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PR00408

Identifier
MITP450  [View Relations]  [View Alignment]  
Accession
PR00408
No. of Motifs
4
Creation Date
09-DEC-1999
Title
Mitochondrial P450 clan signature
Database References
PRINTS; PR00385 P450; PR01238 MITP450CC24
INTERPRO; IPR002399
PDB; 2HPD
SCOP; 2HPD
CATH; 2HPD
Literature References
1. NOMENCLATURE COMMITTEE OF THE INTERNATIONAL UNION OF BIOCHEMISTRY (NC-IUB).
Nomenclature of electron-transfer proteins. Recommendations 1989.
EUR.J.BIOCHEMISTRY 200 599-611 (1991).
 
2. NELSON, D.R.
Metazoan Cytochrome P450 evolution.
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY PART C 121 (1998).
 
3. DEGTYARENKO, K.N. AND ARCHAKOV, A.I.
Molecular evolution of P450 superfamily and P450-containing monooxygenase
systems.
FEBS LETT. 322 1-8 (1993).
 
4. RUETTINGER, R.T., WEN, L.P. AND FULCO, A.J.
Coding nucleotide, 5' regulatory, and deduced amino acid sequences of
P450BM-3, a single peptide cytochrome P450:NADPH-P450 reductase from
Bactillus megaterium.
J.BIOL.CHEM. 264 10987-10995 (1989).
 
5. NELSON, D.R., KAMATAKI, T., WAXMAN, D.J., GUENGERICH, F.P,
ESTABROOK, R.W., FEYEREISEN,R., GONZALEZ, F.J., COON, M.J., GUNSALUS, I.C., GOTOH, O.,
OKUDA, K. AND NERBERT, D.W.
The P450 superfamily:update on new sequences, gene mapping, accession
numbers, early trivial names of enzymes, and nomenclature.
DNA CELL BIOL. 12 1-51 (1993).
 
6. HANUKOGLU, I.
Steroidogenic enzymes: structure, function and regulation of expression.
J.STEROID BIOCHEM.MOL.BIOL. 43 770-804 (1992).
 
7. SAKAGUCHI, M. AND OMURA, T.
Topology and biogenesis of microsomal cytochrome P-450s.
FRONT.BIOTRANSFORM. 8 60-73 (1993).
 
8. MATTESON, K.J., CHUNG, B.C., URDEA, M.S. AND MILLER, W.L.
Study of cholestrol side chain cleavage (20,22 desmolase) deficiency causing
congenital lipid adrenal hyperplasia using bovine-sequence P450scc
oligodeoxyribonucleotide probes.
ENDOCRINOLOGY 118 1296-1305 (1986).
 
9. NOMURA, M., MOROHASHI, K., KIRITA, S., NONAKA, Y., OKAMOTO, M.M.,
NAWATA, H. AND OMURA, T.
Three forms of rat CYP11B genes: 11 beta-hydroxylase gene, aldosterone
synthase gene and a novel gene.
J.BIOCHEMISTRY 113 144-152 (1993).
 
10. CALI, J.J. AND RUSSELL, D.W.
Characterization of human sterol 27 hydroxylase. A mitochondrial cytochrome
P450 that catalyses multiple oxidation reaction in bile acid biosynthesis.
J.BIOL.CHEM. 266 7774-7778 (1991).
 
11. TEUNISSEN, Y., GERAERTS, W.P., VAN HEERIKHUIZEN, H., PLANTA, R.J. AND
JOOSSE, J.
Molecular cloning of a cDNA encoding a member of a novel cytochrome P450
family in the mollusc Lymnaea stagnalis.
J.BIOCHEMISTRY 112 249-252 (1992).

Documentation
P450 enzymes constitute a superfamily of haem-thiolate proteins [1],
widely distributed in bacteria, fungi, plants and animals. The enzymes
are involved in metabolism of a plethora of both exogenous and endogenous
compounds [2]. Usually, they act as terminal oxidases in multi-component
electron transfer chains, called P450-containing monooxygenase systems. 
 
P450-containing monooxygenase systems primarily fall into 2 major classes:
bacterial/mitochondrial (type I); and microsomal (type II). Alternatively,
P450-containing systems can be classified according to the number of their
protein components [3]: mitochondrial and most bacterial P450 systems have
3 components - an FAD-containing flavoprotein (NADPH or NADH-dependent
reductase), an iron-sulphur protein, and P450; the eukaryotic microsomal 
P450 system contains 2 components - NADPH:P450 reductase (a flavoprotein
containing both FAD and FMN) and P450; and a soluble monooxygenase P450BM-3
from Bacillus megaterium exists as a single polypeptide chain with 2 
functional parts (the haem and flavin domains), and represents a unique 
bacterial one-component system - sequence and functional comparisons show
that these domains are more similar to P450 and the flavoprotein of the
microsomal 2-component P450 monooxygenase system than to the relevant
proteins of the 3-component system [4].
 
Current P450 nomenclature, based on divergent evolution of the P450 
superfamily, was proposed and developed by Nebert et al. [5]. On the basis 
of sequence similarity, all P450s can be categorised into 2 main groups, 
the so-called B- and E-classes: P450 proteins of prokaryotic 3-component 
systems and fungal P450nor (CYP55) belong to the B-class; all other known 
P450s from distinct systems are of the E-class. The data suggest that 
divergence of the P450 superfamily into B- and E-classes, and further 
divergence into stable P450 groups within the E-class, must be very ancient
and had occured before the appearance of eukaryotes. 
 
By contrast with the B-class, containing water-soluble haemoproteins, 
most E-class P450s are membrane-bound. Membranous P450s can be divided into
those from the inner mitochondrial membrane (mitochondrial type), and those
from membranes of the endoplasmic reticulum (ER) (microsomal type). In the
mitochondrial P450-containing monooxygenase system, P450 can be reduced by
the 2Fe-2S iron-sulphur protein adrenodoxin, which can accept electrons
from NADPH-dependent adrenodoxin reductase. Both adrenodoxin and
adrenodoxin reductase are soluble, and located in the mitochondrial matrix 
[6]. Microsomal P450s depend on a single NADPH:P450 reductase; the P450s
and the reductase are located on the cytosolic side of the ER membrane, and
are anchored to the membrane by hydrophobic amino-terminal segments [7].  
 
To date, only animal mitochondrial P450s have been sequenced. P450scc
(CYP11A) is responsible for conversion of cholesterol to pregnenolone [8].
P450s from the CYP11B subfamily catalyse 11-beta- or 18-hydroxylation of
steroids [9]. The CYP27 family contain enzymes involved in 25-hydroxylation
of vitamin D3 and sterol 26- and 27-hydroxylation [10]. P450 from pond
snail (CYP10) is highly similar to the mitochondrial P450, although its
cellular location is unknown [11].  
 
MITP450 is a 4-element fingerprint that provides a signature for 
mitochondrial P450s. The fingerprint was derived from an initial alignment
of 7 sequences: the motifs were drawn from conserved regions spanning the 
N-terminal half of the alignment, focusing on those sections that 
characterise mitochondrial P450S but distinguish them from the rest of the
P450 superfamily. Two iterations on SPTR37_10f were required to reach 
convergence, at which point a true set comprising 32 sequences was 
identified. Several partial matches were also found, the majority of which
are mitochondrial P450s. The fingerprint does not distinguish the CC24
P450s, which show distinct sequence differences from the rest of the
mitochondrial P450 proteins (see signature MITP450CC24). Most matches
with two motifs are noise. 
Summary Information
  32 codes involving  4 elements
3 codes involving 3 elements
2 codes involving 2 elements
Composite Feature Index
432323232
32133
21111
1234
True Positives
CP27_HUMAN    CP27_RABIT    CP27_RAT      CP2B_HUMAN    
CP2B_MOUSE CP2B_RAT CPM1_BOVIN CPM1_CAPHI
CPM1_HUMAN CPM1_ONCMY CPM1_PIG CPM1_RAT
CPM1_SHEEP CPN1_BOVIN CPN1_CAVPO CPN1_HUMAN
CPN1_MESAU CPN1_PAPHA CPN1_PIG CPN1_RAT
CPN1_SHEEP CPN2_HUMAN CPN2_MESAU CPN2_MOUSE
CPN2_RAT CPN3_RAT O46515 Q64539
Q64546 Q64586 Q64615 Q9Z0M2
True Positive Partials
Codes involving 3 elements
CPN1_RANCA O13254 Q64639
Codes involving 2 elements
O73852 Q15081
Sequence Titles
CP27_HUMAN  STEROL 26-HYDROXYLASE, MITOCHONDRIAL PRECURSOR (EC 1.14.-.-) (VITAMIN D(3) 25-HYDROXYLASE) (5-BETA-CHOLESTANE-3-ALPHA,7-ALPHA,12-ALPHA-TRIOL 27-HYDROXYLASE) - HOMO SAPIENS (HUMAN). 
CP27_RABIT STEROL 26-HYDROXYLASE, MITOCHONDRIAL PRECURSOR (EC 1.14.-.-) (VITAMIN D(3) 25-HYDROXYLASE) (5-BETA-CHOLESTANE-3-ALPHA,7-ALPHA,12-ALPHA-TRIOL 27-HYDROXYLASE) - ORYCTOLAGUS CUNICULUS (RABBIT).
CP27_RAT STEROL 26-HYDROXYLASE, MITOCHONDRIAL PRECURSOR (EC 1.14.-.-) (VITAMIN D(3) 25-HYDROXYLASE) (5-BETA-CHOLESTANE-3-ALPHA,7-ALPHA,12-ALPHA-TRIOL 27-HYDROXYLASE) - RATTUS NORVEGICUS (RAT).
CP2B_HUMAN 25-HYDROXYVITAMIN D-1 ALPHA HYDROXYLASE, MITOCHONDRIAL PRECURSOR (EC 1.14.-.-) (25-OHD-1 ALPHA-HYDROXYLASE) (25-HYDROXYVITAMIN D3 1- ALPHA-HYDROXYLASE) (VD3 1A HYDROXYLASE) (P450C1 ALPHA) (P450VD1- ALPHA) - HOMO SAPIENS (HUMAN).
CP2B_MOUSE 25-HYDROXYVITAMIN D-1 ALPHA HYDROXYLASE, MITOCHONDRIAL PRECURSOR (EC 1.14.-.-) (25-OHD-1 ALPHA-HYDROXYLASE) (25-HYDROXYVITAMIN D3 1- ALPHA-HYDROXYLASE) (VD3 1A HYDROXYLASE) (P450C1 ALPHA) (P450VD1- ALPHA) - MUS MUSCULUS (MOUSE).
CP2B_RAT 25-HYDROXYVITAMIN D-1 ALPHA HYDROXYLASE, MITOCHONDRIAL PRECURSOR (EC 1.14.-.-) (25-OHD-1 ALPHA-HYDROXYLASE) (25-HYDROXYVITAMIN D3 1- ALPHA-HYDROXYLASE) (VD3 1A HYDROXYLASE) (P450C1 ALPHA) (P450VD1- ALPHA) - RATTUS NORVEGICUS (RAT).
CPM1_BOVIN CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - BOS TAURUS (BOVINE).
CPM1_CAPHI CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - CAPRA HIRCUS (GOAT).
CPM1_HUMAN CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - HOMO SAPIENS (HUMAN).
CPM1_ONCMY CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - ONCORHYNCHUS MYKISS (RAINBOW TROUT) (SALMO GAIRDNERI).
CPM1_PIG CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - SUS SCROFA (PIG).
CPM1_RAT CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - RATTUS NORVEGICUS (RAT).
CPM1_SHEEP CYTOCHROME P450 11A1, MITOCHONDRIAL PRECURSOR (EC 1.14.15.6) (CYPXIA1) (P450(SCC)) (CHOLESTEROL SIDE-CHAIN CLEAVAGE ENZYME) (CHOLESTEROL DESMOLASE) - OVIS ARIES (SHEEP).
CPN1_BOVIN CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) - BOS TAURUS (BOVINE).
CPN1_CAVPO CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) (ALDOSTERONE SYNTHASE) - CAVIA PORCELLUS (GUINEA PIG).
CPN1_HUMAN CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) - HOMO SAPIENS (HUMAN).
CPN1_MESAU CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) - MESOCRICETUS AURATUS (GOLDEN HAMSTER).
CPN1_PAPHA CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) - PAPIO HAMADRYAS (HAMADRYAS BABOON).
CPN1_PIG CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) - SUS SCROFA (PIG).
CPN1_RAT CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) (P450(11 BETA)-DS) - RATTUS NORVEGICUS (RAT).
CPN1_SHEEP CYTOCHROME P450 11B1 PRECURSOR (EC 1.14.15.4) (CYPXIB1) (P450C11) (STEROID 11-BETA-HYDROXYLASE) - OVIS ARIES (SHEEP).
CPN2_HUMAN CYTOCHROME P450 11B2 PRECURSOR (EC 1.14.15.4) (CYPXIB2) (P-450ALDO) (ALDOSTERONE SYNTHASE) (ALDOS) (ALDOSTERONE-SYNTHESIZING ENZYME) (STEROID 18-HYDROXYLASE) (P-450C18) - HOMO SAPIENS (HUMAN).
CPN2_MESAU CYTOCHROME P450 11B2 PRECURSOR (EC 1.14.15.4) (C450XIB2) (ALDOSTERONE SYNTHASE) (P-450ALDO) (ALDOS) (ALDOSTERONE-SYNTHESIZING ENZYME) (STEROID 18-HYDROXYLASE) (P-450C18) - MESOCRICETUS AURATUS (GOLDEN HAMSTER).
CPN2_MOUSE CYTOCHROME P450 11B2 PRECURSOR (EC 1.14.15.4) (CYPXIB2) (P450C11) (STEROID 11-BETA-HYDROXYLASE) (ALDOSTERONE SYNTHASE) - MUS MUSCULUS (MOUSE).
CPN2_RAT CYTOCHROME P450 11B2 PRECURSOR (EC 1.14.15.4) (CYPXIB2) (P450-ALDO-1) (ALDOSTERONE SYNTHASE) - RATTUS NORVEGICUS (RAT).
CPN3_RAT CYTOCHROME P450 11B3 PRECURSOR (EC 1.14.15.4) (CYPXIB3) (P450-ALDO-2) (ALDOSTERONE SYNTHASE) - RATTUS NORVEGICUS (RAT).
O46515 CYTOCHROME P450 CHOLESTEROL SIDE-CHAIN CLEAVAGE - EQUUS CABALLUS (HORSE).
Q64539 CYTOCHROME P450 11-BETA (EC 1.14.14.1) - RATTUS NORVEGICUS (RAT).
Q64546 CYTOCHROME P450 C11B3 (EC 1.14.14.1) - RATTUS NORVEGICUS (RAT).
Q64586 CYTOCHROME P450 (STEROID 11-BETA-HYDROXYLASE) (EC 1.14.14.1) - RATTUS NORVEGICUS (RAT).
Q64615 CYTOCHROME P450 C27/25 (EC 1.14.14.1) - RATTUS NORVEGICUS (RAT).
Q9Z0M2 ALDOSTERONE SYNTHASE PRECURSOR (EC 1.14.15.4) - CAVIA PORCELLUS (GUINEA PIG).

CPN1_RANCA CYTOCHROME P450 11B PRECURSOR (EC 1.14.15.4) (CYPXIB) (P450C11) (STEROID 11-BETA-HYDROXYLASE) (P-450(11 BETA,ALDO)) - RANA CATESBEIANA (BULL FROG).
O13254 CYTOCHROME P450 SCC (EC 1.14.14.1) - GALLUS GALLUS (CHICKEN).
Q64639 CYTOCHROME P450 C27/25 (EC 1.14.14.1) - RATTUS NORVEGICUS (RAT).

O73852 CYTOCHROME P450 CHOLESTEROL SIDE CHAIN CLEAVAGE - ICTALURUS PUNCTATUS (CHANNEL CATFISH).
Q15081 CYTOCHROME P450XIA1 CYTOCHROME P-450 (SSC) EXON 1 (SSC) - HOMO SAPIENS (HUMAN).
Scan History
SPTR37_10f 2  500  NSINGLE    
Initial Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
AIPQYSRNKWLKMI CPN3_RAT 40 40 -
AMPQHPGNRWLRLL CPN2_HUMAN 40 40 -
EIPSPGDNGWLNLY CPM1_BOVIN 50 50 -
EIPGLWRNGLANLY CPM1_ONCMY 48 48 -
SLEELPRLGQLRFF CP27_RABIT 59 59 -
SLEEIPRLGQLRFF CP27_HUMAN 56 56 -
SLSDIPGPSTPSFL CP2B_RAT 29 29 -

Motif 2 width=11
Element Seqn Id St Int Rpt
HLEMHQAFQEL CPN3_RAT 65 11 -
HLEMHQTFQEL CPN2_HUMAN 65 11 -
HFRHIENFQKY CPM1_BOVIN 75 11 -
HRVMVHNFNTF CPM1_ONCMY 73 11 -
HKLQVLNKARY CP27_RABIT 85 12 -
HQLQVLYKAKY CP27_HUMAN 82 12 -
HELQVHGAARY CP2B_RAT 55 12 -

Motif 3 width=16
Element Seqn Id St Int Rpt
WVAHRELRGLRRGVFL CPN3_RAT 116 40 -
WVAYRQHRGHKCGVFL CPN2_HUMAN 116 40 -
WLAYHRYYQKPIGVLF CPM1_BOVIN 126 40 -
WTSYRDYRNRKYGVLL CPM1_ONCMY 124 40 -
WKEHRDHQDLAYGVFT CP27_RABIT 136 40 -
WKEHRDQHDLTYGPFT CP27_HUMAN 133 40 -
WSEHRRRHQRACGLLT CP2B_RAT 106 40 -

Motif 4 width=15
Element Seqn Id St Int Rpt
NVLSPKAVQNFVPMV CPN3_RAT 147 15 -
DVLSPKAVQRFLPMV CPN2_HUMAN 147 15 -
EVMAPEAIKNFIPLL CPM1_BOVIN 157 15 -
EVISPKVLGNFVPLL CPM1_ONCMY 155 15 -
RLLKPAEAALYTDAL CP27_RABIT 167 15 -
RLLKPAEAALYTDAF CP27_HUMAN 164 15 -
LLLRPQAAAGYAGTL CP2B_RAT 137 15 -
Final Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
AIPQYSRNKWLKMI CPN2_RAT 50 50 -
AIPQYSRNKWLKMI CPN3_RAT 40 40 -
AIPQYSRNKWLKMI Q64539 39 39 -
AIPQYSRNKWLKMI Q64586 39 39 -
AIPQYSRNKWLKMI Q64546 39 39 -
AIPQYSRNKWLKMI CPN1_RAT 40 40 -
AIPQYSRNKWLKMI CPN2_MOUSE 40 40 -
AMPQHPGNRWLRLL CPN2_HUMAN 40 40 -
AIPQYSRNRWLKML CPN2_MESAU 40 40 -
AIPQYSRNRWLKML CPN1_MESAU 40 40 -
AMPRRPGNRWLRLL CPN1_PAPHA 40 40 -
AIPQYLGNKWLRVL Q9Z0M2 41 41 -
AMPRRPGNRWLRLL CPN1_HUMAN 40 40 -
AIPQFPGKKWMRVL CPN1_PIG 40 40 -
AMPRCPGNKWMRML CPN1_BOVIN 40 40 -
AMPRCPGNKWMRVL CPN1_SHEEP 40 40 -
EIPSPGDNGWLNLY CPM1_HUMAN 50 50 -
EIPSPGDNGWINLY CPM1_PIG 50 50 -
EIPSPGDNGWLNLY CPM1_BOVIN 50 50 -
EIPSPGDNGWINLY CPM1_RAT 48 48 -
EIPSPGDNGWINLY CPM1_CAPHI 50 50 -
EIPSPGDNGWINLY CPM1_SHEEP 50 50 -
VIPQHQGNKRQRVL CPN1_CAVPO 41 41 -
EIPSPGDNGWINLY O46515 50 50 -
EIPGLWRNGLANLY CPM1_ONCMY 48 48 -
SLAELPGPGTLRFL CP27_RAT 58 58 -
SLEELPRLGQLRFF CP27_RABIT 59 59 -
SLAELPGPGTLRFL Q64615 58 58 -
SLSDIPGPSTLSFL CP2B_MOUSE 36 36 -
SLADIPGPSTPSFL CP2B_HUMAN 36 36 -
SLEEIPRLGQLRFF CP27_HUMAN 56 56 -
SLSDIPGPSTPSFL CP2B_RAT 29 29 -

Motif 2 width=11
Element Seqn Id St Int Rpt
HLEMHQAFQEL CPN2_RAT 75 11 -
HLEMHQAFQEL CPN3_RAT 65 11 -
HLEMHQAFQEL Q64539 64 11 -
HLEMHQAFQEL Q64586 64 11 -
HLEMHQAFQEL Q64546 64 11 -
HLEMHQAFQEL CPN1_RAT 65 11 -
HLEMHQVFREL CPN2_MOUSE 65 11 -
HLEMHQTFQEL CPN2_HUMAN 65 11 -
HLEMHEAFREL CPN2_MESAU 65 11 -
HLEMHEAFREL CPN1_MESAU 65 11 -
HLEVHQTFQEL CPN1_PAPHA 65 11 -
HLEMHRTFQEL Q9Z0M2 66 11 -
HLEVHQTFQEL CPN1_HUMAN 65 11 -
HLEMHQTFQEL CPN1_PIG 65 11 -
HLDMHQTFQEL CPN1_BOVIN 65 11 -
HLDMHQTFQEL CPN1_SHEEP 65 11 -
HLHHVQNFQKY CPM1_HUMAN 75 11 -
HYHHVQNFQKY CPM1_PIG 75 11 -
HFRHIENFQKY CPM1_BOVIN 75 11 -
HYHHMQNFQKY CPM1_RAT 73 11 -
HFRHIENFQKY CPM1_CAPHI 75 11 -
HFHHIENFQKY CPM1_SHEEP 75 11 -
HLEMHQTFQEL CPN1_CAVPO 66 11 -
HYHHFQNFQKY O46515 75 11 -
HRVMVHNFNTF CPM1_ONCMY 73 11 -
HELQALNKAKY CP27_RAT 84 12 -
HKLQVLNKARY CP27_RABIT 85 12 -
HELQALNKAKY Q64615 84 12 -
HELQVHGAARY CP2B_MOUSE 62 12 -
HELQVQGAAHF CP2B_HUMAN 62 12 -
HQLQVLYKAKY CP27_HUMAN 82 12 -
HELQVHGAARY CP2B_RAT 55 12 -

Motif 3 width=16
Element Seqn Id St Int Rpt
WVAHRELRGLRRGVFL CPN2_RAT 126 40 -
WVAHRELRGLRRGVFL CPN3_RAT 116 40 -
WVAHRELRGLRRGVFL Q64539 115 40 -
WVAHRELRGLRRGVFL Q64586 115 40 -
WVAHRELRGLRRGVFL Q64546 115 40 -
WVAHRELRGLRRGVFL CPN1_RAT 116 40 -
WVAHRELRGLRRGVFL CPN2_MOUSE 116 40 -
WVAYRQHRGHKCGVFL CPN2_HUMAN 116 40 -
WVAHREHRGLSRGVFL CPN2_MESAU 116 40 -
WVAHREHRGLSRGVFL CPN1_MESAU 116 40 -
WVAYRQHRGHKCGVFL CPN1_PAPHA 116 40 -
WMAYREHRGQKPGVFL Q9Z0M2 117 40 -
WVAYRQHRGHKCGVFL CPN1_HUMAN 116 40 -
WLAYRHLRGHKCGVFL CPN1_PIG 116 40 -
WLAYRQARGHKCGVFL CPN1_BOVIN 116 40 -
WLAYRQARGHKCGVFL CPN1_SHEEP 116 40 -
WVAYHQYYQRPIGVLL CPM1_HUMAN 126 40 -
WVAYHQHYQKPVGVLL CPM1_PIG 126 40 -
WLAYHRYYQKPIGVLF CPM1_BOVIN 126 40 -
WVAYHQYYQRPIGVLF CPM1_RAT 124 40 -
WLAYHQYYQKPIGVLF CPM1_CAPHI 126 40 -
WLAYHRYYQKPIGVLF CPM1_SHEEP 126 40 -
WMAYREHRRQNLGVFL CPN1_CAVPO 117 40 -
WTAYHQYFQKPVGVLF O46515 126 40 -
WTSYRDYRNRKYGVLL CPM1_ONCMY 124 40 -
WKEHRDHKGLSYGIFI CP27_RAT 135 40 -
WKEHRDHQDLAYGVFT CP27_RABIT 136 40 -
WKEHRDHKGLSYGIFI Q64615 135 40 -
WAEHRRRHQRACGLLT CP2B_MOUSE 113 40 -
WTEHRRCRQRACGLLT CP2B_HUMAN 113 40 -
WKEHRDQHDLTYGPFT CP27_HUMAN 133 40 -
WSEHRRRHQRACGLLT CP2B_RAT 106 40 -

Motif 4 width=15
Element Seqn Id St Int Rpt
NVLSPKAVQNFVPMV CPN2_RAT 157 15 -
NVLSPKAVQNFVPMV CPN3_RAT 147 15 -
NMLSPKAVQSFVPFV Q64539 146 15 -
NMLSPKAVQSFVPFV Q64586 146 15 -
NMLSPKAVQSFVPFV Q64546 146 15 -
NMLSPKAIQSFVPFV CPN1_RAT 147 15 -
NVLSPKAVQKFVPMV CPN2_MOUSE 147 15 -
DVLSPKAVQRFLPMV CPN2_HUMAN 147 15 -
HVLSPKAVQKFVPMV CPN2_MESAU 147 15 -
HMLSPKAVQKFVPMV CPN1_MESAU 147 15 -
DVLSPKAVQRFLPMV CPN1_PAPHA 147 15 -
NVLSPKAVQKFLPMV Q9Z0M2 148 15 -
EVLSPNAVQRFLPMV CPN1_HUMAN 147 15 -
GVLSLQAMQKFTPLV CPN1_PIG 147 15 -
DVLSLPALQKYTPLV CPN1_BOVIN 147 15 -
DVLSLPALQKYTPLV CPN1_SHEEP 147 15 -
EVMAPEATKNFLPLL CPM1_HUMAN 157 15 -
EVMAPEAIKNFIPLL CPM1_PIG 157 15 -
EVMAPEAIKNFIPLL CPM1_BOVIN 157 15 -
EVMAPDSIKNFVPLL CPM1_RAT 155 15 -
EVMAPEAIKNFIPLL CPM1_CAPHI 157 15 -
EVMAPEAIKNFIPLL CPM1_SHEEP 157 15 -
NVLSPKAVQNLLPMV CPN1_CAVPO 148 15 -
EVMALESIKNFIPLL O46515 157 15 -
EVISPKVLGNFVPLL CPM1_ONCMY 155 15 -
RMLKPAEAALYTDAL CP27_RAT 166 15 -
RLLKPAEAALYTDAL CP27_RABIT 167 15 -
RIVKPAEAALYTDAL Q64615 166 15 -
LLLRPQAAAGYAGTL CP2B_MOUSE 144 15 -
LLLRPQAAARYAGTL CP2B_HUMAN 144 15 -
RLLKPAEAALYTDAF CP27_HUMAN 164 15 -
LLLRPQAAAGYAGTL CP2B_RAT 137 15 -