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PR00457

Identifier
ANPEROXIDASE  [View Relations]  [View Alignment]  
Accession
PR00457
No. of Motifs
8
Creation Date
16-APR-1996  (UPDATE 28-JUL-1999)
Title
Animal haem peroxidase signature
Database References

INTERPRO; IPR002007
PDB; 1MYP; 1PRH
SCOP; 1MYP; 1PRH
CATH; 1MYP; 1PRH
Literature References
1. LI, H. AND POULOS, T.L.
Structural variation in heme enzymes: a comparative analysis of
peroxidase and P450 crystal structures.
STRUCTURE 2 461-464 (1994).
 
2. KIMURA, S. AND IKEDA-SAITO, M.
Human myeloperoxidase and thyroid peroxidase, two enzymes with separate 
and distinct physiological functions, are evolutionarily related members 
of the same gene family.
PROTEINS 3 113-120 (1988).
 
3. MARNETT, I.
Prostaglandin H synthase.
IN BIOLOGICAL OXIDATION SYSTEMS, REDDY, C.C., HAMILTON, G.A. AND
MADYASTHA, K.N., EDS. VOL.2 PP.637-655 (1990). ACADEMIC PRESS, SAN DIEGO.
 
4. NELSON, R.E., FESSLER, L.I., TAKAGI, Y., BLUMBERG, B., KEENE, D.R.,
OLSON, P.F., PARKER, C.G. AND FESSLER, J.H.
Peroxidasin: a novel enzyme-matrix protein of Drosophila development.
EMBO J. 13 3438-3447 (1994).
 
5. UETRECHT, J.
Metabolism of drugs by activated leukocytes: implications for drug-induced
lupus and other drug hypersensitivity reactions.
ADV.EXP.MED.BIOL. 283 121-32 (1991).
 
6. SPESSOTTO, P., DRI, P., BULLA, R., ZABUCCHI, G. AND PATRIARCA, C.
Human eosinophil peroxidase enhances tumor necrosis factor and hydrogen
peroxide release by human monocyte-derived macrophages.
EUR.J.IMMUNOL. 25 1366-1373 (1995).
 
7. WEVER, R., KAST, W.M., KASINOEDIN, J.H. AND BOELENS, R.
The peroxidation of thiocyanate catalysed by myeloperoxidase and
lactoperoxidase.
BIOCHIM.BIOPHYS.ACTA 709 212-219 (1982).
 
8. KIMURA, S., HONG, Y.S., KOTANI, T., OHTAKI, S. AND KIKKAWA, F.
Structure of the human thyroid peroxidase gene: comparison and relationship
to the human myeloperoxidase gene.
BIOCHEMISTRY 28 4481-4489 (1989).
 
9. ZENG, J. AND FENNA, R.E.
X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
J.MOL.BIOL. 226 185-207 (1992).
 
10. PICOT, D., LOLL, P.J. AND GARAVITO, R.M.
The X-ray crystal structure of the membrane protein prostaglandin H2
synthase-1.
NATURE 367 243-249 (1994).

Documentation
Peroxidases are haem-containing enzymes that use hydrogen peroxide as
the electron acceptor to catalyse a number of oxidative reactions.
Most haem peroxidases follow the reaction scheme:
 
Fe(3+) + H2O2            --> [Fe(4+)=O]R' (Compound I) + H2O
[Fe(4+)=O]R' + substrate --> [Fe(4+)=O]R (Compound II) + oxidised substrate
[Fe(4+)=O]R  + substrate -->  Fe(3+) + H2O + oxidised substrate
 
In this mechanism, the enzyme reacts with one equivalent of H2O2 to give 
[Fe(4+)=O]R' (compound I). This is a two-electron oxidation/reduction 
reaction where H2O2 is reduced to water and the enzyme is oxidised. One 
oxidising equivalent resides on iron, giving the oxyferryl [Fe(4+)=O] 
intermediate, while in many peroxidases the porphyrin (R) is oxidised to 
the porphyrin pi-cation radical (R'). Compound I then oxidises an organic 
substrate to give a substrate radical [1].
 
Peroxidases are found in bacteria, fungi, plants and animals. On the basis
of sequence similarity, a number of animal haem peroxidases can be
categorised as members of a superfamily: myeloperoxidase (MPO); eosinophil
peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO);
prostaglandin H synthase (PGHS); and peroxidasin [2-4]. MPO plays a major
role in the oxygen-dependent microbicidal system of neutrophils. It has
also been found that certain drugs can be oxidised to reactive metabolites
by the MPO of monocytes, which may play a role in the development of 
idiosyncratic drug reactions [5]. EPO from eosinophilic granulocytes 
participates in immunological reactions, and potentiates tumor necrosis 
factor (TNF) production and hydrogen peroxide release by human monocyte-
derived macrophages [6]. In the main, MPO (and possibly EPO) utilises Cl-
ions and H2O2 to form hypochlorous acid (HOCl), which can effectively kill
bacteria or parasites. In secreted fluids, LPO catalyses the oxidation of 
thiocyanate ions (SCN-) by H2O2, producing the weak oxidising agent 
hypothiocyanite (OSCN-), which has bacteriostatic activity [7]. TPO uses 
I- ions and H2O2 to generate iodine, and plays a central role in the 
biosynthesis of thyroid hormones T(3) and T(4). TPO contains 3 additional 
C-terminal domains, which are similar to C4b-beta 2 glycoprotein, the 
EGF-LDL receptor, and a transmembrane domain, respectively [8]. Peroxidasin
is a fusion protein combining a peroxidase domain with 6 leucine-rich 
regions, four Ig loops, a thrombospondin/procollagen homology and an 
amphipathic alpha-helix [4]. PGHS is a membrane-bound enzyme catalysing 
the first two steps in prostaglandin (PG), thromboxane and prostacyclin 
biosynthesis: the first step involves oxygenation of polyunsaturated fatty 
acids to hydroperoxy endoperoxides (cyclooxygenase activity); the second 
step involves reduction of the hydroperoxy endoperoxides to hydroxy 
endoperoxides (peroxidase activity). The peroxidase activity of PGHS also 
oxidises xenobiotics to reactive derivatives [3].
 
To date, the 3D structures of MPO and PGHS have been reported. MPO is a 
homodimer: each monomer consists of a light (A or B) and a heavy (C or D) 
chain resulting from post-translational excision of 6 residues from the 
common precursor. Monomers are linked by a single inter-chain disulphide. 
Each monomer includes a bound calcium ion [9]. PGHS exists as a symmetric 
dimer, each monomer of which consists of 3 domains: an N-terminal epidermal
growth factor (EGF) like module; a membrane-binding domain; and a large
C-terminal catalytic domain containing the cyclooxygenase and the peroxidase 
active sites. The catalytic domain shows striking structural similarity to 
MPO. The cyclooxygenase active site, which catalyses the formation of 
prostaglandin G2 (PGG2) from arachidonic acid, resides at the apex of a 
long hydrophobic channel, extending from the membrane-binding domain to the
centre of the molecule. The peroxidase active site, which catalyses the
reduction of PGG2 to PGH2, is located on the other side of the molecule, at
the haem binding site [10]. Both MPO and the catalytic domain of PGHS are 
mainly alpha-helical, 19 helices being identified as topologically and
spatially equivalent; PGHS contains 5 additional N-terminal helices that
have no equivalent in MPO. In both proteins, three Asn residues in each
monomer are glycosylated.
 
ANPEROXIDASE is an 8-element fingerprint that provides a signature for
animal haem peroxidases. The fingerprint was derived from an initial
alignment of 8 sequences: motif 2 contains the invariant active site 
("distal") His and a conserved Asp residue, which participates in Ca(2+)
binding in MPO [9] (cf. PROSITE pattern PEROXIDASE_2 (PS00436)); motif 4 
contains the invariant "distal" Arg (on the distal side of the haem, His 
and Arg residues are likely to participate directly in the catalytic 
mechanism, in a manner analogous to the distal His and Arg of the 
non-homologous enzyme cytochrome c peroxidase); motif 6 contains the 
invariant "proximal" His residue at position 9, which serves the axial 
ligand of the haem iron (cf. PROSITE pattern PEROXIDASE_1 (PS00435)). Three
iterations on OWL27.1 were required to reach convergence, at which point a 
true set comprising 42 sequences was identified. Several partial matches 
were also found: squid peroxidase-like proteins PN0667 and JN0867 failed to
match motif 6; C.elegans sequence CEF49E125 lacks motifs 6 and 8; C.elegans
sequence CET05B9 lacks motifs 2, 6 and 7; HUMTPOC is a TPO fragment lacking
the portion of sequence bearing motif 1 and the three C-terminal motifs;
PERL_HUMAN is an LPO fragment lacking the four N-terminal motifs; and S53511
is a cuttlefish peroxidase fragment missing the two N-terminal and three
C-terminal motifs.
 
An update on SPTR37_9f identified a true set of 33 sequences, and 12
partial matches.
Summary Information
  33 codes involving  8 elements
2 codes involving 7 elements
5 codes involving 6 elements
2 codes involving 5 elements
2 codes involving 4 elements
0 codes involving 3 elements
1 codes involving 2 elements
Composite Feature Index
83333333333333333
702222222
614555433
520222002
400222200
300000000
200011000
12345678
True Positives
O17241        O44087        PERE_HUMAN    PERE_MOUSE    
PERL_BOVIN PERM_HUMAN PERM_MOUSE PERO_DROME
PERT_HUMAN PERT_MOUSE PERT_PIG PERT_RAT
PGH1_HUMAN PGH1_MOUSE PGH1_RAT PGH1_SHEEP
PGH2_BOVIN PGH2_CAVPO PGH2_CHICK PGH2_HORSE
PGH2_HUMAN PGH2_MOUSE PGH2_MUSVI PGH2_RABIT
PGH2_RAT PGH2_SHEEP Q13408 Q18647
Q19950 Q23490 Q23991 Q26059
Q63124
True Positive Partials
Codes involving 7 elements
O02634 P91060
Codes involving 6 elements
O01892 O44391 O44392 P90820
Q20616
Codes involving 5 elements
O18504 Q24926
Codes involving 4 elements
O01795 O61213
Codes involving 2 elements
O82031
Sequence Titles
O17241      K10B4.1 PROTEIN - CAENORHABDITIS ELEGANS.     
O44087 ZK994.3 PROTEIN - CAENORHABDITIS ELEGANS.
PERE_HUMAN EOSINOPHIL PEROXIDASE PRECURSOR (EC 1.11.1.7) (EPO) - HOMO SAPIENS (HUMAN).
PERE_MOUSE EOSINOPHIL PEROXIDASE PRECURSOR (EC 1.11.1.7) (EPO) - MUS MUSCULUS (MOUSE).
PERL_BOVIN LACTOPEROXIDASE PRECURSOR (EC 1.11.1.7) (LPO) - BOS TAURUS (BOVINE).
PERM_HUMAN MYELOPEROXIDASE PRECURSOR (EC 1.11.1.7) (MPO) - HOMO SAPIENS (HUMAN).
PERM_MOUSE MYELOPEROXIDASE PRECURSOR (EC 1.11.1.7) (MPO) - MUS MUSCULUS (MOUSE).
PERO_DROME PEROXIDASE PRECURSOR (EC 1.11.1.7) - DROSOPHILA MELANOGASTER (FRUIT FLY).
PERT_HUMAN THYROID PEROXIDASE PRECURSOR (EC 1.11.1.8) (TPO) - HOMO SAPIENS (HUMAN).
PERT_MOUSE THYROID PEROXIDASE PRECURSOR (EC 1.11.1.8) (TPO) - MUS MUSCULUS (MOUSE).
PERT_PIG THYROID PEROXIDASE PRECURSOR (EC 1.11.1.8) (TPO) - SUS SCROFA (PIG).
PERT_RAT THYROID PEROXIDASE PRECURSOR (EC 1.11.1.8) (TPO) - RATTUS NORVEGICUS (RAT).
PGH1_HUMAN PROSTAGLANDIN G/H SYNTHASE 1 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -1) (COX-1) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 1) (PROSTAGLANDIN H2 SYNTHASE 1) (PGH SYNTHASE 1) (PGHS-1) (PHS 1) - HOMO SAPIENS (HUMAN).
PGH1_MOUSE PROSTAGLANDIN G/H SYNTHASE 1 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -1) (COX-1) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 1) (PROSTAGLANDIN H2 SYNTHASE 1) (PGH SYNTHASE 1) (PGHS-1) (PHS 1) - MUS MUSCULUS (MOUSE).
PGH1_RAT PROSTAGLANDIN G/H SYNTHASE 1 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -1) (COX-1) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 1) (PROSTAGLANDIN H2 SYNTHASE 1) (PGH SYNTHASE 1) (PGHS-1) (PHS 1) - RATTUS NORVEGICUS (RAT).
PGH1_SHEEP PROSTAGLANDIN G/H SYNTHASE 1 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -1) (COX-1) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 1) (PROSTAGLANDIN H2 SYNTHASE 1) (PGH SYNTHASE 1) (PGHS-1) (PHS 1) - OVIS ARIES (SHEEP).
PGH2_BOVIN PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - BOS TAURUS (BOVINE).
PGH2_CAVPO PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - CAVIA PORCELLUS (GUINEA PIG).
PGH2_CHICK PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) (MITOGEN-INDUCIBLE PGHS) - GALLUS GALLUS (CHICKEN).
PGH2_HORSE PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - EQUUS CABALLUS (HORSE).
PGH2_HUMAN PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - HOMO SAPIENS (HUMAN).
PGH2_MOUSE PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) (GLUCOCORTICOID- REGULATED INFLAMMATORY CYCLOOXYGENASE) (GRIPGHS) (TIS10 PROTEIN) (MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73) (PES-2) - MUS MUSCULUS (MOUSE).
PGH2_MUSVI PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - MUSTELA VISON (AMERICAN MINK).
PGH2_RABIT PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - ORYCTOLAGUS CUNICULUS (RABBIT).
PGH2_RAT PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - RATTUS NORVEGICUS (RAT).
PGH2_SHEEP PROSTAGLANDIN G/H SYNTHASE 2 PRECURSOR (EC 1.14.99.1) (CYCLOOXYGENASE -2) (COX-2) (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2) (PROSTAGLANDIN H2 SYNTHASE 2) (PGH SYNTHASE 2) (PGHS-2) (PHS II) - OVIS ARIES (SHEEP).
Q13408 SALIVARY PEROXIDASE - HOMO SAPIENS (HUMAN).
Q18647 SIMILAR TO EOSINOPHIL PEROXIDASE AND MYELO-PEROXYDASE - CAENORHABDITIS ELEGANS.
Q19950 SIMILAR TO MUCIN - CAENORHABDITIS ELEGANS.
Q23490 SIMILAR TO PEROXIDASE. NCBI GI: 1125749 - CAENORHABDITIS ELEGANS.
Q23991 PEROXIDASIN PRECURSOR - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q26059 PEROXINECTIN PRECURSOR - PACIFASTACUS LENIUSCULUS (SIGNAL CRAYFISH).
Q63124 CYCLOOXYGENASE-2 - RATTUS NORVEGICUS (RAT).

O02634 OVOPEROXIDASE (EC 1.11.1.7) (MYELOPEROXIDASE) - HEMICENTROTUS PULCHERRIMUS (SEA URCHIN).
P91060 SIMILAR TO PEROXIDASE PRECURSOR - CAENORHABDITIS ELEGANS.

O01892 SIMILAR TO PEROXIDASE - CAENORHABDITIS ELEGANS.
O44391 OVOPEROXIDASE (EC 1.11.1.7) (MYELOPEROXIDASE) - STRONGYLOCENTROTUS PURPURATUS (PURPLE SEA URCHIN).
O44392 OVOPEROXIDASE (EC 1.11.1.7) (MYELOPEROXIDASE) - LYTECHINUS VARIEGATUS (SEA URCHIN).
P90820 HYPOTHETICAL PROTEIN F09F3.5 - CAENORHABDITIS ELEGANS.
Q20616 F49E12.1 PROTEIN - CAENORHABDITIS ELEGANS.

O18504 MELANOGENIC PEROXIDASE - SEPIA OFFICINALIS (COMMON CUTTLEFISH).
Q24926 PEROXIDASE-LIKE PROTEIN - EUPRYMNA SCOLOPES.

O01795 SIMILAR IN THE AMINO-HALF TO PEROXIDASES AND IN THE CARBOXY-HALF TO NAPDH OXIDASES - CAENORHABDITIS ELEGANS.
O61213 F56C11.1 PROTEIN - CAENORHABDITIS ELEGANS.

O82031 OXYGENASE - NICOTIANA TABACUM (COMMON TOBACCO).
Scan History
OWL27_1    3  400  NSINGLE    
SPTR37_9f 3 200 NSINGLE
Initial Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
RSLPPVGHDCPT PGH2_CHICK 136 136 -
RILPSVPRDCPT PGH1_SHEEP 150 150 -
RWLPAEYEDGVS PERM_MOUSE 171 171 -
RWLPAEYEDGLS PERE_HUMAN 157 157 -
RWLPAEYEDGLA PERL_BOVIN 162 162 -
RWLPPVYEDGFS PERT_MOUSE 169 169 -
RLLTPKYADGIS PERO_DROME 129 129 -
RWLPPVYEDGFS PERU_HUMAN 175 175 -

Motif 2 width=16
Element Seqn Id St Int Rpt
MFTFFAQHFTHQFFKT PGH2_CHICK 183 35 -
MFMQWGQFLDHDITLT PERM_MOUSE 225 42 -
MFMQWGQFIDHDLDFS PERE_HUMAN 211 42 -
LFMQWGQIVDHDLDFA PERL_BOVIN 216 42 -
FLPVWGQYIDHDIALT PERT_MOUSE 223 42 -
HNMQWGQIMTHDMSMQ PERO_DROME 175 34 -
LLMAWGQYIDHDIAFT PERU_HUMAN 229 42 -
MFAFFAQHFTHQFFKT PGH1_SHEEP 197 35 -

Motif 3 width=19
Element Seqn Id St Int Rpt
MAVGQEVFGLLPGLMLYAT PGH1_SHEEP 285 72 -
FLAGDTRSTETPKLAAMHT PERE_HUMAN 359 132 -
FLAGDGRASEVPSLTALHT PERU_HUMAN 390 145 -
YRSGDVRVNQNPGLAILQT PERO_DROME 325 134 -
FLAGDGRASEVPALAAVHT PERT_MOUSE 378 139 -
FLAGDFRASEQILLATAHT PERL_BOVIN 366 134 -
FSVGQEVFGLVPGLMMYAT PGH2_CHICK 271 72 -
FLAGDMRSSEMPELTSMHT PERM_MOUSE 373 132 -

Motif 4 width=21
Element Seqn Id St Int Rpt
TLFMREHNRLATELRRLNPRW PERE_HUMAN 377 -1 -
TLWLREHNRLAAALKALNAHW PERU_HUMAN 408 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_CHICK 289 -1 -
TIWLREHNRVCDLLKAEHPTW PGH1_SHEEP 303 -1 -
TLFVREHNRLATQLKRLNPRW PERM_MOUSE 391 -1 -
TLLLREHNRLARELKKLNPHW PERL_BOVIN 384 -1 -
TLWLREHNRLASAFKAINKHW PERT_MOUSE 396 -1 -
TILLREHNRIADALSALNPHY PERO_DROME 343 -1 -

Motif 5 width=27
Element Seqn Id St Int Rpt
LYQEARKILGAFIQIITFRDYLPIVLG PERL_BOVIN 409 4 -
VYQEARKVVGALHQIITLRDYIPRILG PERU_HUMAN 433 4 -
LFQEARKINIAQYQQISYYEWLPIFLG PERO_DROME 368 4 -
AYQEARKVVGALHQIITMRDYIPKILG PERT_MOUSE 421 4 -
LFQTTRLILIGETIKIVIEDYVQHLSG PGH2_CHICK 314 4 -
LFQTARLILIGETIKIVIEEYVQQLSG PGH1_SHEEP 328 4 -
LYQEARKIVGAMVQIITYRDYLPLVLG PERM_MOUSE 416 4 -
LYNEARKIMGAMVQIITYRDFLPLVLG PERE_HUMAN 402 4 -

Motif 6 width=11
Element Seqn Id St Int Rpt
TAAFRFGHATV PERT_MOUSE 475 27 -
FNTLYHWHPLL PGH2_CHICK 367 26 -
FNQLYHWHPLM PGH1_SHEEP 381 26 -
TNAFRYGHTLI PERM_MOUSE 469 26 -
TLAFRFGHTML PERE_HUMAN 455 26 -
TFAFRFGHMEV PERL_BOVIN 461 25 -
TAAFRYFHSQI PERO_DROME 430 35 -
TAAFRFGHATI PERU_HUMAN 487 27 -

Motif 7 width=21
Element Seqn Id St Int Rpt
SPPILEKLKSLYPSHEDVDLT PERO_DROME 552 111 -
EKEMAAELEELYGDIDAMELY PGH2_CHICK 470 92 -
EKEMAAELEELYGDIDALEFY PGH1_SHEEP 484 92 -
NLELARKLMAQYGTPNNIDIW PERM_MOUSE 597 117 -
NQDLARKFLNLYGTPDNIDIW PERE_HUMAN 583 117 -
SRSVADKILDLYKHPDNIDVW PERU_HUMAN 558 60 -
NKILAKKLMDLYKTPDNIDIW PERL_BOVIN 590 118 -
NRSMVNKIMDLYKHADNIDVW PERT_MOUSE 603 117 -

Motif 8 width=15
Element Seqn Id St Int Rpt
VKTATLKKLVCLNTK PGH1_SHEEP 559 54 -
LASISLPRLICDNTG PERM_MOUSE 668 50 -
LRKASMARLLCDNGN PERO_DROME 626 53 -
LEKHSLPRVICDNTG PERT_MOUSE 674 50 -
INTASLQKLICNNVK PGH2_CHICK 545 54 -
LEKHSLSRVICDNTG PERU_HUMAN 629 50 -
LSRISLSRIICDNTG PERE_HUMAN 653 49 -
LQKVSFSRLICDNTH PERL_BOVIN 661 50 -
Final Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
RALPPVPDDCPT PGH2_SHEEP 135 135 -
RALPPVADDCPT PGH2_RABIT 136 136 -
RALPPVPDDCPT PGH2_BOVIN 136 136 -
RALPPVPDDCPT PGH2_HUMAN 136 136 -
RALPPVADDCPT Q63124 136 136 -
RALPPVADDCPT PGH2_RAT 136 136 -
RALPPVADDCPT PGH2_MOUSE 136 136 -
RALPPVADGCPT PGH2_HORSE 136 136 -
RALPPVADDCPT PGH2_CAVPO 136 136 -
RSLPPVGHDCPT PGH2_CHICK 136 136 -
RALPPVADDCPT PGH2_MUSVI 136 136 -
RILPSVPKDCPT PGH1_MOUSE 152 152 -
RILPSVPKDCPT PGH1_RAT 152 152 -
RILPSVPRDCPT PGH1_SHEEP 150 150 -
RILPSVPKDCPT PGH1_HUMAN 149 149 -
RWLPAEYEDGVS PERM_MOUSE 171 171 -
RWLPAEYEDGFS PERM_HUMAN 197 197 -
RWLPPVYEDGFS PERT_HUMAN 175 175 -
RWLPAEYEDGLS Q13408 162 162 -
RWLPAEYEDGLS PERE_HUMAN 157 157 -
RWLPAEYEDGLA PERL_BOVIN 162 162 -
RWLPPVYEDGFS PERT_RAT 169 169 -
RWLPPVYEDGFS PERT_MOUSE 169 169 -
RWLPPAYEDGVT PERT_PIG 175 175 -
RWLPAEYEDHRS PERE_MOUSE 170 170 -
RLLDPAYDDGFD Q18647 856 856 -
RILPPTYDDGVH Q26059 271 271 -
RLLPTIYDNEVS Q19950 487 487 -
RLLKPVYENGFN O44087 373 373 -
RLAPPIYENGFS Q23991 805 805 -
RHFPAQYDDGKG Q23490 215 215 -
RLLPPAYEDGID O17241 686 686 -
RLLTPKYADGIS PERO_DROME 129 129 -

Motif 2 width=16
Element Seqn Id St Int Rpt
MFAFFAQHFTHQFFKT PGH2_SHEEP 182 35 -
MFAFFAQHFTHQFFKT PGH2_RABIT 183 35 -
MFAFFAQHFTHQFFKT PGH2_BOVIN 183 35 -
MFAFFAQHFTHQFFKT PGH2_HUMAN 183 35 -
MFAFFAQHFTHQFFKT Q63124 183 35 -
MFAFFAQHFTHQFFKT PGH2_RAT 183 35 -
MFAFFAQHFTHQFFKT PGH2_MOUSE 183 35 -
MFAFFAQHFTHQFFKT PGH2_HORSE 183 35 -
MFAFFAQHFTHQFFKS PGH2_CAVPO 183 35 -
MFTFFAQHFTHQFFKT PGH2_CHICK 183 35 -
MFAFFAQHFTHQFFKT PGH2_MUSVI 183 35 -
LFAFFAQHFTHQFFKT PGH1_MOUSE 199 35 -
LFAFFAQHFTHQFFKT PGH1_RAT 199 35 -
MFAFFAQHFTHQFFKT PGH1_SHEEP 197 35 -
MFAFFAQHFTHQFFKT PGH1_HUMAN 196 35 -
MFMQWGQFLDHDITLT PERM_MOUSE 225 42 -
MFMQWGQLLDHDLDFT PERM_HUMAN 251 42 -
LLMAWGQYIDHDIAFT PERT_HUMAN 229 42 -
LFMQWGQIVDHDLDFA Q13408 216 42 -
MFMQWGQFIDHDLDFS PERE_HUMAN 211 42 -
LFMQWGQIVDHDLDFA PERL_BOVIN 216 42 -
FLPVWGQYIDHDIALT PERT_RAT 223 42 -
FLPVWGQYIDHDIALT PERT_MOUSE 223 42 -
LLMAWGQYIDHDIAFT PERT_PIG 229 42 -
MFMQWGQFIDHDLDFS PERE_MOUSE 224 42 -
MLMQFGQILDHDMMHS Q18647 903 35 -
SVMQWAQFIDHEFAHV Q26059 318 35 -
LIMQFGQFISHDMAKT Q19950 534 35 -
MVMQWGQFVDHDLTHT O44087 425 40 -
MVMQWGQFLDHDLDHA Q23991 857 40 -
MMMQWGQFMSHDMSKT Q23490 261 34 -
FVMEFGQFIDHDITHS O17241 733 35 -
HNMQWGQIMTHDMSMQ PERO_DROME 175 34 -

Motif 3 width=19
Element Seqn Id St Int Rpt
FAVGQEVFGLVPGLMMYAT PGH2_SHEEP 270 72 -
FAVGQEVFGLVPGLMMYAT PGH2_RABIT 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_BOVIN 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_HUMAN 271 72 -
FAVGQEVFGLVPGLMMYAT Q63124 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_RAT 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_MOUSE 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_HORSE 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_CAVPO 271 72 -
FSVGQEVFGLVPGLMMYAT PGH2_CHICK 271 72 -
FAVGQEVFGLVPGLMMYAT PGH2_MUSVI 271 72 -
MAVGQEVFGLLPGLMLFST PGH1_MOUSE 287 72 -
MAVGQEVFGLLPGLMLFST PGH1_RAT 287 72 -
MAVGQEVFGLLPGLMLYAT PGH1_SHEEP 285 72 -
MAVGQEVFGLLPGLMLYAT PGH1_HUMAN 284 72 -
FLAGDMRSSEMPELTSMHT PERM_MOUSE 373 132 -
FLAGDTRSSEMPELTSMHT PERM_HUMAN 399 132 -
FLAGDGRASEVPSLTALHT PERT_HUMAN 390 145 -
FLAGDSRASEHILLATSHT Q13408 366 134 -
FLAGDTRSTETPKLAAMHT PERE_HUMAN 359 132 -
FLAGDFRASEQILLATAHT PERL_BOVIN 366 134 -
FLAGDGRASEVPALAAVHT PERT_RAT 378 139 -
FLAGDGRASEVPALAAVHT PERT_MOUSE 378 139 -
FLAGDSRASEVPGLTALHT PERT_PIG 389 144 -
FLAGDTRSSETPKLTALHT PERE_MOUSE 372 132 -
FVAGDERSNEQPGLTAIHN Q18647 1050 131 -
FMAGDSRVNEQPGLTALHT Q26059 463 129 -
FTAGDSRVNLFVGLSAWHT Q19950 666 116 -
FLAGDLRANEQLALAATHT O44087 583 142 -
FVSGDIRVNEQVGLLAMHT Q23991 1010 137 -
FTAGDIRANLFIGLSSLHI Q23490 390 113 -
FIAGDDRNSQQTLLIAVHS O17241 877 128 -
YRSGDVRVNQNPGLAILQT PERO_DROME 325 134 -

Motif 4 width=21
Element Seqn Id St Int Rpt
TIWLREHNRVCDVLKQEHPEW PGH2_SHEEP 288 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_RABIT 289 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_BOVIN 289 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_HUMAN 289 -1 -
TIWLREHNRVCDILKQEHPEW Q63124 289 -1 -
TIWLREHNRVCDILKQEHPEW PGH2_RAT 289 -1 -
TIWLREHNRVCDILKQEHPEW PGH2_MOUSE 289 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_HORSE 289 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_CAVPO 289 -1 -
TIWLREHNRVCDVLKQEHPEW PGH2_CHICK 289 -1 -
TIWLREHNRVCDVLKQEQGEW PGH2_MUSVI 289 -1 -
TIWLREHNRVCDLLKEEHPTW PGH1_MOUSE 305 -1 -
TIWLREHNRVCDLLKEEHPTW PGH1_RAT 305 -1 -
TIWLREHNRVCDLLKAEHPTW PGH1_SHEEP 303 -1 -
TLWLREHNRVCDLLKAEHPTW PGH1_HUMAN 302 -1 -
TLFVREHNRLATQLKRLNPRW PERM_MOUSE 391 -1 -
TLLLREHNRLATELKSLNPRW PERM_HUMAN 417 -1 -
TLWLREHNRLAAALKALNAHW PERT_HUMAN 408 -1 -
TLFLREHNRLARELKRLNPQW Q13408 384 -1 -
TLFMREHNRLATELRRLNPRW PERE_HUMAN 377 -1 -
TLLLREHNRLARELKKLNPHW PERL_BOVIN 384 -1 -
TLWLREHNRLATAFKAINTHW PERT_RAT 396 -1 -
TLWLREHNRLASAFKAINKHW PERT_MOUSE 396 -1 -
TLWLREHNRLAAAFKALNAHW PERT_PIG 407 -1 -
TLFVREHNRLAAELRRLNPHW PERE_MOUSE 390 -1 -
NIFLREHNRIARYLKQINNFW Q18647 1068 -1 -
TLLVRQHNLVARDLKALNPQW Q26059 481 -1 -
TIFTEEHNRLVTAFKRLNPHW Q19950 684 -1 -
TIFIREHNRIAKKLKSMNGNW O44087 601 -1 -
TIWMREHNRIASKLKQINSHW Q23991 1028 -1 -
IMFAREHNRIAQKLTELNPTW Q23490 408 -1 -
SVFHREHERITTTLKEINPNW O17241 895 -1 -
TILLREHNRIADALSALNPHY PERO_DROME 343 -1 -

Motif 5 width=27
Element Seqn Id St Int Rpt
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_SHEEP 313 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_RABIT 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_BOVIN 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_HUMAN 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG Q63124 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_RAT 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_MOUSE 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_HORSE 314 4 -
LFQTSRLILIGETIKIVIEDYVQHLSG PGH2_CAVPO 314 4 -
LFQTTRLILIGETIKIVIEDYVQHLSG PGH2_CHICK 314 4 -
LFRRSRLILIGETIKIVIEDYVRHLSG PGH2_MUSVI 314 4 -
LFQTTRLILIGETIKIVIEEYVQHLSG PGH1_MOUSE 330 4 -
LFQTTRLILIGETIKIIIEEYVQHLSG PGH1_RAT 330 4 -
LFQTARLILIGETIKIVIEEYVQQLSG PGH1_SHEEP 328 4 -
LFQTTRLILIGETIKIVIEEYVQQLSG PGH1_HUMAN 327 4 -
LYQEARKIVGAMVQIITYRDYLPLVLG PERM_MOUSE 416 4 -
LYQEARKIVGAMVQIITYRDYLPLVLG PERM_HUMAN 442 4 -
VYQEARKVVGALHQIITLRDYIPRILG PERT_HUMAN 433 4 -
LYQEARKILGAFVQIITFRDYLPILLG Q13408 409 4 -
LYNEARKIMGAMVQIITYRDFLPLVLG PERE_HUMAN 402 4 -
LYQEARKILGAFIQIITFRDYLPIVLG PERL_BOVIN 409 4 -
AYQEARKVVGALHQIITMRDYIPKILG PERT_RAT 421 4 -
AYQEARKVVGALHQIITMRDYIPKILG PERT_MOUSE 421 4 -
VYQEARKVVGALHQIVTLRDYVPKILG PERT_PIG 432 4 -
LYNEARKIVGAMVQIITYRDFLPLVLG PERE_MOUSE 415 4 -
LFQESRRINIAQLQHIIYKEWLPVVLG Q18647 1093 4 -
LFQETRRIIIAQTQHIIFNEWLPIILG Q26059 506 4 -
LYQEARKMIGAQVQAIVYREWLPKVLG Q19950 709 4 -
IYHETRKIVGAMMQHITYKHWMPIIFG O44087 626 4 -
LYQEARKIVGAQMQHITFKQWLPLIIG Q23991 1053 4 -
VFQEARKIVGAQIQNVLYKEYLPKLLG Q23490 433 4 -
IYQETRKLISAEFAHIVYNEYLPIIIG O17241 920 4 -
LFQEARKINIAQYQQISYYEWLPIFLG PERO_DROME 368 4 -

Motif 6 width=11
Element Seqn Id St Int Rpt
FNTLYHWHPLL PGH2_SHEEP 366 26 -
FNTLYHWHPLL PGH2_RABIT 367 26 -
FNTLYHWHPLL PGH2_BOVIN 367 26 -
FNTLYHWHPLL PGH2_HUMAN 367 26 -
FNTLYHWHPLL Q63124 367 26 -
FNTLYHWHPLL PGH2_RAT 367 26 -
FNTLYHWHPLL PGH2_MOUSE 367 26 -
FNTLYHWHPLL PGH2_HORSE 367 26 -
FNTLYHWHPLL PGH2_CAVPO 367 26 -
FNTLYHWHPLL PGH2_CHICK 367 26 -
FNTLYHWHPLL PGH2_MUSVI 367 26 -
FNHLYHWHPLM PGH1_MOUSE 383 26 -
FNHLYHWHPLM PGH1_RAT 383 26 -
FNQLYHWHPLM PGH1_SHEEP 381 26 -
FNHLYHWHPLM PGH1_HUMAN 380 26 -
TNAFRYGHTLI PERM_MOUSE 469 26 -
TNAFRYGHTLI PERM_HUMAN 495 26 -
TAAFRFGHATI PERT_HUMAN 487 27 -
TFAFRFGHLEV Q13408 461 25 -
TLAFRFGHTML PERE_HUMAN 455 26 -
TFAFRFGHMEV PERL_BOVIN 461 25 -
TAAFRFGHATV PERT_RAT 475 27 -
TAAFRFGHATV PERT_MOUSE 475 27 -
TAAFRFGHATI PERT_PIG 486 27 -
TLAFRFGHTML PERE_MOUSE 468 26 -
TSAFRFGHSLI Q18647 1153 33 -
TAAFRFGHTLV Q26059 566 33 -
SAAFRFGHGMI Q19950 762 26 -
TAAFRFGHTII O44087 681 28 -
TAALRFGHTII Q23991 1105 25 -
TSAFRFGHGMI Q23490 486 26 -
TAAFRFGHSTV O17241 979 32 -
TAAFRYFHSQI PERO_DROME 430 35 -

Motif 7 width=21
Element Seqn Id St Int Rpt
EKEMAAELEALYGDIDAMELY PGH2_SHEEP 469 92 -
EKEMAAELEALYGDIDAVELY PGH2_RABIT 470 92 -
EKEMAAELEALYGDIDAMEFY PGH2_BOVIN 470 92 -
EKEMSAELEALYGDIDAVELY PGH2_HUMAN 470 92 -
EKEMAAELKALYHDIDAMELY Q63124 470 92 -
EKEMAAELKALYHDIDAMELY PGH2_RAT 470 92 -
EKEMAAELKALYSDIDVMELY PGH2_MOUSE 470 92 -
EKEMAAELEALYGDIDAMELY PGH2_HORSE 470 92 -
EKEMAAGLEALYGDIDAMELY PGH2_CAVPO 470 92 -
EKEMAAELEELYGDIDAMELY PGH2_CHICK 470 92 -
EKEMAGELKALYQDIDAMELY PGH2_MUSVI 470 92 -
EKEMAAELEELYGDIDALEFY PGH1_MOUSE 486 92 -
EKEMAAELEELYGDIDALEFY PGH1_RAT 486 92 -
EKEMAAELEELYGDIDALEFY PGH1_SHEEP 484 92 -
EKEMAAELEELYGDIDALEFY PGH1_HUMAN 483 92 -
NLELARKLMAQYGTPNNIDIW PERM_MOUSE 597 117 -
NLKLARKLMEQYGTPNNIDIW PERM_HUMAN 623 117 -
SRSVADKILDLYKHPDNIDVW PERT_HUMAN 615 117 -
SKMLAKKLLGLYGTPDNIDIW Q13408 590 118 -
NQDLARKFLNLYGTPDNIDIW PERE_HUMAN 583 117 -
NKILAKKLMDLYKTPDNIDIW PERL_BOVIN 590 118 -
NRSMVNKIMELYKHADNIDVW PERT_RAT 603 117 -
NRSMVNKIMDLYKHADNIDVW PERT_MOUSE 603 117 -
NGRVADRILGLYQHPDNIDVW PERT_PIG 613 116 -
NQDLARKFLRLYKTPDNIDIW PERE_MOUSE 596 117 -
NSEAVTALETAYAHVDDIDLF Q18647 1280 116 -
SPENVQKLARIYKNVDDIDLF Q26059 688 111 -
NTGTRNKLQEIYGSVDKIDLW Q19950 881 108 -
DDMIIQKLRGLYGVPQNIDLW O44087 808 116 -
SAEIRQKMKELYGHPDNVDVW Q23991 1232 116 -
DRNLRAGLARNYNTTNDVDFY Q23490 605 108 -
NQDGLTAIGKVYESPDDIDLF O17241 1104 114 -
SPPILEKLKSLYPSHEDVDLT PERO_DROME 552 111 -

Motif 8 width=15
Element Seqn Id St Int Rpt
INTASIQSLICSNVK PGH2_SHEEP 544 54 -
VNTASIQSLICNNVK PGH2_RABIT 545 54 -
INTASIQSLICSNVK PGH2_BOVIN 545 54 -
INTASIQSLICNNVK PGH2_HUMAN 545 54 -
INTASIQSLICNNVK Q63124 545 54 -
INTASIQSLICNNVK PGH2_RAT 545 54 -
INTASIQSLICNNVK PGH2_MOUSE 545 54 -
INTASIQSLICNNVK PGH2_HORSE 545 54 -
VNTASIQSLICNNVK PGH2_CAVPO 545 54 -
INTASLQKLICNNVK PGH2_CHICK 545 54 -
INTASIQSLICNNVK PGH2_MUSVI 545 54 -
VNTASLKKLVCLNTK PGH1_MOUSE 561 54 -
VNTASLKKLVCLNTK PGH1_RAT 561 54 -
VKTATLKKLVCLNTK PGH1_SHEEP 559 54 -
VKTATLKKLVCLNTK PGH1_HUMAN 558 54 -
LASISLPRLICDNTG PERM_MOUSE 668 50 -
LAQISLPRIICDNTG PERM_HUMAN 694 50 -
LEKHSLSRVICDNTG PERT_HUMAN 686 50 -
LQKMSFSRLVCDNTR Q13408 661 50 -
LSRISLSRIICDNTG PERE_HUMAN 653 49 -
LQKVSFSRLICDNTH PERL_BOVIN 661 50 -
LEKHSLPRVICDNTG PERT_RAT 674 50 -
LEKHSLPRVICDNTG PERT_MOUSE 674 50 -
LSRHSMSRVICDNSG PERT_PIG 684 50 -
LRRISLSRIVCDNTG PERE_MOUSE 667 50 -
IRKASLSRIICDNSE Q18647 1354 53 -
IRASSWARIICDTAN Q26059 762 53 -
IRKSSLSRIICDNTN Q19950 952 50 -
IKKITLARLFCDNGD O44087 879 50 -
IKQANFGRVLCDVGD Q23991 1303 50 -
IKKSSLSRIICDNAD Q23490 676 50 -
VRKTSMSALICANTK O17241 1178 53 -
LRKASMARLLCDNGN PERO_DROME 626 53 -