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Conserved domains on  [gi|18104967|ref|NP_000953|]
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prostaglandin G/H synthase 1 isoform 1 precursor [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
89-575 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  Cd Length: 490  Bit Score: 762.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  89 HFLLTHGRWFWEFVNAT-FIREMLMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkg 166
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIpFLRRLINRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 167 kkQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLF 246
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 247 KDGKLKYQVLDGEMYPPSV-EEAPVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLL 315
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 316 KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFK 395
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 396 VGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIgGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYT 475
Cdd:cd09816 311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 476 SFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGF 555
Cdd:cd09816 390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                       490       500
                ....*....|....*....|.
gi 18104967 556 NIVKTATLKKLVCLNTK-TCP 575
Cdd:cd09816 470 DIVKTATLQDLVCRNVKgGCP 490
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
32-69 1.22e-04

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: 40.31  E-value: 1.22e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18104967  32 VNPCC-YYPCQHQGICVRfGLDRYQCDCtRTGYSGPNCT 69
Cdd:cd00054   2 IDECAsGNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNCE 38
An_peroxidase pfam03098
Animal haem peroxidase;
145-581 4.99e-130

Animal haem peroxidase;


:

Pssm-ID: 251728 [Multi-domain]  Cd Length: 518  Bit Score: 393.99  E-value: 4.99e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   145 SYYTRILPSVPKD-CPTPMGTKGKKQLPDAQLLARRFLLRRKF-IPDPQGTNLMFAFFAQHFTHQFFKTSGKMG------ 216
Cdd:pfam03098  21 TPFGRLLPPVYEDgVSTPRGSVNGSPLPSPRLVSNKLLARKNGlDPPDPGLTLMLAQWGQFIDHDLTFTPHSRCcadppe 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   217 --------------------------------------PGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQvldg 258
Cdd:pfam03098 101 cfpipvppgdpyfsplgrclpffrsapacgpgpscnlpREQINQLTSYLDLSQVYGSSEEEADKLRTFKDGKLKVN---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   259 emYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGE 338
Cdd:pfam03098 177 --SPPNGKGLLPFDPPGPGSFCLACFLAGDSRANENPGLTALHTLFLREHNRIADELKALNPHWSDEQLFQEARLIVIAE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   339 TIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEF-NHLYHW-HPLMPDSFKVGS------QEYSYEQFLFNT 410
Cdd:pfam03098 255 YQKITYNEYLPALLGPDAMNANWLLYYTGYDPNVDPSISNEFaTAAYRFgHSLIPPTFERLDefngiaPEIPLHDTFFNP 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   411 SMLVD-YGVEALV------------DAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSF 477
Cdd:pfam03098 335 SRIVEeGGIDPLLrgllsqpaelldNSLSDELRNRLFGPRNVPGSGLDLAALNIQRGRDHGLPPYNEYRRFCGLKPATSF 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   478 QEL---VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICspeYWKPSTFGGEVG 554
Cdd:pfam03098 415 EDLtdeIGDEELAEKLKELYGDPDDIDLYVGGLAEKPVPGGLVGPTFSCIIAEQFLRLRDGDRFW---YENPSTFTPEQL 491
                         490       500
                  ....*....|....*....|....*..
gi 18104967   555 FNIVKTaTLKKLVCLNTKTCPYVSFRV 581
Cdd:pfam03098 492 EEIRKT-TLARLICDNTDGITRVQPNA 517
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
89-575 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  Cd Length: 490  Bit Score: 762.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  89 HFLLTHGRWFWEFVNAT-FIREMLMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkg 166
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIpFLRRLINRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 167 kkQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLF 246
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 247 KDGKLKYQVLDGEMYPPSV-EEAPVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLL 315
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 316 KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFK 395
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 396 VGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIgGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYT 475
Cdd:cd09816 311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 476 SFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGF 555
Cdd:cd09816 390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                       490       500
                ....*....|....*....|.
gi 18104967 556 NIVKTATLKKLVCLNTK-TCP 575
Cdd:cd09816 470 DIVKTATLQDLVCRNVKgGCP 490
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
32-69 1.22e-04

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: 40.31  E-value: 1.22e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18104967  32 VNPCC-YYPCQHQGICVRfGLDRYQCDCtRTGYSGPNCT 69
Cdd:cd00054   2 IDECAsGNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNCE 38
PLN02283 PLN02283
alpha-dioxygenase
232-510 2.30e-21

alpha-dioxygenase


Pssm-ID: 177921  Cd Length: 633  Bit Score: 97.14  E-value: 2.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  232 IYGDNLERQYQLRLFKDGKLKyqvldgemyppsVEEAPVLMHYPRGIPpqsqmaVGQEVFGLLPGLMLYATLWLREHNRV 311
Cdd:PLN02283 219 IYGSNEKGLRRVRTFKDGKLK------------ISEDGLLLHDEDGIP------ISGDVRNSWAGVSLLQALFVKEHNAV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  312 CDLLKAEHPTWGDEQLFQTTRLILIGETIKI-VIEEYVQQLSG-----------Y-FLQLKFDP-------ELLFGVQFQ 371
Cdd:PLN02283 281 CDALKEEYPDFDDEELYRHARLVTSAVIAKIhTIDWTVELLKTdtllagmranwYgLLGKKFKDtfghiggPILSGLVGL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  372 YRNR-------IAMEFNHLYHWHPLMPDSF----------------------------KVGSQEYSYEQFlfnTSMLVDY 416
Cdd:PLN02283 361 KKPNnhgvpysLTEEFTSVYRMHSLLPDHLilrditaapgenkspplieeipmpeligLKGEKKLSKIGF---EKLMVSM 437
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  417 GVE---ALV----DAFSRQIAGRIGGGRNMDHHILHVAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAE 489
Cdd:PLN02283 438 GHQacgALElwnyPSWMRDLVPQDIDGEDRPDHVDMAALEIYRD-RERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEV 516
                        330       340
                 ....*....|....*....|..
gi 18104967  490 LEELYG-DIDALEFYPGLLLEK 510
Cdd:PLN02283 517 LREVYGdDVEKLDLLVGLMAEK 538
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
39-67 2.18e-03

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: 249503  Cd Length: 32  Bit Score: 36.25  E-value: 2.18e-03
                          10        20
                  ....*....|....*....|....*....
gi 18104967    39 PCQHQGICVRFGlDRYQCDCTRtGYSGPN 67
Cdd:pfam00008   6 PCSNGGTCVDTP-GGYTCECPP-GYTGKR 32
An_peroxidase pfam03098
Animal haem peroxidase;
145-581 4.99e-130

Animal haem peroxidase;


Pssm-ID: 251728 [Multi-domain]  Cd Length: 518  Bit Score: 393.99  E-value: 4.99e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   145 SYYTRILPSVPKD-CPTPMGTKGKKQLPDAQLLARRFLLRRKF-IPDPQGTNLMFAFFAQHFTHQFFKTSGKMG------ 216
Cdd:pfam03098  21 TPFGRLLPPVYEDgVSTPRGSVNGSPLPSPRLVSNKLLARKNGlDPPDPGLTLMLAQWGQFIDHDLTFTPHSRCcadppe 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   217 --------------------------------------PGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQvldg 258
Cdd:pfam03098 101 cfpipvppgdpyfsplgrclpffrsapacgpgpscnlpREQINQLTSYLDLSQVYGSSEEEADKLRTFKDGKLKVN---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   259 emYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGE 338
Cdd:pfam03098 177 --SPPNGKGLLPFDPPGPGSFCLACFLAGDSRANENPGLTALHTLFLREHNRIADELKALNPHWSDEQLFQEARLIVIAE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   339 TIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEF-NHLYHW-HPLMPDSFKVGS------QEYSYEQFLFNT 410
Cdd:pfam03098 255 YQKITYNEYLPALLGPDAMNANWLLYYTGYDPNVDPSISNEFaTAAYRFgHSLIPPTFERLDefngiaPEIPLHDTFFNP 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   411 SMLVD-YGVEALV------------DAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSF 477
Cdd:pfam03098 335 SRIVEeGGIDPLLrgllsqpaelldNSLSDELRNRLFGPRNVPGSGLDLAALNIQRGRDHGLPPYNEYRRFCGLKPATSF 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   478 QEL---VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICspeYWKPSTFGGEVG 554
Cdd:pfam03098 415 EDLtdeIGDEELAEKLKELYGDPDDIDLYVGGLAEKPVPGGLVGPTFSCIIAEQFLRLRDGDRFW---YENPSTFTPEQL 491
                         490       500
                  ....*....|....*....|....*..
gi 18104967   555 FNIVKTaTLKKLVCLNTKTCPYVSFRV 581
Cdd:pfam03098 492 EEIRKT-TLARLICDNTDGITRVQPNA 517
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
89-575 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  Cd Length: 490  Bit Score: 762.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  89 HFLLTHGRWFWEFVNAT-FIREMLMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkg 166
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIpFLRRLINRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 167 kkQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLF 246
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 247 KDGKLKYQVLDGEMYPPSV-EEAPVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLL 315
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 316 KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFK 395
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 396 VGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIgGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYT 475
Cdd:cd09816 311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 476 SFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGF 555
Cdd:cd09816 390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                       490       500
                ....*....|....*....|.
gi 18104967 556 NIVKTATLKKLVCLNTK-TCP 575
Cdd:cd09816 470 DIVKTATLQDLVCRNVKgGCP 490
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
32-69 1.22e-04

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: 40.31  E-value: 1.22e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18104967  32 VNPCC-YYPCQHQGICVRfGLDRYQCDCtRTGYSGPNCT 69
Cdd:cd00054   2 IDECAsGNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNCE 38
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
225-570 6.07e-105

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  Cd Length: 370  Bit Score: 324.00  E-value: 6.07e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 225 HGVDLGHIYGDNLERQYQLRLFKDGKLKYQvldgEMYPPSVEEAPVLMHYP------RGIPPQSQMAVGQEVFGLLPGLM 298
Cdd:cd05396   7 PYLDGSSIYGSNPDVARALRTFKGGLLKTN----EVKGPSYGTELLPFNNPnpsmgtIGLPPTRCFIAGDPRVNENLLLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 299 LYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAM 378
Cdd:cd05396  83 AVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVVPYVLSE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 379 EFNHLYHW-HPLMPDSFKV--------GSQEYSYEQFLFNTSM--LVDYGVEALVDAFSRQIAGRIGGG--------RNM 439
Cdd:cd05396 163 FFTAAYRFgHSLVPEGVDRidengqpkEIPDVPLKDFFFNTSRsiLSDTGLDPLLRGFLRQPAGLIDQNvddvmflfGPL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 440 DHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 519
Cdd:cd05396 243 EGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTDPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGE 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 18104967 520 SMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEvgfNIVKTATLKKLVCLN 570
Cdd:cd05396 323 LLATIILEQFKRLVDGDRFYYVNYNPFGKSGKE---ELEKLISLADIICLN 370
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
232-521 1.74e-34

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: 134.36  E-value: 1.74e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 232 IYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPsvEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRV 311
Cdd:cd09822  63 VYGSDEERADALRSFGGGKLKTSVANAGDLLP--FNEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 312 CDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGyflqlkfdpELLFGVQFQYRN----RIAMEF-NHLYHW 386
Cdd:cd09822 141 ADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLG---------ENALPAYSGYDEtvnpGISNEFsTAAYRF 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 387 -HPLMPDSFKVGSQEYSYEQFL------FNTSMLVDYGVEALVDAFSRQIAgrigggRNMDHHILH-------------- 445
Cdd:cd09822 212 gHSMLSSELLRGDEDGTEATSLalrdafFNPDELEENGIDPLLRGLASQVA------QEIDTFIVDdvrnflfgppgagg 285
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18104967 446 ---VAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESM 521
Cdd:cd09822 286 fdlAALNIQRG-RDHGLPSYNQLREALGLPAVTSFSDITSDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETF 363
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
225-518 4.78e-34

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  Cd Length: 378  Bit Score: 132.31  E-value: 4.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 225 HGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPvLMHYPRGIPPQSQMAvGQEVFGLLPGLMLYATLW 304
Cdd:cd09823   9 SFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPT-DDCSLSSAGKPCFLA-GDGRVNEQPGLTSMHTLF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 305 LREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQ-YRNR----IAME 379
Cdd:cd09823  87 LREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNgYDPNvdpsILNE 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 380 FNHLYHW--HPLMPDSFKVGSQEYSYEQFL------FNTSMLVDYG-VEALVDAFSRQIAGRIggGRNMDHHILH----- 445
Cdd:cd09823 167 FAAAAFRfgHSLVPGTFERLDENYRPQGSVnlhdlfFNPDRLYEEGgLDPLLRGLATQPAQKV--DRFFTDELTThfffr 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 446 ---------VAVDVIReSREMRLQPFNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPN 514
Cdd:cd09823 245 ggnpfgldlAALNIQR-GRDHGLPGYNDYREFCGLPRATTFDDLLGImsPETIQKLRRLYKSVDDIDLYVGGLSEKPVPG 323

                ....
gi 18104967 515 SIFG 518
Cdd:cd09823 324 GLVG 327
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
185-570 2.74e-31

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  Cd Length: 484  Bit Score: 125.86  E-value: 2.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 185 KFIPDPQgTNLMFAFFAQHFTHQFFkTSGKmgPGFTKALGHGVDLGHIYGDNLERQYQLRLF-KDGKLKyqvLDGEMYPP 263
Cdd:cd09818  56 EFKPATS-LNLLAAAWIQFMVHDWF-SHGP--PTYINTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLK---LDADGLLP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 264 SVEEAPVlmhyprgipPQSQMAVGQEVfgllpGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIV 343
Cdd:cd09818 129 VDEHTGL---------PLTGFNDNWWV-----GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIH 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 344 IEEYVQQ-----------------LSGYFLQLKF----DPELL----------FGVQFQyrnrIAMEFNHLYHWHPLMPD 392
Cdd:cd09818 195 TVEWTPAilahptleiamranwwgLLGERLKRVLgrdgTSELLsgipgsppnhHGVPYS----LTEEFVAVYRMHPLIPD 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 393 SFKVGS-------QEYSYEQFLFNTS--MLVDYGVEALVDAFSRQIAGRIgGGRNMDHHILHV-----------AVDVIR 452
Cdd:cd09818 271 DIDFRSaddgatgEEISLTDLAGGKAreLLRKLGFADLLYSFGITHPGAL-TLHNYPRFLRDLhrpdgrvidlaAIDILR 349
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 453 eSREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYG-DIDALEFYPGLLLEKCHPNSIFGESMIEIgapFSL- 530
Cdd:cd09818 350 -DRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGgDVEKVDLLVGLLAEPLPPGFGFSDTAFRI---FILm 425
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 18104967 531 --KGLLGNPICSpEYWKPSTFgGEVGFNIVKTATLKKLVCLN 570
Cdd:cd09818 426 asRRLKSDRFFT-NDFRPEVY-TPEGMDWVNNNTMKSVLLRH 465
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
145-510 3.30e-25

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  Cd Length: 550  Bit Score: 108.58  E-value: 3.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 145 SYYTRILPsvPKDCPTPMgtkgkkqLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGK-MGPGFTKAL 223
Cdd:cd09817  53 SPYARSVP--PKHDQPGV-------LPDPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDIFRTDHRdMNINNTSSY 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 224 ghgVDLGHIYGDNLERQYQLRLFKDGKLKyqvldgemyppsveeaPVLMHYPRgippqsqmavgqeVFGLLPGLMLYATL 303
Cdd:cd09817 124 ---LDLSPLYGSNQEEQNKVRTMKDGKLK----------------PDTFSDKR-------------LLGQPPGVCALLVM 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 304 WLREHNRVCDLL-----------------KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSG---YFLQLKFDP- 362
Cdd:cd09817 172 FNRFHNYVVEQLaqineggrftppgdkldSSAKEEKLDEDLFQTARLITCGLYINIVLHDYVRAILNlnrTDSTWTLDPr 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 363 -ELLFGVQFQYR---NRIAMEFNHLYHWHPL--------MPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVD------- 423
Cdd:cd09817 252 vEIGRSLTGVPRgtgNQVSVEFNLLYRWHSAisardekwTEDLFESLFGGKSPDEVTLKEFMQALGRFEALIPkdpsqrt 331
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 424 --AFSRQIAGRI-----------------GG-GRNMDHHILHVaVDV--IRESREMRLQPFNEYRKRFGMKPYTSFQELV 481
Cdd:cd09817 332 fgGLKRGPDGRFrdedlvrilkdsiedpaGAfGARNVPASLKV-IEIlgILQAREWNVATLNEFRKFFGLKPYETFEDIN 410
                       410       420
                ....*....|....*....|....*....
gi 18104967 482 GEKEMAAELEELYGDIDALEFYPGLLLEK 510
Cdd:cd09817 411 SDPEVAEALELLYGHPDNVELYPGLVAED 439
PLN02283 PLN02283
alpha-dioxygenase
232-510 2.30e-21

alpha-dioxygenase


Pssm-ID: 177921  Cd Length: 633  Bit Score: 97.14  E-value: 2.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  232 IYGDNLERQYQLRLFKDGKLKyqvldgemyppsVEEAPVLMHYPRGIPpqsqmaVGQEVFGLLPGLMLYATLWLREHNRV 311
Cdd:PLN02283 219 IYGSNEKGLRRVRTFKDGKLK------------ISEDGLLLHDEDGIP------ISGDVRNSWAGVSLLQALFVKEHNAV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  312 CDLLKAEHPTWGDEQLFQTTRLILIGETIKI-VIEEYVQQLSG-----------Y-FLQLKFDP-------ELLFGVQFQ 371
Cdd:PLN02283 281 CDALKEEYPDFDDEELYRHARLVTSAVIAKIhTIDWTVELLKTdtllagmranwYgLLGKKFKDtfghiggPILSGLVGL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  372 YRNR-------IAMEFNHLYHWHPLMPDSF----------------------------KVGSQEYSYEQFlfnTSMLVDY 416
Cdd:PLN02283 361 KKPNnhgvpysLTEEFTSVYRMHSLLPDHLilrditaapgenkspplieeipmpeligLKGEKKLSKIGF---EKLMVSM 437
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967  417 GVE---ALV----DAFSRQIAGRIGGGRNMDHHILHVAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAE 489
Cdd:PLN02283 438 GHQacgALElwnyPSWMRDLVPQDIDGEDRPDHVDMAALEIYRD-RERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEV 516
                        330       340
                 ....*....|....*....|..
gi 18104967  490 LEELYG-DIDALEFYPGLLLEK 510
Cdd:PLN02283 517 LREVYGdDVEKLDLLVGLMAEK 538
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
228-509 1.93e-18

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: 87.35  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 228 DLGHIYGDNLERQYQLRLFKDGKLKYQVlDGEMYPPSVEEAPVLMHYPrgiPPQSQMAVGQEVFGL-------LPGLMLY 300
Cdd:cd09820 142 DGSSIYGSSKAWSDALRSFSGGRLASGD-DGGFPRRNTNRLPLANPPP---PSYHGTRGPERLFKLgnprgneNPFLLTF 217
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 301 ATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQL--------SGYflQLKFDPELlfGVQFQy 372
Cdd:cd09820 218 GILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALlgtnvppyTGY--KPHVDPGI--SHEFQ- 292
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 373 rnRIAMEFNHL----------YHWHPLMPDSFKVGSQEYSyeqfLFNT-----SMLVDYGVEALVDAFSRQIAGRigggr 437
Cdd:cd09820 293 --AAAFRFGHTlvppgvyrrnRQCNFREVLTTSGGSPALR----LCNTywnsqEPLLKSDIDELLLGMASQIAER----- 361
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 438 nmDHHIL------------------HVAVDVIReSREMRLQPFNEYRKRFGMKPYTSFQELVGE-----KEMAAELEELY 494
Cdd:cd09820 362 --EDNIIvedlrdylfgplefsrrdLMALNIQR-GRDHGLPDYNTAREAFGLPPRTTWSDINPDlfkkdPELLERLAELY 438
                       330
                ....*....|....*.
gi 18104967 495 G-DIDALEFYPGLLLE 509
Cdd:cd09820 439 GnDLSKLDLYVGGMLE 454
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
296-518 8.94e-11

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 [Multi-domain]  Cd Length: 440  Bit Score: 62.71  E-value: 8.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 296 GLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLIlIGETI----------KIV-------IEEYvqqlSGYflql 358
Cdd:cd09826 120 GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKI-VGAQMqhityshwlpKILgpvgmemLGEY----RGY---- 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 359 kfDPE-------------LLFG---VQfQYRNRIAMEFNHLYHWHPLMPDSFkvgsqeysyeqflFNTSMLVDygvEALV 422
Cdd:cd09826 191 --NPNvnpsianefataaFRFGhtlIN-PILFRLDEDFQPIPEGHLPLHKAF-------------FAPYRLVN---EGGI 251
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 423 DAFSRQIAGRIGGGRNMD--------HHILH----VAVDV----IRESREMRLQPFNEYRKRFGMKPYTSFQELVGE--- 483
Cdd:cd09826 252 DPLLRGLFATAAKDRVPDqllnteltEKLFEmaheVALDLaalnIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEikn 331
                       250       260       270
                ....*....|....*....|....*....|....*
gi 18104967 484 KEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFG 518
Cdd:cd09826 332 DDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVG 366
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
208-353 2.83e-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: 58.22  E-value: 2.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 208 FFKTSGKMGPGFTKALGHGV----------------DLGHIYGDNLERQYQLRLF--KDGKLKYQVL---DGEMYPPSVE 266
Cdd:cd09825 123 FFRSSAVCGTGDTSTLFGNLslanpreqingltsfiDASTVYGSTLALARSLRDLssDDGLLRVNSKfddSGRDYLPFQP 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 267 EAPVlmhyprgiPPQSQMAVGQEVFGLLPG-------LMLYA--TLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIG 337
Cdd:cd09825 203 EEVS--------SCNPDPNGGERVPCFLAGdgrasevLTLTAshTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGA 274
                       170
                ....*....|....*.
gi 18104967 338 ETIKIVIEEYVQQLSG 353
Cdd:cd09825 275 LHQIITFRDYIPKILG 290
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
295-353 1.41e-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  Cd Length: 411  Bit Score: 46.26  E-value: 1.41e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18104967 295 PGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSG 353
Cdd:cd09824  95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILG 153
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
39-67 2.18e-03

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: 249503  Cd Length: 32  Bit Score: 36.25  E-value: 2.18e-03
                          10        20
                  ....*....|....*....|....*....
gi 18104967    39 PCQHQGICVRFGlDRYQCDCTRtGYSGPN 67
Cdd:pfam00008   6 PCSNGGTCVDTP-GGYTCECPP-GYTGKR 32
An_peroxidase_bacterial_2 cd09821
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
296-382 4.55e-03

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: 38.55  E-value: 4.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967 296 GLMLYATLWLREHNRVCDLLKA----------------EHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGyflQLK 359
Cdd:cd09821 190 GLTAVHTVFHREHNRLVDQIKDtllqsadlafaneaggNNLAWDGERLFQAARFANEMQYQHLVFEEFARRIQP---GID 266
                        90       100
                ....*....|....*....|....*..
gi 18104967 360 FdpellFGVQFQYRN----RIAMEFNH 382
Cdd:cd09821 267 G-----FGSFNGYNPeinpSISAEFAH 288
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
40-68 4.96e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 254557  Cd Length: 31  Bit Score: 35.50  E-value: 4.96e-03
                          10        20
                  ....*....|....*....|....*....
gi 18104967    40 CQHQGICVRFgldRYQCDCTRtGYSGPNC 68
Cdd:pfam07974   7 CGGRGTCVRP---CGKCVCDS-GYQGATC 31
An_peroxidase pfam03098
Animal haem peroxidase;
145-581 4.99e-130

Animal haem peroxidase;


Pssm-ID: 251728 [Multi-domain]  Cd Length: 518  Bit Score: 393.99  E-value: 4.99e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   145 SYYTRILPSVPKD-CPTPMGTKGKKQLPDAQLLARRFLLRRKF-IPDPQGTNLMFAFFAQHFTHQFFKTSGKMG------ 216
Cdd:pfam03098  21 TPFGRLLPPVYEDgVSTPRGSVNGSPLPSPRLVSNKLLARKNGlDPPDPGLTLMLAQWGQFIDHDLTFTPHSRCcadppe 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   217 --------------------------------------PGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQvldg 258
Cdd:pfam03098 101 cfpipvppgdpyfsplgrclpffrsapacgpgpscnlpREQINQLTSYLDLSQVYGSSEEEADKLRTFKDGKLKVN---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   259 emYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGE 338
Cdd:pfam03098 177 --SPPNGKGLLPFDPPGPGSFCLACFLAGDSRANENPGLTALHTLFLREHNRIADELKALNPHWSDEQLFQEARLIVIAE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   339 TIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEF-NHLYHW-HPLMPDSFKVGS------QEYSYEQFLFNT 410
Cdd:pfam03098 255 YQKITYNEYLPALLGPDAMNANWLLYYTGYDPNVDPSISNEFaTAAYRFgHSLIPPTFERLDefngiaPEIPLHDTFFNP 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   411 SMLVD-YGVEALV------------DAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSF 477
Cdd:pfam03098 335 SRIVEeGGIDPLLrgllsqpaelldNSLSDELRNRLFGPRNVPGSGLDLAALNIQRGRDHGLPPYNEYRRFCGLKPATSF 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18104967   478 QEL---VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICspeYWKPSTFGGEVG 554
Cdd:pfam03098 415 EDLtdeIGDEELAEKLKELYGDPDDIDLYVGGLAEKPVPGGLVGPTFSCIIAEQFLRLRDGDRFW---YENPSTFTPEQL 491
                         490       500
                  ....*....|....*....|....*..
gi 18104967   555 FNIVKTaTLKKLVCLNTKTCPYVSFRV 581
Cdd:pfam03098 492 EEIRKT-TLARLICDNTDGITRVQPNA 517
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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