|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
167-734 |
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: 1076.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 167 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 246
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 247 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 326
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 327 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACApepGIPGETRGPCFLAGDGRASEVPSLTAL 406
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP---DPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 407 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 486
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 487 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFV 566
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 567 LSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 646
Cdd:cd09825 398 LSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 647 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 726
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 28558982 727 MNLEAWRE 734
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
151-709 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 699.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 151 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 230
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 231 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 307
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 308 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 387
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 388 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 466
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 467 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTLLrGGGLDPLIRGLLA 544
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLAT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 545 RPAKLqvQDQLMNEELTERLFVLSNSST-LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKIL 623
Cdd:pfam03098 366 QPAQA--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 624 DLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-G 700
Cdd:pfam03098 443 ELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdI 522
|
....*....
gi 28558982 701 LTRVPMDAF 709
Cdd:pfam03098 523 IETIQPNVF 531
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
796-839 |
8.15e-10 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 54.56 E-value: 8.15e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558982 796 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 839
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
796-825 |
1.15e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 54.17 E-value: 1.15e-09
10 20 30
....*....|....*....|....*....|
gi 28558982 796 DVNECADGAHPpCHASARCRNTKGGFQCLC 825
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
796-839 |
1.81e-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: 53.79 E-value: 1.81e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558982 796 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 839
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
742-795 |
5.48e-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: 5.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558982 742 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 795
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
742-794 |
4.19e-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: 50.60 E-value: 4.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558982 742 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 794
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
742-794 |
6.29e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.41 E-value: 6.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558982 742 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 794
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
689-798 |
8.43e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 689 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 749
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558982 750 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 798
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICKMIN 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
167-734 |
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: 1076.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 167 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 246
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 247 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 326
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 327 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACApepGIPGETRGPCFLAGDGRASEVPSLTAL 406
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNP---DPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 407 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 486
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 487 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFV 566
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 567 LSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 646
Cdd:cd09825 398 LSNSSTLDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 647 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 726
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 28558982 727 MNLEAWRE 734
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
151-709 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 699.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 151 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 230
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 231 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 307
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 308 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 387
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 388 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 466
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 467 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTLLrGGGLDPLIRGLLA 544
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLAT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 545 RPAKLqvQDQLMNEELTERLFVLSNSST-LDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKIL 623
Cdd:pfam03098 366 QPAQA--VDNNFTEELTNHLFGPPGEFSgLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 624 DLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-G 700
Cdd:pfam03098 443 ELYGSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdI 522
|
....*....
gi 28558982 701 LTRVPMDAF 709
Cdd:pfam03098 523 IETIQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
275-723 |
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: 558.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 275 PEEARPAAGTACLPFYRSSAACGTGDQGALFGNLStanPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHA 354
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVT---PREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 355 RLRdSGRAYLPFVPPRAPAACAPepgiPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVY 434
Cdd:cd09826 78 VSE-AGKPLLPFERDSPMDCRRD----PNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 435 QEARKVVGALHQIITLRDYIPRILGPEAFQQyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHP-- 512
Cdd:cd09826 153 HETRKIVGAQMQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPeg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 513 DLPglwLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYN 592
Cdd:cd09826 232 HLP---LHKAFFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEVALDLAALNIQRGRDHGLPGYN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 593 EWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWW 672
Cdd:cd09826 309 DYRKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 28558982 673 ENSHVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAFQVGKFPEDFESCDS 723
Cdd:cd09826 389 ENPGVFSPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
312-718 |
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: 535.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 312 NPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGipgeTRGPCFL 391
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTS----ANIPCFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 392 AGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAfQQYVGPYE 471
Cdd:cd09824 86 AGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA-AARLPPYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 472 GYDSTANPTVSNVFSTAaFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQV 551
Cdd:cd09824 165 GYNESVDPRIANVFTTA-FRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAKLNN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 552 QDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDN 631
Cdd:cd09824 244 QNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 632 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 711
Cdd:cd09824 324 IDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQP 403
|
....*..
gi 28558982 712 GKFPEDF 718
Cdd:cd09824 404 NSYPRDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
314-698 |
1.99e-168 |
|
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.
Pssm-ID: 188655 [Multi-domain] Cd Length: 378 Bit Score: 495.56 E-value: 1.99e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 314 RQQMNGLTSFLDASTVYGSSPALERQLRNWTsaEGLLRVHarlRDSGRAYLPFVPPRAPAacapepGIPGETRGPCFLAG 393
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFK--GGLLKTQ---RRNGRELLPFSNNPTDD------CSLSSAGKPCFLAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 394 DGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY------V 467
Cdd:cd09823 70 DGRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 468 GPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglwLHQAFFSPWTLLRGGGLDPLIRGLLARPA 547
Cdd:cd09823 150 GYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVN---LHDLFFNPDRLYEEGGLDPLLRGLATQPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 548 KlQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYK 627
Cdd:cd09823 227 Q-KVDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYK 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28558982 628 HPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHV---FTDAQRRELEKHSLSRVICDN 698
Cdd:cd09823 305 SVDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
202-711 |
2.32e-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: 2.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 202 LPPVREVtrhviqvSNEVVTDD-----DRY-SDLLMAWGQYIDHDIAFTPQstskaafgggadcqmtcenqnpcfpiqlp 275
Cdd:cd09822 2 RPSPREI-------SNAVADQTesipnSRGlSDWFWVWGQFLDHDIDLTPD----------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 276 eearpaagtaclpfyrssaacgtgdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHar 355
Cdd:cd09822 46 ------------------------------------NPREQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTS-- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 356 lRDSGRAYLPFvpprapAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQ 435
Cdd:cd09822 86 -VANAGDLLPF------NEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 436 EARKVVGALHQIITLRDYIPRILGPEAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLP 515
Cdd:cd09822 159 AARAIVIAEIQAITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 516 glwLHQAFFSPwTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWR 595
Cdd:cd09822 235 ---LRDAFFNP-DELEENGIDPLLRGLASQVA--QEIDTFIVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 596 EFCGLPRLETPADlstaIASR-SVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWEN 674
Cdd:cd09822 309 EALGLPAVTSFSD----ITSDpDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEN 384
|
490 500 510
....*....|....*....|....*....|....*..
gi 28558982 675 ShVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 711
Cdd:cd09822 385 D-DLLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
316-698 |
1.21e-98 |
|
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: 313.98 E-value: 1.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 316 QMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHARLRDS-GRAYLPFVPPRAPAacapepGIPGETRGPCFLAGD 394
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR--TFKGGLLKTNEVKGPSyGTELLPFNNPNPSM------GTIGLPPTRCFIAGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 395 GRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYD 474
Cdd:cd05396 73 PRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 475 STANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQ--EHPDLPglwLHQAFFSPW-TLLRGGGLDPLIRGLLARPAKLQV 551
Cdd:cd05396 153 PDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQpkEIPDVP---LKDFFFNTSrSILSDTGLDPLLRGFLRQPAGLID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 552 QdqlmNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDN 631
Cdd:cd05396 230 Q----NVDDVMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDD 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28558982 632 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEK-HSLSRVICDN 698
Cdd:cd05396 303 VDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
159-728 |
1.68e-70 |
|
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.
Pssm-ID: 188652 [Multi-domain] Cd Length: 558 Bit Score: 244.13 E-value: 1.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 159 NNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyngfpLPPVRevtrhviQVSNEVVTDDD------RYSDLLMA 232
Cdd:cd09820 6 NNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPR-------SLSNLLMKGESglpstrNRTALLVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 233 WGQYIDHDIAftpqstskaafgggadcqmtcENQNP-C----FPIQLPEE----ARPAAGTACLPFYRSSAACGTGDqga 303
Cdd:cd09820 70 FGQHVVSEIL---------------------DASRPgCppeyFNIEIPKGdpvfDPECTGNIELPFQRSRYDKNTGY--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 304 lfgnlSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAegllrvhaRLRDSGRAYLPFVPPRAPAACAPEPGIPG 383
Cdd:cd09820 126 -----SPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSGG--------RLASGDDGGFPRRNTNRLPLANPPPPSYH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 384 ETRGP--CFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPE 461
Cdd:cd09820 193 GTRGPerLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 462 afqqyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLV--RRLDASFQEHPDL----PGLWLHQAFFSPWTLLRGGGL 535
Cdd:cd09820 273 -----VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVyrRNRQCNFREVLTTsggsPALRLCNTYWNSQEPLLKSDI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 536 DPLIRGLLARPAKLqvQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIAS 615
Cdd:cd09820 348 DELLLGMASQIAER--EDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDLFK 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 616 R--SVADKILDLYKH-PDNIDVWLGGLAEnfLPRARTGPLFACLIGKQMKALRDGDWFWWENSH--VFTDAQRRELEKHS 690
Cdd:cd09820 426 KdpELLERLAELYGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKngLFTAEEIEEIRNTT 503
|
570 580 590
....*....|....*....|....*....|....*....
gi 28558982 691 LSRVIcdnTGLTRVPMDAFQVGKFPEDFES-CDSITGMN 728
Cdd:cd09820 504 LRDVI---LAVTDIDNTDLQKNVFFWKNGDpCPQPKQLT 539
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
226-715 |
8.52e-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: 8.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 226 YSDLLMAWGQYIDHDIAFTPQSTSKAAFgggadcqmtcenqnpcfpIQLPEEARPA-AGTACLPFYRSSAACGTGDQGAL 304
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGNGTVL------------------IPLPPDDPLYdLGRGTNGMALDRGTNNAGPDGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 305 fgNLSTANPRQQmNGLTSFLDASTVYGSSPALERQLRNWT-----------SAEGLLRV--HARLRDSGRAYLPFVPPRA 371
Cdd:cd09821 75 --GTADGEGEHT-NVTTPFVDQNQTYGSHASHQVFLREYDgdgvatgrlleGATGGSARtgHAFLDDIAHNAAPKGGLGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 372 PAACAPepGIPGETRGPC----------FLAGDGRASEVPSLTALHTLWLREHNR----------------LAAALKALN 425
Cdd:cd09821 152 LRDNPT--EDPPGPGAPGsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRlvdqikdtllqsadlaFANEAGGNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 426 AHWSADAVYQEARKVVGALHQIITLRDYIPRILGP-EAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRL 504
Cdd:cd09821 230 LAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 505 DASFQEHPDLP-GL---WLHQAFFSPWTLLRGGGLDPLIRGLLARPAklQVQDQLMNEELTERLFVLSnsstLDLASINL 580
Cdd:cd09821 306 GPDADEGLDNQvGLidaFLNPVAFLPATLYAEEGAGAILRGMTRQVG--NEIDEFVTDALRNNLVGLP----LDLAALNI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 581 QRGRDHGLPGYNE--------------------WREFcgLPRLETPADLSTAIAS----------RSVADKI-----LDL 625
Cdd:cd09821 380 ARGRDTGLPTLNEaraqlfaatgdtilkapyesWNDF--GARLKNPESLINFIAAygthltitgaTTLAAKRaaaqdLVD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 626 YKHP----------------------DNIDVWLGGLAENFLP-RARTGPLFACLIGKQMKALRDGDWFWWENShvfTDAQ 682
Cdd:cd09821 458 GGDGapadradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR---TAGL 534
|
570 580 590
....*....|....*....|....*....|....*
gi 28558982 683 --RRELEKHSLSRVICDNTGLTRVPMDAFQVGKFP 715
Cdd:cd09821 535 dlLNQLENNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
316-699 |
9.72e-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: 90.40 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 316 QMNGLTSFLDASTVYGSSPALERQLRnwtsaeglLRVHARLRDS---GRAYLPFVPPRA-------PAACAPEPGIPGET 385
Cdd:cd09816 123 RRNTSNHGIDLSQIYGLTEARTHALR--------LFKDGKLKSQminGEEYPPYLFEDGgvkmefpPLVPPLGDELTPER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 386 RGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIprilgpeafqQ 465
Cdd:cd09816 195 EAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYI----------N 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 466 YVGPYeGYDSTANPTVsnVFST-------AAFRFGHA-TIHPLV-RRLDASFQEHPdlpglwLHQAFFSPwTLLRGGGLD 536
Cdd:cd09816 265 HLSPY-HFKLFFDPEL--AFNEpwqrqnrIALEFNLLyRWHPLVpDTFNIGGQRYP------LSDFLFNN-DLVVDHGLG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 537 PLIRGLLARPAKlqvqdqlmneELTER---LFVLsnssTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLStai 613
Cdd:cd09816 335 ALVDAASRQPAG----------RIGLRntpPFLL----PVEVRSI--EQGRKLRLASFNDYRKRFGLPPYTSFEELT--- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 614 ASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIG----KQmkALRD--GDWFWWeNSHVFTDAQRRELE 687
Cdd:cd09816 396 GDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIV 472
|
410
....*....|...
gi 28558982 688 K-HSLSRVICDNT 699
Cdd:cd09816 473 KtATLQDLVCRNV 485
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
318-645 |
5.91e-13 |
|
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death.
Pssm-ID: 188650 [Multi-domain] Cd Length: 484 Bit Score: 72.32 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 318 NGLTSFLDASTVYGSSPALERQLRnwTSAEGllrvhARLRDSGRAYLPfvpprapaaCAPEPGIPgetrgpcfLAGDGRA 397
Cdd:cd09818 88 NTNTHWWDGSQIYGSTEEAQKRLR--TFPPD-----GKLKLDADGLLP---------VDEHTGLP--------LTGFNDN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 398 SEVpSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQqyVGPYEGYDSTA 477
Cdd:cd09818 144 WWV-GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPTLE--IAMRANWWGLL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 478 NPTVSNVfstaafrFGHATIHPLVRRLDASFQE------------------HPDLPGLWlhqAFFS----------PWTL 529
Cdd:cd09818 221 GERLKRV-------LGRDGTSELLSGIPGSPPNhhgvpyslteefvavyrmHPLIPDDI---DFRSaddgatgeeiSLTD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 530 LRGGGLDPLIRGL----------LARPAKLqvqdQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCG 599
Cdd:cd09818 291 LAGGKARELLRKLgfadllysfgITHPGAL----TLHNYPRFLRDLHRPDGRVIDLAAIDILRDRERGVPRYNEFRRLLH 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 28558982 600 LPRLETPADLSTAiasRSVADKILDLY-KHPDNIDVWLGGLAENFLP 645
Cdd:cd09818 367 LPPAKSFEDLTGD---EEVAAELREVYgGDVEKVDLLVGLLAEPLPP 410
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
311-589 |
2.79e-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: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 311 ANPRQQMNGLTSFLDASTVYGSSPALERQLRnwtsaegllrVHARLRDSGRAYLPFVPPRAPAACAPEPG--IP--GETR 386
Cdd:cd09819 74 IDPAELRNFRTPALDLDSVYGGGPDGSPYLY----------DQATPNDGAKLRVGRESPGGPGGLPGDGArdLPrnGQGT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 387 GpcfLAGDGRASEVPSLTALHTLWLREHNRLAAALKALnaHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY 466
Cdd:cd09819 144 A---LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAH--GTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPDVVDDV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 467 V----GPYEGYDSTAnPTVSNVFSTAAFRFGHATIHPLVrRLDASFQEHPdlpglwlHQAFFSpwtllRGGGLDPLIRGL 542
Cdd:cd09819 219 LangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVRASY-DYNRNFPDAS-------LELLFT-----FTGGGEGDLGGF 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28558982 543 LARPAKLQVQ-------------------DQLMNEELtERLF---VLSNSSTLDLASINLQRGRDHGLP 589
Cdd:cd09819 285 SPLPENWIIDwrrffdidgsappqfarkiDTKLAPPL-FDLPnggVGLAPPMKSLAFRNLLRGYRLGLP 352
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
796-839 |
8.15e-10 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 54.56 E-value: 8.15e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558982 796 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgdDGRTCV 839
Cdd:smart00179 1 DIDECASG--NPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39
|
|
| EGF_CA |
pfam07645 |
Calcium-binding EGF domain; |
796-825 |
1.15e-09 |
|
Calcium-binding EGF domain;
Pssm-ID: 429571 Cd Length: 32 Bit Score: 54.17 E-value: 1.15e-09
10 20 30
....*....|....*....|....*....|
gi 28558982 796 DVNECADGAHPpCHASARCRNTKGGFQCLC 825
Cdd:pfam07645 1 DVDECATGTHN-CPANTVCVNTIGSFECRC 29
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
796-839 |
1.81e-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: 53.79 E-value: 1.81e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 28558982 796 DVNECADGahPPCHASARCRNTKGGFQCLCADPYElgddGRTCV 839
Cdd:cd00054 1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
742-795 |
5.48e-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: 5.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558982 742 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 795
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| EGF_3 |
pfam12947 |
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ... |
800-838 |
7.37e-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: 7.37e-09
10 20 30
....*....|....*....|....*....|....*....
gi 28558982 800 CADGAHPpCHASARCRNTKGGFQCLCADPYELgdDGRTC 838
Cdd:pfam12947 1 CSDNNGG-CHPNATCTNTGGSFTCTCNDGYTG--DGVTC 36
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
742-794 |
4.19e-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: 50.60 E-value: 4.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558982 742 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 794
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
742-794 |
6.29e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.41 E-value: 6.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28558982 742 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 794
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| FXa_inhibition |
pfam14670 |
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ... |
811-838 |
2.37e-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: 42.23 E-value: 2.37e-05
10 20
....*....|....*....|....*...
gi 28558982 811 SARCRNTKGGFQCLCADPYELGDDGRTC 838
Cdd:pfam14670 9 SHLCLNTPGGYTCSCPEGYELQDDGRTC 36
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
569-641 |
9.34e-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: 9.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28558982 569 NSSTLDLASInlQRGRDHGLPGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAE 641
Cdd:cd09817 371 SLKVIEILGI--LQAREWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAE 438
|
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
799-831 |
1.02e-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: 1.02e-04
10 20 30
....*....|....*....|....*....|...
gi 28558982 799 ECAdgAHPPCHASARCRNTKGGFQCLCADPYEL 831
Cdd:cd00053 1 ECA--ASNPCSNGGTCVNTPGSYRCVCPPGYTG 31
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
689-798 |
8.43e-04 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 42.34 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558982 689 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 749
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 28558982 750 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCKDVN 798
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICKMIN 148
|
|
| EGF |
smart00181 |
Epidermal growth factor-like domain; |
799-839 |
7.43e-03 |
|
Epidermal growth factor-like domain;
Pssm-ID: 214544 Cd Length: 35 Bit Score: 35.19 E-value: 7.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 28558982 799 ECADgaHPPCHaSARCRNTKGGFQCLCADPYELgddGRTCV 839
Cdd:smart00181 1 ECAS--GGPCS-NGTCINTPGSYTCSCPPGYTG---DKRCE 35
|
|
| |
