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Conserved domains on  [gi|238550173|ref|NP_536345|]
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lactoperoxidase precursor [Mus musculus]

Protein Classification

peroxidase family protein( domain architecture ID 10176955)

peroxidase family protein similar to Homo sapiens myeloperoxidase, eosinophil peroxidase, and lactoperoxidase

EC:  1.11.-.-
PubMed:  11054546

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
281-692 0e+00

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: 728.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 281 VCPTPPYKSLAREQINALTSFLDASLVYSPEPSLANRLRNLSSPLGLMAVNEEVSDNGRPFPPFVKMKPSPCEVINATAG 360
Cdd:cd09824    1 SCGACTSKRNVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTSAN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 361 VPCFLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWI 440
Cdd:cd09824   81 IPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 441 PPYQGYNESVDPRISNVFTFALRFGHLEIPSTVYRLDENYQPWGSESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAK 520
Cdd:cd09824  161 PPYRGYNESVDPRIANVFTTAFRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 521 LMHQNKMMTGELRNKLFQPNHTIhGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAKKLMDLYG 600
Cdd:cd09824  241 LNNQNQMLVDELRERLFQQTKRM-GLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 601 TPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKMSFSRLVCDNTGIDKVPLN 680
Cdd:cd09824  320 TPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRD 399
                        410
                 ....*....|..
gi 238550173 681 PFQANAYPHGFV 692
Cdd:cd09824  400 PFQPNSYPRDFV 411
 
Name Accession Description Interval E-value
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
281-692 0e+00

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: 728.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 281 VCPTPPYKSLAREQINALTSFLDASLVYSPEPSLANRLRNLSSPLGLMAVNEEVSDNGRPFPPFVKMKPSPCEVINATAG 360
Cdd:cd09824    1 SCGACTSKRNVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTSAN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 361 VPCFLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWI 440
Cdd:cd09824   81 IPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 441 PPYQGYNESVDPRISNVFTFALRFGHLEIPSTVYRLDENYQPWGSESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAK 520
Cdd:cd09824  161 PPYRGYNESVDPRIANVFTTAFRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 521 LMHQNKMMTGELRNKLFQPNHTIhGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAKKLMDLYG 600
Cdd:cd09824  241 LNNQNQMLVDELRERLFQQTKRM-GLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 601 TPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKMSFSRLVCDNTGIDKVPLN 680
Cdd:cd09824  320 TPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRD 399
                        410
                 ....*....|..
gi 238550173 681 PFQANAYPHGFV 692
Cdd:cd09824  400 PFQPNSYPRDFV 411
An_peroxidase pfam03098
Animal haem peroxidase;
136-682 0e+00

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 717.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  136 YRTITGYCNNRKNPALGSANRALARWLPAEYEDGLSLPYGWTpgkmrNGFPLPQPREVSNQIAAylNEEDVLDQKRSMLF 215
Cdd:pfam03098   1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  216 MQWGQIVDHDMDFAPETEMGSDTYTKAQCDEHCIQgDNCFPIMFPPGDPKLKTQGK-CMPFFRAGFVCPTPPYkslaREQ 294
Cdd:pfam03098  74 MQWGQFIDHDLTLTPESTSPNGSSCDCCCPPENLH-PPCFPIPIPPDDPFFSPFGVrCMPFVRSAPGCGLGNP----REQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  295 INALTSFLDASLVYSPEPSLANRLRNLSSplGLMAVNeeVSDNGRPFPPFVKMKPSPCeviNATAGVPCFLAGDSRASEQ 374
Cdd:pfam03098 149 INQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKVN--RSDDGKELLPFDPDGPCCC---NSSGGVPCFLAGDSRANEN 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  375 ILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKW----IPPYQGYNESV 450
Cdd:pfam03098 222 PGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWfgllPLPYNGYDPNV 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  451 DPRISNVF-TFALRFGHLEIPSTVYRLDENyqPWGSESELPLHTVFFNTWRLVkDGGIDPLVRGLLAKNAKLMHQNkmMT 529
Cdd:pfam03098 302 DPSISNEFaTAAFRFGHSLIPPFLYRLDEN--NVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQAVDNN--FT 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  530 GELRNKLFQPNHTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAkKLMDLYGTPSNIDIWL 609
Cdd:pfam03098 377 EELTNHLFGPPGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIA-KLRELYGSVDDIDLWV 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550173  610 GAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENP--GVFTEKQRESLQKMSFSRLVCDNT-GIDKVPLNPF 682
Cdd:pfam03098 456 GGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIETIQPNVF 531
PLN02283 PLN02283
alpha-dioxygenase
135-432 1.81e-03

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 41.67  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 135 PYRTITGYCNNRKNPALGSANRALAR-WLPAEYEDGLslpygwtpgkMRngfplPQPREVSNQIAAYLNEEDVLDQkRSM 213
Cdd:PLN02283  84 PYRTADGKCNDPFNEGAGSQGTFFGRnMPPVDQKDKL----------LD-----PHPSVVATKLLARKKFIDTGKQ-FNM 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 214 LFMQWGQIVDHD-MDFAPET---EMGSDTYTKAQCdehciqgdncfPImfppgdpklktqgKCMPFFRAGFVcPT--PPY 287
Cdd:PLN02283 148 IAASWIQFMIHDwIDHLEDTqqiELTAPKEVASQC-----------PL-------------KSFKFYKTKEV-PTgsPDI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 288 KSLAreqINALTSFLDASLVYSPEPSLANRLRNLS------SPLGLMAVNEevsdngrpfppfvKMKPSPCEVINATAGV 361
Cdd:PLN02283 203 KTGS---LNIRTPWWDGSVIYGSNEKGLRRVRTFKdgklkiSEDGLLLHDE-------------DGIPISGDVRNSWAGV 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550173 362 pcflagdsraseqillATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFI-QITTFrDYLPILL 432
Cdd:PLN02283 267 ----------------SLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIaKIHTI-DWTVELL 321
 
Name Accession Description Interval E-value
myeloperoxidase_like cd09824
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ...
281-692 0e+00

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: 728.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 281 VCPTPPYKSLAREQINALTSFLDASLVYSPEPSLANRLRNLSSPLGLMAVNEEVSDNGRPFPPFVKMKPSPCEVINATAG 360
Cdd:cd09824    1 SCGACTSKRNVREQINALTSFVDASMVYGSEPSLAK*LRNLTNQLGLLAVNQRFTDNGLALLPFENLHNDPCALRNTSAN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 361 VPCFLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWI 440
Cdd:cd09824   81 IPCFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDAAARL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 441 PPYQGYNESVDPRISNVFTFALRFGHLEIPSTVYRLDENYQPWGSESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAK 520
Cdd:cd09824  161 PPYRGYNESVDPRIANVFTTAFRRGHTTVQPFVFRLDENYQPHPPNPQVPLHKAFFASWRIIREGGIDPILRGLMATPAK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 521 LMHQNKMMTGELRNKLFQPNHTIhGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAKKLMDLYG 600
Cdd:cd09824  241 LNNQNQMLVDELRERLFQQTKRM-GLDLAALNLQRGRDHGLPGYNAWRRFCGLSQPQNLAELAAVLNNTVLARKLLDLYG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 601 TPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKMSFSRLVCDNTGIDKVPLN 680
Cdd:cd09824  320 TPDNIDIWIGGVAEPLVPGGRVGPLLACLISRQFRRIRDGDRFWWENPGVFTEEQRESLRSVSLSRIICDNTGITKVPRD 399
                        410
                 ....*....|..
gi 238550173 681 PFQANAYPHGFV 692
Cdd:cd09824  400 PFQPNSYPRDFV 411
An_peroxidase pfam03098
Animal haem peroxidase;
136-682 0e+00

Animal haem peroxidase;


Pssm-ID: 460804 [Multi-domain]  Cd Length: 531  Bit Score: 717.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  136 YRTITGYCNNRKNPALGSANRALARWLPAEYEDGLSLPYGWTpgkmrNGFPLPQPREVSNQIAAylNEEDVLDQKRSMLF 215
Cdd:pfam03098   1 YRTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSAPRGSS-----SGSPLPSPRLVSNKLFA--GDSGIPDPNLTLLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  216 MQWGQIVDHDMDFAPETEMGSDTYTKAQCDEHCIQgDNCFPIMFPPGDPKLKTQGK-CMPFFRAGFVCPTPPYkslaREQ 294
Cdd:pfam03098  74 MQWGQFIDHDLTLTPESTSPNGSSCDCCCPPENLH-PPCFPIPIPPDDPFFSPFGVrCMPFVRSAPGCGLGNP----REQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  295 INALTSFLDASLVYSPEPSLANRLRNLSSplGLMAVNeeVSDNGRPFPPFVKMKPSPCeviNATAGVPCFLAGDSRASEQ 374
Cdd:pfam03098 149 INQVTSFLDGSQVYGSSEETARSLRSFSG--GLLKVN--RSDDGKELLPFDPDGPCCC---NSSGGVPCFLAGDSRANEN 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  375 ILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKW----IPPYQGYNESV 450
Cdd:pfam03098 222 PGLTALHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNMNWfgllPLPYNGYDPNV 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  451 DPRISNVF-TFALRFGHLEIPSTVYRLDENyqPWGSESELPLHTVFFNTWRLVkDGGIDPLVRGLLAKNAKLMHQNkmMT 529
Cdd:pfam03098 302 DPSISNEFaTAAFRFGHSLIPPFLYRLDEN--NVPEEPSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQAVDNN--FT 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173  530 GELRNKLFQPNHTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAkKLMDLYGTPSNIDIWL 609
Cdd:pfam03098 377 EELTNHLFGPPGEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLPPAKSFEDLTDVIPNEVIA-KLRELYGSVDDIDLWV 455
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550173  610 GAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENP--GVFTEKQRESLQKMSFSRLVCDNT-GIDKVPLNPF 682
Cdd:pfam03098 456 GGLAEKPLPGGLVGPTFACIIGDQFRRLRDGDRFWYENGnqGSFTPEQLEEIRKTSLARVICDNTdIIETIQPNVF 531
thyroid_peroxidase cd09825
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ...
152-705 0e+00

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: 656.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 152 GSANRALARWLPAEYEDGLSLPYGWTPGKMRNGFPLPQPREVSNQIAAYLNEEDVLDQKRSMLFMQWGQIVDHDMDFAPE 231
Cdd:cd09825    1 GASNTPLARWLPPIYEDGFSEPVGWNKERLYNGFTLPSVREVSNKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIDFTPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 232 TEMGSDTYTKAQCDEHCIQGDNCFPIMFPPGDPKLkTQGKCMPFFRAGFVCPTPPYKSL--------AREQINALTSFLD 303
Cdd:cd09825   81 SVSRTMFIGSTDCKMTCENQNPCFPIQLPSEDPRI-LGRACLPFFRSSAVCGTGDTSTLfgnlslanPREQINGLTSFID 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 304 ASLVYSPEPSLANRLRNLSSPLGLMAVNEEVSDNGRPFPPFVKMKPSPCEVINATAG-VPCFLAGDSRASEQILLATSHT 382
Cdd:cd09825  160 ASTVYGSTLALARSLRDLSSDDGLLRVNSKFDDSGRDYLPFQPEEVSSCNPDPNGGErVPCFLAGDGRASEVLTLTASHT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 383 LFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDE-MQKWIPPYQGYNESVDPRISNVF-TF 460
Cdd:cd09825  240 LWLREHNRLARALKSINPHWDGEQIYQEARKIVGALHQIITFRDYIPKILGPEaFDQYGGYYEGYDPTVNPTVSNVFsTA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 461 ALRFGHLEIPSTVYRLDENYQPWGSESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAKLMHQNKMMTGELRNKLFQPN 540
Cdd:cd09825  320 AFRFGHATIHPTVRRLDENFQEHPVLPNLALHDAFFSPWRLVREGGLDPVIRGLIGGPAKLVTPDDLMNEELTEKLFVLS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 541 HTIHgFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAKKLMDLYGTPSNIDIWLGAVAEPLVHRG 620
Cdd:cd09825  400 NSST-LDLASLNLQRGRDHGLPGYNDWREFCGLPRLATPADLATAIADQAVADKILDLYKHPDNIDVWLGGLAEDFLPGA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 621 RVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKMSFSRLVCDNTGIDKVPLNPFQANAYPHGFVDCSSIDKL 700
Cdd:cd09825  479 RTGPLFACLIGKQMKALRDGDRFWWENSNVFTDAQRRELRKHSLSRVICDNTGLTRVPPDAFQLGKFPEDFVSCDSIPGI 558

                 ....*
gi 238550173 701 DLSPW 705
Cdd:cd09825  559 NLEAW 563
peroxidasin_like cd09826
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ...
260-696 0e+00

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: 533.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 260 PPGDPKlKTQGKCMPFFRAGFVCPT----PPYKSLA-REQINALTSFLDASLVYSPEPSLANRLRNLSSPLGLMAVNEeV 334
Cdd:cd09826    1 PPDDPR-RRGHRCIEFVRSSAVCGSgstsLLFNSVTpREQINQLTSYIDASNVYGSSDEEALELRDLASDRGLLRVGI-V 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 335 SDNGRPFPPFvkMKPSPCEVINATAG--VPCFLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEAR 412
Cdd:cd09826   79 SEAGKPLLPF--ERDSPMDCRRDPNEspIPCFLAGDHRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 413 KIMGAFIQITTFRDYLPILLGDEMQKWIPPYQGYNESVDPRISNVF-TFALRFGHLEIPSTVYRLDENYQPWgSESELPL 491
Cdd:cd09826  157 KIVGAQMQHITYSHWLPKILGPVGMEMLGEYRGYNPNVNPSIANEFaTAAFRFGHTLINPILFRLDEDFQPI-PEGHLPL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 492 HTVFFNTWRLVKDGGIDPLVRGLLAKNAKLMHQNKMMTGELRNKLFQPNHTIhGFDLASINIQRSRDHGQPGYNSWRAFC 571
Cdd:cd09826  236 HKAFFAPYRLVNEGGIDPLLRGLFATAAKDRVPDQLLNTELTEKLFEMAHEV-ALDLAALNIQRGRDHGLPGYNDYRKFC 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 572 GLSQPKTLEELSAVMKNEVLAKKLMDLYGTPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVF 651
Cdd:cd09826  315 NLSVAETFEDLKNEIKNDDVREKLKRLYGHPGNIDLFVGGILEDLLPGARVGPTLACLLAEQFRRLRDGDRFWYENPGVF 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 238550173 652 TEKQRESLQKMSFSRLVCDNT-GIDKVPLNPFQANAYPHGFVDCSS 696
Cdd:cd09826  395 SPAQLTQIKKTSLARVLCDNGdNITRVQEDVFLVPGNPHGYVSCES 440
peroxinectin_like cd09823
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ...
292-671 1.84e-166

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: 482.84  E-value: 1.84e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 292 REQINALTSFLDASLVYSPEPSLANRLRNLSSplGLMAVNeevSDNGRPFPPFVKMKPSPCevINATAGVPCFLAGDSRA 371
Cdd:cd09823    1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKG--GLLKTQ---RRNGRELLPFSNNPTDDC--SLSSAGKPCFLAGDGRV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 372 SEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWI-------PPYQ 444
Cdd:cd09823   74 NEQPGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELMEKFglylltsGYFN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 445 GYNESVDPRISNVF-TFALRFGHLEIPSTVYRLDENYQPwgsESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAKLMH 523
Cdd:cd09823  154 GYDPNVDPSILNEFaAAAFRFGHSLVPGTFERLDENYRP---QGSVNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQKVD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 524 QNkmMTGELRNKLFQPNHTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMkNEVLAKKLMDLYGTPS 603
Cdd:cd09823  231 RF--FTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLPRATTFDDLLGIM-SPETIQKLRRLYKSVD 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238550173 604 NIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGV---FTEKQRESLQKMSFSRLVCDN 671
Cdd:cd09823  308 DIDLYVGGLSEKPVPGGLVGPTFACIIGEQFRRLRRGDRFWYENGGQpssFTPAQLNEIRKVSLARIICDN 378
An_peroxidase_like cd05396
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ...
294-671 1.33e-126

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: 380.62  E-value: 1.33e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 294 QINALTSFLDASLVYSPEPSLANRLRNLssPLGLMAVNEEVSDN-GRPFPPFVKMKPSPCEVINATagVPCFLAGDSRAS 372
Cdd:cd05396    1 QLNARTPYLDGSSIYGSNPDVARALRTF--KGGLLKTNEVKGPSyGTELLPFNNPNPSMGTIGLPP--TRCFIAGDPRVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 373 EQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWIPPYQ--GYNESV 450
Cdd:cd05396   77 ENLLLLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDDLVLlfPDPDVV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 451 DPRISNVFTFALRFGHLEIPSTVYRLDENYQpWGSESELPLHTVFFNTWRLV-KDGGIDPLVRGLLAKNAKLMHQNKMMT 529
Cdd:cd05396  157 PYVLSEFFTAAYRFGHSLVPEGVDRIDENGQ-PKEIPDVPLKDFFFNTSRSIlSDTGLDPLLRGFLRQPAGLIDQNVDDV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 530 gelrnKLFQPNHTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEelsAVMKNEVLAKKLMDLYGTPSNIDIWL 609
Cdd:cd05396  236 -----MFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLKPPTSFQ---DILTDPELAKKLAELYGDPDDVDLWV 307
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238550173 610 GAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKM-SFSRLVCDN 671
Cdd:cd05396  308 GGLLEKKVPPARLGELLATIILEQFKRLVDGDRFYYVNYNPFGKSGKEELEKLiSLADIICLN 370
peroxinectin_like_bacterial cd09822
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ...
187-684 2.96e-116

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: 355.85  E-value: 2.96e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 187 LPQPREVSNQIAA----YLNEEDVLDqkrsmLFMQWGQIVDHDMDFAPetemgsdtytkaqcdehciqgDNCfpimfppg 262
Cdd:cd09822    2 RPSPREISNAVADqtesIPNSRGLSD-----WFWVWGQFLDHDIDLTP---------------------DNP-------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 263 dpklktqgkcmpffragfvcptppykslaREQINALTSFLDASLVYSPEPSLANRLRNLSSplGLMAVNEEVSDNgrpFP 342
Cdd:cd09822   48 -----------------------------REQINAITAYIDGSNVYGSDEERADALRSFGG--GKLKTSVANAGD---LL 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 343 PFvkmkpSPCEVINATAGVPC---FLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFI 419
Cdd:cd09822   94 PF-----NEAGLPNDNGGVPAddlFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEI 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 420 QITTFRDYLPILLGDEMqkwIPPYQGYNESVDPRISNVF-TFALRFGHLEIPSTVYRLDENyqpwGSESE-LPLHTVFFN 497
Cdd:cd09822  169 QAITYNEFLPALLGENA---LPAYSGYDETVNPGISNEFsTAAYRFGHSMLSSELLRGDED----GTEATsLALRDAFFN 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 498 TwRLVKDGGIDPLVRGlLAKNakLMHQNKM-MTGELRNKLFQPNhTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQP 576
Cdd:cd09822  242 P-DELEENGIDPLLRG-LASQ--VAQEIDTfIVDDVRNFLFGPP-GAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAV 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 577 KTLEELSavmKNEVLAKKLMDLYGTPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPgVFTEKQR 656
Cdd:cd09822  317 TSFSDIT---SDPDLAARLASVYGDVDQIDLWVGGLAEDHVNGGLVGETFSTIIADQFTRLRDGDRFFYEND-DLLLDEI 392
                        490       500
                 ....*....|....*....|....*...
gi 238550173 657 ESLQKMSFSRLVCDNTGIDKVPLNPFQA 684
Cdd:cd09822  393 ADIENTTLADVIRRNTDVDDIQDNVFLV 420
dual_peroxidase_like cd09820
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ...
141-664 3.21e-83

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: 274.18  E-value: 3.21e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 141 GYCNNRKNPALGSANRALARWLPAEYEDGLSLPYGWTpgkmrngfpLPQPREVSNQIAAylnEEDVL--DQKRSMLFMQW 218
Cdd:cd09820    3 GWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEE---------RPNPRSLSNLLMK---GESGLpsTRNRTALLVFF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 219 GQIVDHDMdfapetemgSDTytkaqcdehciQGDNC----FPIMFPPGDP---KLKTQGKCMPFFRAGFVCPTPPYKSLA 291
Cdd:cd09820   71 GQHVVSEI---------LDA-----------SRPGCppeyFNIEIPKGDPvfdPECTGNIELPFQRSRYDKNTGYSPNNP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 292 REQINALTSFLDASLVYSPEPSLANRLRNLSspLGLMAvneevSDNGRPFPPFVKMK------PSPCEviNATAGVPCFL 365
Cdd:cd09820  131 REQLNEVTSWIDGSSIYGSSKAWSDALRSFS--GGRLA-----SGDDGGFPRRNTNRlplanpPPPSY--HGTRGPERLF 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 366 A-GDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEmqkwIPPYQ 444
Cdd:cd09820  202 KlGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWSDEDIFQEARKWVIATYQNIVFYEWLPALLGTN----VPPYT 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 445 GYNESVDPRISNVFTFAL-RFGHLEIPSTVYRLDE--NYQPWGSESelplhtVFFNTWRL----------VKDGGIDPLV 511
Cdd:cd09820  278 GYKPHVDPGISHEFQAAAfRFGHTLVPPGVYRRNRqcNFREVLTTS------GGSPALRLcntywnsqepLLKSDIDELL 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 512 RGLLAKNAKLmhQNKMMTGELRNKLFQPNHtIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEEL--SAVMKNE 589
Cdd:cd09820  352 LGMASQIAER--EDNIIVEDLRDYLFGPLE-FSRRDLMALNIQRGRDHGLPDYNTAREAFGLPPRTTWSDInpDLFKKDP 428
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238550173 590 VLAKKLMDLYG-TPSNIDIWLGAVAEplVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENP--GVFTEKQRESLQKMSF 664
Cdd:cd09820  429 ELLERLAELYGnDLSKLDLYVGGMLE--SKGGGPGELFRAIILDQFQRLRDGDRFWFENVknGLFTAEEIEEIRNTTL 504
An_peroxidase_bacterial_2 cd09821
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
211-689 1.62e-32

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: 132.92  E-value: 1.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 211 RSMLFMQWGQIVDHDMDFAPETemGSDTYTKaqcdehciqgdncfPImfPPGDP--KLKTQGKCMPFFRAGFVCPTPPYK 288
Cdd:cd09821   13 YNSWMTFFGQFFDHGLDFIPKG--GNGTVLI--------------PL--PPDDPlyDLGRGTNGMALDRGTNNAGPDGIL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 289 SLA---REQINALTSFLDASLVYSPEPSLANRLRN-----------LSSPLGLMAV-----NEEVSDNGRPFPPFVKMKP 349
Cdd:cd09821   75 GTAdgeGEHTNVTTPFVDQNQTYGSHASHQVFLREydgdgvatgrlLEGATGGSARtghafLDDIAHNAAPKGGLGSLRD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 350 SPCEVINATAGVPC---------FLAGDSRASEQILLATSHTLFIREHNRL----------------ATELSRLNPHWDR 404
Cdd:cd09821  155 NPTEDPPGPGAPGSydnelldahFVAGDGRVNENIGLTAVHTVFHREHNRLvdqikdtllqsadlafANEAGGNNLAWDG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 405 ETLYQEARKIMGAFIQITTFRDYlpillGDEMQKWIPPY---QGYNESVDPRISNVFTFAL-RFGHLEIPSTVYRLDENY 480
Cdd:cd09821  235 ERLFQAARFANEMQYQHLVFEEF-----ARRIQPGIDGFgsfNGYNPEINPSISAEFAHAVyRFGHSMLTETVTRIGPDA 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 481 QPWGSES----ELPLHTVFFNTWRLVKDGGIDPLVRGllaknakLMHQ-----NKMMTGELRNKLF-QPNhtihgfDLAS 550
Cdd:cd09821  310 DEGLDNQvgliDAFLNPVAFLPATLYAEEGAGAILRG-------MTRQvgneiDEFVTDALRNNLVgLPL------DLAA 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 551 INIQRSRDHGQPG--------------------YNSWRAFCG-LSQPKTLEELSAVMKNEVLAKKLMDLYGTPS------ 603
Cdd:cd09821  377 LNIARGRDTGLPTlnearaqlfaatgdtilkapYESWNDFGArLKNPESLINFIAAYGTHLTITGATTLAAKRAaaqdlv 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 604 ----------------------------NIDIWLGAVAE-PLVHRGRVGPLLTCLLGQQFQRIRDGDRFWW--ENPGVFT 652
Cdd:cd09821  457 dggdgapadradfmnaagagagtvkgldNVDLWVGGLAEkQVPFGGMLGSTFNFVFEEQMDRLQDGDRFYYlsRTAGLDL 536
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 238550173 653 EKQresLQKMSFSRLVCDNTGIDKVPLNPFQANAYPH 689
Cdd:cd09821  537 LNQ---LENNTFADMIMRNTGATHLPQDIFSVPDYDT 570
prostaglandin_endoperoxide_synthase cd09816
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ...
337-675 1.01e-23

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: 105.42  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 337 NGRPFPPF------VKMKPSPCEVINATAGVPC-----FLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRE 405
Cdd:cd09816  161 NGEEYPPYlfedggVKMEFPPLVPPLGDELTPEreaklFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDE 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 406 TLYQEARKIM-GAFIQItTFRDYLPILLGDEMQKWIPPYQGYNE--SVDPRISNVFTFALRFgHLEIPSTVYrldenyqp 482
Cdd:cd09816  241 RLFQTARNILiGELIKI-VIEDYINHLSPYHFKLFFDPELAFNEpwQRQNRIALEFNLLYRW-HPLVPDTFN-------- 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 483 WGsESELPLHTVFFNTwRLVKDGGIDPLVRGLLAKNA-KLMHQNkmmTGElrnklfqpnhTIHGFDLASINIQRSRDHgq 561
Cdd:cd09816  311 IG-GQRYPLSDFLFNN-DLVVDHGLGALVDAASRQPAgRIGLRN---TPP----------FLLPVEVRSIEQGRKLRL-- 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 562 PGYNSWRAFCGLSQPKTLEELSAvmkNEVLAKKLMDLYGTPSNIDIWLGAVAEPLVHRGRVGPLLTCLLG-QQFQRIRD- 639
Cdd:cd09816  374 ASFNDYRKRFGLPPYTSFEELTG---DPEVAAELEELYGDVDAVEFYVGLFAEDPRPNSPLPPLMVEMVApDAFSGALTn 450
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 238550173 640 --GDRFWWeNPGVFT-EKQRESLQKMSFSRLVCDNTGID 675
Cdd:cd09816  451 plLSPEVW-KPSTFGgEGGFDIVKTATLQDLVCRNVKGG 488
PIOX_like cd09818
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ...
137-616 2.35e-13

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: 73.09  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 137 RTITGYCNNRKNPALGSANRALARWLPAEYedglslpygwTPGKMRNGFPLPQPREVSNQI--------AAYLNeedvld 208
Cdd:cd09818    1 RTADGSYNDLDNPSMGSVGTRFGRNVPLDA----------TFPEDKDELLTPNPRVISRRLlartefkpATSLN------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 209 qkrsMLFMQWGQIVDHDMdfapetemgsdtytkaqcdehciqgdncfpimFPPGdpklktqgkcmpffragfvcpTPPYk 288
Cdd:cd09818   65 ----LLAAAWIQFMVHDW--------------------------------FSHG---------------------PPTY- 86
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 289 slareqINALTSFLDASLVYSPEPSLANRLRNLSSPLGLmavneEVSDNGrpfppfvKMKPSPCEVINATAGVPCFLAGd 368
Cdd:cd09818   87 ------INTNTHWWDGSQIYGSTEEAQKRLRTFPPDGKL-----KLDADG-------LLPVDEHTGLPLTGFNDNWWVG- 147
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 369 sraseqilLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFI-QITTFrDYLPILLGDE-----MQ----- 437
Cdd:cd09818  148 --------LSLLHTLFVREHNAICDALRKEYPDWSDEQLFDKARLVNAALMaKIHTV-EWTPAILAHPtleiaMRanwwg 218
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 438 ------KWIPPYQGYNESV------DPRISNV-FTFALRFghleipSTVYRL-----DE-NYQPWGS---ESELPLHTVF 495
Cdd:cd09818  219 llgerlKRVLGRDGTSELLsgipgsPPNHHGVpYSLTEEF------VAVYRMhplipDDiDFRSADDgatGEEISLTDLA 292
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 496 FNTwrlvkdggidplVRGLLAKN--AKLMHQnkMMT---GELRN----KLFQPNHTIHG--FDLASINIQRSRDHGQPGY 564
Cdd:cd09818  293 GGK------------ARELLRKLgfADLLYS--FGIthpGALTLhnypRFLRDLHRPDGrvIDLAAIDILRDRERGVPRY 358
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 238550173 565 NSWRAFCGLSQPKTLEELSavmKNEVLAKKLMDLYG-TPSNIDIWLGAVAEPL 616
Cdd:cd09818  359 NEFRRLLHLPPAKSFEDLT---GDEEVAAELREVYGgDVEKVDLLVGLLAEPL 408
PLN02283 PLN02283
alpha-dioxygenase
135-432 1.81e-03

alpha-dioxygenase


Pssm-ID: 177921 [Multi-domain]  Cd Length: 633  Bit Score: 41.67  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 135 PYRTITGYCNNRKNPALGSANRALAR-WLPAEYEDGLslpygwtpgkMRngfplPQPREVSNQIAAYLNEEDVLDQkRSM 213
Cdd:PLN02283  84 PYRTADGKCNDPFNEGAGSQGTFFGRnMPPVDQKDKL----------LD-----PHPSVVATKLLARKKFIDTGKQ-FNM 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 214 LFMQWGQIVDHD-MDFAPET---EMGSDTYTKAQCdehciqgdncfPImfppgdpklktqgKCMPFFRAGFVcPT--PPY 287
Cdd:PLN02283 148 IAASWIQFMIHDwIDHLEDTqqiELTAPKEVASQC-----------PL-------------KSFKFYKTKEV-PTgsPDI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 288 KSLAreqINALTSFLDASLVYSPEPSLANRLRNLS------SPLGLMAVNEevsdngrpfppfvKMKPSPCEVINATAGV 361
Cdd:PLN02283 203 KTGS---LNIRTPWWDGSVIYGSNEKGLRRVRTFKdgklkiSEDGLLLHDE-------------DGIPISGDVRNSWAGV 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550173 362 pcflagdsraseqillATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFI-QITTFrDYLPILL 432
Cdd:PLN02283 267 ----------------SLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIaKIHTI-DWTVELL 321
An_peroxidase_bacterial_1 cd09819
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ...
365-480 1.97e-03

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


Pssm-ID: 188651  Cd Length: 465  Bit Score: 41.17  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550173 365 LAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRetLYQEARkimgafiQITTFR-------DYLPILLG---- 433
Cdd:cd09819  145 LIGDPRNDENLIVAQLHLAFLRFHNAVVDALRAHGTPGDE--LFEEAR-------RLVRWHyqwlvlnDFLPRICDpdvv 215
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 238550173 434 -DEMQKWIPPYQGYNESVdPRISNVF-TFALRFGHleipSTV---YRLDENY 480
Cdd:cd09819  216 dDVLANGRRFYRFFREGK-PFMPVEFsVAAYRFGH----SMVrasYDYNRNF 262
linoleate_diol_synthase_like cd09817
Linoleate (8R)-dioxygenase and related enzymes; These fungal enzymes, related to animal heme ...
553-614 2.44e-03

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: 41.17  E-value: 2.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238550173 553 IQRSRDHGQPGYNSWRAFCGLSQPKTLEElsaVMKNEVLAKKLMDLYGTPSNIDIWLGAVAE 614
Cdd:cd09817  380 ILQAREWNVATLNEFRKFFGLKPYETFED---INSDPEVAEALELLYGHPDNVELYPGLVAE 438
 
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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