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Conserved domains on  [gi|15219521|ref|NP_177509|]
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alpha dioxygenase [Arabidopsis thaliana]

Protein Classification

peroxidase family protein( domain architecture ID 10010754)

peroxidase family protein similar to Danio rerio eosinophil peroxidase isoform 2 precursor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02283 PLN02283
alpha-dioxygenase
1-631 0e+00

alpha-dioxygenase


:

Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 1284.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521    1 MGFSPSSSWFLHPQLHHVVSKMSYFDAFLFYIVHLVDKLGLWHRFPVLLGVAYLGLRRHLHQRYNLVHVGPI-NGQGYDT 79
Cdd:PLN02283   1 MLFSASLSWFIHPDLHEVVSKMSLFDRFLFLIVHFVDKLGLWHRLPVFLGLAYLALRRHLHQRYNLLNVGQTpNGQRYDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   80 DEFCYRTADGKCNHPSDNTIGSQGSFIGRNMPPSTSQYGILDPHPSVVATKLLARKRFIDNGDQFNVIACSWIQFMIHDW 159
Cdd:PLN02283  81 AEYPYRTADGKCNDPFNEGAGSQGTFFGRNMPPVDQKDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHDW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  160 VDHLEDTHQIELEAPEEVASGCPLKSFKFLRTKKVPTDDHH-KSGAVNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKI 238
Cdd:PLN02283 161 IDHLEDTQQIELTAPKEVASQCPLKSFKFYKTKEVPTGSPDiKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  239 SGDGLLERDERGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIEL 318
Cdd:PLN02283 241 SEDGLLLHDEDGIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  319 LKTDTLTAGMRINWYGFFGKKVKDMVGARFGPLFSGLVGLKKPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMNSENV 398
Cdd:PLN02283 321 LKTDTLLAGMRANWYGLLGKKFKDTFGHIGGPILSGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLLPDHLILRDITAAPG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  399 DKENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDIDGEDRPHLIDMAALEIYR 478
Cdd:PLN02283 401 ENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVSMGHQACGALELWNYPSWMRDLVPQDIDGEDRPDHVDMAALEIYR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  479 DRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRR 558
Cdd:PLN02283 481 DRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRR 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219521  559 LEADRFFTTNFNEKTYTKEGLEWVNTTETLKDVIDRHFPRLTDQWMRCSSAFSVWGSDPNPKNWVPLYLRSAP 631
Cdd:PLN02283 561 LEADRFFTSNFNEKTYTKKGLEWVNTTESLKDVIDRHYPEMTDKWMNSSSAFSVWDSPPNPHNWIPLYLRPPP 633
 
Name Accession Description Interval E-value
PLN02283 PLN02283
alpha-dioxygenase
1-631 0e+00

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 1284.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521    1 MGFSPSSSWFLHPQLHHVVSKMSYFDAFLFYIVHLVDKLGLWHRFPVLLGVAYLGLRRHLHQRYNLVHVGPI-NGQGYDT 79
Cdd:PLN02283   1 MLFSASLSWFIHPDLHEVVSKMSLFDRFLFLIVHFVDKLGLWHRLPVFLGLAYLALRRHLHQRYNLLNVGQTpNGQRYDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   80 DEFCYRTADGKCNHPSDNTIGSQGSFIGRNMPPSTSQYGILDPHPSVVATKLLARKRFIDNGDQFNVIACSWIQFMIHDW 159
Cdd:PLN02283  81 AEYPYRTADGKCNDPFNEGAGSQGTFFGRNMPPVDQKDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHDW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  160 VDHLEDTHQIELEAPEEVASGCPLKSFKFLRTKKVPTDDHH-KSGAVNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKI 238
Cdd:PLN02283 161 IDHLEDTQQIELTAPKEVASQCPLKSFKFYKTKEVPTGSPDiKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  239 SGDGLLERDERGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIEL 318
Cdd:PLN02283 241 SEDGLLLHDEDGIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  319 LKTDTLTAGMRINWYGFFGKKVKDMVGARFGPLFSGLVGLKKPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMNSENV 398
Cdd:PLN02283 321 LKTDTLLAGMRANWYGLLGKKFKDTFGHIGGPILSGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLLPDHLILRDITAAPG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  399 DKENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDIDGEDRPHLIDMAALEIYR 478
Cdd:PLN02283 401 ENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVSMGHQACGALELWNYPSWMRDLVPQDIDGEDRPDHVDMAALEIYR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  479 DRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRR 558
Cdd:PLN02283 481 DRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRR 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219521  559 LEADRFFTTNFNEKTYTKEGLEWVNTTETLKDVIDRHFPRLTDQWMRCSSAFSVWGSDPNPKNWVPLYLRSAP 631
Cdd:PLN02283 561 LEADRFFTSNFNEKTYTKKGLEWVNTTESLKDVIDRHYPEMTDKWMNSSSAFSVWDSPPNPHNWIPLYLRPPP 633
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
85-613 0e+00

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: 661.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  85 RTADGKCNHPSDNTIGSQGSFIGRNMPPST----SQYGILDPHPSVVATKLLARKRFIdNGDQFNVIACSWIQFMIHDWV 160
Cdd:cd09818   1 RTADGSYNDLDNPSMGSVGTRFGRNVPLDAtfpeDKDELLTPNPRVISRRLLARTEFK-PATSLNLLAAAWIQFMVHDWF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 161 DHLEDTHqieleapeevasgcplksfkflrtkkvptddhhksgaVNTRTPWWDGSVIYGNDETGMRRVRVF-KDGKLKIS 239
Cdd:cd09818  80 SHGPPTY-------------------------------------INTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLKLD 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 240 GDGLLERDE-RGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIEL 318
Cdd:cd09818 123 ADGLLPVDEhTGLPLTGFNDNWWVGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAI 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 319 LKTDTLTAGMRINWYGFFGKKVKDMVGARFG-PLFSGLVGLKkPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMnsen 397
Cdd:cd09818 203 LAHPTLEIAMRANWWGLLGERLKRVLGRDGTsELLSGIPGSP-PNHHGVPYSLTEEFVAVYRMHPLIPDDIDFRSA---- 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 398 vdkENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDidgedrPHLIDMAALEIY 477
Cdd:cd09818 278 ---DDGATGEEISLTDLAGGKARELLRKLGFADLLYSFGITHPGALTLHNYPRFLRDLHRPD------GRVIDLAAIDIL 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 478 RDRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASR 557
Cdd:cd09818 349 RDRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGGDVEKVDLLVGLLAEPLPPGFGFSDTAFRIFILMASR 428
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15219521 558 RLEADRFFTTNFNEKTYTKEGLEWVNTTeTLKDVIDRHFPRLTDqWMR-CSSAFSVW 613
Cdd:cd09818 429 RLKSDRFFTNDFRPEVYTPEGMDWVNNN-TMKSVLLRHFPELAP-ALRgVENAFAPW 483
An_peroxidase pfam03098
Animal haem peroxidase;
84-601 3.11e-127

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 385.37  E-value: 3.11e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521    84 YRTADGKCNHPSDNTIGSQGSFIGRNMP---------PSTSQYGILDPHPSVVATKLLARKRFIDNgDQFNVIACSWIQF 154
Cdd:pfam03098   1 YRTIDGSCNNLKNPSWGAAGTPFARLLPpayedgvsaPRGSSSGSPLPSPRLVSNKLFAGDSGIPD-PNLTLLLMQWGQF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   155 MIHDWVDHLEDTHQIE-----LEAPEEVASGC-PLKsfkflrtkkVPTDDHHKSGA----------------------VN 206
Cdd:pfam03098  80 IDHDLTLTPESTSPNGsscdcCCPPENLHPPCfPIP---------IPPDDPFFSPFgvrcmpfvrsapgcglgnpreqIN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   207 TRTPWWDGSVIYGNDETGMRRVRVFKDGKLKIS----GDGLLERDERGVP-----------ISGDIR-NSWSGFSLLQAL 270
Cdd:pfam03098 151 QVTSFLDGSQVYGSSEETARSLRSFSGGLLKVNrsddGKELLPFDPDGPCccnssggvpcfLAGDSRaNENPGLTALHTL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   271 FVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTdtltagMRINWYGFFGKKVKDMvgarfgp 350
Cdd:pfam03098 231 FLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGE------DNMNWFGLLPLPYNGY------- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   351 lfsglvglkkpnDHGVPYSLTEEFVS-VYRM-HCLLPETLILRdmnsenvDKENPAIEREIPMTELIGKKAgeKASKLGF 428
Cdd:pfam03098 298 ------------DPNVDPSISNEFATaAFRFgHSLIPPFLYRL-------DENNVPEEPSLRLHDSFFNPD--RLYEGGI 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   429 EQLLVSMGHQSCGALtLWNYPNWMRNLVAQDidgEDRPHLIDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWEELTD- 507
Cdd:pfam03098 357 DPLLRGLATQPAQAV-DNNFTEELTNHLFGP---PGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDv 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   508 -DEEAIKVLREVYeDDIEKLDLNVGLHAEKKIKGfAISETAFFIFLLVASRRLE-ADRFFTTNFNEKTYTKEGLEWVNTT 585
Cdd:pfam03098 433 iPNEVIAKLRELY-GSVDDIDLWVGGLAEKPLPG-GLVGPTFACIIGDQFRRLRdGDRFWYENGNQGSFTPEQLEEIRKT 510
                         570
                  ....*....|....*.
gi 15219521   586 eTLKDVIDRHFPRLTD 601
Cdd:pfam03098 511 -SLARVICDNTDIIET 525
 
Name Accession Description Interval E-value
PLN02283 PLN02283
alpha-dioxygenase
1-631 0e+00

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 1284.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521    1 MGFSPSSSWFLHPQLHHVVSKMSYFDAFLFYIVHLVDKLGLWHRFPVLLGVAYLGLRRHLHQRYNLVHVGPI-NGQGYDT 79
Cdd:PLN02283   1 MLFSASLSWFIHPDLHEVVSKMSLFDRFLFLIVHFVDKLGLWHRLPVFLGLAYLALRRHLHQRYNLLNVGQTpNGQRYDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   80 DEFCYRTADGKCNHPSDNTIGSQGSFIGRNMPPSTSQYGILDPHPSVVATKLLARKRFIDNGDQFNVIACSWIQFMIHDW 159
Cdd:PLN02283  81 AEYPYRTADGKCNDPFNEGAGSQGTFFGRNMPPVDQKDKLLDPHPSVVATKLLARKKFIDTGKQFNMIAASWIQFMIHDW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  160 VDHLEDTHQIELEAPEEVASGCPLKSFKFLRTKKVPTDDHH-KSGAVNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKI 238
Cdd:PLN02283 161 IDHLEDTQQIELTAPKEVASQCPLKSFKFYKTKEVPTGSPDiKTGSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  239 SGDGLLERDERGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIEL 318
Cdd:PLN02283 241 SEDGLLLHDEDGIPISGDVRNSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVEL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  319 LKTDTLTAGMRINWYGFFGKKVKDMVGARFGPLFSGLVGLKKPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMNSENV 398
Cdd:PLN02283 321 LKTDTLLAGMRANWYGLLGKKFKDTFGHIGGPILSGLVGLKKPNNHGVPYSLTEEFTSVYRMHSLLPDHLILRDITAAPG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  399 DKENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDIDGEDRPHLIDMAALEIYR 478
Cdd:PLN02283 401 ENKSPPLIEEIPMPELIGLKGEKKLSKIGFEKLMVSMGHQACGALELWNYPSWMRDLVPQDIDGEDRPDHVDMAALEIYR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  479 DRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRR 558
Cdd:PLN02283 481 DRERGVARYNEFRRNLLMIPISKWEDLTDDEEAIEVLREVYGDDVEKLDLLVGLMAEKKIKGFAISETAFFIFLLMASRR 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219521  559 LEADRFFTTNFNEKTYTKEGLEWVNTTETLKDVIDRHFPRLTDQWMRCSSAFSVWGSDPNPKNWVPLYLRSAP 631
Cdd:PLN02283 561 LEADRFFTSNFNEKTYTKKGLEWVNTTESLKDVIDRHYPEMTDKWMNSSSAFSVWDSPPNPHNWIPLYLRPPP 633
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
85-613 0e+00

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: 661.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  85 RTADGKCNHPSDNTIGSQGSFIGRNMPPST----SQYGILDPHPSVVATKLLARKRFIdNGDQFNVIACSWIQFMIHDWV 160
Cdd:cd09818   1 RTADGSYNDLDNPSMGSVGTRFGRNVPLDAtfpeDKDELLTPNPRVISRRLLARTEFK-PATSLNLLAAAWIQFMVHDWF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 161 DHLEDTHqieleapeevasgcplksfkflrtkkvptddhhksgaVNTRTPWWDGSVIYGNDETGMRRVRVF-KDGKLKIS 239
Cdd:cd09818  80 SHGPPTY-------------------------------------INTNTHWWDGSQIYGSTEEAQKRLRTFpPDGKLKLD 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 240 GDGLLERDE-RGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIEL 318
Cdd:cd09818 123 ADGLLPVDEhTGLPLTGFNDNWWVGLSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPAI 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 319 LKTDTLTAGMRINWYGFFGKKVKDMVGARFG-PLFSGLVGLKkPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMnsen 397
Cdd:cd09818 203 LAHPTLEIAMRANWWGLLGERLKRVLGRDGTsELLSGIPGSP-PNHHGVPYSLTEEFVAVYRMHPLIPDDIDFRSA---- 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 398 vdkENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDidgedrPHLIDMAALEIY 477
Cdd:cd09818 278 ---DDGATGEEISLTDLAGGKARELLRKLGFADLLYSFGITHPGALTLHNYPRFLRDLHRPD------GRVIDLAAIDIL 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 478 RDRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASR 557
Cdd:cd09818 349 RDRERGVPRYNEFRRLLHLPPAKSFEDLTGDEEVAAELREVYGGDVEKVDLLVGLLAEPLPPGFGFSDTAFRIFILMASR 428
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15219521 558 RLEADRFFTTNFNEKTYTKEGLEWVNTTeTLKDVIDRHFPRLTDqWMR-CSSAFSVW 613
Cdd:cd09818 429 RLKSDRFFTNDFRPEVYTPEGMDWVNNN-TMKSVLLRHFPELAP-ALRgVENAFAPW 483
An_peroxidase pfam03098
Animal haem peroxidase;
84-601 3.11e-127

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 385.37  E-value: 3.11e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521    84 YRTADGKCNHPSDNTIGSQGSFIGRNMP---------PSTSQYGILDPHPSVVATKLLARKRFIDNgDQFNVIACSWIQF 154
Cdd:pfam03098   1 YRTIDGSCNNLKNPSWGAAGTPFARLLPpayedgvsaPRGSSSGSPLPSPRLVSNKLFAGDSGIPD-PNLTLLLMQWGQF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   155 MIHDWVDHLEDTHQIE-----LEAPEEVASGC-PLKsfkflrtkkVPTDDHHKSGA----------------------VN 206
Cdd:pfam03098  80 IDHDLTLTPESTSPNGsscdcCCPPENLHPPCfPIP---------IPPDDPFFSPFgvrcmpfvrsapgcglgnpreqIN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   207 TRTPWWDGSVIYGNDETGMRRVRVFKDGKLKIS----GDGLLERDERGVP-----------ISGDIR-NSWSGFSLLQAL 270
Cdd:pfam03098 151 QVTSFLDGSQVYGSSEETARSLRSFSGGLLKVNrsddGKELLPFDPDGPCccnssggvpcfLAGDSRaNENPGLTALHTL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   271 FVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTdtltagMRINWYGFFGKKVKDMvgarfgp 350
Cdd:pfam03098 231 FLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGE------DNMNWFGLLPLPYNGY------- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   351 lfsglvglkkpnDHGVPYSLTEEFVS-VYRM-HCLLPETLILRdmnsenvDKENPAIEREIPMTELIGKKAgeKASKLGF 428
Cdd:pfam03098 298 ------------DPNVDPSISNEFATaAFRFgHSLIPPFLYRL-------DENNVPEEPSLRLHDSFFNPD--RLYEGGI 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   429 EQLLVSMGHQSCGALtLWNYPNWMRNLVAQDidgEDRPHLIDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWEELTD- 507
Cdd:pfam03098 357 DPLLRGLATQPAQAV-DNNFTEELTNHLFGP---PGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDv 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521   508 -DEEAIKVLREVYeDDIEKLDLNVGLHAEKKIKGfAISETAFFIFLLVASRRLE-ADRFFTTNFNEKTYTKEGLEWVNTT 585
Cdd:pfam03098 433 iPNEVIAKLRELY-GSVDDIDLWVGGLAEKPLPG-GLVGPTFACIIGDQFRRLRdGDRFWYENGNQGSFTPEQLEEIRKT 510
                         570
                  ....*....|....*.
gi 15219521   586 eTLKDVIDRHFPRLTD 601
Cdd:pfam03098 511 -SLARVICDNTDIIET 525
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
205-595 1.63e-84

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: 269.30  E-value: 1.63e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 205 VNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKISGDGLLERDERGVPIS-------------------GDIR-NSWSGF 264
Cdd:cd05396   2 LNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYGTELLPFNnpnpsmgtiglpptrcfiaGDPRvNENLLL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 265 SLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTDTLTAGMRINWYGFFGKkvkdmv 344
Cdd:cd05396  82 LAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLLFPDPDV------ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 345 garfgplfsglvglkkpndhgVPYSLTEEFVSVYRM-HCLLPETLILRDMNseNVDKENPaierEIPMTELIGKKAGEKA 423
Cdd:cd05396 156 ---------------------VPYVLSEFFTAAYRFgHSLVPEGVDRIDEN--GQPKEIP----DVPLKDFFFNTSRSIL 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 424 SKLGFEQLLVSMGHQSCGALTLWNYPnwmrnlvAQDIDGEDRPHLIDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWE 503
Cdd:cd05396 209 SDTGLDPLLRGFLRQPAGLIDQNVDD-------VMFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQ 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 504 ELTDDEEAIKVLREVYeDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRRLEADRFFTTNFNEktYTKEGLEWVN 583
Cdd:cd05396 282 DILTDPELAKKLAELY-GDPDDVDLWVGGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNP--FGKSGKEELE 358
                       410
                ....*....|..
gi 15219521 584 TTETLKDVIDRH 595
Cdd:cd05396 359 KLISLADIICLN 370
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
104-597 1.03e-34

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: 137.78  E-value: 1.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 104 SFIGRNMPPSTSQYGILDPHPSVVATKLLARKRFIDNGDQFNVIACSWIQfmihdwvdHLedTHQieleapeevasgcpl 183
Cdd:cd09816  59 TYYGRHLPPVPRDCPTELPDVEELAELFLRRREFIPDPQKTTLLFPFFAQ--------WF--TDQ--------------- 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 184 ksfkFLRTkkvptddHHKSGAVNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLK---ISGD---GLLERD-------ERG 250
Cdd:cd09816 114 ----FLRT-------DPGDPRRNTSNHGIDLSQIYGLTEARTHALRLFKDGKLKsqmINGEeypPYLFEDggvkmefPPL 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 251 VPISGDIR----------------NSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVtaaVIakVHTIDW 314
Cdd:cd09816 183 VPPLGDELtpereaklfavgherfNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNI---LI--GELIKI 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 315 TIEllktDTLTagmRINWYGFfgkKVKDMVGARFGPLFSglvglkKPNDhgvpysLTEEFVSVYRMHCLLPETLILRDmn 394
Cdd:cd09816 258 VIE----DYIN---HLSPYHF---KLFFDPELAFNEPWQ------RQNR------IALEFNLLYRWHPLVPDTFNIGG-- 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 395 senvdkenpaieREIPM------TELIGKKagekasklGFEQLLVSMGHQSCGALTLWNYPnwmrnlvaqdidgedrPHL 468
Cdd:cd09816 314 ------------QRYPLsdflfnNDLVVDH--------GLGALVDAASRQPAGRIGLRNTP----------------PFL 357
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 469 IDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYeDDIEKLDLNVGLHAEKKIKGFAISETaf 548
Cdd:cd09816 358 LPVEVRSIEQGRKLRLASFNDYRKRFGLPPYTSFEELTGDPEVAAELEELY-GDVDAVEFYVGLFAEDPRPNSPLPPL-- 434
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219521 549 fIFLLVASrrlEADRFFTTN-------FNEKTYTKEGLEWVNTTETLKDVIDRHFP 597
Cdd:cd09816 435 -MVEMVAP---DAFSGALTNpllspevWKPSTFGGEGGFDIVKTATLQDLVCRNVK 486
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
205-594 6.24e-34

Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.


Pssm-ID: 188654 [Multi-domain]  Cd Length: 420  Bit Score: 134.36  E-value: 6.24e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 205 VNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKIS---GDGLLERDERGVP------------ISGDIR-NSWSGFSLLQ 268
Cdd:cd09822  51 INAITAYIDGSNVYGSDEERADALRSFGGGKLKTSvanAGDLLPFNEAGLPndnggvpaddlfLAGDVRaNENPGLTALH 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 269 ALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVtaaVIAKVHTIDWTiELLKTdtltagmrinwygffgkkvkdMVGARF 348
Cdd:cd09822 131 TLFVREHNRLADELARRNPSLSDEEIYQAARAI---VIAEIQAITYN-EFLPA---------------------LLGENA 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 349 GPLFSGLvglkkpnDHGVPYSLTEEFVSV-YRM-HCLLPETLILRDmnsenvdkENPAIEREIPMteligKKAGEKASKL 426
Cdd:cd09822 186 LPAYSGY-------DETVNPGISNEFSTAaYRFgHSMLSSELLRGD--------EDGTEATSLAL-----RDAFFNPDEL 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 427 ---GFEQLLVSMGHQSCGALTLWnYPNWMRNLVAqdidGEDRPHLIDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWE 503
Cdd:cd09822 246 eenGIDPLLRGLASQVAQEIDTF-IVDDVRNFLF----GPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAVTSFS 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 504 ELTDDEEAIKVLREVYeDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRRLEADRFFTTNFNEktyTKEGLEWVN 583
Cdd:cd09822 321 DITSDPDLAARLASVY-GDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYENDDL---LLDEIADIE 396
                       410
                ....*....|.
gi 15219521 584 TTeTLKDVIDR 594
Cdd:cd09822 397 NT-TLADVIRR 406
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
205-571 1.76e-27

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: 114.59  E-value: 1.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 205 VNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLK---ISGDGLL----------ERDERGVP--ISGDIRNSWS-GFSLLQ 268
Cdd:cd09823   4 LNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKtqrRNGRELLpfsnnptddcSLSSAGKPcfLAGDGRVNEQpGLTSMH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 269 ALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKvhtidwtiellktdtltagmrINWYGF----FGKKVKDMV 344
Cdd:cd09823  84 TLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQH---------------------ITYNEFlpilLGRELMEKF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 345 garfgplfsGLVGLKKPNDHG----VPYSLTEEF-VSVYRM-HCLLPETLILRDmnsenvdkENPAIEREIPMTELIgkk 418
Cdd:cd09823 143 ---------GLYLLTSGYFNGydpnVDPSILNEFaAAAFRFgHSLVPGTFERLD--------ENYRPQGSVNLHDLF--- 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 419 agEKASKL----GFEQLLVSMGHQSCGALTLwNYPNWMRNLVAQDidgEDRPHLIDMAALEIYRDRERGVPRYNEFRKNL 494
Cdd:cd09823 203 --FNPDRLyeegGLDPLLRGLATQPAQKVDR-FFTDELTTHFFFR---GGNPFGLDLAALNIQRGRDHGLPGYNDYREFC 276
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 495 LMSPISKWEELTD--DEEAIKVLREVYE--DDIeklDLNVGLHAEKKIKGFAISETAFFI----FllvasRRL-EADRFF 565
Cdd:cd09823 277 GLPRATTFDDLLGimSPETIQKLRRLYKsvDDI---DLYVGGLSEKPVPGGLVGPTFACIigeqF-----RRLrRGDRFW 348

                ....*.
gi 15219521 566 TTNFNE 571
Cdd:cd09823 349 YENGGQ 354
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
205-592 8.22e-20

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: 93.13  E-value: 8.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 205 VNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKISGDGLLERDERG--------VPISGDIRNSWSGFSL---------- 266
Cdd:cd09820 134 LNEVTSWIDGSSIYGSSKAWSDALRSFSGGRLASGDDGGFPRRNTNrlplanppPPSYHGTRGPERLFKLgnprgnenpf 213
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 267 LQA---LFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTDtltagmRINWYGFfgkkvkdm 343
Cdd:cd09820 214 LLTfgiLWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN------VPPYTGY-------- 279
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 344 vgarfgplfsglvglkKPndhGVPYSLTEEFVS-VYRM-HCLLPETLILRDMNSENVDkenpaiereipmteligkkage 421
Cdd:cd09820 280 ----------------KP---HVDPGISHEFQAaAFRFgHTLVPPGVYRRNRQCNFRE---------------------- 318
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 422 kasklgfeqllVSMGHQSCGALTLWN-YpnWMRN--LVAQDIDG------------EDrpHLI----------------- 469
Cdd:cd09820 319 -----------VLTTSGGSPALRLCNtY--WNSQepLLKSDIDElllgmasqiaerED--NIIvedlrdylfgplefsrr 383
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 470 DMAALEIYRDRERGVPRYNEFRKNLLMSPISKWEELTD-----DEEAIKVLREVYEDDIEKLDLNVGLHAEKkiKGFAIS 544
Cdd:cd09820 384 DLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDINPdlfkkDPELLERLAELYGNDLSKLDLYVGGMLES--KGGGPG 461
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 15219521 545 ETAFFIFLLVASRRLEADRFFTTNFNEKTYTKEGLEWVNTTeTLKDVI 592
Cdd:cd09820 462 ELFRAIILDQFQRLRDGDRFWFENVKNGLFTAEEIEEIRNT-TLRDVI 508
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
71-599 3.36e-15

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: 78.92  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521  71 PINGQGYDTDEFCYRTADGKCNHPSDNTIGSQGSFIGRNMPPSTSQYGILdPHPSVVATKLLARKRFIDNGDQFNVIACS 150
Cdd:cd09817  20 PHPPDSYLGDNYKYRKADGSNNNILNPRLGAAGSPYARSVPPKHDQPGVL-PDPGLIFDTLLARDTGKFHPNGISSMLFY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 151 WIQFMIHDwvdhledthqieleapeevasgcplkSFKflrtkkvpTDdhHKSGAVNTRTPWWDGSVIYGNDETGMRRVRV 230
Cdd:cd09817  99 LATIIIHD--------------------------IFR--------TD--HRDMNINNTSSYLDLSPLYGSNQEEQNKVRT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 231 FKDGKLKisGDGLLERDERGVPisgdirnswSGFSLLQALFVKEHNSVCDML-----------------KERYPDFDDEK 293
Cdd:cd09817 143 MKDGKLK--PDTFSDKRLLGQP---------PGVCALLVMFNRFHNYVVEQLaqineggrftppgdkldSSAKEEKLDED 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 294 LYRTARLVTAAVIAKVHTIDW--TIELL-KTDTL-TAGMRINwygfFGKKVKDM-------VGARF-------------- 348
Cdd:cd09817 212 LFQTARLITCGLYINIVLHDYvrAILNLnRTDSTwTLDPRVE----IGRSLTGVprgtgnqVSVEFnllyrwhsaisard 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 349 ----GPLFSGLVGLKKPNDhgvpYSLTEEFVSVYRMHCLLPETLILRDMNsenvdkenpAIEREIpmtelIGKKAGEKAS 424
Cdd:cd09817 288 ekwtEDLFESLFGGKSPDE----VTLKEFMQALGRFEALIPKDPSQRTFG---------GLKRGP-----DGRFRDEDLV 349
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 425 KLgfeqlLVSMGHQSCGALTLWNYPNWMRNlvaqdidgedrphlIDMaaLEIYRDRERGVPRYNEFRKNLLMSPISKWEE 504
Cdd:cd09817 350 RI-----LKDSIEDPAGAFGARNVPASLKV--------------IEI--LGILQAREWNVATLNEFRKFFGLKPYETFED 408
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 505 LTDDEEAIKVLREVYeDDIEKLDLNVGLHAE--KKIK----GFAISETAFFIFLL--VASRRleADRFFTTNFNEKTYTK 576
Cdd:cd09817 409 INSDPEVAEALELLY-GHPDNVELYPGLVAEdaKPPMppgsGLCPGYTISRAILSdaVALVR--GDRFYTVDYNPNNLTN 485
                       570       580
                ....*....|....*....|....
gi 15219521 577 EGlewVNTTETLKDVIDR-HFPRL 599
Cdd:cd09817 486 WG---YAEVSPDPDVAFGgVFYKL 506
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
205-580 9.17e-15

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: 76.96  E-value: 9.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 205 VNTRTPWWDGSVIYGNDETGMRRVRVFKD--GKLKI-----SGDGLL----------ERDERGVPIS----GDIR-NSWS 262
Cdd:cd09826  40 INQLTSYIDASNVYGSSDEEALELRDLASdrGLLRVgivseAGKPLLpferdspmdcRRDPNESPIPcflaGDHRaNEQL 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 263 GFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWtieLLKtdtltagmrinwygFFGKKVKD 342
Cdd:cd09826 120 GLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHITYSHW---LPK--------------ILGPVGME 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 343 MVGA---------------------RFG-----PLFSGLVGLKKPNDHGvPYSLTEEFVSVYRmhcLLPETLI---LRDM 393
Cdd:cd09826 183 MLGEyrgynpnvnpsianefataafRFGhtlinPILFRLDEDFQPIPEG-HLPLHKAFFAPYR---LVNEGGIdplLRGL 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 394 NSENVDKENPAierEIPMTELIGKkagekasklgfeqlLVSMGHQscgaltlwnypnwmrnlVAQDidgedrphlidMAA 473
Cdd:cd09826 259 FATAAKDRVPD---QLLNTELTEK--------------LFEMAHE-----------------VALD-----------LAA 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 474 LEIYRDRERGVPRYNEFRKNLLMSPISKWEELTD---DEEAIKVLREVYeDDIEKLDLNVGLHAEKKIKGFAISETaFFI 550
Cdd:cd09826 294 LNIQRGRDHGLPGYNDYRKFCNLSVAETFEDLKNeikNDDVREKLKRLY-GHPGNIDLFVGGILEDLLPGARVGPT-LAC 371
                       410       420       430
                ....*....|....*....|....*....|.
gi 15219521 551 FLLVASRRL-EADRFFTTnfNEKTYTKEGLE 580
Cdd:cd09826 372 LLAEQFRRLrDGDRFWYE--NPGVFSPAQLT 400
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
205-323 4.58e-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: 49.34  E-value: 4.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219521 205 VNTRTPWWDGSVIYGNDETGMRRVRVFKD--GKLKIS------GDGLLERDE------------RGVP--ISGDIR-NSW 261
Cdd:cd09824  15 INALTSFVDASMVYGSEPSLAK*LRNLTNqlGLLAVNqrftdnGLALLPFENlhndpcalrntsANIPcfLAGDTRvSEN 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219521 262 SGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTDT 323
Cdd:cd09824  95 PGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA 156
 
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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