWLREHNRLAAALKALnaHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY 478
Cdd:cd09819 144 A---LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAH--GTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPDVVDDV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 479 V----GPYEGYDSTAnPTVSNVFSTAAFRFGHATIHPLVrRLDASFQEHPdlpglwlHQAFFSpwtllRGGGLDPLIRGL 554
Cdd:cd09819 219 LangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVRASY-DYNRNFPDAS-------LELLFT-----FTGGGEGDLGGF 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370478767 555 LARPAKLQVQ-------------------DQLMNEELtERLF---VLSNSSTLDLASINLQRGRDHGLP 601
Cdd:cd09819 285 SPLPENWIIDwrrffdidgsappqfarkiDTKLAPPL-FDLPnggVGLAPPMKSLAFRNLLRGYRLGLP 352
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
754-807 |
6.89e-09 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 52.85 E-value: 6.89e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478767 754 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 807
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
754-806 |
5.49e-08 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 50.22 E-value: 5.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478767 754 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 806
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
754-806 |
6.91e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.03 E-value: 6.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478767 754 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 806
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
581-653 |
9.51e-05 |
|
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: 46.18 E-value: 9.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370478767 581 NSSTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAE 653
Cdd:cd09817 371 SLKVIEILGI--LQAREWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAE 438
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
701-807 |
4.12e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 40.42 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478767 701 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 761
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370478767 762 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCK 807
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICK 145
|
|
| |
