NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18104969|ref|NP_542158|]
View 

prostaglandin G/H synthase 1 isoform 2 precursor [Homo sapiens]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 10042121)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
89-538 0e+00

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: 694.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  89 HFLLTHGRWFWEFVNAT-FIREMLMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkg 166
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIpFLRRLINRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 167 kkQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLF 246
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 247 KDGKLKYQVLDGEMYPPSV-EEAPVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLL 315
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 316 KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFK 395
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 396 IGG------------------------------------GRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTS 439
Cdd:cd09816 311 IGGqryplsdflfnndlvvdhglgalvdaasrqpagrigLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTS 390
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 440 FQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFN 519
Cdd:cd09816 391 FEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFD 470
                       490       500
                ....*....|....*....|
gi 18104969 520 IVKTATLKKLVCLNTK-TCP 538
Cdd:cd09816 471 IVKTATLQDLVCRNVKgGCP 490
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
32-69 9.97e-05

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: 39.54  E-value: 9.97e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18104969  32 VNPCC-YYPCQHQGICVRfGLDRYQCDCtRTGYSGPNCT 69
Cdd:cd00054   2 IDECAsGNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNCE 38
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
89-538 0e+00

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: 694.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  89 HFLLTHGRWFWEFVNAT-FIREMLMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkg 166
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIpFLRRLINRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 167 kkQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLF 246
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 247 KDGKLKYQVLDGEMYPPSV-EEAPVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLL 315
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 316 KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFK 395
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 396 IGG------------------------------------GRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTS 439
Cdd:cd09816 311 IGGqryplsdflfnndlvvdhglgalvdaasrqpagrigLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTS 390
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 440 FQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFN 519
Cdd:cd09816 391 FEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFD 470
                       490       500
                ....*....|....*....|
gi 18104969 520 IVKTATLKKLVCLNTK-TCP 538
Cdd:cd09816 471 IVKTATLQDLVCRNVKgGCP 490
An_peroxidase pfam03098
Animal haem peroxidase;
147-482 8.09e-41

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 155.02  E-value: 8.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   147 YTRILPSVPKDCP-TPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQgTNLMFAFFAQHFTH------------------- 206
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFIDHdltltpestspngsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   207 ------------------------------QFFKTSGKMGPGFTK----ALGHGVDLGHIYGDNLERQYQLRLFKDGKLK 252
Cdd:pfam03098 102 cppenlhppcfpipippddpffspfgvrcmPFVRSAPGCGLGNPReqinQVTSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   253 YQV-LDGEMYPPSVEEAPVLMHYPRGIPpqsqmavgQEVFG-----LLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQ 326
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVP--------CFLAGdsranENPGLTALHTLFLREHNRIADELAKLNPHWSDET 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   327 LFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDpeLLFGVQFQYRNRI-----------AMEFNH--------LYHWH 387
Cdd:pfam03098 254 LFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPNVdpsisnefataAFRFGHslippflyRLDEN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   388 P-------------LMPDSFKIGG------------GRNMDHHI-------LH-----------VAVDVIReSREMRLQP 424
Cdd:pfam03098 332 NvpeepslrlhdsfFNPDRLYEGGidpllrglatqpAQAVDNNFteeltnhLFgppgefsgldlAALNIQR-GRDHGLPG 410
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   425 FNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 482
Cdd:pfam03098 411 YNDYREFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGP 470
PLN02283 PLN02283
alpha-dioxygenase
232-473 6.06e-18

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 87.51  E-value: 6.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  232 IYGDNLERQYQLRLFKDGKLKyqvldgemyppsVEEAPVLMHYPRGIPpqsqmaVGQEVFGLLPGLMLYATLWLREHNRV 311
Cdd:PLN02283 219 IYGSNEKGLRRVRTFKDGKLK------------ISEDGLLLHDEDGIP------ISGDVRNSWAGVSLLQALFVKEHNAV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  312 CDLLKAEHPTWGDEQLFQTTRLILIGETIKI-VIEEYVQQLSG-----------Y-FLQLKFDP-------ELLFGVQFQ 371
Cdd:PLN02283 281 CDALKEEYPDFDDEELYRHARLVTSAVIAKIhTIDWTVELLKTdtllagmranwYgLLGKKFKDtfghiggPILSGLVGL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  372 YRNR-------IAMEFNHLYHWHPLMPDSF------------------------------------KIG----------- 397
Cdd:PLN02283 361 KKPNnhgvpysLTEEFTSVYRMHSLLPDHLilrditaapgenkspplieeipmpeliglkgekklsKIGfeklmvsmghq 440
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  398 ----------------------GGRNMDHHILHVAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEE 455
Cdd:PLN02283 441 acgalelwnypswmrdlvpqdiDGEDRPDHVDMAALEIYRD-RERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLRE 519
                        330
                 ....*....|....*....
gi 18104969  456 LYG-DIDALEFYPGLLLEK 473
Cdd:PLN02283 520 VYGdDVEKLDLLVGLMAEK 538
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
32-69 9.97e-05

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: 39.54  E-value: 9.97e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18104969  32 VNPCC-YYPCQHQGICVRfGLDRYQCDCtRTGYSGPNCT 69
Cdd:cd00054   2 IDECAsGNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
38-67 3.72e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.13  E-value: 3.72e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 18104969    38 YPCQHQGICVRfGLDRYQCDCTrTGYSGPN 67
Cdd:pfam00008   4 NPCSNGGTCVD-TPGGYTCICP-EGYTGKR 31
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
89-538 0e+00

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: 694.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  89 HFLLTHGRWFWEFVNAT-FIREMLMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkg 166
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIpFLRRLINRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 167 kkQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLF 246
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 247 KDGKLKYQVLDGEMYPPSV-EEAPVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLL 315
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 316 KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFK 395
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 396 IGG------------------------------------GRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTS 439
Cdd:cd09816 311 IGGqryplsdflfnndlvvdhglgalvdaasrqpagrigLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTS 390
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 440 FQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFN 519
Cdd:cd09816 391 FEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFD 470
                       490       500
                ....*....|....*....|
gi 18104969 520 IVKTATLKKLVCLNTK-TCP 538
Cdd:cd09816 471 IVKTATLQDLVCRNVKgGCP 490
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
225-533 2.76e-90

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: 282.39  E-value: 2.76e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 225 HGVDLGHIYGDNLERQYQLRLFKDGKLKYQvldgEMYPPSVEEAPVLMHYP------RGIPPQSQMAVGQEVFGLLPGLM 298
Cdd:cd05396   7 PYLDGSSIYGSNPDVARALRTFKGGLLKTN----EVKGPSYGTELLPFNNPnpsmgtIGLPPTRCFIAGDPRVNENLLLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 299 LYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAM 378
Cdd:cd05396  83 AVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVVPYVLSE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 379 EFNHLYHW-HPLMPDSFKIG-------------------------------------------------------GGRNM 402
Cdd:cd05396 163 FFTAAYRFgHSLVPEGVDRIdengqpkeipdvplkdfffntsrsilsdtgldpllrgflrqpaglidqnvddvmfLFGPL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 403 DHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 482
Cdd:cd05396 243 EGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTDPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGE 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 18104969 483 SMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEvgfNIVKTATLKKLVCLN 533
Cdd:cd05396 323 LLATIILEQFKRLVDGDRFYYVNYNPFGKSGKE---ELEKLISLADIICLN 370
An_peroxidase pfam03098
Animal haem peroxidase;
147-482 8.09e-41

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 155.02  E-value: 8.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   147 YTRILPSVPKDCP-TPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQgTNLMFAFFAQHFTH------------------- 206
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFIDHdltltpestspngsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   207 ------------------------------QFFKTSGKMGPGFTK----ALGHGVDLGHIYGDNLERQYQLRLFKDGKLK 252
Cdd:pfam03098 102 cppenlhppcfpipippddpffspfgvrcmPFVRSAPGCGLGNPReqinQVTSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   253 YQV-LDGEMYPPSVEEAPVLMHYPRGIPpqsqmavgQEVFG-----LLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQ 326
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVP--------CFLAGdsranENPGLTALHTLFLREHNRIADELAKLNPHWSDET 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   327 LFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDpeLLFGVQFQYRNRI-----------AMEFNH--------LYHWH 387
Cdd:pfam03098 254 LFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPNVdpsisnefataAFRFGHslippflyRLDEN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   388 P-------------LMPDSFKIGG------------GRNMDHHI-------LH-----------VAVDVIReSREMRLQP 424
Cdd:pfam03098 332 NvpeepslrlhdsfFNPDRLYEGGidpllrglatqpAQAVDNNFteeltnhLFgppgefsgldlAALNIQR-GRDHGLPG 410
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969   425 FNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 482
Cdd:pfam03098 411 YNDYREFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGP 470
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
225-481 7.94e-31

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: 123.84  E-value: 7.94e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 225 HGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPvLMHYPRGIPPQSQMAvGQEVFGLLPGLMLYATLW 304
Cdd:cd09823   9 SFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPT-DDCSLSSAGKPCFLA-GDGRVNEQPGLTSMHTLF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 305 LREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQ-YRNRI------- 376
Cdd:cd09823  87 LREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNgYDPNVdpsilne 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 377 ----AMEFNH--------LYHWH-------PLM-----PDSFKIGGG-------------RNMDHHILH----------- 408
Cdd:cd09823 167 faaaAFRFGHslvpgtfeRLDENyrpqgsvNLHdlffnPDRLYEEGGldpllrglatqpaQKVDRFFTDeltthfffrgg 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 409 -------VAVDVIReSREMRLQPFNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPNSI 479
Cdd:cd09823 247 npfgldlAALNIQR-GRDHGLPGYNDYREFCGLPRATTFDDLLGImsPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGL 325

                ..
gi 18104969 480 FG 481
Cdd:cd09823 326 VG 327
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
232-484 6.92e-29

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: 118.95  E-value: 6.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 232 IYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPsvEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRV 311
Cdd:cd09822  63 VYGSDEERADALRSFGGGKLKTSVANAGDLLP--FNEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 312 CDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGyflqlkfdpELLFGVQFQYRN----RIAMEFN----HL 383
Cdd:cd09822 141 ADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLG---------ENALPAYSGYDEtvnpGISNEFStaayRF 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 384 YH--------------------------WHP-----LMPDSFKIGGGRNMDHHI-LHVAVDV------------------ 413
Cdd:cd09822 212 GHsmlssellrgdedgteatslalrdafFNPdeleeNGIDPLLRGLASQVAQEIdTFIVDDVrnflfgppgaggfdlaal 291
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18104969 414 -IRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESM 484
Cdd:cd09822 292 nIQRGRDHGLPSYNQLREALGLPAVTSFSDITSDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETF 363
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
185-533 1.09e-26

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: 113.53  E-value: 1.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 185 KFIPDPQgTNLMFAFFAQHFTHQFFkTSGKmgPGFTKALGHGVDLGHIYGDNLERQYQLRLF-KDGKLKyqvLDGEMYPP 263
Cdd:cd09818  56 EFKPATS-LNLLAAAWIQFMVHDWF-SHGP--PTYINTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLK---LDADGLLP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 264 SVEEAPVlmhyprgipPQSQMAVGQEVfgllpGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIV 343
Cdd:cd09818 129 VDEHTGL---------PLTGFNDNWWV-----GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIH 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 344 IEEYVQQ-----------------LSGYFLQLKF----DPELL----------FGVQFQyrnrIAMEFNHLYHWHPLMPD 392
Cdd:cd09818 195 TVEWTPAilahptleiamranwwgLLGERLKRVLgrdgTSELLsgipgsppnhHGVPYS----LTEEFVAVYRMHPLIPD 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 393 SF-----------------------------KIGGGR----------------NMDHHILHV-----------AVDVIRe 416
Cdd:cd09818 271 DIdfrsaddgatgeeisltdlaggkarellrKLGFADllysfgithpgaltlhNYPRFLRDLhrpdgrvidlaAIDILR- 349
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 417 SREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYG-DIDALEFYPGLLLEKCHPNSIFGESMIEIgapFSL-- 493
Cdd:cd09818 350 DRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGgDVEKVDLLVGLLAEPLPPGFGFSDTAFRI---FILma 426
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 18104969 494 -KGLLGNPICSpEYWKPSTFgGEVGFNIVKTATLKKLVCLN 533
Cdd:cd09818 427 sRRLKSDRFFT-NDFRPEVY-TPEGMDWVNNNTMKSVLLRH 465
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
145-473 3.59e-22

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: 100.10  E-value: 3.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 145 SYYTRILPsvPKDCPTPMgtkgkkqLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGK-MGPGFTKAL 223
Cdd:cd09817  53 SPYARSVP--PKHDQPGV-------LPDPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDIFRTDHRdMNINNTSSY 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 224 ghgVDLGHIYGDNLERQYQLRLFKDGKLKyqvldgemyppsveeaPVLMHYPRgippqsqmavgqeVFGLLPGLMLYATL 303
Cdd:cd09817 124 ---LDLSPLYGSNQEEQNKVRTMKDGKLK----------------PDTFSDKR-------------LLGQPPGVCALLVM 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 304 WLREHNRVCDLL-----------------KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSG---YFLQLKFDP- 362
Cdd:cd09817 172 FNRFHNYVVEQLaqineggrftppgdkldSSAKEEKLDEDLFQTARLITCGLYINIVLHDYVRAILNlnrTDSTWTLDPr 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 363 -ELLFGVQFQYR---NRIAMEFNHLYHWH-------------------------------------------PLMPDSFK 395
Cdd:cd09817 252 vEIGRSLTGVPRgtgNQVSVEFNLLYRWHsaisardekwtedlfeslfggkspdevtlkefmqalgrfealiPKDPSQRT 331
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 396 IGG------GRNMDH-----------------HILHV-----AVDV--IRESREMRLQPFNEYRKRFGMKPYTSFQELVG 445
Cdd:cd09817 332 FGGlkrgpdGRFRDEdlvrilkdsiedpagafGARNVpaslkVIEIlgILQAREWNVATLNEFRKFFGLKPYETFEDINS 411
                       410       420
                ....*....|....*....|....*...
gi 18104969 446 EKEMAAELEELYGDIDALEFYPGLLLEK 473
Cdd:cd09817 412 DPEVAEALELLYGHPDNVELYPGLVAED 439
PLN02283 PLN02283
alpha-dioxygenase
232-473 6.06e-18

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 87.51  E-value: 6.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  232 IYGDNLERQYQLRLFKDGKLKyqvldgemyppsVEEAPVLMHYPRGIPpqsqmaVGQEVFGLLPGLMLYATLWLREHNRV 311
Cdd:PLN02283 219 IYGSNEKGLRRVRTFKDGKLK------------ISEDGLLLHDEDGIP------ISGDVRNSWAGVSLLQALFVKEHNAV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  312 CDLLKAEHPTWGDEQLFQTTRLILIGETIKI-VIEEYVQQLSG-----------Y-FLQLKFDP-------ELLFGVQFQ 371
Cdd:PLN02283 281 CDALKEEYPDFDDEELYRHARLVTSAVIAKIhTIDWTVELLKTdtllagmranwYgLLGKKFKDtfghiggPILSGLVGL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  372 YRNR-------IAMEFNHLYHWHPLMPDSF------------------------------------KIG----------- 397
Cdd:PLN02283 361 KKPNnhgvpysLTEEFTSVYRMHSLLPDHLilrditaapgenkspplieeipmpeliglkgekklsKIGfeklmvsmghq 440
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969  398 ----------------------GGRNMDHHILHVAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEE 455
Cdd:PLN02283 441 acgalelwnypswmrdlvpqdiDGEDRPDHVDMAALEIYRD-RERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLRE 519
                        330
                 ....*....|....*....
gi 18104969  456 LYG-DIDALEFYPGLLLEK 473
Cdd:PLN02283 520 VYGdDVEKLDLLVGLMAEK 538
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
228-472 1.10e-14

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: 76.95  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 228 DLGHIYGDNLERQYQLRLFKDGKLKYQVlDGEMYPPSVEEAPVLMHYPrgiPPQSQMAVGQEVFGL-------LPGLMLY 300
Cdd:cd09820 142 DGSSIYGSSKAWSDALRSFSGGRLASGD-DGGFPRRNTNRLPLANPPP---PSYHGTRGPERLFKLgnprgneNPFLLTF 217
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 301 ATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQL--------SGYflQLKFDPELlfGVQFQy 372
Cdd:cd09820 218 GILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALlgtnvppyTGY--KPHVDPGI--SHEFQ- 292
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 373 rnRIAMEFNhlyhwHPLMP-------------DSFKIGGGR-------------------NMDHHIL-----------HV 409
Cdd:cd09820 293 --AAAFRFG-----HTLVPpgvyrrnrqcnfrEVLTTSGGSpalrlcntywnsqepllksDIDELLLgmasqiaeredNI 365
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 410 AVDVIRES--------------------REMRLQPFNEYRKRFGMKPYTSFQELVGE-----KEMAAELEELYG-DIDAL 463
Cdd:cd09820 366 IVEDLRDYlfgplefsrrdlmalniqrgRDHGLPDYNTAREAFGLPPRTTWSDINPDlfkkdPELLERLAELYGnDLSKL 445

                ....*....
gi 18104969 464 EFYPGLLLE 472
Cdd:cd09820 446 DLYVGGMLE 454
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
296-481 7.24e-10

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: 61.17  E-value: 7.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 296 GLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLIlIGETI----------KIV-------IEEYvqqlSGYflql 358
Cdd:cd09826 120 GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKI-VGAQMqhityshwlpKILgpvgmemLGEY----RGY---- 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 359 kfDPE-------------LLFG---VQfQYRNRIAMEFNHLYHWHPLMPDSF-------KIGG----------------- 398
Cdd:cd09826 191 --NPNvnpsianefataaFRFGhtlIN-PILFRLDEDFQPIPEGHLPLHKAFfapyrlvNEGGidpllrglfataakdrv 267
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 399 -GRNMDHHILH--------VAVDV----IRESREMRLQPFNEYRKRFGMKPYTSFQELVGE---KEMAAELEELYGDIDA 462
Cdd:cd09826 268 pDQLLNTELTEklfemaheVALDLaalnIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEiknDDVREKLKRLYGHPGN 347
                       250
                ....*....|....*....
gi 18104969 463 LEFYPGLLLEKCHPNSIFG 481
Cdd:cd09826 348 IDLFVGGILEDLLPGARVG 366
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
208-478 3.27e-09

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: 59.37  E-value: 3.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 208 FFKTSGKMGPGFTKALGHGV----------------DLGHIYGDNLERQYQLRLF--KDGKLKYQVL---DGEMYPPSVE 266
Cdd:cd09825 123 FFRSSAVCGTGDTSTLFGNLslanpreqingltsfiDASTVYGSTLALARSLRDLssDDGLLRVNSKfddSGRDYLPFQP 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 267 EAPVlmhyprgiPPQSQMAVGQEVFGLLPG-------LMLYA--TLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIG 337
Cdd:cd09825 203 EEVS--------SCNPDPNGGERVPCFLAGdgrasevLTLTAshTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGA 274
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 338 ETIKIVIEEYV---------QQLSGYFlqLKFDPellfGVQFQYRNRIAM---------------EFNHLYHWHPLMP-- 391
Cdd:cd09825 275 LHQIITFRDYIpkilgpeafDQYGGYY--EGYDP----TVNPTVSNVFSTaafrfghatihptvrRLDENFQEHPVLPnl 348
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104969 392 ---DSF-------KIGGgrnMDHHI---------LHVAVDVIRES------------------------REMRLQPFNEY 428
Cdd:cd09825 349 alhDAFfspwrlvREGG---LDPVIrgliggpakLVTPDDLMNEElteklfvlsnsstldlaslnlqrgRDHGLPGYNDW 425
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 18104969 429 RKRFGMKPYTSFQEL---VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNS 478
Cdd:cd09825 426 REFCGLPRLATPADLataIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGA 478
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
295-353 4.03e-05

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: 46.26  E-value: 4.03e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18104969 295 PGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSG 353
Cdd:cd09824  95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILG 153
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
32-69 9.97e-05

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: 39.54  E-value: 9.97e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18104969  32 VNPCC-YYPCQHQGICVRfGLDRYQCDCtRTGYSGPNCT 69
Cdd:cd00054   2 IDECAsGNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
38-67 3.72e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 38.13  E-value: 3.72e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 18104969    38 YPCQHQGICVRfGLDRYQCDCTrTGYSGPN 67
Cdd:pfam00008   4 NPCSNGGTCVD-TPGGYTCICP-EGYTGKR 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH