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Conserved domains on  [gi|4506265|ref|NP_000954|]
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prostaglandin G/H synthase 2 precursor [Homo sapiens]

Protein Classification

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

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

Graphical summary

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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 ...
75-562 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: 813.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   75 HYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNAD-YGYKSWEAFSNLSYYTRALPPVPDDCPTplgvkg 153
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTmHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  154 kkQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHkrGPAFTNGLGHGVDLNHIYGETLARQRKLRLF 233
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDP--GDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  234 KDGKMKYQIIDGEMYPPTV-KDTQAEMIYPPQVP----------EHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVL 302
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPplgdeltperEAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  303 KQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQ 382
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  383 IHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRVaGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYE 462
Cdd:cd09816 311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  463 SFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGF 542
Cdd:cd09816 390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                       490       500
                ....*....|....*....|.
gi 4506265  543 QIINTASIQSLICNNVK-GCP 562
Cdd:cd09816 470 DIVKTATLQDLVCRNVKgGCP 490
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
19-54 1.09e-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: 39.54  E-value: 1.09e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4506265   19 NPCCS-HPCQNRGVCMSvGFDQYKCDCtRTGFYGENC 54
Cdd:cd00054   3 DECASgNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNC 37
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
75-562 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: 813.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   75 HYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNAD-YGYKSWEAFSNLSYYTRALPPVPDDCPTplgvkg 153
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTmHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  154 kkQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHkrGPAFTNGLGHGVDLNHIYGETLARQRKLRLF 233
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDP--GDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  234 KDGKMKYQIIDGEMYPPTV-KDTQAEMIYPPQVP----------EHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVL 302
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPplgdeltperEAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  303 KQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQ 382
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  383 IHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRVaGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYE 462
Cdd:cd09816 311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  463 SFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGF 542
Cdd:cd09816 390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                       490       500
                ....*....|....*....|.
gi 4506265  543 QIINTASIQSLICNNVK-GCP 562
Cdd:cd09816 470 DIVKTATLQDLVCRNVKgGCP 490
An_peroxidase pfam03098
Animal haem peroxidase;
134-508 7.01e-57

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 200.09  E-value: 7.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    134 YTRALPPVPDDCP-TPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGsNMMFAFFAQHFTH------------------- 193
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPNL-TLLLMQWGQFIDHdltltpestspngsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    194 -------------------QFFKTDHKR--------------GPA-FTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMK 239
Cdd:pfam03098 102 cppenlhppcfpipippddPFFSPFGVRcmpfvrsapgcglgNPReQINQVTSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    240 YQI-IDGEMYPPTVKDTQAEMIYPPQVPehlRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTS 318
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVP---CFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    319 RLILIGETIKIVIEDYVQHLSGYHFKLKFDpeLLFNKQFQYQN----RIAAEFNTL-YHW-HPLLPDTFQIHDQKYNYQ- 391
Cdd:pfam03098 259 RKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPnvdpSISNEFATAaFRFgHSLIPPFLYRLDENNVPEe 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    392 ------QFIYNNSILLEHGITQFVESFTRQIAGRVAggRNVPPAVQ------KVSQ-----ASID--QSRQMKYQSFNEY 452
Cdd:pfam03098 337 pslrlhDSFFNPDRLYEGGIDPLLRGLATQPAQAVD--NNFTEELTnhlfgpPGEFsgldlAALNiqRGRDHGLPGYNDY 414
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506265    453 RKRFMLKPYESFEELTGE--KEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETM 508
Cdd:pfam03098 415 REFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTF 472
PLN02283 PLN02283
alpha-dioxygenase
129-497 1.37e-22

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 102.15  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   129 SNLSYYTRALPPVPDdcptplgvKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTH--------------- 193
Cdd:PLN02283 102 SQGTFFGRNMPPVDQ--------KDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHdwidhledtqqielt 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   194 --------------QFFKTdhKRGPAFTNGLGHGV--------DLNHIYGETLARQRKLRLFKDGKMKyqiidgemyppt 251
Cdd:PLN02283 174 apkevasqcplksfKFYKT--KEVPTGSPDIKTGSlnirtpwwDGSVIYGSNEKGLRRVRTFKDGKLK------------ 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   252 vkdtqaemIYPPQVPEHLR--FAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKI 329
Cdd:PLN02283 240 --------ISEDGLLLHDEdgIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKI 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   330 VIEDYVQHLsgyhfkLKFDPEL---------LFNKQFQ--------------------------YQnrIAAEFNTLYHWH 374
Cdd:PLN02283 312 HTIDWTVEL------LKTDTLLagmranwygLLGKKFKdtfghiggpilsglvglkkpnnhgvpYS--LTEEFTSVYRMH 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   375 PLLPDTFQIHD--------------QKYNYQQFIYN--NSILLEHGITQFVESFTRQIAGRVA------GGRNVPPA--- 429
Cdd:PLN02283 384 SLLPDHLILRDitaapgenksppliEEIPMPELIGLkgEKKLSKIGFEKLMVSMGHQACGALElwnypsWMRDLVPQdid 463
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506265   430 ----VQKVSQASID--QSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYG-DIDAVELYPALLVEK 497
Cdd:PLN02283 464 gedrPDHVDMAALEiyRDRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGdDVEKLDLLVGLMAEK 538
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
19-54 1.09e-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: 39.54  E-value: 1.09e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4506265   19 NPCCS-HPCQNRGVCMSvGFDQYKCDCtRTGFYGENC 54
Cdd:cd00054   3 DECASgNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNC 37
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
75-562 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: 813.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   75 HYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNAD-YGYKSWEAFSNLSYYTRALPPVPDDCPTplgvkg 153
Cdd:cd09816   1 HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTmHDYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  154 kkQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHkrGPAFTNGLGHGVDLNHIYGETLARQRKLRLF 233
Cdd:cd09816  75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDP--GDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  234 KDGKMKYQIIDGEMYPPTV-KDTQAEMIYPPQVP----------EHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVL 302
Cdd:cd09816 151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPplgdeltperEAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  303 KQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQ 382
Cdd:cd09816 231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  383 IHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRVaGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYE 462
Cdd:cd09816 311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  463 SFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGF 542
Cdd:cd09816 390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                       490       500
                ....*....|....*....|.
gi 4506265  543 QIINTASIQSLICNNVK-GCP 562
Cdd:cd09816 470 DIVKTATLQDLVCRNVKgGCP 490
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
212-557 2.94e-75

Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.


Pssm-ID: 188647 [Multi-domain]  Cd Length: 370  Bit Score: 244.64  E-value: 2.94e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  212 HGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMY----PPTVKDtQAEMIYPPQVPEHLrFAVGQEVFGLVPGLMMY 287
Cdd:cd05396   7 PYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYgtelLPFNNP-NPSMGTIGLPPTRC-FIAGDPRVNENLLLLAV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  288 ATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEF 367
Cdd:cd05396  85 HTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVVPYVLSEFF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  368 NTLYHW-HPLLPDTFQIHDQKYN--------YQQFIYNNS--ILLEHGITQFVESFTRQIAGRV--------AGGRNVPP 428
Cdd:cd05396 165 TAAYRFgHSLVPEGVDRIDENGQpkeipdvpLKDFFFNTSrsILSDTGLDPLLRGFLRQPAGLIdqnvddvmFLFGPLEG 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  429 AVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETM 508
Cdd:cd05396 245 VGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTDPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGELL 324
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 4506265  509 VEVGAPFSLKGLMGNVICSPAYWKPSTFGGEvgfQIINTASIQSLICNN 557
Cdd:cd05396 325 ATIILEQFKRLVDGDRFYYVNYNPFGKSGKE---ELEKLISLADIICLN 370
An_peroxidase pfam03098
Animal haem peroxidase;
134-508 7.01e-57

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 200.09  E-value: 7.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    134 YTRALPPVPDDCP-TPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGsNMMFAFFAQHFTH------------------- 193
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPNL-TLLLMQWGQFIDHdltltpestspngsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    194 -------------------QFFKTDHKR--------------GPA-FTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMK 239
Cdd:pfam03098 102 cppenlhppcfpipippddPFFSPFGVRcmpfvrsapgcglgNPReQINQVTSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    240 YQI-IDGEMYPPTVKDTQAEMIYPPQVPehlRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTS 318
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVP---CFLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    319 RLILIGETIKIVIEDYVQHLSGYHFKLKFDpeLLFNKQFQYQN----RIAAEFNTL-YHW-HPLLPDTFQIHDQKYNYQ- 391
Cdd:pfam03098 259 RKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPnvdpSISNEFATAaFRFgHSLIPPFLYRLDENNVPEe 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265    392 ------QFIYNNSILLEHGITQFVESFTRQIAGRVAggRNVPPAVQ------KVSQ-----ASID--QSRQMKYQSFNEY 452
Cdd:pfam03098 337 pslrlhDSFFNPDRLYEGGIDPLLRGLATQPAQAVD--NNFTEELTnhlfgpPGEFsgldlAALNiqRGRDHGLPGYNDY 414
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506265    453 RKRFMLKPYESFEELTGE--KEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETM 508
Cdd:pfam03098 415 REFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTF 472
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
157-507 5.49e-44

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: 163.61  E-value: 5.49e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  157 LPDSNEIVEKLLLRRKFIPDPQgSNMMFAFFAQHFTHQFFktDHkRGPAFTNGLGHGVDLNHIYGETLARQRKLRLF-KD 235
Cdd:cd09818  41 TPNPRVISRRLLARTEFKPATS-LNLLAAAWIQFMVHDWF--SH-GPPTYINTNTHWWDGSQIYGSTEEAQKRLRTFpPD 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  236 GKMKyqiIDGEMYPPTVKDTqaemiyppqvpehlrfavGQEVFGLVP----GLMMYATIWLREHNRVCDVLKQEHPEWGD 311
Cdd:cd09818 117 GKLK---LDADGLLPVDEHT------------------GLPLTGFNDnwwvGLSLLHTLFVREHNAICDALRKEYPDWSD 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  312 EQLFQTSRLI---------------------------------LIGETIKIVIEDYVQH--LSGY------HFKlkfDPE 350
Cdd:cd09818 176 EQLFDKARLVnaalmakihtvewtpailahptleiamranwwgLLGERLKRVLGRDGTSelLSGIpgsppnHHG---VPY 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  351 LLfnkqfqyqnriAAEFNTLYHWHPLLPDTFQI-------HDQKYNYQQFIYN--NSILLEHGITQFVESFTRQIAGRVA 421
Cdd:cd09818 253 SL-----------TEEFVAVYRMHPLIPDDIDFrsaddgaTGEEISLTDLAGGkaRELLRKLGFADLLYSFGITHPGALT 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  422 gGRNVPPAVQ--------KVSQASID--QSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYG-DIDAVELY 490
Cdd:cd09818 322 -LHNYPRFLRdlhrpdgrVIDLAAIDilRDRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGgDVEKVDLL 400
                       410
                ....*....|....*..
gi 4506265  491 PALLVEKPRPDAIFGET 507
Cdd:cd09818 401 VGLLAEPLPPGFGFSDT 417
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
208-508 1.46e-43

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: 160.05  E-value: 1.46e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  208 NGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPPtvKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMY 287
Cdd:cd09823   5 NQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLP--FSNNPTDDCSLSSAGKPCFLAGDGRVNEQPGLTSM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  288 ATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQ-YQNR---- 362
Cdd:cd09823  83 HTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNgYDPNvdps 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  363 IAAEFNTLYHW--HPLLPDTFQIHDQKYNYQQFI-----YNN--SILLEHGITQFVESFTRQIAGRVagGRNVPPAVQK- 432
Cdd:cd09823 163 ILNEFAAAAFRfgHSLVPGTFERLDENYRPQGSVnlhdlFFNpdRLYEEGGLDPLLRGLATQPAQKV--DRFFTDELTTh 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  433 ----------VSQASID--QSRQMKYQSFNEYRKRFMLKPYESFEELTGekEMSAE----LEALYGDIDAVELYPALLVE 496
Cdd:cd09823 241 fffrggnpfgLDLAALNiqRGRDHGLPGYNDYREFCGLPRATTFDDLLG--IMSPEtiqkLRRLYKSVDDIDLYVGGLSE 318
                       330
                ....*....|..
gi 4506265  497 KPRPDAIFGETM 508
Cdd:cd09823 319 KPVPGGLVGPTF 330
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
174-508 4.91e-37

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: 142.83  E-value: 4.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  174 IPDPQGSNMMFAFFAQHFTHQF-FKTDHKRgpAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPPtv 252
Cdd:cd09822  19 IPNSRGLSDWFWVWGQFLDHDIdLTPDNPR--EQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVANAGDLLP-- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  253 KDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIE 332
Cdd:cd09822  95 FNEAGLPNDNGGVPADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYN 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  333 DYVQHLSGYHfklKFDPELLFNKQFqyQNRIAAEFNTL-YHW-HPLLPDTFQIHDQKYNYQQFI------YNNSILLEHG 404
Cdd:cd09822 175 EFLPALLGEN---ALPAYSGYDETV--NPGISNEFSTAaYRFgHSMLSSELLRGDEDGTEATSLalrdafFNPDELEENG 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  405 ItqfvESFTRQIAGRVA---------GGRNV---PPAVQKVSQAS--IDQSRQMKYQSFNEYRKRFMLKPYESFEELTGE 470
Cdd:cd09822 250 I----DPLLRGLASQVAqeidtfivdDVRNFlfgPPGAGGFDLAAlnIQRGRDHGLPSYNQLREALGLPAVTSFSDITSD 325
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 4506265  471 KEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETM 508
Cdd:cd09822 326 PDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETF 363
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
147-500 8.50e-37

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: 144.40  E-value: 8.50e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  147 TPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKrgPAFTNGLGHGVDLNHIYGETLAR 226
Cdd:cd09817  59 VPPKHDQPGVLPDPGLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDIFRTDHR--DMNINNTSSYLDLSPLYGSNQEE 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  227 QRKLRLFKDGKMKyqiidgemypptvKDTQAEmiyppqvPEHLRFAVGQEVFglvpgLMMYAtiwlREHNRVCDVL---- 302
Cdd:cd09817 137 QNKVRTMKDGKLK-------------PDTFSD-------KRLLGQPPGVCAL-----LVMFN----RFHNYVVEQLaqin 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  303 -------------KQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYH-----FKLkfDPELLFNKQFQYQ---- 360
Cdd:cd09817 188 eggrftppgdkldSSAKEEKLDEDLFQTARLITCGLYINIVLHDYVRAILNLNrtdstWTL--DPRVEIGRSLTGVprgt 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  361 -NRIAAEFNTLYHWHPLLPDTfqihDQKY--NYQQFIYNNSILLEHGITQFVES-------------------FTRQIAG 418
Cdd:cd09817 266 gNQVSVEFNLLYRWHSAISAR----DEKWteDLFESLFGGKSPDEVTLKEFMQAlgrfealipkdpsqrtfggLKRGPDG 341
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  419 R----------------VA---GGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEA 479
Cdd:cd09817 342 RfrdedlvrilkdsiedPAgafGARNVPASLKVIEILGILQAREWNVATLNEFRKFFGLKPYETFEDINSDPEVAEALEL 421
                       410       420
                ....*....|....*....|.
gi 4506265  480 LYGDIDAVELYPALLVEKPRP 500
Cdd:cd09817 422 LYGHPDNVELYPGLVAEDAKP 442
PLN02283 PLN02283
alpha-dioxygenase
129-497 1.37e-22

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 102.15  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   129 SNLSYYTRALPPVPDdcptplgvKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTH--------------- 193
Cdd:PLN02283 102 SQGTFFGRNMPPVDQ--------KDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHdwidhledtqqielt 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   194 --------------QFFKTdhKRGPAFTNGLGHGV--------DLNHIYGETLARQRKLRLFKDGKMKyqiidgemyppt 251
Cdd:PLN02283 174 apkevasqcplksfKFYKT--KEVPTGSPDIKTGSlnirtpwwDGSVIYGSNEKGLRRVRTFKDGKLK------------ 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   252 vkdtqaemIYPPQVPEHLR--FAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKI 329
Cdd:PLN02283 240 --------ISEDGLLLHDEdgIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKI 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   330 VIEDYVQHLsgyhfkLKFDPEL---------LFNKQFQ--------------------------YQnrIAAEFNTLYHWH 374
Cdd:PLN02283 312 HTIDWTVEL------LKTDTLLagmranwygLLGKKFKdtfghiggpilsglvglkkpnnhgvpYS--LTEEFTSVYRMH 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265   375 PLLPDTFQIHD--------------QKYNYQQFIYN--NSILLEHGITQFVESFTRQIAGRVA------GGRNVPPA--- 429
Cdd:PLN02283 384 SLLPDHLILRDitaapgenksppliEEIPMPELIGLkgEKKLSKIGFEKLMVSMGHQACGALElwnypsWMRDLVPQdid 463
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506265   430 ----VQKVSQASID--QSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYG-DIDAVELYPALLVEK 497
Cdd:PLN02283 464 gedrPDHVDMAALEiyRDRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGdDVEKLDLLVGLMAEK 538
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
219-496 2.71e-16

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: 81.96  E-value: 2.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  219 IYGETLARQRKLRLFKDGKMKYQiiDGEMYPPtvKDTQAEMIYPPQVPEHLRFAVGQEVFGL-------VPGLMMYATIW 291
Cdd:cd09820 146 IYGSSKAWSDALRSFSGGRLASG--DDGGFPR--RNTNRLPLANPPPPSYHGTRGPERLFKLgnprgneNPFLLTFGILW 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  292 LREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHL--------SGYHfklKF-DPELlfNKQFQyqnr 362
Cdd:cd09820 222 FRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALlgtnvppyTGYK---PHvDPGI--SHEFQ---- 292
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  363 iAAEFNTLyhwHPLLPDTFQIHDQKYNYQQFIYN----------------NSILLEHGITQFVESFTRQIAGR-----VA 421
Cdd:cd09820 293 -AAAFRFG---HTLVPPGVYRRNRQCNFREVLTTsggspalrlcntywnsQEPLLKSDIDELLLGMASQIAERedniiVE 368
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  422 GGRNVPPAVQKVSQ-----ASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGE-----KEMSAELEALYG-DIDAVELY 490
Cdd:cd09820 369 DLRDYLFGPLEFSRrdlmaLNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDlfkkdPELLERLAELYGnDLSKLDLY 448

                ....*.
gi 4506265  491 PALLVE 496
Cdd:cd09820 449 VGGMLE 454
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
207-507 2.96e-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  Cd Length: 440  Bit Score: 65.79  E-value: 2.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  207 TNGLGHGVDLNHIYGETLARQRKLR-LFKD-GKMKYQIID--GEMYPPTVKDTQAE-MIYPPQVP------------EHL 269
Cdd:cd09826  40 INQLTSYIDASNVYGSSDEEALELRdLASDrGLLRVGIVSeaGKPLLPFERDSPMDcRRDPNESPipcflagdhranEQL 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  270 rfavgqevfglvpGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLIlIGETI----------KIVIEDYVQHLS 339
Cdd:cd09826 120 -------------GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKI-VGAQMqhityshwlpKILGPVGMEMLG 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  340 GYHfklKFDPELlfnkqfqyQNRIAAEFNT--LYHWHPL-------LPDTFQIHDQKYN--YQQFIYNNSILLEHGI--- 405
Cdd:cd09826 186 EYR---GYNPNV--------NPSIANEFATaaFRFGHTLinpilfrLDEDFQPIPEGHLplHKAFFAPYRLVNEGGIdpl 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  406 --------------TQFVES-FTRQI---AGRVAggrnvppavQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEEL 467
Cdd:cd09826 255 lrglfataakdrvpDQLLNTeLTEKLfemAHEVA---------LDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDL 325
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4506265  468 TGE---KEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGET 507
Cdd:cd09826 326 KNEiknDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPT 368
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
208-335 7.96e-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: 58.60  E-value: 7.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  208 NGLGHGVDLNHIYGETLARQRKLRLF--KDGKMKYQI---IDGEMYPP--TVKDTQAEMIYP--PQVPEhlrFAVGQEVF 278
Cdd:cd09825 152 NGLTSFIDASTVYGSTLALARSLRDLssDDGLLRVNSkfdDSGRDYLPfqPEEVSSCNPDPNggERVPC---FLAGDGRA 228
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4506265  279 GLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYV 335
Cdd:cd09825 229 SEVLTLTASHTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYI 285
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
282-389 1.86e-06

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: 50.50  E-value: 1.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  282 PGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFqyQN 361
Cdd:cd09824  95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARLPPYRGYNESV--DP 172
                        90       100
                ....*....|....*....|....*....
gi 4506265  362 RIAAEFNTLYHW-HPLLPDTFQIHDQKYN 389
Cdd:cd09824 173 RIANVFTTAFRRgHTTVQPFVFRLDENYQ 201
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
19-54 1.09e-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: 39.54  E-value: 1.09e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4506265   19 NPCCS-HPCQNRGVCMSvGFDQYKCDCtRTGFYGENC 54
Cdd:cd00054   3 DECASgNPCQNGGTCVN-TVGSYRCSC-PPGYTGRNC 37
An_peroxidase_bacterial_2 cd09821
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
283-493 1.32e-04

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: 44.71  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  283 GLMMYATIWLREHNRVCDVLKQ----------------EHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGyhfklK 346
Cdd:cd09821 190 GLTAVHTVFHREHNRLVDQIKDtllqsadlafaneaggNNLAWDGERLFQAARFANEMQYQHLVFEEFARRIQP-----G 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  347 FDPELLFNKQFQYQN-RIAAEF-NTLYHW-HPLLPDTFQIHD--------------QKYNYQQFIYNNSILLEHGITQFV 409
Cdd:cd09821 265 IDGFGSFNGYNPEINpSISAEFaHAVYRFgHSMLTETVTRIGpdadegldnqvgliDAFLNPVAFLPATLYAEEGAGAIL 344
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506265  410 ESFTRQIAGRVagGRNVPPAVQK-------------------VSQASIDQSRQMKYQSFNEYrkrFMLKPYESFEELTGE 470
Cdd:cd09821 345 RGMTRQVGNEI--DEFVTDALRNnlvglpldlaalniargrdTGLPTLNEARAQLFAATGDT---ILKAPYESWNDFGAR 419
                       250       260
                ....*....|....*....|....*.
gi 4506265  471 KEMSAELE---ALYGDIDAVELYPAL 493
Cdd:cd09821 420 LKNPESLInfiAAYGTHLTITGATTL 445
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
23-54 8.70e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 34.37  E-value: 8.70e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 4506265   23 SHPCQNRGVCMSVGfDQYKCDCtRTGFYGE-NC 54
Cdd:cd00053   5 SNPCSNGGTCVNTP-GSYRCVC-PPGYTGDrSC 35
 
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.
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