|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
179-689 |
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: 931.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 179 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 258
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 259 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 338
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 339 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVpprAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTAL 418
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQ---PEEVSSCNPDPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 419 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 498
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 499 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGG--------------------------------- 545
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGgldpvirgliggpaklvtpddlmneelteklfv 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 546 ------------------------YNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 601
Cdd:cd09825 398 lsnsstldlaslnlqrgrdhglpgYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 602 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 681
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 1370478783 682 MNLEAWRE 689
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
163-664 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 599.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 163 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 242
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 243 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 319
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 320 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 399
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 400 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 478
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 479 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTL--------LRG---- 544
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLyeggidplLRGlatq 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 545 -------------------------------------------GYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLY 581
Cdd:pfam03098 367 paqavdnnfteeltnhlfgppgefsgldlaalniqrgrdhglpGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELY 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 582 KHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-GLTR 658
Cdd:pfam03098 446 GSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIET 525
|
....*.
gi 1370478783 659 VPMDAF 664
Cdd:pfam03098 526 IQPNVF 531
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
697-750 |
4.27e-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: 53.24 E-value: 4.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478783 697 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 750
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
697-749 |
3.34e-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: 3.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478783 697 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 749
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
697-749 |
5.00e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.41 E-value: 5.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478783 697 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 749
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
644-750 |
3.60e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 40.42 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 644 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 704
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370478783 705 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCK 750
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICK 145
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
179-689 |
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: 931.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 179 GASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQ 258
Cdd:cd09825 1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 259 STSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDA 338
Cdd:cd09825 81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRILGRACLPFFRSSAVCGTGDTSTLFGNLSLANPREQINGLTSFIDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 339 STVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVpprAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTAL 418
Cdd:cd09825 161 STVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQ---PEEVSSCNPDPNGGERVPCFLAGDGRASEVLTLTAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 419 HTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFS 498
Cdd:cd09825 238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEAFDQYGGYYEGYDPTVNPTVSNVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 499 TAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGG--------------------------------- 545
Cdd:cd09825 318 TAAFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGgldpvirgliggpaklvtpddlmneelteklfv 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 546 ------------------------YNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPR 601
Cdd:cd09825 398 lsnsstldlaslnlqrgrdhglpgYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 602 ARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITG 681
Cdd:cd09825 478 ARTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPG 557
|
....*...
gi 1370478783 682 MNLEAWRE 689
Cdd:cd09825 558 INLEAWRE 565
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
163-664 |
0e+00 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 599.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 163 YRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyNGFPLPPVREVTRHVIQvsNEVVTDDDRYSDLL 242
Cdd:pfam03098 1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 243 MAWGQYIDHDIAFTPQSTSKAAFGGgaDCQMTCENQNP-CFPIQLPEEAR--PAAGTACLPFYRSSAACGTGdqgalfgn 319
Cdd:pfam03098 74 MQWGQFIDHDLTLTPESTSPNGSSC--DCCCPPENLHPpCFPIPIPPDDPffSPFGVRCMPFVRSAPGCGLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 320 lstaNPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSaeGLLRVhaRLRDSGRAYLPFvpprapaACAPEPGIPGETRG 399
Cdd:pfam03098 144 ----NPREQINQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKV--NRSDDGKELLPF-------DPDGPCCCNSSGGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 400 PCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY- 478
Cdd:pfam03098 209 PCFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 479 --VGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDasFQEHPDLPGLWLHQAFFSPWTL--------LRG---- 544
Cdd:pfam03098 289 llPLPYNGYDPNVDPSISNEFATAAFRFGHSLIPPFLYRLD--ENNVPEEPSLRLHDSFFNPDRLyeggidplLRGlatq 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 545 -------------------------------------------GYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLY 581
Cdd:pfam03098 367 paqavdnnfteeltnhlfgppgefsgldlaalniqrgrdhglpGYNDYREFCGLPPAKSFEDLTDVI-PNEVIAKLRELY 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 582 KHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENS--HVFTDAQRRELEKHSLSRVICDNT-GLTR 658
Cdd:pfam03098 446 GSVDDIDLWVGGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIET 525
|
....*.
gi 1370478783 659 VPMDAF 664
Cdd:pfam03098 526 IQPNVF 531
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
287-678 |
3.26e-145 |
|
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix.
Pssm-ID: 188658 Cd Length: 440 Bit Score: 435.20 E-value: 3.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 287 PEEARPAAGTACLPFYRSSAACGTGDQGALFGNLStanPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHA 366
Cdd:cd09826 1 PPDDPRRRGHRCIEFVRSSAVCGSGSTSLLFNSVT---PREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 367 RLRdSGRAYLPFVPPRAPAACAPepgiPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVY 446
Cdd:cd09826 78 VSE-AGKPLLPFERDSPMDCRRD----PNESPIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 447 QEARKVVGALHQIITLRDYIPRILGPEAFQQyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHP-- 524
Cdd:cd09826 153 HETRKIVGAQMQHITYSHWLPKILGPVGMEM-LGEYRGYNPNVNPSIANEFATAAFRFGHTLINPILFRLDEDFQPIPeg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 525 DLPglwLHQAFFSPWTL---------LRG------------------------------------------------GYN 547
Cdd:cd09826 232 HLP---LHKAFFAPYRLvneggidplLRGlfataakdrvpdqllntelteklfemahevaldlaalniqrgrdhglpGYN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 548 EWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWW 627
Cdd:cd09826 309 DYRKFCNLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1370478783 628 ENSHVFTDAQRRELEKHSLSRVICDNT-GLTRVPMDAFQVGKFPEDFESCDS 678
Cdd:cd09826 389 ENPGVFSPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
324-673 |
2.74e-140 |
|
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of animal heme peroxidases contains members with somewhat diverse functions. Myeloperoxidases are lysosomal proteins found in azurophilic granules of neutrophils and the lysosomes of monocytes. They are involved in the formation of microbicidal agents upon activation of activated neutrophils (neutrophils undergoing respiratory bursts as a result of phagocytosis), by catalyzing the conversion of hydrogen peroxide to hypochlorous acid. As a heme protein, myeloperoxidase is responsible for the greenish tint of pus, which is rich in neutrophils. Eosinophil peroxidases are haloperoxidases as well, preferring bromide over chloride. Expressed by eosinophil granulocytes, they are involved in attacking multicellular parasites and play roles in various inflammatory diseases such as asthma. The haloperoxidase lactoperoxidase is secreted from mucosal glands and provides antibacterial activity by oxidizing a variety of substrates such as bromide or chloride in the presence of hydrogen peroxide.
Pssm-ID: 188656 [Multi-domain] Cd Length: 411 Bit Score: 421.44 E-value: 2.74e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 324 NPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGipgeTRGPCFL 403
Cdd:cd09824 10 NVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTS----ANIPCFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 404 AGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAfQQYVGPYE 483
Cdd:cd09824 86 AGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA-AARLPPYR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 484 GYDSTANPTVSNVFSTaAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWT---------LLRG---------- 544
Cdd:cd09824 165 GYNESVDPRIANVFTT-AFRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRiireggidpILRGlmatpaklnn 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 545 --------------------------------------GYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDN 586
Cdd:cd09824 244 qnqmlvdelrerlfqqtkrmgldlaalnlqrgrdhglpGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYGTPDN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 587 IDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 666
Cdd:cd09824 324 IDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRDPFQP 403
|
....*..
gi 1370478783 667 GKFPEDF 673
Cdd:cd09824 404 NSYPRDF 410
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
326-653 |
9.38e-133 |
|
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: 400.80 E-value: 9.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 326 RQQMNGLTSFLDASTVYGSSPALERQLRNWTsaEGLLRVHarlRDSGRAYLPFVPPRAPAacapepGIPGETRGPCFLAG 405
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFK--GGLLKTQ---RRNGRELLPFSNNPTDD------CSLSSAGKPCFLAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 406 DGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY------V 479
Cdd:cd09823 70 DGRVNEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 480 GPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPglwLHQAFFSPWT---------LLRG------ 544
Cdd:cd09823 150 GYFNGYDPNVDPSILNEFAAAAFRFGHSLVPGTFERLDENYRPQGSVN---LHDLFFNPDRlyeeggldpLLRGlatqpa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 545 -----------------------------------------GYNEWREFCGLPRLETPADLSTAIaSRSVADKILDLYKH 583
Cdd:cd09823 227 qkvdrfftdeltthfffrggnpfgldlaalniqrgrdhglpGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYKS 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370478783 584 PDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHV---FTDAQRRELEKHSLSRVICDN 653
Cdd:cd09823 306 VDDIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
214-666 |
1.22e-83 |
|
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.
Pssm-ID: 188654 [Multi-domain] Cd Length: 420 Bit Score: 273.80 E-value: 1.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 214 LPPVREVtrhviqvSNEVVTDD-----DRY-SDLLMAWGQYIDHDIAFTPQstskaafgggadcqmtcenqnpcfpiqlp 287
Cdd:cd09822 2 RPSPREI-------SNAVADQTesipnSRGlSDWFWVWGQFLDHDIDLTPD----------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 288 eearpaagtaclpfyrssaacgtgdqgalfgnlstaNPRQQMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHar 367
Cdd:cd09822 46 ------------------------------------NPREQINAITAYIDGSNVYGSDEERADALR--SFGGGKLKTS-- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 368 lRDSGRAYLPFvpprapAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQ 447
Cdd:cd09822 86 -VANAGDLLPF------NEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 448 EARKVVGALHQIITLRDYIPRILGPEAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLP 527
Cdd:cd09822 159 AARAIVIAEIQAITYNEFLPALLGENAL----PAYSGYDETVNPGISNEFSTAAYRFGHSMLSSELLRGDEDGTEATSLA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 528 glwLHQAFFSPW--------TLLRG----------------------------------------------GYNEWREFC 553
Cdd:cd09822 235 ---LRDAFFNPDeleengidPLLRGlasqvaqeidtfivddvrnflfgppgaggfdlaalniqrgrdhglpSYNQLREAL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 554 GLPRLETPADlstaIASR-SVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENShV 632
Cdd:cd09822 312 GLPAVTSFSD----ITSDpDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-D 386
|
490 500 510
....*....|....*....|....*....|....
gi 1370478783 633 FTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQV 666
Cdd:cd09822 387 LLLDEIADIENTTLADVIRRNTDVDDIQDNVFLV 420
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
328-653 |
2.36e-75 |
|
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.
Pssm-ID: 188647 [Multi-domain] Cd Length: 370 Bit Score: 250.04 E-value: 2.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 328 QMNGLTSFLDASTVYGSSPALERQLRnwTSAEGLLRVHARLRDS-GRAYLPFVPPRAPAacapepGIPGETRGPCFLAGD 406
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALR--TFKGGLLKTNEVKGPSyGTELLPFNNPNPSM------GTIGLPPTRCFIAGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 407 GRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYD 486
Cdd:cd05396 73 PRVNENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 487 STANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQ--EHPDLPglwLHQAFFSPW----------TLLRG---------- 544
Cdd:cd05396 153 PDVVPYVLSEFFTAAYRFGHSLVPEGVDRIDENGQpkEIPDVP---LKDFFFNTSrsilsdtgldPLLRGflrqpaglid 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 545 ----------------------------------GYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVW 590
Cdd:cd05396 230 qnvddvmflfgplegvgldlaalniqrgrdlglpSYNEVRRFIGLKPPTSFQDILT---DPELAKKLAELYGDPDDVDLW 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370478783 591 LGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEK-HSLSRVICDN 653
Cdd:cd05396 307 VGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKlISLADIICLN 370
|
|
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
171-683 |
4.74e-52 |
|
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.
Pssm-ID: 188652 [Multi-domain] Cd Length: 558 Bit Score: 191.36 E-value: 4.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 171 NNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNpgflyngfpLPPVRevtrhviQVSNEVVTDDD------RYSDLLMA 244
Cdd:cd09820 6 NNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPR-------SLSNLLMKGESglpstrNRTALLVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 245 WGQYIDHDIAftpqstskaafgggadcqmtcENQNP-C----FPIQLPEE----ARPAAGTACLPFYRSSAACGTGDqga 315
Cdd:cd09820 70 FGQHVVSEIL---------------------DASRPgCppeyFNIEIPKGdpvfDPECTGNIELPFQRSRYDKNTGY--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 316 lfgnlSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAegllrvhaRLRDSGRAYLPFVPPRAPAACAPEPGIPG 395
Cdd:cd09820 126 -----SPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSFSGG--------RLASGDDGGFPRRNTNRLPLANPPPPSYH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 396 ETRGP--CFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPE 473
Cdd:cd09820 193 GTRGPerLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 474 afqqyVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHP--LVRRLDASFQEH---------------------------- 523
Cdd:cd09820 273 -----VPPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPgvYRRNRQCNFREVlttsggspalrlcntywnsqepllksdi 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 524 --------------------PDLPGLWLHQAFFS-----PWTLLRG------GYNEWREFCGLPRLETPADLSTAIASR- 571
Cdd:cd09820 348 delllgmasqiaeredniivEDLRDYLFGPLEFSrrdlmALNIQRGrdhglpDYNTAREAFGLPPRTTWSDINPDLFKKd 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 572 -SVADKILDLYKH-PDNIDVWLGGLAEnfLPRARTGPLFACLIGKQMKALRDGDWFWWENSH--VFTDAQRRELEKHSLS 647
Cdd:cd09820 428 pELLERLAELYGNdLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVKngLFTAEEIEEIRNTTLR 505
|
570 580 590
....*....|....*....|....*....|....*..
gi 1370478783 648 RVIcdnTGLTRVPMDAFQVGKFPEDFES-CDSITGMN 683
Cdd:cd09820 506 DVI---LAVTDIDNTDLQKNVFFWKNGDpCPQPKQLT 539
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
238-670 |
4.17e-26 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188653 [Multi-domain] Cd Length: 570 Bit Score: 114.05 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 238 YSDLLMAWGQYIDHDIAFTPQSTSKAAFgggadcqmtcenqnpcfpIQLPEEARPA-AGTACLPFYRSSAACGTGDQGAL 316
Cdd:cd09821 13 YNSWMTFFGQFFDHGLDFIPKGGNGTVL------------------IPLPPDDPLYdLGRGTNGMALDRGTNNAGPDGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 317 fgNLSTANPRQQmNGLTSFLDASTVYGSSPALERQLRNWT-----------SAEGLLRV--HARLRDSGRAYLPFVPPRA 383
Cdd:cd09821 75 --GTADGEGEHT-NVTTPFVDQNQTYGSHASHQVFLREYDgdgvatgrlleGATGGSARtgHAFLDDIAHNAAPKGGLGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 384 PAACAPepGIPGETRGPC----------FLAGDGRASEVPSLTALHTLWLREHNR----------------LAAALKALN 437
Cdd:cd09821 152 LRDNPT--EDPPGPGAPGsydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRlvdqikdtllqsadlaFANEAGGNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 438 AHWSADAVYQEARKVVGALHQIITLRDYIPRILGP-EAFqqyvGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRL 516
Cdd:cd09821 230 LAWDGERLFQAARFANEMQYQHLVFEEFARRIQPGiDGF----GSFNGYNPEINPSISAEFAHAVYRFGHSMLTETVTRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 517 DASFQEHPDLP-GL---WLHQAFFSPWTL---------LRG-----GyNEWREF-------------------------- 552
Cdd:cd09821 306 GPDADEGLDNQvGLidaFLNPVAFLPATLyaeegagaiLRGmtrqvG-NEIDEFvtdalrnnlvglpldlaalniargrd 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 553 CGLPRL-ETPADLSTA---------------IASR-----SVADKILDLYKHP--------------------------- 584
Cdd:cd09821 385 TGLPTLnEARAQLFAAtgdtilkapyeswndFGARlknpeSLINFIAAYGTHLtitgattlaakraaaqdlvdggdgapa 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 585 -------------------DNIDVWLGGLAENFLP-RARTGPLFACLIGKQMKALRDGDWFWWENShvfTDAQ--RRELE 642
Cdd:cd09821 465 dradfmnaagagagtvkglDNVDLWVGGLAEKQVPfGGMLGSTFNFVFEEQMDRLQDGDRFYYLSR---TAGLdlLNQLE 541
|
570 580
....*....|....*....|....*...
gi 1370478783 643 KHSLSRVICDNTGLTRVPMDAFQVGKFP 670
Cdd:cd09821 542 NNTFADMIMRNTGATHLPQDIFSVPDYD 569
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
328-654 |
8.98e-16 |
|
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1.
Pssm-ID: 188648 [Multi-domain] Cd Length: 490 Bit Score: 81.16 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 328 QMNGLTSFLDASTVYGSSPALERQLRnwtsaeglLRVHARLRDS---GRAYLPFVPPRA-------PAACAPEPGIPGET 397
Cdd:cd09816 123 RRNTSNHGIDLSQIYGLTEARTHALR--------LFKDGKLKSQminGEEYPPYLFEDGgvkmefpPLVPPLGDELTPER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 398 RGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIprilgpeafqQ 477
Cdd:cd09816 195 EAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYI----------N 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 478 YVGPYeGYDSTANPTVsnVFST-------AAFRFGHA-TIHPLV---------RRLDASFQEHPDL---PGLwlhQAFFS 537
Cdd:cd09816 265 HLSPY-HFKLFFDPEL--AFNEpwqrqnrIALEFNLLyRWHPLVpdtfniggqRYPLSDFLFNNDLvvdHGL---GALVD 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 538 ---------------PWTLLR--------------GGYNEWREFCGLPRLETPADLStaiASRSVADKILDLYKHPDNID 588
Cdd:cd09816 339 aasrqpagriglrntPPFLLPvevrsieqgrklrlASFNDYRKRFGLPPYTSFEELT---GDPEVAAELEELYGDVDAVE 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370478783 589 VWLGGLAENFLPRARTGPLFACLIG----KQmkALRD--GDWFWWeNSHVFTDAQRRELEK-HSLSRVICDNT 654
Cdd:cd09816 416 FYVGLFAEDPRPNSPLPPLMVEMVApdafSG--ALTNplLSPEVW-KPSTFGGEGGFDIVKtATLQDLVCRNV 485
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
323-607 |
2.13e-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: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 323 ANPRQQMNGLTSFLDASTVYGSSPALERQLRnwtsaegllrVHARLRDSGRAYLPFVPPRAPAACAPEPG--IP--GETR 398
Cdd:cd09819 74 IDPAELRNFRTPALDLDSVYGGGPDGSPYLY----------DQATPNDGAKLRVGRESPGGPGGLPGDGArdLPrnGQGT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 399 GpcfLAGDGRASEVPSLTALHTLWLREHNRLAAALKALnaHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQY 478
Cdd:cd09819 144 A---LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAH--GTPGDELFEEARRLVRWHYQWLVLNDFLPRICDPDVVDDV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 479 V----GPYEGYDSTAnPTVSNVFSTAAFRFGHATI------------HPLVRRLDASFQEHPDLPGlwlHQAFFSPWTLl 542
Cdd:cd09819 219 LangrRFYRFFREGK-PFMPVEFSVAAYRFGHSMVrasydynrnfpdASLELLFTFTGGGEGDLGG---FSPLPENWII- 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370478783 543 rggynEWREFCGLPRlETPADLSTAIASRsVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPL 607
Cdd:cd09819 294 -----DWRRFFDIDG-SAPPQFARKIDTK-LAPPLFDLPNGGVGLAPPMKSLAFRNLLRGYRLGL 351
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
697-750 |
4.27e-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: 53.24 E-value: 4.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478783 697 CGFPESVENGDFVH--CEESGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLCK 750
Cdd:cd00033 1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGgWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
697-749 |
3.34e-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: 3.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478783 697 CGFPESVENGDFVHCEE--SGRRVLVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 749
Cdd:smart00032 1 CPPPPDIENGTVTSSSGtySYGDTVTYSCDPGYTLIGSSTITCLENGtWSPPPPTC 56
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
697-749 |
5.00e-06 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 44.41 E-value: 5.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478783 697 CGFPESVENGDfVHCEESGRRV---LVYSCRHGYELQGREQLTCTQEG-WDFQPPLC 749
Cdd:pfam00084 1 CPPPPDIPNGK-VSATKNEYNYgasVSYECDPGYRLVGSPTITCQEDGtWSPPFPEC 56
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
330-474 |
1.09e-04 |
|
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death.
Pssm-ID: 188650 [Multi-domain] Cd Length: 484 Bit Score: 45.74 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 330 NGLTSFLDASTVYGSSPALERQLRnwTSAEGllrvhARLRDSGRAYLPfvpprapaaCAPEPGIPgetrgpcfLAGDGRA 409
Cdd:cd09818 88 NTNTHWWDGSQIYGSTEEAQKRLR--TFPPD-----GKLKLDADGLLP---------VDEHTGLP--------LTGFNDN 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370478783 410 SEVpSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEA 474
Cdd:cd09818 144 WWV-GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAILAHPT 207
|
|
| linoleate_diol_synthase_like |
cd09817 |
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ... |
540-596 |
2.08e-03 |
|
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme peroxidases, catalyze the oxygenation of linoleate and similar targets. Linoleate (8R)-dioxygenase, also called linoleate:oxygen 7S,8S-oxidoreductase, generates (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate as a product. Other members are 5,8-linoleate dioxygenase (LDS, ppoA) and linoleate 10R-dioxygenase (ppoC), involved in the biosynthesis of oxylipins.
Pssm-ID: 188649 [Multi-domain] Cd Length: 550 Bit Score: 41.55 E-value: 2.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478783 540 TLLRGGYNEWREFCGLPRLETPADLSTaiaSRSVADKILDLYKHPDNIDVWLGGLAE 596
Cdd:cd09817 385 EWNVATLNEFRKFFGLKPYETFEDINS---DPEVAEALELLYGHPDNVELYPGLVAE 438
|
|
| PHA02639 |
PHA02639 |
EEV host range protein; Provisional |
644-750 |
3.60e-03 |
|
EEV host range protein; Provisional
Pssm-ID: 165022 [Multi-domain] Cd Length: 295 Bit Score: 40.42 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478783 644 HSLSRVICD-----NTGLTRVPMDAFQVGKFPE------------DFESCdsITGMNLEAWRETFP--QDDKCGFPESVE 704
Cdd:PHA02639 15 HGVKSIYCDkpddiSNGFITELMEKYEIGKLIEytcntdyaligdRFRTC--IKDKNNAIWSNKAPfcMLKECNDPPSII 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370478783 705 NGDFVHCEESGR--RVLVYSCRH----GYELQGREQLTCTQE-GWDFQPPLCK 750
Cdd:PHA02639 93 NGKIYNKREMYKvgDEIYYVCNEhkgvQYSLVGNEKITCIQDkSWKPDPPICK 145
|
|
| |
