|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
13-573 |
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: 875.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 13 MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQRnlkkrGILSPAQLLSFSKLP 92
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLY-----SHMLTVWGQYIDHDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 93 EPTSGVIARAAeimetSIQAMKRKVNLKTQQSQHPTDALSED-------LLSIIANMSGCLPYMLPPKCPNTCLANKYRP 165
Cdd:cd09825 76 DFTPQSVSRTM-----FIGSTDCKMTCENQNPCFPIQLPSEDprilgraCLPFFRSSAVCGTGDTSTLFGNLSLANPREQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 166 ITGACNNRDHPRWGASNTALARWLPPVY-EDGFSQPRGWNPGFLYNGFPLPPVREVT----RHVIQVSNEVVTDDDRYSD 240
Cdd:cd09825 151 INGLTSFIDASTVYGSTLALARSLRDLSsDDGLLRVNSKFDDSGRDYLPFQPEEVSScnpdPNGGERVPCFLAGDGRASE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 241 LLMAWGQYIDHDIAFTPQSTSKAAFGGG--ADCQMTCENQNPCFPIQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANP 318
Cdd:cd09825 231 VLTLTASHTLWLREHNRLARALKSINPHwdGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 319 TVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEE 398
Cdd:cd09825 311 TVSNVFSTAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 399 LTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGL 478
Cdd:cd09825 391 LTEKLFVLSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 479 AENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFE 558
Cdd:cd09825 471 AEDFLPGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFV 550
|
570
....*....|....*
gi 1370478785 559 SCDSITGMNLEAWRE 573
Cdd:cd09825 551 SCDSIPGINLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
163-548 |
5.37e-157 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 466.65 E-value: 5.37e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 163 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 242
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 243 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPI------------------------------------- 284
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIpippddpffspfgvrcmpfvrsapgcglgnpreqinq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 --------------------------------------------------------------------------------
Cdd:pfam03098 152 vtsfldgsqvygsseetarslrsfsggllkvnrsddgkellpfdpdgpcccnssggvpcflagdsranenpgltalhtlf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 285 -----------------------------------QIITLRDYIPRILGPEAFQQY---VGPYEGYDSTANPTVSNVFST 326
Cdd:pfam03098 232 lrehnriadelaklnphwsdetlfqearkiviaqiQHITYNEWLPAILGEDNMNWFgllPLPYNGYDPNVDPSISNEFAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 327 AAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTLLRGGgLDPLIRGLLARPAKLQvqDQLMNEELTERLFVL 406
Cdd:pfam03098 312 AAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLYEGG-IDPLLRGLATQPAQAV--DNNFTEELTNHLFGP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 407 SNSST-LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYKHPDNIDVWLGGLAENFLPR 485
Cdd:pfam03098 387 PGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELYGSVDDIDLWVGGLAEKPLPG 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478785 486 ARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAF 548
Cdd:pfam03098 466 GLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIETIQPNVF 531
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
635-678 |
1.38e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 53.79 E-value: 1.38e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1370478785 635 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 678
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
635-664 |
1.80e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 53.40 E-value: 1.80e-09
10 20 30
....*....|....*....|....*....|
gi 1370478785 635 DVNECADGAHPpCHASARCRNTKGGFQCLC 664
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
635-678 |
2.97e-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: 2.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1370478785 635 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 678
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
581-634 |
7.09e-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: 7.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478785 581 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 634
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
581-633 |
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: 49.83 E-value: 5.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478785 581 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 633
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
581-633 |
7.47e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.03 E-value: 7.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478785 581 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 633
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
528-637 |
6.72e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 528 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 588
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478785 589 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 637
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 ... |
13-573 |
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: 875.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 13 MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQRnlkkrGILSPAQLLSFSKLP 92
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLY-----SHMLTVWGQYIDHDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 93 EPTSGVIARAAeimetSIQAMKRKVNLKTQQSQHPTDALSED-------LLSIIANMSGCLPYMLPPKCPNTCLANKYRP 165
Cdd:cd09825 76 DFTPQSVSRTM-----FIGSTDCKMTCENQNPCFPIQLPSEDprilgraCLPFFRSSAVCGTGDTSTLFGNLSLANPREQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 166 ITGACNNRDHPRWGASNTALARWLPPVY-EDGFSQPRGWNPGFLYNGFPLPPVREVT----RHVIQVSNEVVTDDDRYSD 240
Cdd:cd09825 151 INGLTSFIDASTVYGSTLALARSLRDLSsDDGLLRVNSKFDDSGRDYLPFQPEEVSScnpdPNGGERVPCFLAGDGRASE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 241 LLMAWGQYIDHDIAFTPQSTSKAAFGGG--ADCQMTCENQNPCFPIQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANP 318
Cdd:cd09825 231 VLTLTASHTLWLREHNRLARALKSINPHwdGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 319 TVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEE 398
Cdd:cd09825 311 TVSNVFSTAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 399 LTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGL 478
Cdd:cd09825 391 LTEKLFVLSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 479 AENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFE 558
Cdd:cd09825 471 AEDFLPGARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFV 550
|
570
....*....|....*
gi 1370478785 559 SCDSITGMNLEAWRE 573
Cdd:cd09825 551 SCDSIPGINLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
163-548 |
5.37e-157 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 466.65 E-value: 5.37e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 163 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 242
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 243 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPI------------------------------------- 284
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIpippddpffspfgvrcmpfvrsapgcglgnpreqinq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 --------------------------------------------------------------------------------
Cdd:pfam03098 152 vtsfldgsqvygsseetarslrsfsggllkvnrsddgkellpfdpdgpcccnssggvpcflagdsranenpgltalhtlf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 285 -----------------------------------QIITLRDYIPRILGPEAFQQY---VGPYEGYDSTANPTVSNVFST 326
Cdd:pfam03098 232 lrehnriadelaklnphwsdetlfqearkiviaqiQHITYNEWLPAILGEDNMNWFgllPLPYNGYDPNVDPSISNEFAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 327 AAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTLLRGGgLDPLIRGLLARPAKLQvqDQLMNEELTERLFVL 406
Cdd:pfam03098 312 AAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLYEGG-IDPLLRGLATQPAQAV--DNNFTEELTNHLFGP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 407 SNSST-LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYKHPDNIDVWLGGLAENFLPR 485
Cdd:pfam03098 387 PGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELYGSVDDIDLWVGGLAEKPLPG 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478785 486 ARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAF 548
Cdd:pfam03098 466 GLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIETIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
284-562 |
6.45e-129 |
|
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: 391.28 E-value: 6.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 284 IQIITLRDYIPRILGPEAFQQyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHP--DLPglwLHQA 361
Cdd:cd09826 163 MQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPegHLP---LHKA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 362 FFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPR 441
Cdd:cd09826 239 FFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYNDYRKFCNLSV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 442 LETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQ 521
Cdd:cd09826 319 AETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQ 398
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370478785 522 RRELEKHSLSRVICDNT-GLTRVPMDAFQVGKFPEDFESCDS 562
Cdd:cd09826 399 LTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
284-557 |
6.61e-129 |
|
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: 389.86 E-value: 6.61e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 284 IQIITLRDYIPRILGPEAfQQYVGPYEGYDSTANPTVSNVFSTAaFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFF 363
Cdd:cd09824 139 VQIITYRDYLPLILGEDA-AARLPPYRGYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 364 SPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLE 443
Cdd:cd09824 217 ASWRIIREGGIDPILRGLMATPAKLNNQNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 444 TPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRR 523
Cdd:cd09824 297 NLAELAAVLNNTVLARKLLDLYGTPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRE 376
|
250 260 270
....*....|....*....|....*....|....
gi 1370478785 524 ELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDF 557
Cdd:cd09824 377 SLRSVSLSRIICDNTGITKVPRDPFQPNSYPRDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
284-537 |
1.08e-112 |
|
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: 346.87 E-value: 1.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 284 IQIITLRDYIPRILGPEAFQQY------VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglw 357
Cdd:cd09823 121 MQHITYNEFLPILLGRELMEKFglylltSGYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVN--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 358 LHQAFFSPWTLLRGGGLDPLIRGLLARPAKlQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFC 437
Cdd:cd09823 198 LHDLFFNPDRLYEEGGLDPLLRGLATQPAQ-KVDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 438 GLPRLETPADLSTAIaSRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHV- 516
Cdd:cd09823 277 GLPRATTFDDLLGIM-SPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQp 355
|
250 260
....*....|....*....|...
gi 1370478785 517 --FTDAQRRELEKHSLSRVICDN 537
Cdd:cd09823 356 ssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
284-550 |
1.05e-70 |
|
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: 237.98 E-value: 1.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 284 IQIITLRDYIPRILGPEAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglwLHQAFF 363
Cdd:cd09822 168 IQAITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA---LRDAFF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 364 SPwTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLE 443
Cdd:cd09822 241 NP-DELEENGIDPLLRGLASQVA--QEIDTFIVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVT 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 444 TPADlstaIASR-SVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENShVFTDAQR 522
Cdd:cd09822 318 SFSD----ITSDpDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-DLLLDEI 392
|
250 260
....*....|....*....|....*...
gi 1370478785 523 RELEKHSLSRVICDNTGLTRVPMDAFQV 550
Cdd:cd09822 393 ADIENTTLADVIRRNTDVDDIQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
284-537 |
1.21e-59 |
|
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: 206.51 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 284 IQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQ--EHPDLPglwLHQA 361
Cdd:cd05396 123 YQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQpkEIPDVP---LKDF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 362 FFSPW-TLLRGGGLDPLIRGLLARPAKLQVQdqlmNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLP 440
Cdd:cd05396 200 FFNTSrSILSDTGLDPLLRGFLRQPAGLIDQ----NVDDVMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 441 RLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDA 520
Cdd:cd05396 276 PPTSFQDILT---DPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKS 352
|
250
....*....|....*...
gi 1370478785 521 QRRELEK-HSLSRVICDN 537
Cdd:cd05396 353 GKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
285-567 |
7.13e-37 |
|
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: 146.29 E-value: 7.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 285 QIITLRDYIPRILGPEafqqyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLV--RRLDASFQEHPDL----PGLWL 358
Cdd:cd09820 257 QNIVFYEWLPALLGTN-----VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVyrRNRQCNFREVLTTsggsPALRL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 359 HQAFFSPWTLLRGGGLDPLIRGLLARPAKLQvqDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCG 438
Cdd:cd09820 332 CNTYWNSQEPLLKSDIDELLLGMASQIAERE--DNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 439 LPRLETPADLSTAIASR--SVADKILDLYKH-PDNIDVWLGGLAEnfLPRARTGPLFACLIGKQMKALRDGDWFWWENSH 515
Cdd:cd09820 410 LPPRTTWSDINPDLFKKdpELLERLAELYGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVK 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1370478785 516 --VFTDAQRRELEKHSLSRVIcdnTGLTRVPMDAFQVGKFPEDFES-CDSITGMN 567
Cdd:cd09820 488 ngLFTAEEIEEIRNTTLRDVI---LAVTDIDNTDLQKNVFFWKNGDpCPQPKQLT 539
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
307-554 |
1.65e-21 |
|
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: 99.41 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 307 GPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLP-GL---WLHQAFFSPWTLLRGGGLDPLIRGLL 382
Cdd:cd09821 269 GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRIGPDADEGLDNQvGLidaFLNPVAFLPATLYAEEGAGAILRGMT 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 383 ARPAK---LQVQDQLMNEelterLFVLSnsstLDLASINLQRGRDHGLPGYNE--------------------WREFcgL 439
Cdd:cd09821 349 RQVGNeidEFVTDALRNN-----LVGLP----LDLAALNIARGRDTGLPTLNEaraqlfaatgdtilkapyesWNDF--G 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 440 PRLETPADLSTAIAS----------RSVADKI-----LDLYKHP----------------------DNIDVWLGGLAENF 482
Cdd:cd09821 418 ARLKNPESLINFIAAygthltitgaTTLAAKRaaaqdLVDGGDGapadradfmnaagagagtvkglDNVDLWVGGLAEKQ 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370478785 483 LP-RARTGPLFACLIGKQMKALRDGDWFWWENShvfTDAQ--RRELEKHSLSRVICDNTGLTRVPMDAFQVGKFP 554
Cdd:cd09821 498 VPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR---TAGLdlLNQLENNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
635-678 |
1.38e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 53.79 E-value: 1.38e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1370478785 635 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 678
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
635-664 |
1.80e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 53.40 E-value: 1.80e-09
10 20 30
....*....|....*....|....*....|
gi 1370478785 635 DVNECADGAHPpCHASARCRNTKGGFQCLC 664
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
635-678 |
2.97e-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: 2.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1370478785 635 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 678
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
581-634 |
7.09e-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: 7.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478785 581 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 634
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| EGF_3 |
pfam12947 |
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ... |
639-677 |
9.68e-09 |
|
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: 9.68e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1370478785 639 CADGAHPpCHASARCRNTKGGFQCLCADPYELgdDGRTC 677
Cdd:pfam12947 1 CSDNNGG-CHPNATCTNTGGSFTCTCNDGYTG--DGVTC 36
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
581-633 |
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: 49.83 E-value: 5.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478785 581 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 633
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
413-538 |
2.32e-07 |
|
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: 54.19 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 413 DLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLStaiASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLF 492
Cdd:cd09816 361 EVRSI--EQGRKLRLASFNDYRKRFGLPPYTSFEELT---GDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLM 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370478785 493 ACLIG----KQmkALRD--GDWFWWeNSHVFTDAQRRELEK-HSLSRVICDNT 538
Cdd:cd09816 436 VEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIVKtATLQDLVCRNV 485
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
402-484 |
6.97e-07 |
|
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: 52.67 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 402 RLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAiasRSVADKILDLY-KHPDNIDVWLGGLAE 480
Cdd:cd09818 330 RDLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKSFEDLTGD---EEVAAELREVYgGDVEKVDLLVGLLAE 406
|
....
gi 1370478785 481 NFLP 484
Cdd:cd09818 407 PLPP 410
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
581-633 |
7.47e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.03 E-value: 7.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478785 581 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 633
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
285-428 |
2.14e-05 |
|
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: 47.72 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 285 QIITLRDYIPRILGPEAFQQYV----GPYEGYDSTAnPTVSNVFSTAAFRFGHATIHPLVrRLDASFQEHPdlpglwlHQ 360
Cdd:cd09819 198 QWLVLNDFLPRICDPDVVDDVLangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVRASY-DYNRNFPDAS-------LE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 361 AFFSpwtllRGGGLDPLIRGLLARPAKLQVQ-------------------DQLMNEELtERLF---VLSNSSTLDLASIN 418
Cdd:cd09819 269 LLFT-----FTGGGEGDLGGFSPLPENWIIDwrrffdidgsappqfarkiDTKLAPPL-FDLPnggVGLAPPMKSLAFRN 342
|
170
....*....|
gi 1370478785 419 LQRGRDHGLP 428
Cdd:cd09819 343 LLRGYRLGLP 352
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
650-677 |
2.77e-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: 41.46 E-value: 2.77e-05
10 20
....*....|....*....|....*...
gi 1370478785 650 SARCRNTKGGFQCLCADPYELGDDGRTC 677
Cdd:pfam14670 9 SHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
408-480 |
7.36e-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: 7.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370478785 408 NSSTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAE 480
Cdd:cd09817 371 SLKVIEILGI--LQAREWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAE 438
|
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
638-670 |
1.23e-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: 1.23e-04
10 20 30
....*....|....*....|....*....|...
gi 1370478785 638 ECAdgAHPPCHASARCRNTKGGFQCLCADPYEL 670
Cdd:cd00053 1 ECA--ASNPCSNGGTCVNTPGSYRCVCPPGYTG 31
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
528-637 |
6.72e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478785 528 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 588
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478785 589 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 637
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICKMIN 148
|
|
| |
