|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
194-761 |
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: 1078.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 194 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 273
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 274 STSKAAFGGGSDCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 353
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 354 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACApepGIPGETRGPCFLAGDGRASEVPSLTAL 433
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP---DPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 434 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 513
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 514 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFV 593
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 594 LSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 673
Cdd:cd09825 398 LSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 674 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSIPG 753
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 2462576581 754 MNLEAWRE 761
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
151-736 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 685.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 151 YRPITGACNNRagmgasllstgqcfqvaapiciprskvDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLP 230
Cdd:pfam03098 1 YRTIDGSCNNL---------------------------KNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLP 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 231 PVREVTRHVIQvsNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQSTSKAAFGGgsDCQMTCENQNP-CFPIQLPEEAR--P 307
Cdd:pfam03098 49 SPRLVSNKLFA--GDSGIPDPNLTLLLMQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 308 AAGTACLPFYRSSAACGTGdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSG 387
Cdd:pfam03098 125 PFGVRCMPFVRSAPGCGLG------------NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 388 RAYLPFvpprapaACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKV 467
Cdd:pfam03098 189 KELLPF-------DPDGPCCCNSSGGVPCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 468 VGALHQIITLRDYIPRILGPEAFQQY---VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGL 544
Cdd:pfam03098 262 VIAQIQHITYNEWLPAILGEDNMNWFgllPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 545 WLHQAFFSPWTLLrGGGLDPLIRGLLARPAKLqvQDQLMNEELTERLFVLSNSST-LDLASINLQRGRDHGLPGYNEWRE 623
Cdd:pfam03098 340 RLHDSFFNPDRLY-EGGIDPLLRGLATQPAQA--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYRE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 624 FCGLPRLETPADLSTAIaSRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS- 702
Cdd:pfam03098 417 FCGLPPAKSFEDLTDVI-PNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGn 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462576581 703 -HVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAF 736
Cdd:pfam03098 496 qGSFTPEQLEEIRKTSLARVICDNTdIIETIQPNVF 531
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
823-866 |
1.04e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 54.56 E-value: 1.04e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2462576581 823 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 866
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
823-852 |
1.34e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 54.17 E-value: 1.34e-09
10 20 30
....*....|....*....|....*....|
gi 2462576581 823 DVNECADGAHPpCHASARCRNTKGGFQCLC 852
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
823-866 |
2.38e-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: 53.41 E-value: 2.38e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2462576581 823 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 866
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
769-822 |
6.59e-09 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 52.85 E-value: 6.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462576581 769 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 822
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
769-821 |
5.10e-08 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 50.22 E-value: 5.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462576581 769 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 821
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
769-821 |
7.00e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.03 E-value: 7.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462576581 769 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 821
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
716-825 |
9.69e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 716 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsIPGMNLEAWRETFP--QDDKCGFPESVE 776
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462576581 777 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 825
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 ... |
194-761 |
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: 1078.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 194 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 273
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 274 STSKAAFGGGSDCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 353
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 354 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACApepGIPGETRGPCFLAGDGRASEVPSLTAL 433
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP---DPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 434 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 513
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 514 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFV 593
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 594 LSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 673
Cdd:cd09825 398 LSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 674 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSIPG 753
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 2462576581 754 MNLEAWRE 761
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
151-736 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 685.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 151 YRPITGACNNRagmgasllstgqcfqvaapiciprskvDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLP 230
Cdd:pfam03098 1 YRTIDGSCNNL---------------------------KNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLP 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 231 PVREVTRHVIQvsNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQSTSKAAFGGgsDCQMTCENQNP-CFPIQLPEEAR--P 307
Cdd:pfam03098 49 SPRLVSNKLFA--GDSGIPDPNLTLLLMQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 308 AAGTACLPFYRSSAACGTGdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSG 387
Cdd:pfam03098 125 PFGVRCMPFVRSAPGCGLG------------NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 388 RAYLPFvpprapaACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKV 467
Cdd:pfam03098 189 KELLPF-------DPDGPCCCNSSGGVPCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 468 VGALHQIITLRDYIPRILGPEAFQQY---VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGL 544
Cdd:pfam03098 262 VIAQIQHITYNEWLPAILGEDNMNWFgllPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 545 WLHQAFFSPWTLLrGGGLDPLIRGLLARPAKLqvQDQLMNEELTERLFVLSNSST-LDLASINLQRGRDHGLPGYNEWRE 623
Cdd:pfam03098 340 RLHDSFFNPDRLY-EGGIDPLLRGLATQPAQA--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYRE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 624 FCGLPRLETPADLSTAIaSRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS- 702
Cdd:pfam03098 417 FCGLPPAKSFEDLTDVI-PNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGn 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462576581 703 -HVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAF 736
Cdd:pfam03098 496 qGSFTPEQLEEIRKTSLARVICDNTdIIETIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
302-750 |
0e+00 |
|
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix.
Pssm-ID: 188658 Cd Length: 440 Bit Score: 558.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 302 PEEARPAAGTACLPFYRSSAACGTGDQGALFGNLStanPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHA 381
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVT---PREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 382 RLRdSGRAYLPFVPPRAPAACAPepgiPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVY 461
Cdd:cd09826 78 VSE-AGKPLLPFERDSPMDCRRD----PNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 462 QEARKVVGALHQIITLRDYIPRILGPEAFQQyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHP-- 539
Cdd:cd09826 153 HETRKIVGAQMQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPeg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 540 DLPglwLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYN 619
Cdd:cd09826 232 HLP---LHKAFFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 620 EWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWW 699
Cdd:cd09826 309 DYRKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462576581 700 ENSHVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAFQVGKFPEDFESCDS 750
Cdd:cd09826 389 ENPGVFSPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
339-745 |
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: 535.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 339 NPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGipgeTRGPCFL 418
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTS----ANIPCFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 419 AGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAfQQYVGPYE 498
Cdd:cd09824 86 AGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA-AARLPPYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 499 GYDSTANPTVSNVFSTAaFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQV 578
Cdd:cd09824 165 GYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAKLNN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 579 QDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDN 658
Cdd:cd09824 244 QNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 659 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 738
Cdd:cd09824 324 IDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQP 403
|
....*..
gi 2462576581 739 GKFPEDF 745
Cdd:cd09824 404 NSYPRDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
341-725 |
1.94e-168 |
|
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.
Pssm-ID: 188655 [Multi-domain] Cd Length: 378 Bit Score: 496.33 E-value: 1.94e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 341 RQQMNGLTSFLDASTVYGSSPALERQLRNWTsaEGLLRVHarlRDSGRAYLPFVPPRAPAacapepGIPGETRGPCFLAG 420
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFK--GGLLKTQ---RRNGRELLPFSNNPTDD------CSLSSAGKPCFLAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 421 DGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY------V 494
Cdd:cd09823 70 DGRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 495 GPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglwLHQAFFSPWTLLRGGGLDPLIRGLLARPA 574
Cdd:cd09823 150 GYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVN---LHDLFFNPDRLYEEGGLDPLLRGLATQPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 575 KlQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYK 654
Cdd:cd09823 227 Q-KVDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYK 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462576581 655 HPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHV---FTDAQRRELEKHSLSRVICDN 725
Cdd:cd09823 305 SVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
229-738 |
4.14e-112 |
|
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.
Pssm-ID: 188654 [Multi-domain] Cd Length: 420 Bit Score: 351.61 E-value: 4.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 229 LPPVREVtrhviqvSNEVVTDD-----DRY-SDLLMAWGQYIDHDIAFTPQstskaafgggsdcqmtcenqnpcfpiqlp 302
Cdd:cd09822 2 RPSPREI-------SNAVADQTesipnSRGlSDWFWVWGQFLDHDIDLTPD----------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 303 eearpaagtaclpfyrssaacgtgdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHar 382
Cdd:cd09822 46 ------------------------------------NPREQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTS-- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 383 lRDSGRAYLPFvpprapAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQ 462
Cdd:cd09822 86 -VANAGDLLPF------NEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 463 EARKVVGALHQIITLRDYIPRILGPEAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLP 542
Cdd:cd09822 159 AARAIVIAEIQAITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 543 glwLHQAFFSPwTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWR 622
Cdd:cd09822 235 ---LRDAFFNP-DELEENGIDPLLRGLASQVA--QEIDTFIVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 623 EFCGLPRLETPADlstaIASR-SVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWEN 701
Cdd:cd09822 309 EALGLPAVTSFSD----ITSDpDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEN 384
|
490 500 510
....*....|....*....|....*....|....*..
gi 2462576581 702 ShVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 738
Cdd:cd09822 385 D-DLLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
343-725 |
9.36e-99 |
|
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.
Pssm-ID: 188647 [Multi-domain] Cd Length: 370 Bit Score: 314.75 E-value: 9.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 343 QMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHARLRDS-GRAYLPFVPPRAPAacapepGIPGETRGPCFLAGD 421
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR--TFKGGLLKTNEVKGPSyGTELLPFNNPNPSM------GTIGLPPTRCFIAGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 422 GRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYD 501
Cdd:cd05396 73 PRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 502 STANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEhPDLPGLWLHQAFFSPW-TLLRGGGLDPLIRGLLARPAklqvqd 580
Cdd:cd05396 153 PDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQP-KEIPDVPLKDFFFNTSrSILSDTGLDPLLRGFLRQPA------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 581 QLMNEELTERLFVLSNSST--LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDN 658
Cdd:cd05396 226 GLIDQNVDDVMFLFGPLEGvgLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDD 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462576581 659 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEK-HSLSRVICDN 725
Cdd:cd05396 303 VDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
188-745 |
2.06e-67 |
|
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: 236.04 E-value: 2.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 188 VDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyngfpLPPVRevtrhviQVSNEVVTDDD------RYSDLLMAWG 261
Cdd:cd09820 8 LAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPR-------SLSNLLMKGESglpstrNRTALLVFFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 262 QYIDHDIAftpqstskaafgggsdcqmtcENQNP-C----FPIQLPEE----ARPAAGTACLPFYRSSAACGTGDqgalf 332
Cdd:cd09820 72 QHVVSEIL---------------------DASRPgCppeyFNIEIPKGdpvfDPECTGNIELPFQRSRYDKNTGY----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 333 gnlSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAegllrvhaRLRDSGRAYLPFVPPRAPAACAPEPGIPGET 412
Cdd:cd09820 126 ---SPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSGG--------RLASGDDGGFPRRNTNRLPLANPPPPSYHGT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 413 RGP--CFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEaf 490
Cdd:cd09820 195 RGPerLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN-- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 491 qqyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHP--LVRRLDASFQEHPDL----PGLWLHQAFFSPWTLLRGGGLDP 564
Cdd:cd09820 273 ---VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPgvYRRNRQCNFREVLTTsggsPALRLCNTYWNSQEPLLKSDIDE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 565 LIRGLLARPAKLqvQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASR- 643
Cdd:cd09820 350 LLLGMASQIAER--EDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLFKKd 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 644 -SVADKILDLYKH-PDNIDVWLGGLAEnfLPRARTGPLFACLIGKQMKALRDGDWFWWENSH--VFTDAQRRELEKHSLS 719
Cdd:cd09820 428 pELLERLAELYGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKngLFTAEEIEEIRNTTLR 505
|
570 580
....*....|....*....|....*.
gi 2462576581 720 RVIcdnTGLTRVPMDAFQVGKFPEDF 745
Cdd:cd09820 506 DVI---LAVTDIDNTDLQKNVFFWKN 528
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
253-742 |
9.17e-40 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188653 [Multi-domain] Cd Length: 570 Bit Score: 156.04 E-value: 9.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 253 YSDLLMAWGQYIDHDIAFTPQSTSKAAFgggsdcqmtcenqnpcfpIQLPEEARPA-AGTACLPFYRSSAACGTGDQGAL 331
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGNGTVL------------------IPLPPDDPLYdLGRGTNGMALDRGTNNAGPDGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 332 fgNLSTANPRQQmNGLTSFLDASTVYGSSPALERQLRNWT-----------SAEGLLRV--HARLRDSGRAYLPFVPPRA 398
Cdd:cd09821 75 --GTADGEGEHT-NVTTPFVDQNQTYGSHASHQVFLREYDgdgvatgrlleGATGGSARtgHAFLDDIAHNAAPKGGLGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 399 PAACAPepGIPGETRGPC----------FLAGDGRASEVPSLTALHTLWLREHNR----------------LAAALKALN 452
Cdd:cd09821 152 LRDNPT--EDPPGPGAPGsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRlvdqikdtllqsadlaFANEAGGNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 453 AHWSADAVYQEARKVVGALHQIITLRDYIPRILGP-EAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRL 531
Cdd:cd09821 230 LAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 532 DASFQEHPDLP-GL---WLHQAFFSPWTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSnsstLDLASINL 607
Cdd:cd09821 306 GPDADEGLDNQvGLidaFLNPVAFLPATLYAEEGAGAILRGMTRQVG--NEIDEFVTDALRNNLVGLP----LDLAALNI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 608 QRGRDHGLPGYNE--------------------WREFcgLPRLETPADLSTAIAS----------RSVADKI-----LDL 652
Cdd:cd09821 380 ARGRDTGLPTLNEaraqlfaatgdtilkapyesWNDF--GARLKNPESLINFIAAygthltitgaTTLAAKRaaaqdLVD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 653 YKHP----------------------DNIDVWLGGLAENFLP-RARTGPLFACLIGKQMKALRDGDWFWWENShvfTDAQ 709
Cdd:cd09821 458 GGDGapadradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR---TAGL 534
|
570 580 590
....*....|....*....|....*....|....*
gi 2462576581 710 --RRELEKHSLSRVICDNTGLTRVPMDAFQVGKFP 742
Cdd:cd09821 535 dlLNQLENNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
343-726 |
6.75e-19 |
|
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: 91.17 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 343 QMNGLTSFLDASTVYGSSPALERQLRnwtsaeglLRVHARLRDS---GRAYLPFVPPRA-------PAACAPEPGIPGET 412
Cdd:cd09816 123 RRNTSNHGIDLSQIYGLTEARTHALR--------LFKDGKLKSQminGEEYPPYLFEDGgvkmefpPLVPPLGDELTPER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 413 RGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIprilgpeafqQ 492
Cdd:cd09816 195 EAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYI----------N 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 493 YVGPYeGYDSTANPTVsnVFST-------AAFRFGHA-TIHPLV-RRLDASFQEHPdlpglwLHQAFFSPwTLLRGGGLD 563
Cdd:cd09816 265 HLSPY-HFKLFFDPEL--AFNEpwqrqnrIALEFNLLyRWHPLVpDTFNIGGQRYP------LSDFLFNN-DLVVDHGLG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 564 PLIRGLLARPAKlqvqdqlmneELTER---LFVLsnssTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLStai 640
Cdd:cd09816 335 ALVDAASRQPAG----------RIGLRntpPFLL----PVEVRSI--EQGRKLRLASFNDYRKRFGLPPYTSFEELT--- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 641 ASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIG----KQmkALRD--GDWFWWeNSHVFTDAQRRELE 714
Cdd:cd09816 396 GDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIV 472
|
410
....*....|...
gi 2462576581 715 K-HSLSRVICDNT 726
Cdd:cd09816 473 KtATLQDLVCRNV 485
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
345-672 |
4.77e-13 |
|
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death.
Pssm-ID: 188650 [Multi-domain] Cd Length: 484 Bit Score: 72.70 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 345 NGLTSFLDASTVYGSSPALERQLRnwTSAEGllrvhARLRDSGRAYLPfvpprapaaCAPEPGIPgetrgpcfLAGDGRA 424
Cdd:cd09818 88 NTNTHWWDGSQIYGSTEEAQKRLR--TFPPD-----GKLKLDADGLLP---------VDEHTGLP--------LTGFNDN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 425 SEVpSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQqyVGPYEGYDSTA 504
Cdd:cd09818 144 WWV-GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPTLE--IAMRANWWGLL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 505 NPTVSNVfstaafrFGHATIHPLVRRLDAS------------------FQEHPDLPGLWlhqAFFS----------PWTL 556
Cdd:cd09818 221 GERLKRV-------LGRDGTSELLSGIPGSppnhhgvpyslteefvavYRMHPLIPDDI---DFRSaddgatgeeiSLTD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 557 LRGGGLDPLIRGL----------LARPAKLqvqdQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCG 626
Cdd:cd09818 291 LAGGKARELLRKLgfadllysfgITHPGAL----TLHNYPRFLRDLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLH 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462576581 627 LPRLETPADLSTAiasRSVADKILDLY-KHPDNIDVWLGGLAENFLP 672
Cdd:cd09818 367 LPPAKSFEDLTGD---EEVAAELREVYgGDVEKVDLLVGLLAEPLPP 410
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
338-616 |
2.57e-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: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 338 ANPRQQMNGLTSFLDASTVYGSSPALERQLRnwtsaegllrVHARLRDSGRAYLPFVPPRAPAACAPEPG--IP--GETR 413
Cdd:cd09819 74 IDPAELRNFRTPALDLDSVYGGGPDGSPYLY----------DQATPNDGAKLRVGRESPGGPGGLPGDGArdLPrnGQGT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 414 GpcfLAGDGRASEVPSLTALHTLWLREHNRLAAALKALnaHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY 493
Cdd:cd09819 144 A---LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAH--GTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPDVVDDV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 494 V----GPYEGYDSTAnPTVSNVFSTAAFRFGHATIHPLVrRLDASFQEHPdlpglwlHQAFFSpwtllRGGGLDPLIRGL 569
Cdd:cd09819 219 LangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVRASY-DYNRNFPDAS-------LELLFT-----FTGGGEGDLGGF 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462576581 570 LARPAKLQVQ-------------------DQLMNEELtERLF---VLSNSSTLDLASINLQRGRDHGLP 616
Cdd:cd09819 285 SPLPENWIIDwrrffdidgsappqfarkiDTKLAPPL-FDLPnggVGLAPPMKSLAFRNLLRGYRLGLP 352
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
823-866 |
1.04e-09 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 54.56 E-value: 1.04e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2462576581 823 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 866
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
823-852 |
1.34e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 54.17 E-value: 1.34e-09
10 20 30
....*....|....*....|....*....|
gi 2462576581 823 DVNECADGAHPpCHASARCRNTKGGFQCLC 852
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
823-866 |
2.38e-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: 53.41 E-value: 2.38e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2462576581 823 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 866
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
769-822 |
6.59e-09 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 52.85 E-value: 6.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462576581 769 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 822
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| EGF_3 |
pfam12947 |
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ... |
827-865 |
9.32e-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: 51.83 E-value: 9.32e-09
10 20 30
....*....|....*....|....*....|....*....
gi 2462576581 827 CADGAHPpCHASARCRNTKGGFQCLCADPYELgdDGRTC 865
Cdd:pfam12947 1 CSDNNGG-CHPNATCTNTGGSFTCTCNDGYTG--DGVTC 36
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
769-821 |
5.10e-08 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 50.22 E-value: 5.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462576581 769 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 821
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
769-821 |
7.00e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.03 E-value: 7.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462576581 769 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 821
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
838-865 |
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: 41.84 E-value: 2.77e-05
10 20
....*....|....*....|....*...
gi 2462576581 838 SARCRNTKGGFQCLCADPYELGDDGRTC 865
Cdd:pfam14670 9 SHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
596-668 |
9.67e-05 |
|
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme peroxidases, catalyze the oxygenation of linoleate and similar targets. Linoleate (8R)-dioxygenase, also called linoleate:oxygen 7S,8S-oxidoreductase, generates (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate as a product. Other members are 5,8-linoleate dioxygenase (LDS, ppoA) and linoleate 10R-dioxygenase (ppoC), involved in the biosynthesis of oxylipins.
Pssm-ID: 188649 [Multi-domain] Cd Length: 550 Bit Score: 46.18 E-value: 9.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462576581 596 NSSTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAE 668
Cdd:cd09817 371 SLKVIEILGI--LQAREWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAE 438
|
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
826-858 |
1.26e-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: 40.15 E-value: 1.26e-04
10 20 30
....*....|....*....|....*....|...
gi 2462576581 826 ECAdgAHPPCHASARCRNTKGGFQCLCADPYEL 858
Cdd:cd00053 1 ECA--ASNPCSNGGTCVNTPGSYRCVCPPGYTG 31
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
716-825 |
9.69e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462576581 716 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsIPGMNLEAWRETFP--QDDKCGFPESVE 776
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462576581 777 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 825
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICKMIN 148
|
|
| EGF |
smart00181 |
Epidermal growth factor-like domain; |
826-866 |
9.59e-03 |
|
Epidermal growth factor-like domain;
Pssm-ID: 214544 Cd Length: 35 Bit Score: 34.80 E-value: 9.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2462576581 826 ECADgaHPPCHaSARCRNTKGGFQCLCADPYELgddGRTCV 866
Cdd:smart00181 1 ECAS--GGPCS-NGTCINTPGSYTCSCPPGYTG---DKRCE 35
|
|
| |
