|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
161-722 |
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: 1004.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 161 GASNTALARWLPPVYEDGFSQPKGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQ 240
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 241 STSTAAFWGGVDCQLTCENQNPCFPIQLPS--NSSGTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDA 318
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSedPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 319 STVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPF-ATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTL 397
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFqPEEVSSCNPDPNGGERVPCFLAGDGRASEVLTLTASHTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 398 WLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVNPTVSNIFSTAA 477
Cdd:cd09825 241 WLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFSTAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 478 FRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSN 557
Cdd:cd09825 321 FRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFVLSN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 558 VGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGART 637
Cdd:cd09825 401 SSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGART 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 638 GPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFPQDFESCEDIPSMDL 717
Cdd:cd09825 481 GPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPGINL 560
|
....*
gi 755541300 718 ELWRE 722
Cdd:cd09825 561 EAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
145-697 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 728.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 145 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNPnflyhGFPLPPVREVTRHLIQvsNEAVTEDDQYSDFL 224
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSS-----GSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 225 PVWGQYIDHDIALTPQSTSTAAFwgGVDCQLTCENQNP-CFPIQLPSN----SSGTTACLPFYRSSAACGTGdqgalfgn 299
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGS--SCDCCCPPENLHPpCFPIPIPPDdpffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 300 lsaaNPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSsaGLLRVNtlHLDAGRAYLPFATAacaPEPGTPRTNRTPCFL 379
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKVN--RSDDGKELLPFDPD---GPCCCNSSGGVPCFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 380 AGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQY---VG 456
Cdd:pfam03098 213 AGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFgllPL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 457 PYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNtdFQEHTELPRLQLRDVFFRPWRLIqEGGLDPIVRGLLARAAK 536
Cdd:pfam03098 293 PYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 537 LqvQGQLMNEELTERLFVLSNVGT-LDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSmVNKIMDLYK 615
Cdd:pfam03098 370 A--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEV-IAKLRELYG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 616 HADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTN--VFTDAQRQELEKHSLPRVICDNT-GLTRV 692
Cdd:pfam03098 447 SVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGNqgSFTPEQLEEIRKTSLARVICDNTdIIETI 526
|
....*
gi 755541300 693 PVDAF 697
Cdd:pfam03098 527 QPNVF 531
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
784-813 |
3.61e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 52.62 E-value: 3.61e-09
10 20 30
....*....|....*....|....*....|
gi 755541300 784 DVNECADLTHPpCHPSAQCKNTKGSFQCVC 813
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
730-783 |
5.32e-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: 5.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755541300 730 CVFPEEVDNGNFVHCEESGKL--VLVYSCFHGYKLQGQEQVTCTQKG-WDSEPPVCK 783
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYgsTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
784-827 |
5.60e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 52.25 E-value: 5.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 755541300 784 DVNECAdlTHPPCHPSAQCKNTKGSFQCVCTDPYVLGedeKTCI 827
Cdd:smart00179 1 DIDECA--SGNPCQNGGTCVNTVGSYRCECPPGYTDG---RNCE 39
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
784-827 |
1.07e-08 |
|
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: 51.48 E-value: 1.07e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 755541300 784 DVNECAdlTHPPCHPSAQCKNTKGSFQCVCTDPYVLgedeKTCI 827
Cdd:cd00054 1 DIDECA--SGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
730-782 |
5.63e-07 |
|
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: 47.14 E-value: 5.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755541300 730 CVFPEEVDNGNFVHCEESGKL--VLVYSCFHGYKLQGQEQVTCTQKG-WDSEPPVC 782
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTYSYgdTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
730-782 |
3.10e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 45.18 E-value: 3.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755541300 730 CVFPEEVDNGNFVHCEES---GKlVLVYSCFHGYKLQGQEQVTCTQKG-WDSEPPVC 782
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEynyGA-SVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
706-786 |
3.72e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 40.42 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 706 FESCedIPSMDLELWRETFP--QDDKCVFPEEVDNGNFVHCEESGKL--VLVYSCFH----GYKLQGQEQVTCTQ-KGWD 776
Cdd:PHA02639 61 FRTC--IKDKNNAIWSNKAPfcMLKECNDPPSIINGKIYNKREMYKVgdEIYYVCNEhkgvQYSLVGNEKITCIQdKSWK 138
|
90
....*....|
gi 755541300 777 SEPPVCKDVN 786
Cdd:PHA02639 139 PDPPICKMIN 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 ... |
161-722 |
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: 1004.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 161 GASNTALARWLPPVYEDGFSQPKGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQ 240
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 241 STSTAAFWGGVDCQLTCENQNPCFPIQLPS--NSSGTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDA 318
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSedPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 319 STVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPF-ATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTL 397
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFqPEEVSSCNPDPNGGERVPCFLAGDGRASEVLTLTASHTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 398 WLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVNPTVSNIFSTAA 477
Cdd:cd09825 241 WLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFSTAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 478 FRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSN 557
Cdd:cd09825 321 FRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFVLSN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 558 VGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGART 637
Cdd:cd09825 401 SSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGART 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 638 GPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFPQDFESCEDIPSMDL 717
Cdd:cd09825 481 GPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPGINL 560
|
....*
gi 755541300 718 ELWRE 722
Cdd:cd09825 561 EAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
145-697 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 728.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 145 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNPnflyhGFPLPPVREVTRHLIQvsNEAVTEDDQYSDFL 224
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSSS-----GSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 225 PVWGQYIDHDIALTPQSTSTAAFwgGVDCQLTCENQNP-CFPIQLPSN----SSGTTACLPFYRSSAACGTGdqgalfgn 299
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGS--SCDCCCPPENLHPpCFPIPIPPDdpffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 300 lsaaNPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSsaGLLRVNtlHLDAGRAYLPFATAacaPEPGTPRTNRTPCFL 379
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKVN--RSDDGKELLPFDPD---GPCCCNSSGGVPCFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 380 AGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQY---VG 456
Cdd:pfam03098 213 AGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFgllPL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 457 PYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNtdFQEHTELPRLQLRDVFFRPWRLIqEGGLDPIVRGLLARAAK 536
Cdd:pfam03098 293 PYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 537 LqvQGQLMNEELTERLFVLSNVGT-LDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSmVNKIMDLYK 615
Cdd:pfam03098 370 A--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEV-IAKLRELYG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 616 HADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTN--VFTDAQRQELEKHSLPRVICDNT-GLTRV 692
Cdd:pfam03098 447 SVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGNqgSFTPEQLEEIRKTSLARVICDNTdIIETI 526
|
....*
gi 755541300 693 PVDAF 697
Cdd:pfam03098 527 QPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
278-711 |
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: 569.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 278 CLPFYRSSAACGTGDQGALFGNLSaanPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSSAGLLRVNTlHLDAGRAYLP 357
Cdd:cd09826 12 CIEFVRSSAVCGSGSTSLLFNSVT---PREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI-VSEAGKPLLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 358 FATAACAPEPGTPRTNRTPCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIIT 437
Cdd:cd09826 88 FERDSPMDCRRDPNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 438 MRDYIPKILGPDAFRQyVGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHTELPrLQLRDVFFRPWRL 517
Cdd:cd09826 168 YSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPEGH-LPLHKAFFAPYRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 518 IQEGGLDPIVRGLLARAAKLQVQGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAEL 597
Cdd:cd09826 246 VNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 598 NKAIANRSMVNKIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKH 677
Cdd:cd09826 326 KNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVFSPAQLTQIKKT 405
|
410 420 430
....*....|....*....|....*....|....*
gi 755541300 678 SLPRVICDNT-GLTRVPVDAFRIGKFPQDFESCED 711
Cdd:cd09826 406 SLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
304-706 |
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: 557.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 304 NPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSSAGLLRVNTLHLDAGRAYLPFATAACAPEPGTPRTNRTPCFLAGDG 383
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTSANIPCFLAGDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 384 RASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQyVGPYEGYNP 463
Cdd:cd09824 90 RVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAAR-LPPYRGYNE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 464 TVNPTVSNIFSTAaFRFGHATVHPLVRRLNTDFQEHTELPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKLQVQGQL 543
Cdd:cd09824 169 SVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAKLNNQNQM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 544 MNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAIANRSMVNKIMDLYKHADNIDVW 623
Cdd:cd09824 248 LVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDNIDIW 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 624 LGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEKHSLPRVICDNTGLTRVPVDAFRIGKFP 703
Cdd:cd09824 328 IGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQPNSYP 407
|
...
gi 755541300 704 QDF 706
Cdd:cd09824 408 RDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
306-686 |
2.57e-174 |
|
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: 510.19 E-value: 2.57e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 306 RQQMNGLTSFLDASTVYGSSPGVEKQLRNWSSsaGLLRVNTLHldaGRAYLPFATAACapEPGTPRTNRTPCFLAGDGRA 385
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKG--GLLKTQRRN---GRELLPFSNNPT--DDCSLSSAGKPCFLAGDGRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 386 SEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQY------VGPYE 459
Cdd:cd09823 74 NEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltSGYFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 460 GYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHtelPRLQLRDVFFRPWRLIQEGGLDPIVRGLLARAAKlQV 539
Cdd:cd09823 154 GYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQ---GSVNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQ-KV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 540 QGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELnKAIANRSMVNKIMDLYKHADN 619
Cdd:cd09823 230 DRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDL-LGIMSPETIQKLRRLYKSVDD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 620 IDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNV---FTDAQRQELEKHSLPRVICDN 686
Cdd:cd09823 309 IDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
196-698 |
1.76e-118 |
|
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: 367.41 E-value: 1.76e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 196 LPPVREVTRHLIQvSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQststaafwggvdcqltcenqnpcfpiqlpsnssgt 275
Cdd:cd09822 2 RPSPREISNAVAD-QTESIPNSRGLSDWFWVWGQFLDHDIDLTPD----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 276 taclpfyrssaacgtgdqgalfgnlsaaNPRQQMNGLTSFLDASTVYGSSPGVEKQLRnwSSSAGLLRVNTlhlDAGRAY 355
Cdd:cd09822 46 ----------------------------NPREQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTSV---ANAGDL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 356 LPFATAACAPEPGTPrtNRTPCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQI 435
Cdd:cd09822 93 LPFNEAGLPNDNGGV--PADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 436 ITMRDYIPKILGPDAFrqyvGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEHTELPrlqLRDVFFRPw 515
Cdd:cd09822 171 ITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA---LRDAFFNP- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 516 RLIQEGGLDPIVRGLLARAAklQVQGQLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPA 595
Cdd:cd09822 243 DELEENGIDPLLRGLASQVA--QEIDTFIVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFS 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 596 EL--NKAIANRsmvnkIMDLYKHADNIDVWLGGLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNvFTDAQRQE 673
Cdd:cd09822 321 DItsDPDLAAR-----LASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDD-LLLDEIAD 394
|
490 500
....*....|....*....|....*
gi 755541300 674 LEKHSLPRVICDNTGLTRVPVDAFR 698
Cdd:cd09822 395 IENTTLADVIRRNTDVDDIQDNVFL 419
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
308-686 |
8.37e-114 |
|
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: 353.27 E-value: 8.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 308 QMNGLTSFLDASTVYGSSPGVEKQLRNWSSsaGLLRVN-TLHLDAGRAYLPFATAAcaPEPGTPRTNRTPCFLAGDGRAS 386
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKG--GLLKTNeVKGPSYGTELLPFNNPN--PSMGTIGLPPTRCFIAGDPRVN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 387 EVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFRQYVGPYEGYNPTVN 466
Cdd:cd05396 77 ENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 467 PTVSNIFSTAAFRFGHATVHPLVRRLNTDFQEhTELPRLQLRDVFFRPWRLIQ-EGGLDPIVRGLLARAAKLQVQgqlmN 545
Cdd:cd05396 157 PYVLSEFFTAAYRFGHSLVPEGVDRIDENGQP-KEIPDVPLKDFFFNTSRSILsDTGLDPLLRGFLRQPAGLIDQ----N 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 546 EELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKaiaNRSMVNKIMDLYKHADNIDVWLG 625
Cdd:cd05396 232 VDDVMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDDVDLWVG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755541300 626 GLAEKFLPGARTGPLFACIIGKQMKALRDGDRFWWENTNVFTDAQRQELEK-HSLPRVICDN 686
Cdd:cd05396 309 GLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
153-737 |
8.18e-81 |
|
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: 272.25 E-value: 8.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 153 NNRDHPRWGASNTALARWLPPVYEDGFSQPKGWNpnflyhgfpLPPVRevtrhliQVSNEAVT-EDDQYSdflpvwgqyi 231
Cdd:cd09820 6 NNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPR-------SLSNLLMKgESGLPS---------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 232 dhdialTPQSTSTAAFWGGVDCQLTCENQNP-C----FPIQLP-------SNSSGTTAcLPFYRSSAACGTGDqgalfgn 299
Cdd:cd09820 60 ------TRNRTALLVFFGQHVVSEILDASRPgCppeyFNIEIPkgdpvfdPECTGNIE-LPFQRSRYDKNTGY------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 300 lSAANPRQQMNGLTSFLDASTVYGSSPGVEKQLRNWS-------SSAGLLRVNTLHLdagraylPFATAACAPEPGTPRT 372
Cdd:cd09820 126 -SPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSggrlasgDDGGFPRRNTNRL-------PLANPPPPSYHGTRGP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 373 NRTpcFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDafr 452
Cdd:cd09820 198 ERL--FKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 453 qyVGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTD--FQEHT----ELPRLQLRDVFFRPWRLIQEGGLDPI 526
Cdd:cd09820 273 --VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQcnFREVLttsgGSPALRLCNTYWNSQEPLLKSDIDEL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 527 VRGLLARAAKLqvQGQLMNEELTERLFvlsnvGTL-----DLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNKAI 601
Cdd:cd09820 351 LLGMASQIAER--EDNIIVEDLRDYLF-----GPLefsrrDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDL 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 602 ANRSM--VNKIMDLYKHA-DNIDVWLGGLAEkfLPGARTGPLFACIIGKQMKALRDGDRFWWENTN--VFTDAQRQELEK 676
Cdd:cd09820 424 FKKDPelLERLAELYGNDlSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKngLFTAEEIEEIRN 501
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755541300 677 HSLPRVIcdnTGLTRVPVDAFRigkfPQDFESCEDIPSMDLELWRETFPQddKCVFPEEVD 737
Cdd:cd09820 502 TTLRDVI---LAVTDIDNTDLQ----KNVFFWKNGDPCPQPKQLTENMLE--PCTPLTVYD 553
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
220-703 |
1.08e-47 |
|
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: 179.53 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 220 YSDFLPVWGQYIDHDIALTPQSTStaafwGGVDCQLTceNQNPCFPIQLPSNSSGTTACLPFYRSSAACGTGDQGalfgn 299
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGN-----GTVLIPLP--PDDPLYDLGRGTNGMALDRGTNNAGPDGILGTADGE----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 300 lsaanpRQQMNGLTSFLDASTVYGSSPGVEKQLRNW-----------------SSSAGLLRVNTLHLDA-GRAYLPFATA 361
Cdd:cd09821 81 ------GEHTNVTTPFVDQNQTYGSHASHQVFLREYdgdgvatgrllegatggSARTGHAFLDDIAHNAaPKGGLGSLRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 362 ACAPEPGTPRTNRT-------PCFLAGDGRASEVPALAAVHTLWLREHNRLASAFKAI----------------NKHWSA 418
Cdd:cd09821 155 NPTEDPPGPGAPGSydnelldAHFVAGDGRVNENIGLTAVHTVFHREHNRLVDQIKDTllqsadlafaneaggnNLAWDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 419 NTAYQEARKVVGALHQIITMRDYIPKILGP-DAFrqyvGPYEGYNPTVNPTVSNIFSTAAFRFGHATVHPLVRRLNTDFQ 497
Cdd:cd09821 235 ERLFQAARFANEMQYQHLVFEEFARRIQPGiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRIGPDAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 498 EH----TELPRLQLRDVFFRPWRLIQEGGLDPIVRGLlaraakLQVQGQLMNEELTErlfVLSN--VG-TLDLASLNLQR 570
Cdd:cd09821 311 EGldnqVGLIDAFLNPVAFLPATLYAEEGAGAILRGM------TRQVGNEIDEFVTD---ALRNnlVGlPLDLAALNIAR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 571 GRDHGLPDYNEWR----EFCGLSRLETPAELNKAIANR-----SMVNKIMDLYKHA------------------------ 617
Cdd:cd09821 382 GRDTGLPTLNEARaqlfAATGDTILKAPYESWNDFGARlknpeSLINFIAAYGTHLtitgattlaakraaaqdlvdggdg 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 618 ----------------------DNIDVWLGGLAEKFLP-GARTGPLFACIIGKQMKALRDGDRFWW----ENTNVFTdaq 670
Cdd:cd09821 462 apadradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYlsrtAGLDLLN--- 538
|
570 580 590
....*....|....*....|....*....|...
gi 755541300 671 rqELEKHSLPRVICDNTGLTRVPVDAFRIGKFP 703
Cdd:cd09821 539 --QLENNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
308-687 |
6.67e-17 |
|
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: 84.62 E-value: 6.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 308 QMNGLTSFLDASTVYGSSPGVEKQLRnwSSSAGLLRVNTLhldAGRAYLP--FATAACAPE----PGTPRTNRTPC---- 377
Cdd:cd09816 123 RRNTSNHGIDLSQIYGLTEARTHALR--LFKDGKLKSQMI---NGEEYPPylFEDGGVKMEfpplVPPLGDELTPEreak 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 378 -FLAGDGRASEVPALAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIpKILGPDAFRQYVG 456
Cdd:cd09816 198 lFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYI-NHLSPYHFKLFFD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 457 PYEGYNPTVNPT--VSNIFSTaAFRFghatvHPLVrrlNTDFQEHTElpRLQLRDVFFRPwRLIQEGGLDPIVrgllaRA 534
Cdd:cd09816 277 PELAFNEPWQRQnrIALEFNL-LYRW-----HPLV---PDTFNIGGQ--RYPLSDFLFNN-DLVVDHGLGALV-----DA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 535 AKLQVQGQLmneelterlfVLSNVG--TLDLASLNLQRGRDHGLPDYNEWREFCGLSRLETPAELNkaiANRSMVNKIMD 612
Cdd:cd09816 340 ASRQPAGRI----------GLRNTPpfLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELT---GDPEVAAELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 613 LYKHADNIDVWLGGLAEKFLPGARTGPLFACIIG----KQmkALRD--GDRFWWeNTNVFTDAQRQELEK-HSLPRVICD 685
Cdd:cd09816 407 LYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIVKtATLQDLVCR 483
|
..
gi 755541300 686 NT 687
Cdd:cd09816 484 NV 485
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
310-634 |
8.69e-17 |
|
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: 84.26 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 310 NGLTSFLDASTVYGSSPGVEKQLRNwSSSAGLLRVNtlhldaGRAYLPFATAACAPEPGTPRTnrtpcFLAGdgrasevp 389
Cdd:cd09818 88 NTNTHWWDGSQIYGSTEEAQKRLRT-FPPDGKLKLD------ADGLLPVDEHTGLPLTGFNDN-----WWVG-------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 390 aLAAVHTLWLREHNRLASAFKAINKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDA----------------FRQ 453
Cdd:cd09818 148 -LSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPTleiamranwwgllgerLKR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 454 YVGpyegyNPTVNPTVSNIFSTAAFRFG--------HATV---HPLVRRlNTDFQEHTELPRLQ---LRDVFFrpwrliq 519
Cdd:cd09818 227 VLG-----RDGTSELLSGIPGSPPNHHGvpyslteeFVAVyrmHPLIPD-DIDFRSADDGATGEeisLTDLAG------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 520 eGGLDPIVRGL-LARAA-KLQVQG----QLMNEELTERLFVLSNVGTLDLASLNLQRGRDHGLPDYNEWREFCGLSRLET 593
Cdd:cd09818 294 -GKARELLRKLgFADLLySFGITHpgalTLHNYPRFLRDLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLHLPPAKS 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755541300 594 PAEL--NKAIANRsmvnkIMDLY-KHADNIDVWLGGLAEKFLPG 634
Cdd:cd09818 373 FEDLtgDEEVAAE-----LREVYgGDVEKVDLLVGLLAEPLPPG 411
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
302-577 |
4.98e-16 |
|
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: 81.62 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 302 AANPRQQMNGLTSFLDASTVYGSSPGvekqlrnwsSSAGLLRVNTlhlDAGRAYLPFATAACAPEPGT--------PRT- 372
Cdd:cd09819 73 QIDPAELRNFRTPALDLDSVYGGGPD---------GSPYLYDQAT---PNDGAKLRVGRESPGGPGGLpgdgardlPRNg 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 373 NRTPcfLAGDGRASEVPALAAVHTLWLREHNRLASAFKAinKHWSANTAYQEARKVVGALHQIITMRDYIPKILGPDAFR 452
Cdd:cd09819 141 QGTA--LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRA--HGTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPDVVD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 453 QYV----GPYEGYNPTVNPtvsnI---FSTAAFRFGHATVHPLVrRLNTDFQEHTelprlqLRDVF-FRPWRLIQEGGLD 524
Cdd:cd09819 217 DVLangrRFYRFFREGKPF----MpveFSVAAYRFGHSMVRASY-DYNRNFPDAS------LELLFtFTGGGEGDLGGFS 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755541300 525 PIV-------RGLLARAAKLQVQ-GQLMNEELTERLFVLSNVGTL------DLASLNLQRGRDHGLP 577
Cdd:cd09819 286 PLPenwiidwRRFFDIDGSAPPQfARKIDTKLAPPLFDLPNGGVGlappmkSLAFRNLLRGYRLGLP 352
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
784-813 |
3.61e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 52.62 E-value: 3.61e-09
10 20 30
....*....|....*....|....*....|
gi 755541300 784 DVNECADLTHPpCHPSAQCKNTKGSFQCVC 813
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
730-783 |
5.32e-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: 5.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755541300 730 CVFPEEVDNGNFVHCEESGKL--VLVYSCFHGYKLQGQEQVTCTQKG-WDSEPPVCK 783
Cdd:cd00033 1 CPPPPVPENGTVTGSKGSYSYgsTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
784-827 |
5.60e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 52.25 E-value: 5.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 755541300 784 DVNECAdlTHPPCHPSAQCKNTKGSFQCVCTDPYVLGedeKTCI 827
Cdd:smart00179 1 DIDECA--SGNPCQNGGTCVNTVGSYRCECPPGYTDG---RNCE 39
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
784-827 |
1.07e-08 |
|
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: 51.48 E-value: 1.07e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 755541300 784 DVNECAdlTHPPCHPSAQCKNTKGSFQCVCTDPYVLgedeKTCI 827
Cdd:cd00054 1 DIDECA--SGNPCQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38
|
|
| EGF_3 |
pfam12947 |
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ... |
788-826 |
3.60e-07 |
|
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: 47.21 E-value: 3.60e-07
10 20 30
....*....|....*....|....*....|....*....
gi 755541300 788 CADLTHPpCHPSAQCKNTKGSFQCVCTDPYVLgeDEKTC 826
Cdd:pfam12947 1 CSDNNGG-CHPNATCTNTGGSFTCTCNDGYTG--DGVTC 36
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
730-782 |
5.63e-07 |
|
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: 47.14 E-value: 5.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755541300 730 CVFPEEVDNGNFVHCEESGKL--VLVYSCFHGYKLQGQEQVTCTQKG-WDSEPPVC 782
Cdd:smart00032 1 CPPPPDIENGTVTSSSGTYSYgdTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
730-782 |
3.10e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 45.18 E-value: 3.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755541300 730 CVFPEEVDNGNFVHCEES---GKlVLVYSCFHGYKLQGQEQVTCTQKG-WDSEPPVC 782
Cdd:pfam00084 1 CPPPPDIPNGKVSATKNEynyGA-SVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
566-658 |
4.79e-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: 46.95 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 566 LNLQRGRDHGLPDYNEWREFCGLSRLETPAELN--KAIANRsmvnkIMDLYKHADNIDVWLGGLAEK----FLPGARTGP 639
Cdd:cd09817 378 LGILQAREWNVATLNEFRKFFGLKPYETFEDINsdPEVAEA-----LELLYGHPDNVELYPGLVAEDakppMPPGSGLCP 452
|
90 100
....*....|....*....|..
gi 755541300 640 LF---ACIIGKQMkALRDGDRF 658
Cdd:cd09817 453 GYtisRAILSDAV-ALVRGDRF 473
|
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
787-826 |
8.96e-05 |
|
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: 40.54 E-value: 8.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 755541300 787 ECAdlTHPPCHPSAQCKNTKGSFQCVCTDPYVLgedEKTC 826
Cdd:cd00053 1 ECA--ASNPCSNGGTCVNTPGSYRCVCPPGYTG---DRSC 35
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
706-786 |
3.72e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 40.42 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755541300 706 FESCedIPSMDLELWRETFP--QDDKCVFPEEVDNGNFVHCEESGKL--VLVYSCFH----GYKLQGQEQVTCTQ-KGWD 776
Cdd:PHA02639 61 FRTC--IKDKNNAIWSNKAPfcMLKECNDPPSIINGKIYNKREMYKVgdEIYYVCNEhkgvQYSLVGNEKITCIQdKSWK 138
|
90
....*....|
gi 755541300 777 SEPPVCKDVN 786
Cdd:PHA02639 139 PDPPICKMIN 148
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
799-826 |
4.52e-03 |
|
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: 35.68 E-value: 4.52e-03
10 20
....*....|....*....|....*...
gi 755541300 799 SAQCKNTKGSFQCVCTDPYVLGEDEKTC 826
Cdd:pfam14670 9 SHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| vWA_Matrilin |
cd01475 |
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
781-825 |
7.21e-03 |
|
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.
Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 38.91 E-value: 7.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 755541300 781 VCKDVNECADLTHPPCHPsaqCKNTKGSFQCVCTDPYVLGEDEKT 825
Cdd:cd01475 183 ICVVPDLCATLSHVCQQV---CISTPGSYLCACTEGYALLEDNKT 224
|
|
| EGF |
smart00181 |
Epidermal growth factor-like domain; |
787-827 |
9.05e-03 |
|
Epidermal growth factor-like domain;
Pssm-ID: 214544 Cd Length: 35 Bit Score: 34.80 E-value: 9.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 755541300 787 ECAdlTHPPCHPsAQCKNTKGSFQCVCTDPYvlgEDEKTCI 827
Cdd:smart00181 1 ECA--SGGPCSN-GTCINTPGSYTCSCPPGY---TGDKRCE 35
|
|
| |
