NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|403310643|ref|NP_001258095|]
View 

prostaglandin G/H synthase 1 isoform 5 [Homo sapiens]

Protein Classification

prostaglandin_endoperoxide_synthase domain-containing protein( domain architecture ID 10176871)

prostaglandin_endoperoxide_synthase domain-containing protein

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 ...
2-429 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: 667.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   2 LMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkgkkQLPDAQLLARRFLLRRKFIPD 80
Cdd:cd09816   24 INRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT--------ELPDVEELAELFLRRREFIPD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  81 PQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSV-EEA 159
Cdd:cd09816   96 PQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLFKDGKLKSQMINGEEYPPYLfEDG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 160 PVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGE 229
Cdd:cd09816  174 GVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 230 TIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKIGG-------------------- 289
Cdd:cd09816  254 LIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFNIGGqryplsdflfnndlvvdhgl 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 290 ----------------GRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDA 353
Cdd:cd09816  334 galvdaasrqpagrigLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELYGDVDA 413
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403310643 354 LEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTK-TCP 429
Cdd:cd09816  414 VEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFDIVKTATLQDLVCRNVKgGCP 490
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
2-429 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: 667.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   2 LMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkgkkQLPDAQLLARRFLLRRKFIPD 80
Cdd:cd09816   24 INRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT--------ELPDVEELAELFLRRREFIPD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  81 PQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSV-EEA 159
Cdd:cd09816   96 PQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLFKDGKLKSQMINGEEYPPYLfEDG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 160 PVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGE 229
Cdd:cd09816  174 GVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 230 TIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKIGG-------------------- 289
Cdd:cd09816  254 LIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFNIGGqryplsdflfnndlvvdhgl 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 290 ----------------GRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDA 353
Cdd:cd09816  334 galvdaasrqpagrigLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELYGDVDA 413
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403310643 354 LEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTK-TCP 429
Cdd:cd09816  414 VEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFDIVKTATLQDLVCRNVKgGCP 490
An_peroxidase pfam03098
Animal haem peroxidase;
38-373 2.16e-42

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 156.95  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   38 YTRILPSVPKDCP-TPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQgTNLMFAFFAQHFTH------------------- 97
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFIDHdltltpestspngsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   98 ------------------------------QFFKTSGKMGPGFTK----ALGHGVDLGHIYGDNLERQYQLRLFKDGKLK 143
Cdd:pfam03098 102 cppenlhppcfpipippddpffspfgvrcmPFVRSAPGCGLGNPReqinQVTSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  144 YQV-LDGEMYPPSVEEAPVLMHYPRGIPpqsqmavgQEVFG-----LLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQ 217
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVP--------CFLAGdsranENPGLTALHTLFLREHNRIADELAKLNPHWSDET 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  218 LFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDpeLLFGVQFQYRNRI-----------AMEFNH--------LYHWH 278
Cdd:pfam03098 254 LFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPNVdpsisnefataAFRFGHslippflyRLDEN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  279 P-------------LMPDSFKIGG------------GRNMDHHI-------LH-----------VAVDVIReSREMRLQP 315
Cdd:pfam03098 332 NvpeepslrlhdsfFNPDRLYEGGidpllrglatqpAQAVDNNFteeltnhLFgppgefsgldlAALNIQR-GRDHGLPG 410
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  316 FNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 373
Cdd:pfam03098 411 YNDYREFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGP 470
PLN02283 PLN02283
alpha-dioxygenase
123-364 5.05e-18

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 86.74  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 123 IYGDNLERQYQLRLFKDGKLKyqvldgemyppsVEEAPVLMHYPRGIPpqsqmaVGQEVFGLLPGLMLYATLWLREHNRV 202
Cdd:PLN02283 219 IYGSNEKGLRRVRTFKDGKLK------------ISEDGLLLHDEDGIP------ISGDVRNSWAGVSLLQALFVKEHNAV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 203 CDLLKAEHPTWGDEQLFQTTRLILIGETIKI-VIEEYVQQLSG-----------Y-FLQLKFDP-------ELLFGVQFQ 262
Cdd:PLN02283 281 CDALKEEYPDFDDEELYRHARLVTSAVIAKIhTIDWTVELLKTdtllagmranwYgLLGKKFKDtfghiggPILSGLVGL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 263 YRNR-------IAMEFNHLYHWHPLMPDSF------------------------------------KIG----------- 288
Cdd:PLN02283 361 KKPNnhgvpysLTEEFTSVYRMHSLLPDHLilrditaapgenkspplieeipmpeliglkgekklsKIGfeklmvsmghq 440
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 289 ----------------------GGRNMDHHILHVAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEE 346
Cdd:PLN02283 441 acgalelwnypswmrdlvpqdiDGEDRPDHVDMAALEIYRD-RERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLRE 519
                        330
                 ....*....|....*....
gi 403310643 347 LYG-DIDALEFYPGLLLEK 364
Cdd:PLN02283 520 VYGdDVEKLDLLVGLMAEK 538
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
2-429 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: 667.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   2 LMRLVLTVRSNLIPSPPTYNS-AHDYISWESFSNVSYYTRILPSVPKDCPTpmgtkgkkQLPDAQLLARRFLLRRKFIPD 80
Cdd:cd09816   24 INRLVINSRVDLIPSRPTPLStMHDYTSWESLTDRTYYGRHLPPVPRDCPT--------ELPDVEELAELFLRRREFIPD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  81 PQGTNLMFAFFAQHFTHQFFKTsgKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSV-EEA 159
Cdd:cd09816   96 PQKTTLLFPFFAQWFTDQFLRT--DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLFKDGKLKSQMINGEEYPPYLfEDG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 160 PVLMHYPRGIPP----------QSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGE 229
Cdd:cd09816  174 GVKMEFPPLVPPlgdeltpereAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 230 TIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKIGG-------------------- 289
Cdd:cd09816  254 LIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFNIGGqryplsdflfnndlvvdhgl 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 290 ----------------GRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDA 353
Cdd:cd09816  334 galvdaasrqpagrigLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELYGDVDA 413
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403310643 354 LEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTK-TCP 429
Cdd:cd09816  414 VEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGFDIVKTATLQDLVCRNVKgGCP 490
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
116-424 2.11e-91

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: 281.62  E-value: 2.11e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 116 HGVDLGHIYGDNLERQYQLRLFKDGKLKYQvldgEMYPPSVEEAPVLMHYP------RGIPPQSQMAVGQEVFGLLPGLM 189
Cdd:cd05396    7 PYLDGSSIYGSNPDVARALRTFKGGLLKTN----EVKGPSYGTELLPFNNPnpsmgtIGLPPTRCFIAGDPRVNENLLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 190 LYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAM 269
Cdd:cd05396   83 AVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVVPYVLSE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 270 EFNHLYHW-HPLMPDSFKIG-------------------------------------------------------GGRNM 293
Cdd:cd05396  163 FFTAAYRFgHSLVPEGVDRIdengqpkeipdvplkdfffntsrsilsdtgldpllrgflrqpaglidqnvddvmfLFGPL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 294 DHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 373
Cdd:cd05396  243 EGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTDPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGE 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 403310643 374 SMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEvgfNIVKTATLKKLVCLN 424
Cdd:cd05396  323 LLATIILEQFKRLVDGDRFYYVNYNPFGKSGKE---ELEKLISLADIICLN 370
An_peroxidase pfam03098
Animal haem peroxidase;
38-373 2.16e-42

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 156.95  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   38 YTRILPSVPKDCP-TPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQgTNLMFAFFAQHFTH------------------- 97
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFIDHdltltpestspngsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643   98 ------------------------------QFFKTSGKMGPGFTK----ALGHGVDLGHIYGDNLERQYQLRLFKDGKLK 143
Cdd:pfam03098 102 cppenlhppcfpipippddpffspfgvrcmPFVRSAPGCGLGNPReqinQVTSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  144 YQV-LDGEMYPPSVEEAPVLMHYPRGIPpqsqmavgQEVFG-----LLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQ 217
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVP--------CFLAGdsranENPGLTALHTLFLREHNRIADELAKLNPHWSDET 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  218 LFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDpeLLFGVQFQYRNRI-----------AMEFNH--------LYHWH 278
Cdd:pfam03098 254 LFQEARKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPNVdpsisnefataAFRFGHslippflyRLDEN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  279 P-------------LMPDSFKIGG------------GRNMDHHI-------LH-----------VAVDVIReSREMRLQP 315
Cdd:pfam03098 332 NvpeepslrlhdsfFNPDRLYEGGidpllrglatqpAQAVDNNFteeltnhLFgppgefsgldlAALNIQR-GRDHGLPG 410
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  316 FNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGE 373
Cdd:pfam03098 411 YNDYREFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGP 470
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
116-372 1.89e-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: 1.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 116 HGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPvLMHYPRGIPPQSQMAvGQEVFGLLPGLMLYATLW 195
Cdd:cd09823    9 SFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLPFSNNPT-DDCSLSSAGKPCFLA-GDGRVNEQPGLTSMHTLF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 196 LREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQ-YRNRI------- 267
Cdd:cd09823   87 LREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNgYDPNVdpsilne 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 268 ----AMEFNH--------LYHWH-------PLM-----PDSFKIGGG-------------RNMDHHILH----------- 299
Cdd:cd09823  167 faaaAFRFGHslvpgtfeRLDENyrpqgsvNLHdlffnPDRLYEEGGldpllrglatqpaQKVDRFFTDeltthfffrgg 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 300 -------VAVDVIReSREMRLQPFNEYRKRFGMKPYTSFQELVGE--KEMAAELEELYGDIDALEFYPGLLLEKCHPNSI 370
Cdd:cd09823  247 npfgldlAALNIQR-GRDHGLPGYNDYREFCGLPRATTFDDLLGImsPETIQKLRRLYKSVDDIDLYVGGLSEKPVPGGL 325

                 ..
gi 403310643 371 FG 372
Cdd:cd09823  326 VG 327
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
123-375 2.24e-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: 2.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 123 IYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPsvEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRV 202
Cdd:cd09822   63 VYGSDEERADALRSFGGGKLKTSVANAGDLLP--FNEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 203 CDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGyflqlkfdpELLFGVQFQYRN----RIAMEFN----HL 274
Cdd:cd09822  141 ADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLG---------ENALPAYSGYDEtvnpGISNEFStaayRF 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 275 YH--------------------------WHP-----LMPDSFKIGGGRNMDHHI-LHVAVDV------------------ 304
Cdd:cd09822  212 GHsmlssellrgdedgteatslalrdafFNPdeleeNGIDPLLRGLASQVAQEIdTFIVDDVrnflfgppgaggfdlaal 291
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 403310643 305 -IRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESM 375
Cdd:cd09822  292 nIQRGRDHGLPSYNQLREALGLPAVTSFSDITSDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETF 363
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
76-424 2.50e-27

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: 113.92  E-value: 2.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  76 KFIPDPQgTNLMFAFFAQHFTHQFFkTSGKmgPGFTKALGHGVDLGHIYGDNLERQYQLRLF-KDGKLKyqvLDGEMYPP 154
Cdd:cd09818   56 EFKPATS-LNLLAAAWIQFMVHDWF-SHGP--PTYINTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLK---LDADGLLP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 155 SVEEAPVlmhyprgipPQSQMAVGQEVfgllpGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIV 234
Cdd:cd09818  129 VDEHTGL---------PLTGFNDNWWV-----GLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIH 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 235 IEEYVQQ-----------------LSGYFLQLKF----DPELL----------FGVQFQyrnrIAMEFNHLYHWHPLMPD 283
Cdd:cd09818  195 TVEWTPAilahptleiamranwwgLLGERLKRVLgrdgTSELLsgipgsppnhHGVPYS----LTEEFVAVYRMHPLIPD 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 284 SF-----------------------------KIGGGR----------------NMDHHILHV-----------AVDVIRe 307
Cdd:cd09818  271 DIdfrsaddgatgeeisltdlaggkarellrKLGFADllysfgithpgaltlhNYPRFLRDLhrpdgrvidlaAIDILR- 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 308 SREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYG-DIDALEFYPGLLLEKCHPNSIFGESMIEIgapFSL-- 384
Cdd:cd09818  350 DRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGgDVEKVDLLVGLLAEPLPPGFGFSDTAFRI---FILma 426
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 403310643 385 -KGLLGNPICSpEYWKPSTFgGEVGFNIVKTATLKKLVCLN 424
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 ...
36-364 1.30e-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: 100.49  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  36 SYYTRILPsvPKDCPTPMgtkgkkqLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGK-MGPGFTKAL 114
Cdd:cd09817   53 SPYARSVP--PKHDQPGV-------LPDPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDIFRTDHRdMNINNTSSY 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 115 ghgVDLGHIYGDNLERQYQLRLFKDGKLKyqvldgemyppsveeaPVLMHYPRgippqsqmavgqeVFGLLPGLMLYATL 194
Cdd:cd09817  124 ---LDLSPLYGSNQEEQNKVRTMKDGKLK----------------PDTFSDKR-------------LLGQPPGVCALLVM 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 195 WLREHNRVCDLL-----------------KAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSG---YFLQLKFDP- 253
Cdd:cd09817  172 FNRFHNYVVEQLaqineggrftppgdkldSSAKEEKLDEDLFQTARLITCGLYINIVLHDYVRAILNlnrTDSTWTLDPr 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 254 -ELLFGVQFQYR---NRIAMEFNHLYHWH-------------------------------------------PLMPDSFK 286
Cdd:cd09817  252 vEIGRSLTGVPRgtgNQVSVEFNLLYRWHsaisardekwtedlfeslfggkspdevtlkefmqalgrfealiPKDPSQRT 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 287 IGG------GRNMDH-----------------HILHV-----AVDV--IRESREMRLQPFNEYRKRFGMKPYTSFQELVG 336
Cdd:cd09817  332 FGGlkrgpdGRFRDEdlvrilkdsiedpagafGARNVpaslkVIEIlgILQAREWNVATLNEFRKFFGLKPYETFEDINS 411
                        410       420
                 ....*....|....*....|....*...
gi 403310643 337 EKEMAAELEELYGDIDALEFYPGLLLEK 364
Cdd:cd09817  412 DPEVAEALELLYGHPDNVELYPGLVAED 439
PLN02283 PLN02283
alpha-dioxygenase
123-364 5.05e-18

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 86.74  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 123 IYGDNLERQYQLRLFKDGKLKyqvldgemyppsVEEAPVLMHYPRGIPpqsqmaVGQEVFGLLPGLMLYATLWLREHNRV 202
Cdd:PLN02283 219 IYGSNEKGLRRVRTFKDGKLK------------ISEDGLLLHDEDGIP------ISGDVRNSWAGVSLLQALFVKEHNAV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 203 CDLLKAEHPTWGDEQLFQTTRLILIGETIKI-VIEEYVQQLSG-----------Y-FLQLKFDP-------ELLFGVQFQ 262
Cdd:PLN02283 281 CDALKEEYPDFDDEELYRHARLVTSAVIAKIhTIDWTVELLKTdtllagmranwYgLLGKKFKDtfghiggPILSGLVGL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 263 YRNR-------IAMEFNHLYHWHPLMPDSF------------------------------------KIG----------- 288
Cdd:PLN02283 361 KKPNnhgvpysLTEEFTSVYRMHSLLPDHLilrditaapgenkspplieeipmpeliglkgekklsKIGfeklmvsmghq 440
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 289 ----------------------GGRNMDHHILHVAVDVIREsREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEE 346
Cdd:PLN02283 441 acgalelwnypswmrdlvpqdiDGEDRPDHVDMAALEIYRD-RERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLRE 519
                        330
                 ....*....|....*....
gi 403310643 347 LYG-DIDALEFYPGLLLEK 364
Cdd:PLN02283 520 VYGdDVEKLDLLVGLMAEK 538
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
119-363 2.68e-15

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: 78.11  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 119 DLGHIYGDNLERQYQLRLFKDGKLKYQVlDGEMYPPSVEEAPVLMHYPrgiPPQSQMAVGQEVFGL-------LPGLMLY 191
Cdd:cd09820  142 DGSSIYGSSKAWSDALRSFSGGRLASGD-DGGFPRRNTNRLPLANPPP---PSYHGTRGPERLFKLgnprgneNPFLLTF 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 192 ATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQL--------SGYflQLKFDPELlfGVQFQy 263
Cdd:cd09820  218 GILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALlgtnvppyTGY--KPHVDPGI--SHEFQ- 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 264 rnRIAMEFNhlyhwHPLMP-------------DSFKIGGGR-------------------NMDHHIL-----------HV 300
Cdd:cd09820  293 --AAAFRFG-----HTLVPpgvyrrnrqcnfrEVLTTSGGSpalrlcntywnsqepllksDIDELLLgmasqiaeredNI 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 301 AVDVIRES--------------------REMRLQPFNEYRKRFGMKPYTSFQELVGE-----KEMAAELEELYG-DIDAL 354
Cdd:cd09820  366 IVEDLRDYlfgplefsrrdlmalniqrgRDHGLPDYNTAREAFGLPPRTTWSDINPDlfkkdPELLERLAELYGnDLSKL 445

                 ....*....
gi 403310643 355 EFYPGLLLE 363
Cdd:cd09820  446 DLYVGGMLE 454
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
187-372 4.16e-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: 61.55  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 187 GLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLIlIGETI----------KIV-------IEEYvqqlSGYflql 249
Cdd:cd09826  120 GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKI-VGAQMqhityshwlpKILgpvgmemLGEY----RGY---- 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 250 kfDPE-------------LLFG---VQfQYRNRIAMEFNHLYHWHPLMPDSF-------KIGG----------------- 289
Cdd:cd09826  191 --NPNvnpsianefataaFRFGhtlIN-PILFRLDEDFQPIPEGHLPLHKAFfapyrlvNEGGidpllrglfataakdrv 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 290 -GRNMDHHILH--------VAVDV----IRESREMRLQPFNEYRKRFGMKPYTSFQELVGE---KEMAAELEELYGDIDA 353
Cdd:cd09826  268 pDQLLNTELTEklfemaheVALDLaalnIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEiknDDVREKLKRLYGHPGN 347
                        250
                 ....*....|....*....
gi 403310643 354 LEFYPGLLLEKCHPNSIFG 372
Cdd:cd09826  348 IDLFVGGILEDLLPGARVG 366
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
99-369 5.78e-10

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: 61.30  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643  99 FFKTSGKMGPGFTKALGHGV----------------DLGHIYGDNLERQYQLRLF--KDGKLKYQVL---DGEMYPPSVE 157
Cdd:cd09825  123 FFRSSAVCGTGDTSTLFGNLslanpreqingltsfiDASTVYGSTLALARSLRDLssDDGLLRVNSKfddSGRDYLPFQP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 158 EAPVlmhyprgiPPQSQMAVGQEVFGLLPG-------LMLYA--TLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIG 228
Cdd:cd09825  203 EEVS--------SCNPDPNGGERVPCFLAGdgrasevLTLTAshTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGA 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 229 ETIKIVIEEYV---------QQLSGYFlqLKFDPellfGVQFQYRNRIAM---------------EFNHLYHWHPLMP-- 282
Cdd:cd09825  275 LHQIITFRDYIpkilgpeafDQYGGYY--EGYDP----TVNPTVSNVFSTaafrfghatihptvrRLDENFQEHPVLPnl 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403310643 283 ---DSF-------KIGGgrnMDHHI---------LHVAVDVIRES------------------------REMRLQPFNEY 319
Cdd:cd09825  349 alhDAFfspwrlvREGG---LDPVIrgliggpakLVTPDDLMNEElteklfvlsnsstldlaslnlqrgRDHGLPGYNDW 425
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 403310643 320 RKRFGMKPYTSFQEL---VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNS 369
Cdd:cd09825  426 REFCGLPRLATPADLataIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGA 478
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
186-244 2.33e-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: 46.64  E-value: 2.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 403310643 186 PGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSG 244
Cdd:cd09824   95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILG 153
 
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