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Conserved domains on  [gi|1717019538|ref|XP_030061795|]
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prostaglandin G/H synthase 2 [Microcaecilia unicolor]

Protein Classification

calcium-binding EGF-like domain-containing protein; peroxidase family 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| peroxidase family protein similar to Drosophila melanogaster peroxidase that is involved in the chorion hardening process, through protein cross-linking mediated by the formation of di- and tri-tyrosine bonds, as well as chorion peroxidase required for ovarian follicle maturation

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 ...
83-570 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: 842.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538  83 HYILTHFKGVWNIINNIPFLRDTIMRYVLTSRSHLIDSPPTYNSDYA-YKSWEAYSNLSYYTRTLPPVGHDCPTpmgvkg 161
Cdd:cd09816     1 HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTMHdYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 162 kkELPDAKVIVEKFLLRRKFIPDPQGTNIMFAFFAQHFTHQFFKTDTkkGAAFTKGLGHGVDLSHVYGETLDRQHKLRLF 241
Cdd:cd09816    75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDP--GDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 242 KDGKLKYQMIDGEMYPPTV-QDTQVEMIYPPHIP----------QHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVL 310
Cdd:cd09816   151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPplgdeltperEAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 311 KNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQRFQYQNRIAAEFNTLYHWHPLLPDTFQ 390
Cdd:cd09816   231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 391 IQDKEYNYKQFMYNNSVMLEHGVSQMVESFSRQIAGRVaGGRNVPLVVEKVAVASIEQSRQMRYHSMNEYRKRFQLKPFS 470
Cdd:cd09816   311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 471 SFQDLTGEEEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETMVEMGAPFSLKGLMGNAICSPEYWKPSTFGGDVGF 550
Cdd:cd09816   390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                         490       500
                  ....*....|....*....|.
gi 1717019538 551 EIVNTASLQNLVCNNVK-DCP 570
Cdd:cd09816   470 DIVKTATLQDLVCRNVKgGCP 490
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
27-62 7.80e-06

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: 43.01  E-value: 7.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1717019538  27 NPCCS-NPCQNQGVCM-TVGfdKYKCDCtRTGFYGDTC 62
Cdd:cd00054     3 DECASgNPCQNGGTCVnTVG--SYRCSC-PPGYTGRNC 37
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
83-570 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: 842.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538  83 HYILTHFKGVWNIINNIPFLRDTIMRYVLTSRSHLIDSPPTYNSDYA-YKSWEAYSNLSYYTRTLPPVGHDCPTpmgvkg 161
Cdd:cd09816     1 HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTMHdYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 162 kkELPDAKVIVEKFLLRRKFIPDPQGTNIMFAFFAQHFTHQFFKTDTkkGAAFTKGLGHGVDLSHVYGETLDRQHKLRLF 241
Cdd:cd09816    75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDP--GDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 242 KDGKLKYQMIDGEMYPPTV-QDTQVEMIYPPHIP----------QHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVL 310
Cdd:cd09816   151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPplgdeltperEAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 311 KNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQRFQYQNRIAAEFNTLYHWHPLLPDTFQ 390
Cdd:cd09816   231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 391 IQDKEYNYKQFMYNNSVMLEHGVSQMVESFSRQIAGRVaGGRNVPLVVEKVAVASIEQSRQMRYHSMNEYRKRFQLKPFS 470
Cdd:cd09816   311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 471 SFQDLTGEEEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETMVEMGAPFSLKGLMGNAICSPEYWKPSTFGGDVGF 550
Cdd:cd09816   390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                         490       500
                  ....*....|....*....|.
gi 1717019538 551 EIVNTASLQNLVCNNVK-DCP 570
Cdd:cd09816   470 DIVKTATLQDLVCRNVKgGCP 490
An_peroxidase pfam03098
Animal haem peroxidase;
142-516 3.87e-56

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 198.16  E-value: 3.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 142 YTRTLPPVGHDCP-TPMGVKGKKELPDAKVIVEKFLLRRKFIPDPQgTNIMFAFFAQHFTHQFFKTDTKKGAA------- 213
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFIDHDLTLTPESTSPNgsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 214 -------------------------------FTK-----GLG----------HGVDLSHVYGETLDRQHKLRLFKDGKLK 247
Cdd:pfam03098 102 cppenlhppcfpipippddpffspfgvrcmpFVRsapgcGLGnpreqinqvtSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 248 YQM-IDGEMYPPTVQDTQVEMIYPPHIPQhlkFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKNEHPEWDDERIFQTT 326
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVPC---FLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 327 RLILTGETIKIVIEDYVQHLSGYHFKLKFDpeLLFNQRFQYQN----RIAAEFNTL-YHW-HPLLPDTFQIQDKE----- 395
Cdd:pfam03098 259 RKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPnvdpSISNEFATAaFRFgHSLIPPFLYRLDENnvpee 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 396 --YNYKQFMYNNSVMLEHGVSQMVESFSRQIAGRVA------------GGRNVPLVVEKVAVaSIEQSRQM---RYhsmN 458
Cdd:pfam03098 337 psLRLHDSFFNPDRLYEGGIDPLLRGLATQPAQAVDnnfteeltnhlfGPPGEFSGLDLAAL-NIQRGRDHglpGY---N 412
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 459 EYRKRFQLKPFSSFQDLTGE--EEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETM 516
Cdd:pfam03098 413 DYREFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTF 472
PLN02283 PLN02283
alpha-dioxygenase
134-515 5.78e-26

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 112.93  E-value: 5.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 134 EAYSNLSYYTRTLPPVghdcptpmgvKGKKEL--PDAKVIVEKFLLRRKFIPDPQGTNIMFAFFAQHFTH---------- 201
Cdd:PLN02283   99 GAGSQGTFFGRNMPPV----------DQKDKLldPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHdwidhledtq 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 202 -------------------QFFKTDTKKGAAFTKGLGH------GVDLSHVYGETLDRQHKLRLFKDGKLKyqmIDGEMY 256
Cdd:PLN02283  169 qieltapkevasqcplksfKFYKTKEVPTGSPDIKTGSlnirtpWWDGSVIYGSNEKGLRRVRTFKDGKLK---ISEDGL 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 257 PPTVQDTqvemiypphipqhlkFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIK 336
Cdd:PLN02283  246 LLHDEDG---------------IPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAK 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 337 IVIEDYVQHLsgyhfkLKFDPEL---------LFNQRFQ--------------------------YQnrIAAEFNTLYHW 381
Cdd:PLN02283  311 IHTIDWTVEL------LKTDTLLagmranwygLLGKKFKdtfghiggpilsglvglkkpnnhgvpYS--LTEEFTSVYRM 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 382 HPLLPDTFQIQD--------------KEYNYKQFMYN--NSVMLEHGVSQMVESFSRQIAGRVA---------------- 429
Cdd:PLN02283  383 HSLLPDHLILRDitaapgenksppliEEIPMPELIGLkgEKKLSKIGFEKLMVSMGHQACGALElwnypswmrdlvpqdi 462
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 430 GGRNVPlvvEKVAVASIEQSRQ-----MRYhsmNEYRKRFQLKPFSSFQDLTGEEEMATELEKLYG-DIDAMELYPGLLV 503
Cdd:PLN02283  463 DGEDRP---DHVDMAALEIYRDrergvARY---NEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGdDVEKLDLLVGLMA 536
                         490
                  ....*....|..
gi 1717019538 504 EKPRPGAIFGET 515
Cdd:PLN02283  537 EKKIKGFAISET 548
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
27-62 7.80e-06

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: 43.01  E-value: 7.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1717019538  27 NPCCS-NPCQNQGVCM-TVGfdKYKCDCtRTGFYGDTC 62
Cdd:cd00054     3 DECASgNPCQNGGTCVnTVG--SYRCSC-PPGYTGRNC 37
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
34-62 3.93e-03

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


Pssm-ID: 400365  Cd Length: 26  Bit Score: 35.02  E-value: 3.93e-03
                          10        20
                  ....*....|....*....|....*....
gi 1717019538  34 CQNQGVCMTVGFdkyKCDCtRTGFYGDTC 62
Cdd:pfam07974   2 CSGRGTCVNQCG---KCVC-DSGYQGATC 26
 
Name Accession Description Interval E-value
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
83-570 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: 842.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538  83 HYILTHFKGVWNIINNIPFLRDTIMRYVLTSRSHLIDSPPTYNSDYA-YKSWEAYSNLSYYTRTLPPVGHDCPTpmgvkg 161
Cdd:cd09816     1 HFLLTHFRWLWNIVNRIPFLRRLINRLVINSRVDLIPSRPTPLSTMHdYTSWESLTDRTYYGRHLPPVPRDCPT------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 162 kkELPDAKVIVEKFLLRRKFIPDPQGTNIMFAFFAQHFTHQFFKTDTkkGAAFTKGLGHGVDLSHVYGETLDRQHKLRLF 241
Cdd:cd09816    75 --ELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQFLRTDP--GDPRRNTSNHGIDLSQIYGLTEARTHALRLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 242 KDGKLKYQMIDGEMYPPTV-QDTQVEMIYPPHIP----------QHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVL 310
Cdd:cd09816   151 KDGKLKSQMINGEEYPPYLfEDGGVKMEFPPLVPplgdeltperEAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDIL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 311 KNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQRFQYQNRIAAEFNTLYHWHPLLPDTFQ 390
Cdd:cd09816   231 KKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPYHFKLFFDPELAFNEPWQRQNRIALEFNLLYRWHPLVPDTFN 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 391 IQDKEYNYKQFMYNNSVMLEHGVSQMVESFSRQIAGRVaGGRNVPLVVEKVAVASIEQSRQMRYHSMNEYRKRFQLKPFS 470
Cdd:cd09816   311 IGGQRYPLSDFLFNNDLVVDHGLGALVDAASRQPAGRI-GLRNTPPFLLPVEVRSIEQGRKLRLASFNDYRKRFGLPPYT 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 471 SFQDLTGEEEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETMVEMGAPFSLKGLMGNAICSPEYWKPSTFGGDVGF 550
Cdd:cd09816   390 SFEELTGDPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVAPDAFSGALTNPLLSPEVWKPSTFGGEGGF 469
                         490       500
                  ....*....|....*....|.
gi 1717019538 551 EIVNTASLQNLVCNNVK-DCP 570
Cdd:cd09816   470 DIVKTATLQDLVCRNVKgGCP 490
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
220-565 2.65e-76

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: 247.34  E-value: 2.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 220 HGVDLSHVYGETLDRQHKLRLFKDGKLKYQMIDGEMY----PPTVQDtQVEMIYPPHIPQHLkFAVGQEVFGLVPGLMMY 295
Cdd:cd05396     7 PYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYgtelLPFNNP-NPSMGTIGLPPTRC-FIAGDPRVNENLLLLAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 296 ATIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQRFQYQNRIAAEF 375
Cdd:cd05396    85 HTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDVVPYVLSEFF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 376 NTLYHW-HPLLPDTFQIQDKEYNYKQ----------FMYNNSVMLEHGVSQMVESFSRQIAGRV--------AGGRNVPL 436
Cdd:cd05396   165 TAAYRFgHSLVPEGVDRIDENGQPKEipdvplkdffFNTSRSILSDTGLDPLLRGFLRQPAGLIdqnvddvmFLFGPLEG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 437 VVEKVAVASIEQSRQMRYHSMNEYRKRFQLKPFSSFQDLTGEEEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETM 516
Cdd:cd05396   245 VGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQDILTDPELAKKLAELYGDPDDVDLWVGGLLEKKVPPARLGELL 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1717019538 517 VEMGAPFSLKGLMGNAICSPEYWKPSTFGGDvgfEIVNTASLQNLVCNN 565
Cdd:cd05396   325 ATIILEQFKRLVDGDRFYYVNYNPFGKSGKE---ELEKLISLADIICLN 370
An_peroxidase pfam03098
Animal haem peroxidase;
142-516 3.87e-56

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 198.16  E-value: 3.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 142 YTRTLPPVGHDCP-TPMGVKGKKELPDAKVIVEKFLLRRKFIPDPQgTNIMFAFFAQHFTHQFFKTDTKKGAA------- 213
Cdd:pfam03098  23 FARLLPPAYEDGVsAPRGSSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFIDHDLTLTPESTSPNgsscdcc 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 214 -------------------------------FTK-----GLG----------HGVDLSHVYGETLDRQHKLRLFKDGKLK 247
Cdd:pfam03098 102 cppenlhppcfpipippddpffspfgvrcmpFVRsapgcGLGnpreqinqvtSFLDGSQVYGSSEETARSLRSFSGGLLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 248 YQM-IDGEMYPPTVQDTQVEMIYPPHIPQhlkFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKNEHPEWDDERIFQTT 326
Cdd:pfam03098 182 VNRsDDGKELLPFDPDGPCCCNSSGGVPC---FLAGDSRANENPGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 327 RLILTGETIKIVIEDYVQHLSGYHFKLKFDpeLLFNQRFQYQN----RIAAEFNTL-YHW-HPLLPDTFQIQDKE----- 395
Cdd:pfam03098 259 RKIVIAQIQHITYNEWLPAILGEDNMNWFG--LLPLPYNGYDPnvdpSISNEFATAaFRFgHSLIPPFLYRLDENnvpee 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 396 --YNYKQFMYNNSVMLEHGVSQMVESFSRQIAGRVA------------GGRNVPLVVEKVAVaSIEQSRQM---RYhsmN 458
Cdd:pfam03098 337 psLRLHDSFFNPDRLYEGGIDPLLRGLATQPAQAVDnnfteeltnhlfGPPGEFSGLDLAAL-NIQRGRDHglpGY---N 412
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 459 EYRKRFQLKPFSSFQDLTGE--EEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETM 516
Cdd:pfam03098 413 DYREFCGLPPAKSFEDLTDVipNEVIAKLRELYGSVDDIDLWVGGLAEKPLPGGLVGPTF 472
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
220-516 6.71e-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: 158.12  E-value: 6.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 220 HGVDLSHVYGETLDRQHKLRLFKDGKLKYQMIDGEMYPPtVQDTQVEMIYPPHIPQHLkFAVGQEVFGLVPGLMMYATIW 299
Cdd:cd09823     9 SFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRNGRELLP-FSNNPTDDCSLSSAGKPC-FLAGDGRVNEQPGLTSMHTLF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 300 LREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQRFQ-YQNR----IAAE 374
Cdd:cd09823    87 LREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFGLYLLTSGYFNgYDPNvdpsILNE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 375 FNTLYHW--HPLLPDTFQIQDKEY------NYKQFMYNNSVML-EHGVSQMVESFSRQIAGRVagGRNVPLVVEKVAV-- 443
Cdd:cd09823   167 FAAAAFRfgHSLVPGTFERLDENYrpqgsvNLHDLFFNPDRLYeEGGLDPLLRGLATQPAQKV--DRFFTDELTTHFFfr 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 444 ---------ASIEQSRqMRYH---SMNEYRKRFQLKPFSSFQDLTGE--EEMATELEKLYGDIDAMELYPGLLVEKPRPG 509
Cdd:cd09823   245 ggnpfgldlAALNIQR-GRDHglpGYNDYREFCGLPRATTFDDLLGImsPETIQKLRRLYKSVDDIDLYVGGLSEKPVPG 323

                  ....*..
gi 1717019538 510 AIFGETM 516
Cdd:cd09823   324 GLVGPTF 330
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
101-508 2.10e-38

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: 149.02  E-value: 2.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 101 FLRDTIMRYVLTSRSHLIDSPP-TYNSD-YAYKSWE-AYSNLSY---------YTRTLPPvgHDCPTPMgvkgkkeLPDA 168
Cdd:cd09817     2 KLRDKLTGGLVDTLWDDLPHPPdSYLGDnYKYRKADgSNNNILNprlgaagspYARSVPP--KHDQPGV-------LPDP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 169 KVIVEKFLLRRKFIPDPQGTNIMFAFFAQHFTHQFFKTDTKKgaaFTKGLGHG-VDLSHVYGETLDRQHKLRLFKDGKLK 247
Cdd:cd09817    73 GLIFDTLLARDTGKFHPNGISSMLFYLATIIIHDIFRTDHRD---MNINNTSSyLDLSPLYGSNQEEQNKVRTMKDGKLK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 248 yqmidgemyPPTVQDTQVemiypphipqhLKFAVGQEVFglvpgLMMYAtiwlREHNRVCDVL----------------- 310
Cdd:cd09817   150 ---------PDTFSDKRL-----------LGQPPGVCAL-----LVMFN----RFHNYVVEQLaqineggrftppgdkld 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 311 KNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYH-----FKL----KFDPELLFNQRFQYqNRIAAEFNTLYHW 381
Cdd:cd09817   201 SSAKEEKLDEDLFQTARLITCGLYINIVLHDYVRAILNLNrtdstWTLdprvEIGRSLTGVPRGTG-NQVSVEFNLLYRW 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 382 HP------------LLPDTFQIQD-KEYNYKQFMynNSVMLEHGVSQMVES------FSRQIAGR--------------- 427
Cdd:cd09817   280 HSaisardekwtedLFESLFGGKSpDEVTLKEFM--QALGRFEALIPKDPSqrtfggLKRGPDGRfrdedlvrilkdsie 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 428 -VA---GGRNVPLVVEKVAVASIEQSRQMRYHSMNEYRKRFQLKPFSSFQDLTGEEEMATELEKLYGDIDAMELYPGLLV 503
Cdd:cd09817   358 dPAgafGARNVPASLKVIEILGILQAREWNVATLNEFRKFFGLKPYETFEDINSDPEVAEALELLYGHPDNVELYPGLVA 437

                  ....*
gi 1717019538 504 EKPRP 508
Cdd:cd09817   438 EDAKP 442
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
165-515 3.63e-38

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: 147.43  E-value: 3.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 165 LPDAKVIVEKFLLRRKFIPDPQgTNIMFAFFAQHFTHQFFKTDTKkgaAFTKGLGHGVDLSHVYGETLDRQHKLRLF-KD 243
Cdd:cd09818    41 TPNPRVISRRLLARTEFKPATS-LNLLAAAWIQFMVHDWFSHGPP---TYINTNTHWWDGSQIYGSTEEAQKRLRTFpPD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 244 GKLKyqmIDGEMYPPTVQDTqvemiypphipqhlkfavGQEVFGLVP----GLMMYATIWLREHNRVCDVLKNEHPEWDD 319
Cdd:cd09818   117 GKLK---LDADGLLPVDEHT------------------GLPLTGFNDnwwvGLSLLHTLFVREHNAICDALRKEYPDWSD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 320 ERIFQTTRLILTGETIKI-VIE-----------DYVQH-----LSGYHFKLKF---------------------DPELLf 361
Cdd:cd09818   176 EQLFDKARLVNAALMAKIhTVEwtpailahptlEIAMRanwwgLLGERLKRVLgrdgtsellsgipgsppnhhgVPYSL- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 362 nqrfqyqnriAAEFNTLYHWHPLLPDTFQIQD-------KEYNYKQFMYN--NSVMLEHGVSQMVESFSRQIAGRV---- 428
Cdd:cd09818   255 ----------TEEFVAVYRMHPLIPDDIDFRSaddgatgEEISLTDLAGGkaRELLRKLGFADLLYSFGITHPGALtlhn 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 429 ----------AGGRNVPLvvekvAVASIEQSRQM---RYhsmNEYRKRFQLKPFSSFQDLTGEEEMATELEKLYG-DIDA 494
Cdd:cd09818   325 yprflrdlhrPDGRVIDL-----AAIDILRDRERgvpRY---NEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGgDVEK 396
                         410       420
                  ....*....|....*....|.
gi 1717019538 495 MELYPGLLVEKPRPGAIFGET 515
Cdd:cd09818   397 VDLLVGLLAEPLPPGFGFSDT 417
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
222-516 1.74e-35

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: 138.60  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 222 VDLSHVYGETLDRQHKLRLFKDGKLKYQMIDGEMYPPtVQDTQVEMIYPPHIPQHLkFAVGQEVFGLVPGLMMYATIWLR 301
Cdd:cd09822    58 IDGSNVYGSDEERADALRSFGGGKLKTSVANAGDLLP-FNEAGLPNDNGGVPADDL-FLAGDVRANENPGLTALHTLFVR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 302 EHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHfklKFDPELLFNQRFqyQNRIAAEFNTL-YH 380
Cdd:cd09822   136 EHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLGEN---ALPAYSGYDETV--NPGISNEFSTAaYR 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 381 W-HPLLPDTFQIQDKEYNYKQ-----FMYNNSVMLEHGvsqMVESFSRQIAGRVAggRNV-PLVVEKV------------ 441
Cdd:cd09822   211 FgHSMLSSELLRGDEDGTEATslalrDAFFNPDELEEN---GIDPLLRGLASQVA--QEIdTFIVDDVrnflfgppgagg 285
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717019538 442 ---AVASIEQSRQMRYHSMNEYRKRFQLKPFSSFQDLTGEEEMATELEKLYGDIDAMELYPGLLVEKPRPGAIFGETM 516
Cdd:cd09822   286 fdlAALNIQRGRDHGLPSYNQLREALGLPAVTSFSDITSDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETF 363
PLN02283 PLN02283
alpha-dioxygenase
134-515 5.78e-26

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 112.93  E-value: 5.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 134 EAYSNLSYYTRTLPPVghdcptpmgvKGKKEL--PDAKVIVEKFLLRRKFIPDPQGTNIMFAFFAQHFTH---------- 201
Cdd:PLN02283   99 GAGSQGTFFGRNMPPV----------DQKDKLldPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHdwidhledtq 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 202 -------------------QFFKTDTKKGAAFTKGLGH------GVDLSHVYGETLDRQHKLRLFKDGKLKyqmIDGEMY 256
Cdd:PLN02283  169 qieltapkevasqcplksfKFYKTKEVPTGSPDIKTGSlnirtpWWDGSVIYGSNEKGLRRVRTFKDGKLK---ISEDGL 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 257 PPTVQDTqvemiypphipqhlkFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIK 336
Cdd:PLN02283  246 LLHDEDG---------------IPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAK 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 337 IVIEDYVQHLsgyhfkLKFDPEL---------LFNQRFQ--------------------------YQnrIAAEFNTLYHW 381
Cdd:PLN02283  311 IHTIDWTVEL------LKTDTLLagmranwygLLGKKFKdtfghiggpilsglvglkkpnnhgvpYS--LTEEFTSVYRM 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 382 HPLLPDTFQIQD--------------KEYNYKQFMYN--NSVMLEHGVSQMVESFSRQIAGRVA---------------- 429
Cdd:PLN02283  383 HSLLPDHLILRDitaapgenksppliEEIPMPELIGLkgEKKLSKIGFEKLMVSMGHQACGALElwnypswmrdlvpqdi 462
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 430 GGRNVPlvvEKVAVASIEQSRQ-----MRYhsmNEYRKRFQLKPFSSFQDLTGEEEMATELEKLYG-DIDAMELYPGLLV 503
Cdd:PLN02283  463 DGEDRP---DHVDMAALEIYRDrergvARY---NEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGdDVEKLDLLVGLMA 536
                         490
                  ....*....|..
gi 1717019538 504 EKPRPGAIFGET 515
Cdd:PLN02283  537 EKKIKGFAISET 548
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
223-514 9.95e-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: 80.42  E-value: 9.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 223 DLSHVYGETLDRQHKLRLFKDGKLKYqmiDGEMYPPTVQDTQVEMIYPPhIPQHLKFAVGQEVFGL-------VPGLMMY 295
Cdd:cd09820   142 DGSSIYGSSKAWSDALRSFSGGRLAS---GDDGGFPRRNTNRLPLANPP-PPSYHGTRGPERLFKLgnprgneNPFLLTF 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 296 ATIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHL--------SGYHfklKF-DPELlfNQRFQ 366
Cdd:cd09820   218 GILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALlgtnvppyTGYK---PHvDPGI--SHEFQ 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 367 yqnriAAEFNTLyhwHPLLPDTFQIQDKEYNYKQFMYN----------------NSVMLEHGVSQMVESFSRQIAgrvag 430
Cdd:cd09820   293 -----AAAFRFG---HTLVPPGVYRRNRQCNFREVLTTsggspalrlcntywnsQEPLLKSDIDELLLGMASQIA----- 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 431 GRNVPLVVEKVA--------------VA-SIEQSRQMRYHSMNEYRKRFQLKPFSSFQDLTGE-----EEMATELEKLYG 490
Cdd:cd09820   360 EREDNIIVEDLRdylfgplefsrrdlMAlNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPDlfkkdPELLERLAELYG 439
                         330       340
                  ....*....|....*....|....*..
gi 1717019538 491 -DIDAMELYPGLLVE--KPRPGAIFGE 514
Cdd:cd09820   440 nDLSKLDLYVGGMLEskGGGPGELFRA 466
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
222-515 3.02e-14

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: 75.03  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 222 VDLSHVYGETLDRQHKLR-LFKD-GKLKYQMID--GEMYPPTVQDTQVEMIYPPH---IPQHLKFAV-GQEVFGLvpgLM 293
Cdd:cd09826    47 IDASNVYGSSDEEALELRdLASDrGLLRVGIVSeaGKPLLPFERDSPMDCRRDPNespIPCFLAGDHrANEQLGL---TS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 294 MYaTIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILtGETI----------KIVIEDYVQHLSGYHfklKFDPEL---L 360
Cdd:cd09826   124 MH-TLWLREHNRIASELLELNPHWDGETIYHETRKIV-GAQMqhityshwlpKILGPVGMEMLGEYR---GYNPNVnpsI 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 361 FNQ------RFQYQ------NRIAAEFNTLYHWH--------------------PLLPDTFQIQDKEYNYKQFMynNSVM 408
Cdd:cd09826   199 ANEfataafRFGHTlinpilFRLDEDFQPIPEGHlplhkaffapyrlvneggidPLLRGLFATAAKDRVPDQLL--NTEL 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 409 LEHgvsqmveSFSRqiAGRVAggrnvplvvEKVAVASIEQSRQMRYHSMNEYRKRFQLKPFSSFQDLTGE---EEMATEL 485
Cdd:cd09826   277 TEK-------LFEM--AHEVA---------LDLAALNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNEiknDDVREKL 338
                         330       340       350
                  ....*....|....*....|....*....|
gi 1717019538 486 EKLYGDIDAMELYPGLLVEKPRPGAIFGET 515
Cdd:cd09826   339 KRLYGHPGNIDLFVGGILEDLLPGARVGPT 368
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
222-343 5.44e-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: 62.07  E-value: 5.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 222 VDLSHVYGETLDRQHKLRLF--KDGKLKYQM---IDGEMYPPTVQDTQVEMIYPPHIPQHLK-FAVGQEVFGLVPGLMMY 295
Cdd:cd09825   158 IDASTVYGSTLALARSLRDLssDDGLLRVNSkfdDSGRDYLPFQPEEVSSCNPDPNGGERVPcFLAGDGRASEVLTLTAS 237
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1717019538 296 ATIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIKIVIEDYV 343
Cdd:cd09825   238 HTLWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYI 285
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
290-397 1.31e-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: 50.88  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 290 PGLMMYATIWLREHNRVCDVLKNEHPEWDDERIFQTTRLILTGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQrfQYQN 369
Cdd:cd09824    95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARLPPYRGYNE--SVDP 172
                          90       100
                  ....*....|....*....|....*....
gi 1717019538 370 RIAAEFNTLYHW-HPLLPDTFQIQDKEYN 397
Cdd:cd09824   173 RIANVFTTAFRRgHTTVQPFVFRLDENYQ 201
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
27-62 7.80e-06

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: 43.01  E-value: 7.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1717019538  27 NPCCS-NPCQNQGVCM-TVGfdKYKCDCtRTGFYGDTC 62
Cdd:cd00054     3 DECASgNPCQNGGTCVnTVG--SYRCSC-PPGYTGRNC 37
An_peroxidase_bacterial_2 cd09821
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
291-474 2.37e-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: 43.94  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 291 GLMMYATIWLREHNRVCDVLK--------------NEHP--EWDDERIFQTTRLILTGETIKIVIEDYVQHLSGyhfklK 354
Cdd:cd09821   190 GLTAVHTVFHREHNRLVDQIKdtllqsadlafaneAGGNnlAWDGERLFQAARFANEMQYQHLVFEEFARRIQP-----G 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717019538 355 FDPELLFNQRFQYQN-RIAAEF-NTLYHW-HPLLPDTFQIQDKEYNYK-------------QFMYNNSVML-EHGVSQMV 417
Cdd:cd09821   265 IDGFGSFNGYNPEINpSISAEFaHAVYRFgHSMLTETVTRIGPDADEGldnqvglidaflnPVAFLPATLYaEEGAGAIL 344
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717019538 418 ESFSRQIAGRV-----AGGRN----VPLvveKVAVASIEQSRQMRYHSMNEYRKRFQ--------LKPFSSFQD 474
Cdd:cd09821   345 RGMTRQVGNEIdefvtDALRNnlvgLPL---DLAALNIARGRDTGLPTLNEARAQLFaatgdtilKAPYESWND 415
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
31-62 1.72e-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: 36.30  E-value: 1.72e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1717019538  31 SNPCQNQGVCmTVGFDKYKCDCtRTGFYGD-TC 62
Cdd:cd00053     5 SNPCSNGGTC-VNTPGSYRCVC-PPGYTGDrSC 35
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
34-62 3.93e-03

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


Pssm-ID: 400365  Cd Length: 26  Bit Score: 35.02  E-value: 3.93e-03
                          10        20
                  ....*....|....*....|....*....
gi 1717019538  34 CQNQGVCMTVGFdkyKCDCtRTGFYGDTC 62
Cdd:pfam07974   2 CSGRGTCVNQCG---KCVC-DSGYQGATC 26
 
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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