|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
167-677 |
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: 932.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 167 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 246
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 247 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 326
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 327 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVpprAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTAL 406
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQ---PEEVSSCNPDPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 407 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 486
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 487 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGG--------------------------------- 533
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGgldpvirgliggpaklvtpddlmneelteklfv 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 534 ------------------------YNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 589
Cdd:cd09825 398 lsnsstldlaslnlqrgrdhglpgYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 590 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 669
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 28558984 670 MNLEAWRE 677
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
151-652 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 600.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 151 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 230
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 231 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 307
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 308 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 387
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 388 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 466
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 467 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTL--------LRG---- 532
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLyeggidplLRGlatq 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 533 -------------------------------------------GYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLY 569
Cdd:pfam03098 367 paqavdnnfteeltnhlfgppgefsgldlaalniqrgrdhglpGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELY 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 570 KHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-GLTR 646
Cdd:pfam03098 446 GSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIET 525
|
....*.
gi 28558984 647 VPMDAF 652
Cdd:pfam03098 526 IQPNVF 531
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
739-782 |
1.21e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 54.18 E-value: 1.21e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558984 739 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 782
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
739-768 |
1.58e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 53.78 E-value: 1.58e-09
10 20 30
....*....|....*....|....*....|
gi 28558984 739 DVNECADGAHPpCHASARCRNTKGGFQCLC 768
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
739-782 |
2.88e-09 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 53.02 E-value: 2.88e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558984 739 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 782
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
685-738 |
8.46e-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: 52.47 E-value: 8.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558984 685 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 738
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
685-737 |
6.48e-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: 49.83 E-value: 6.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558984 685 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 737
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
685-737 |
9.45e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 43.64 E-value: 9.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558984 685 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 737
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
632-741 |
7.82e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 632 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 692
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558984 693 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 741
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICKMIN 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
167-677 |
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: 932.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 167 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 246
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 247 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 326
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 327 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVpprAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTAL 406
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQ---PEEVSSCNPDPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 407 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 486
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 487 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGG--------------------------------- 533
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGgldpvirgliggpaklvtpddlmneelteklfv 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 534 ------------------------YNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 589
Cdd:cd09825 398 lsnsstldlaslnlqrgrdhglpgYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 590 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 669
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 28558984 670 MNLEAWRE 677
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
151-652 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 600.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 151 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 230
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 231 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 307
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 308 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 387
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 388 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 466
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 467 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTL--------LRG---- 532
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLyeggidplLRGlatq 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 533 -------------------------------------------GYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLY 569
Cdd:pfam03098 367 paqavdnnfteeltnhlfgppgefsgldlaalniqrgrdhglpGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELY 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 570 KHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-GLTR 646
Cdd:pfam03098 446 GSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIET 525
|
....*.
gi 28558984 647 VPMDAF 652
Cdd:pfam03098 526 IQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
275-666 |
7.48e-145 |
|
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: 435.58 E-value: 7.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 275 PEEARPAAGTACLPFYRSSAACGTGDQGALFGNLStanPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHA 354
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVT---PREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 355 RLRdSGRAYLPFVPPRAPAACAPepgiPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVY 434
Cdd:cd09826 78 VSE-AGKPLLPFERDSPMDCRRD----PNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 435 QEARKVVGALHQIITLRDYIPRILGPEAFQQyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHP-- 512
Cdd:cd09826 153 HETRKIVGAQMQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPeg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 513 DLPglwLHQAFFSPWTL---------LRG------------------------------------------------GYN 535
Cdd:cd09826 232 HLP---LHKAFFAPYRLvneggidplLRGlfataakdrvpdqllntelteklfemahevaldlaalniqrgrdhglpGYN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 536 EWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWW 615
Cdd:cd09826 309 DYRKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 28558984 616 ENSHVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAFQVGKFPEDFESCDS 666
Cdd:cd09826 389 ENPGVFSPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
312-661 |
3.43e-140 |
|
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: 422.21 E-value: 3.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 312 NPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGipgeTRGPCFL 391
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTS----ANIPCFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 392 AGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAfQQYVGPYE 471
Cdd:cd09824 86 AGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA-AARLPPYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 472 GYDSTANPTVSNVFSTaAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWT---------LLRG---------- 532
Cdd:cd09824 165 GYNESVDPRIANVFTT-AFRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRiireggidpILRGlmatpaklnn 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 533 --------------------------------------GYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDN 574
Cdd:cd09824 244 qnqmlvdelrerlfqqtkrmgldlaalnlqrgrdhglpGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 575 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 654
Cdd:cd09824 324 IDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQP 403
|
....*..
gi 28558984 655 GKFPEDF 661
Cdd:cd09824 404 NSYPRDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
314-641 |
1.23e-132 |
|
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: 401.57 E-value: 1.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 314 RQQMNGLTSFLDASTVYGSSPALERQLRNWTsaEGLLRVHarlRDSGRAYLPFVPPRAPAacapepGIPGETRGPCFLAG 393
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFK--GGLLKTQ---RRNGRELLPFSNNPTDD------CSLSSAGKPCFLAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 394 DGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY------V 467
Cdd:cd09823 70 DGRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 468 GPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglwLHQAFFSPWT---------LLRG------ 532
Cdd:cd09823 150 GYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVN---LHDLFFNPDRlyeeggldpLLRGlatqpa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 533 -----------------------------------------GYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYKH 571
Cdd:cd09823 227 qkvdrfftdeltthfffrggnpfgldlaalniqrgrdhglpGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYKS 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28558984 572 PDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHV---FTDAQRRELEKHSLSRVICDN 641
Cdd:cd09823 306 VDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
202-654 |
2.14e-83 |
|
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: 273.80 E-value: 2.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 202 LPPVREVtrhviqvSNEVVTDD-----DRY-SDLLMAWGQYIDHDIAFTPQstskaafgggadcqmtcenqnpcfpiqlp 275
Cdd:cd09822 2 RPSPREI-------SNAVADQTesipnSRGlSDWFWVWGQFLDHDIDLTPD----------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 276 eearpaagtaclpfyrssaacgtgdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHar 355
Cdd:cd09822 46 ------------------------------------NPREQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTS-- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 356 lRDSGRAYLPFvpprapAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQ 435
Cdd:cd09822 86 -VANAGDLLPF------NEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 436 EARKVVGALHQIITLRDYIPRILGPEAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLP 515
Cdd:cd09822 159 AARAIVIAEIQAITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 516 glwLHQAFFSPW--------TLLRG----------------------------------------------GYNEWREFC 541
Cdd:cd09822 235 ---LRDAFFNPDeleengidPLLRGlasqvaqeidtfivddvrnflfgppgaggfdlaalniqrgrdhglpSYNQLREAL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 542 GLPRLETPADlstaIASR-SVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENShV 620
Cdd:cd09822 312 GLPAVTSFSD----ITSDpDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-D 386
|
490 500 510
....*....|....*....|....*....|....
gi 28558984 621 FTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 654
Cdd:cd09822 387 LLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
316-641 |
1.87e-75 |
|
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: 250.81 E-value: 1.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 316 QMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHARLRDS-GRAYLPFVPPRAPAacapepGIPGETRGPCFLAGD 394
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR--TFKGGLLKTNEVKGPSyGTELLPFNNPNPSM------GTIGLPPTRCFIAGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 395 GRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYD 474
Cdd:cd05396 73 PRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 475 STANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEhPDLPGLWLHQAFFSPW----------TLLRG------------ 532
Cdd:cd05396 153 PDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQP-KEIPDVPLKDFFFNTSrsilsdtgldPLLRGflrqpaglidqn 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 533 --------------------------------GYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLG 580
Cdd:cd05396 232 vddvmflfgplegvgldlaalniqrgrdlglpSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDDVDLWVG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28558984 581 GLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEK-HSLSRVICDN 641
Cdd:cd05396 309 GLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
159-671 |
4.22e-52 |
|
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: 191.74 E-value: 4.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 159 NNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyngfpLPPVRevtrhviQVSNEVVTDDD------RYSDLLMA 232
Cdd:cd09820 6 NNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPR-------SLSNLLMKGESglpstrNRTALLVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 233 WGQYIDHDIAftpqstskaafgggadcqmtcENQNP-C----FPIQLPEE----ARPAAGTACLPFYRSSAACGTGDqga 303
Cdd:cd09820 70 FGQHVVSEIL---------------------DASRPgCppeyFNIEIPKGdpvfDPECTGNIELPFQRSRYDKNTGY--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 304 lfgnlSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAegllrvhaRLRDSGRAYLPFVPPRAPAACAPEPGIPG 383
Cdd:cd09820 126 -----SPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSGG--------RLASGDDGGFPRRNTNRLPLANPPPPSYH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 384 ETRGP--CFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPE 461
Cdd:cd09820 193 GTRGPerLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 462 afqqyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLV--RRLDASFQEH---------------------------- 511
Cdd:cd09820 273 -----VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVyrRNRQCNFREVlttsggspalrlcntywnsqepllksdi 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 512 --------------------PDLPGLWLHQAFFS-----PWTLLRG------GYNEWREFCGLPRLETPADLSTAIASR- 559
Cdd:cd09820 348 delllgmasqiaeredniivEDLRDYLFGPLEFSrrdlmALNIQRGrdhglpDYNTAREAFGLPPRTTWSDINPDLFKKd 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 560 -SVADKILDLYKH-PDNIDVWLGGLAEnfLPRARTGPLFACLIGKQMKALRDGDWFWWENSH--VFTDAQRRELEKHSLS 635
Cdd:cd09820 428 pELLERLAELYGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKngLFTAEEIEEIRNTTLR 505
|
570 580 590
....*....|....*....|....*....|....*..
gi 28558984 636 RVIcdnTGLTRVPMDAFQVGKFPEDFES-CDSITGMN 671
Cdd:cd09820 506 DVI---LAVTDIDNTDLQKNVFFWKNGDpCPQPKQLT 539
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
226-658 |
4.52e-26 |
|
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: 114.05 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 226 YSDLLMAWGQYIDHDIAFTPQSTSKAAFgggadcqmtcenqnpcfpIQLPEEARPA-AGTACLPFYRSSAACGTGDQGAL 304
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGNGTVL------------------IPLPPDDPLYdLGRGTNGMALDRGTNNAGPDGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 305 fgNLSTANPRQQmNGLTSFLDASTVYGSSPALERQLRNWT-----------SAEGLLRV--HARLRDSGRAYLPFVPPRA 371
Cdd:cd09821 75 --GTADGEGEHT-NVTTPFVDQNQTYGSHASHQVFLREYDgdgvatgrlleGATGGSARtgHAFLDDIAHNAAPKGGLGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 372 PAACAPepGIPGETRGPC----------FLAGDGRASEVPSLTALHTLWLREHNR----------------LAAALKALN 425
Cdd:cd09821 152 LRDNPT--EDPPGPGAPGsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRlvdqikdtllqsadlaFANEAGGNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 426 AHWSADAVYQEARKVVGALHQIITLRDYIPRILGP-EAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRL 504
Cdd:cd09821 230 LAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 505 DASFQEHPDLP-GL---WLHQAFFSPWTL---------LRG-----GyNEWREF-------------------------- 540
Cdd:cd09821 306 GPDADEGLDNQvGLidaFLNPVAFLPATLyaeegagaiLRGmtrqvG-NEIDEFvtdalrnnlvglpldlaalniargrd 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 541 CGLPRL-ETPADLSTA---------------IASR-----SVADKILDLYKHP--------------------------- 572
Cdd:cd09821 385 TGLPTLnEARAQLFAAtgdtilkapyeswndFGARlknpeSLINFIAAYGTHLtitgattlaakraaaqdlvdggdgapa 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 573 -------------------DNIDVWLGGLAENFLP-RARTGPLFACLIGKQMKALRDGDWFWWENShvfTDAQ--RRELE 630
Cdd:cd09821 465 dradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR---TAGLdlLNQLE 541
|
570 580
....*....|....*....|....*...
gi 28558984 631 KHSLSRVICDNTGLTRVPMDAFQVGKFP 658
Cdd:cd09821 542 NNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
316-642 |
5.60e-16 |
|
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: 81.54 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 316 QMNGLTSFLDASTVYGSSPALERQLRnwtsaeglLRVHARLRDS---GRAYLPFVPPRA-------PAACAPEPGIPGET 385
Cdd:cd09816 123 RRNTSNHGIDLSQIYGLTEARTHALR--------LFKDGKLKSQminGEEYPPYLFEDGgvkmefpPLVPPLGDELTPER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 386 RGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIprilgpeafqQ 465
Cdd:cd09816 195 EAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYI----------N 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 466 YVGPYeGYDSTANPTVsnVFST-------AAFRFGHA-TIHPLV---------RRLDASFQEHPDL---PGLwlhQAFFS 525
Cdd:cd09816 265 HLSPY-HFKLFFDPEL--AFNEpwqrqnrIALEFNLLyRWHPLVpdtfniggqRYPLSDFLFNNDLvvdHGL---GALVD 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 526 ---------------PWTLLR--------------GGYNEWREFCGLPRLETPADLStaiASRSVADKILDLYKHPDNID 576
Cdd:cd09816 339 aasrqpagriglrntPPFLLPvevrsieqgrklrlASFNDYRKRFGLPPYTSFEELT---GDPEVAAELEELYGDVDAVE 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28558984 577 VWLGGLAENFLPRARTGPLFACLIG----KQmkALRD--GDWFWWeNSHVFTDAQRRELEK-HSLSRVICDNT 642
Cdd:cd09816 416 FYVGLFAEDPRPNSPLPPLMVEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIVKtATLQDLVCRNV 485
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
311-595 |
2.07e-11 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188651 Cd Length: 465 Bit Score: 66.98 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 311 ANPRQQMNGLTSFLDASTVYGSSPALERQLRnwtsaegllrVHARLRDSGRAYLPFVPPRAPAACAPEPG--IP--GETR 386
Cdd:cd09819 74 IDPAELRNFRTPALDLDSVYGGGPDGSPYLY----------DQATPNDGAKLRVGRESPGGPGGLPGDGArdLPrnGQGT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 387 GpcfLAGDGRASEVPSLTALHTLWLREHNRLAAALKALnaHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY 466
Cdd:cd09819 144 A---LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAH--GTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPDVVDDV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 467 V----GPYEGYDSTAnPTVSNVFSTAAFRFGHATI------------HPLVRRLDASFQEHPDLPGlwlHQAFFSPWTLl 530
Cdd:cd09819 219 LangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVrasydynrnfpdASLELLFTFTGGGEGDLGG---FSPLPENWII- 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28558984 531 rggynEWREFCGLPRlETPADLSTAIASRsVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPL 595
Cdd:cd09819 294 -----DWRRFFDIDG-SAPPQFARKIDTK-LAPPLFDLPNGGVGLAPPMKSLAFRNLLRGYRLGL 351
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
739-782 |
1.21e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 54.18 E-value: 1.21e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558984 739 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 782
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
739-768 |
1.58e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 53.78 E-value: 1.58e-09
10 20 30
....*....|....*....|....*....|
gi 28558984 739 DVNECADGAHPpCHASARCRNTKGGFQCLC 768
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
739-782 |
2.88e-09 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 53.02 E-value: 2.88e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558984 739 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 782
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
685-738 |
8.46e-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: 52.47 E-value: 8.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558984 685 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 738
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| EGF_3 |
pfam12947 |
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ... |
743-781 |
1.17e-08 |
|
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.
Pssm-ID: 463759 [Multi-domain] Cd Length: 36 Bit Score: 51.45 E-value: 1.17e-08
10 20 30
....*....|....*....|....*....|....*....
gi 28558984 743 CADGAHPpCHASARCRNTKGGFQCLCADPYELgdDGRTC 781
Cdd:pfam12947 1 CSDNNGG-CHPNATCTNTGGSFTCTCNDGYTG--DGVTC 36
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
685-737 |
6.48e-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: 49.83 E-value: 6.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558984 685 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 737
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
685-737 |
9.45e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 43.64 E-value: 9.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558984 685 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 737
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
754-781 |
2.93e-05 |
|
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.
Pssm-ID: 464251 [Multi-domain] Cd Length: 36 Bit Score: 41.84 E-value: 2.93e-05
10 20
....*....|....*....|....*...
gi 28558984 754 SARCRNTKGGFQCLCADPYELGDDGRTC 781
Cdd:pfam14670 9 SHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
318-462 |
9.62e-05 |
|
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: 45.74 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 318 NGLTSFLDASTVYGSSPALERQLRnwTSAEGllrvhARLRDSGRAYLPfvpprapaaCAPEPGIPgetrgpcfLAGDGRA 397
Cdd:cd09818 88 NTNTHWWDGSQIYGSTEEAQKRLR--TFPPD-----GKLKLDADGLLP---------VDEHTGLP--------LTGFNDN 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28558984 398 SEVpSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEA 462
Cdd:cd09818 144 WWV-GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPT 207
|
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
742-774 |
1.44e-04 |
|
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.
Pssm-ID: 238010 Cd Length: 36 Bit Score: 39.77 E-value: 1.44e-04
10 20 30
....*....|....*....|....*....|...
gi 28558984 742 ECAdgAHPPCHASARCRNTKGGFQCLCADPYEL 774
Cdd:cd00053 1 ECA--ASNPCSNGGTCVNTPGSYRCVCPPGYTG 31
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
632-741 |
7.82e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558984 632 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 692
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558984 693 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 741
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICKMIN 148
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
528-584 |
2.15e-03 |
|
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: 41.55 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558984 528 TLLRGGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAE 584
Cdd:cd09817 385 EWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAE 438
|
|
| |
