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PR01239

Identifier
EP450IICYP52  [View Relations]  [View Alignment]  
Accession
PR01239
No. of Motifs
4
Creation Date
09-DEC-1999
Title
CYP52 P450 protein signature
Database References
PRINTS; PR00385 P450; PR00464 EP450II
INTERPRO; IPR002974
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. NEBERT, D.W. AND GONZALEZ, F.J.
P450 genes: structure, evolution, and regulation.
ANNU.REV.BIOCHEMISTRY 56 945-993 (1987).
 
3. 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 NEBERT, 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).
 
4. GOTOH, O.
Evolution and differentiation of P-450 genes.
IN CYTOCHROME P-450, OMURA, T., ISHIMURA, Y. AND FUJII-KURIYAMA, Y., EDS.
2ND ED., PP.255-272 (1993). KODANSHA, TOKYO.
 
5. NELSON, D.R.
Metazoan Cytochrome P450 evolution.
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY PART C 121 15-22 (1998).
 
6. NELSON, D.R.
Cytochrome P450 homepage.
http://drnelson.utmem.edu/CytochromeP450.html
 
7. RAVICHANDRAN, K.G., BODDUPALLI, S.S., HASEMANN, C.A., PETERSON, J.A. 
AND DEISENHOFER, J.
Crystal structure of hemoprotein domain of P450BM-3, a prototype for 
microsomal P450s. 
SCIENCE 261 731-736 (1993).

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.
 
Current P450 nomenclature, based on divergent evolution of the P450
superfamily, was proposed and developed by Nebert et al. [3]. On the basis
of sequence similarity, all P450s can be categorised into 2 main classes,
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 [4]. E-class P450S may be
further divided into 5 subclasses (groups) according to protein sequence
similarities. 
 
On the basis of sequence similarity, Nelson introduced the concept of a 
higher order classification of P450 families into clans [6], which is 
similar to the previous grouping into B- and E-classes; both classifications
are still used. According to Nelson's system, clans 3 and 4 correspond to
the E-class group II proteins [5].
 
Group II P450s are distributed widely in life, i.e., in eubacteria (family 
CYP102), cyanobacteria (CYP110), fungi (CYP52, CYP53 and CYP56), insects 
(CYP4 and CYP6) and mammals (CYP3, CYP4 and CYP5). Many group II P450s 
catalyse hydroxylation of linear chains such as alkanes (CYP52), alcohols 
and fatty acids (CYP4, CYP5, CYP102); Aspergillus niger CYP53 carries out
para-hydroxylation of benzoate; yeast CYP56 is possibly involved in 
oxidation of tyrosine residues; insect CYP6 metabolises a wide range of 
toxic compounds; and members of the CYP3 family are omnivorous [4]. The
existence of two prokaryotic P450s in group II strongly suggests that the
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 [4].
 
The CYP52 family is only present in Candida species. Nelson suggests that
this begs the question whether a progenitor CYP52 P450 existed in the common
ancestor that was lost in S.cerevisiae and pombe, or whether alkane
hydroxylases evolved from a CYP51 ancestor? Conversely, did the common
ancestor to all eukaryotes bring with it an alkane or fatty acid hydroxylase
that gave rise to CYP51? [6].
 
CYP52 proteins belong to the eukaryote-like cluster of bacterial P450s,
which includes CYP102 and CYP110. In the original nomenclature, this would 
be group II E-class proteins, while in Nelson's classification the cluster
adjoins CYP4 (clan 4), which includes fatty acid hydroxylases. It has been 
suggested that if the distribution of CYP52 sequences is only among fungi  
related to Candida, they might represent a novel development of Candida
yeasts [6].
 
The 3D structure of the P450 domain of P450BM-3 (CYP102) has been determined
[7] and is used as a model for microsomal P450s. The P450 molecule is an 
alpha/beta protein, shaped like a triangular prism: the overall structure
can be roughly divided into alpha-rich (`right side') and beta-rich (`left 
side') domains. However, this division appears to be artificial since the 
alpha- and beta-rich domains comprise discontinuous assemblies of secondary
structure elements, and do not constitute independent folding units. 
 
EP450IICYP52 is a 4-element fingerprint that provides a signature for CYP52
P450s. The fingerprint was derived from an initial alignment of 12 sequences:
the motifs were drawn from conserved regions spanning the central portion of
the alignment, focusing on those sections that characterise the CYP52 
proteins but distinguish them from the rest of the P450 superfamily and 
clan 4 P450s. Two iterations on SPTR_10f were required to reach convergence,
at which point a true set comprising 29 sequences was identified.
Summary Information
29 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
429292929
30000
20000
1234
True Positives
CP5A_CANTR    CP5B_CANTR    CP5C_CANMA    CP5D_CANMA    
CP5E_CANMA CP5F_CANTR CP5G_CANTR CP5H_CANTR
CP5I_CANMA CP5J_CANMA CP5K_CANMA CP5N_CANTR
CP5P_CANTR CP5Q_CANMA CP5T_CANMA CP5V_CANAP
CP5W_CANAP O74127 O74128 O74129
O74130 O74131 O74132 O74133
O74134 O74626 O94080 Q12581
Q12582
Sequence Titles
CP5A_CANTR  CYTOCHROME P450 52A1 (EC 1.14.14.1) (CYPLIIA1) (ALKANE-INDUCIBLE P450- ALK1) - C 
CP5B_CANTR CYTOCHROME P450 52A2 (EC 1.14.14.1) (CYPLIIA2) (ALKANE-INDUCIBLE P450- ALK2) - C
CP5C_CANMA CYTOCHROME P450 52A3 (EC 1.14.14.1) (CYPLIIA3) (ALKANE-INDUCIBLE P450- ALK1-A) (
CP5D_CANMA CYTOCHROME P450 52A4 (EC 1.14.14.1) (CYPLIIA4) (ALKANE-INDUCIBLE P450- ALK3-A) (
CP5E_CANMA CYTOCHROME P450 52A5 (EC 1.14.14.1) (CYPLIIA5) (ALKANE-INDUCIBLE P450- ALK2-A) (
CP5F_CANTR CYTOCHROME P450 52A6 (EC 1.14.14.1) (CYPLIIA6) (ALKANE-INDUCIBLE P450- ALK3) - C
CP5G_CANTR CYTOCHROME P450 52A7 (EC 1.14.14.1) (CYPLIIA7) (ALKANE-INDUCIBLE P450- ALK4) - C
CP5H_CANTR CYTOCHROME P450 52A8 (EC 1.14.14.1) (CYPLIIA8) (ALKANE-INDUCIBLE P450- ALK5) - C
CP5I_CANMA CYTOCHROME P450 52A9 (EC 1.14.14.1) (CYPLIIA9) (ALKANE-INDUCIBLE P450-ALK5-A) -
CP5J_CANMA CYTOCHROME P450 52A10 (EC 1.14.14.1) (CYPLIIA10) (ALKANE-INDUCIBLE P450-ALK7) -
CP5K_CANMA CYTOCHROME P450 52A11 (EC 1.14.14.1) (CYPLIIA11) (ALKANE-INDUCIBLE P450-ALK8) -
CP5N_CANTR CYTOCHROME P450 52B1 (EC 1.14.14.1) (CYPLIIB1) (ALKANE-INDUCIBLE P450- ALK6) - C
CP5P_CANTR CYTOCHROME P450 52C1 (EC 1.14.14.-) (CYPLIIC1) (ALKANE-INDUCIBLE P450-ALK7) - CA
CP5Q_CANMA CYTOCHROME P450 52C2 (EC 1.14.14.-) (CYPLIIC2) (ALKANE-INDUCIBLE P450-ALK6-A) -
CP5T_CANMA CYTOCHROME P450 52D1 (EC 1.14.14.-) (CYPLIID1) (ALKANE-INDUCIBLE P450-ALK4) - CA
CP5V_CANAP CYTOCHROME P450 52E1 (EC 1.14.14.1) (CYPLIIE1) - CANDIDA APICOLA (YEAST).
CP5W_CANAP CYTOCHROME P450 52E2 (EC 1.14.14.1) (CYPLIIE2) - CANDIDA APICOLA (YEAST).
O74127 ALK1 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74128 ALK2 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74129 ALK3 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74130 ALK4 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74131 ALK5 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74132 ALK6 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74133 ALK7 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74134 ALK8 - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA).
O74626 ALK8 PROTEIN - CANDIDA ALBICANS (YEAST).
O94080 ALKANE HYDROXYLATING CYTOCHROME P-450 - CANDIDA MALTOSA (YEAST).
Q12581 N-ALKANE INDUCIBLE CYTOCHROME P-450 (EC 1.14.14.1) - CANDIDA MALTOSA (YEAST).
Q12582 N-ALKANE INDUCIBLE CYTOCHROME P-450 (EC 1.14.14.1) - CANDIDA MALTOSA (YEAST).
Scan History
SPTR37_10f 2  180  NSINGLE    
Initial Motifs
Motif 1  width=23
Element Seqn Id St Int Rpt
QFNDFSLGTRHSHFAPLLGDGIF CP5B_CANTR 115 115 -
QFNDFSLGTRHDFLYSLLGDGIF CP5D_CANMA 131 131 -
QFNDFSLGTRHDFLYSLLGDGIF CP5A_CANTR 133 133 -
QFSDFSLGKRHTLFKPLLGDGIF CP5H_CANTR 110 110 -
QFNDFALGARHAHFDPLLGDGIF CP5C_CANMA 116 116 -
QFNDFTLGQRLSYFAPLLGKGIF CP5K_CANMA 112 112 -
QFNDFALGARHAHFDPLLGDGIF CP5E_CANMA 116 116 -
QFNDFSLGGRIKFFKPLLGYGIF CP5G_CANTR 106 106 -
QFTDFSLGTRHAHFYPLLGDGIF CP5F_CANTR 117 117 -
QFDEFSLGLRYNQFEPLLGNGIF CP5T_CANMA 104 104 -
VFDKFDYGTRSSAVQPSLGMGIF CP5N_CANTR 118 118 -
EMNSWNLGARPIALRPFIGDGIF CP5P_CANTR 106 106 -

Motif 2 width=19
Element Seqn Id St Int Rpt
PQFAREQVSHVKLLEPHMQ CP5B_CANTR 153 15 -
PQFAREQVAHVKLLEPHVQ CP5D_CANMA 169 15 -
PQFAREQVSHVKLLEPHMQ CP5A_CANTR 171 15 -
PQFAREQVAHVTSLEPHFQ CP5H_CANTR 148 15 -
PQFAREQIAHVKALEPHVQ CP5C_CANMA 154 15 -
PQFSRDQVGHVKMLEPHFQ CP5K_CANMA 150 15 -
PQFAREQIAHVKALEPHVQ CP5E_CANMA 154 15 -
PQFAREQLPMSPSLEPHFN CP5G_CANTR 144 15 -
PQFARDQIGHVKALEPHIQ CP5F_CANTR 155 15 -
PQFIKSQVSHVNRLEPHFN CP5T_CANMA 142 15 -
NMFDRKSIDKVHDFEPHFK CP5N_CANTR 156 15 -
PVFAKEHVKQITSMEPYVQ CP5P_CANTR 144 15 -

Motif 3 width=21
Element Seqn Id St Int Rpt
VHKFADYYVEKALELTPDQLE CP5B_CANTR 267 95 -
VHKFADFYVQKALSLTDDDLE CP5D_CANMA 283 95 -
VHKFADHYVQKALELTDEDLE CP5A_CANTR 285 95 -
VHKFTNYYVQRALDATPEELE CP5H_CANTR 262 95 -
VHKLAQYFVNTALNATEKEVE CP5C_CANMA 267 94 -
VHKFSDYYIKKALTATPEELE CP5K_CANMA 264 95 -
VHKLAQYFVNKALDASEDEVA CP5E_CANMA 267 94 -
VHKFTNYYVQKALDATPEELE CP5G_CANTR 255 92 -
VHYLAKYFVNKALNFTPEEIE CP5F_CANTR 268 94 -
VQDFSQRCVDKVLNMSNSEID CP5T_CANMA 245 84 -
VQAFCDYLVQKSLENTCNDKF CP5N_CANTR 256 81 -
QKDFVDVYIDRVVGMSEEELN CP5P_CANTR 258 95 -

Motif 4 width=17
Element Seqn Id St Int Rpt
LPRGGGKDGLSPVLVRK CP5B_CANTR 401 113 -
LPRGGGKDGMSPIAIKK CP5D_CANMA 417 113 -
LPRGGGEGGLSPIAIKK CP5A_CANTR 419 113 -
LPRGGGSDGNSPVLVKK CP5H_CANTR 396 113 -
LPRGGGKDGNSPIFVPK CP5C_CANMA 403 115 -
LPHGGGPDGMSPILVRK CP5K_CANMA 398 113 -
LPRGGGKDGTSPIFVPK CP5E_CANMA 403 115 -
LPRGGGPDGKDPILVRK CP5G_CANTR 389 113 -
LPRGGGPNGTDPIFIPK CP5F_CANTR 404 115 -
LPHGGGVDGMSPILIKK CP5T_CANMA 376 110 -
LPKGGGPDGQDPILVKK CP5N_CANTR 382 105 -
IPRGGGKSCTDPILVHK CP5P_CANTR 388 109 -
Final Motifs
Motif 1  width=23
Element Seqn Id St Int Rpt
QFSDFSLGTRHAHFAPLIGDGIF Q12581 119 119 -
QFNDFSLGTRHSHFAPLLGDGIF CP5B_CANTR 115 115 -
QFEDFSLGKRLDFFKPLLGYGIF CP5I_CANMA 114 114 -
QFNDFSLGTRHDFLYSLLGDGIF Q12582 131 131 -
QFNDFSLGTRHDFLYSLLGDGIF CP5D_CANMA 131 131 -
QFNDFSLGRRYDFFKPLLGKGIF O74626 112 112 -
QFNDFSLGTRHDFLYSLLGDGIF CP5A_CANTR 133 133 -
QFSDFSLGKRHTLFKPLLGDGIF CP5H_CANTR 110 110 -
QFNDFALGARHAHFDPLLGDGIF CP5C_CANMA 116 116 -
QFNDFALGARHAHFDPLLGDGIF O94080 116 116 -
QFNDFTLGQRLSYFAPLLGKGIF CP5K_CANMA 112 112 -
QFNDFALGARHAHFDPLLGDGIF CP5E_CANMA 116 116 -
QFNDFSLGGRIKFFKPLLGYGIF CP5G_CANTR 106 106 -
QFNEYTLGQRLNFLAPLLGKGIF CP5J_CANMA 112 112 -
QFTDFSLGTRHAHFYPLLGDGIF CP5F_CANTR 117 117 -
QFKDFCLGQRHGQLAPVLGDGIF O74128 105 105 -
QFKDFSLGTRHKIMLPTLGDGIF O74132 104 104 -
QFKDFCLGERHAQFLPVLGNGIF O74127 110 110 -
QFKDFSLGLRKEALAPSLGYGIF O74129 102 102 -
QFKDFCLGIRHRALSPSIGDGIF O74130 104 104 -
QFDEFSLGLRYNQFEPLLGNGIF CP5T_CANMA 104 104 -
SFKDYSLGFRYDIMYGLLGNGIF CP5V_CANAP 109 109 -
QFKDFSLGTRYRSLAPTLGDGIF O74131 104 104 -
SFKDYSLGFRYNAMYGLLGNGIF CP5W_CANAP 109 109 -
QFKDFCLIARYKALGPMLGDGIF O74133 104 104 -
HMKDWTIGYRPFALKPLLGDGIF CP5Q_CANMA 107 107 -
VFDKFDYGTRSSAVQPSLGMGIF CP5N_CANTR 118 118 -
FSDYDLGKTRHALLFTLMGDGIF O74134 114 114 -
EMNSWNLGARPIALRPFIGDGIF CP5P_CANTR 106 106 -

Motif 2 width=19
Element Seqn Id St Int Rpt
PQFAREQVGHVKLLEPHVQ Q12581 157 15 -
PQFAREQVSHVKLLEPHMQ CP5B_CANTR 153 15 -
PQFAREQVGHVKLIEPHFQ CP5I_CANMA 152 15 -
PQFAREQVAHVKLLEPHVQ Q12582 169 15 -
PQFAREQVAHVKLLEPHVQ CP5D_CANMA 169 15 -
PQFAREQIAHVKALEPHFQ O74626 150 15 -
PQFAREQVSHVKLLEPHMQ CP5A_CANTR 171 15 -
PQFAREQVAHVTSLEPHFQ CP5H_CANTR 148 15 -
PQFAREQIAHVKALEPHVQ CP5C_CANMA 154 15 -
PQFAREQIAHVKALEPHVQ O94080 154 15 -
PQFSRDQVGHVKMLEPHFQ CP5K_CANMA 150 15 -
PQFAREQIAHVKALEPHVQ CP5E_CANMA 154 15 -
PQFAREQLPMSPSLEPHFN CP5G_CANTR 144 15 -
PQFSRDQIGHVKMLEPHFQ CP5J_CANMA 150 15 -
PQFARDQIGHVKALEPHIQ CP5F_CANTR 155 15 -
PQFARDQVSDVEMIERHVQ O74128 143 15 -
PQFARDQVSHVASLERHIQ O74132 142 15 -
PQFARDQVSDVEMIEEHIQ O74127 148 15 -
PQFSREQISRLESVETHVQ O74129 140 15 -
PQFSRQQISRVHSLERLMQ O74130 142 15 -
PQFIKSQVSHVNRLEPHFN CP5T_CANMA 142 15 -
PQFSREQVSHLESMRTHIN CP5V_CANAP 147 15 -
PQFAREQVSRLDSLEAHFQ O74131 142 15 -
PQFSREQVSHLESMRTHIN CP5W_CANAP 147 15 -
PQFAREQVSRLDSIEHHFQ O74133 142 15 -
PIFAKEHIKQITAMEPYML CP5Q_CANMA 145 15 -
NMFDRKSIDKVHDFEPHFK CP5N_CANTR 156 15 -
PQFSKETVSPLSSLETSLQ O74134 152 15 -
PVFAKEHVKQITSMEPYVQ CP5P_CANTR 144 15 -

Motif 3 width=21
Element Seqn Id St Int Rpt
VHKFADHYVQKALNLTEADLE Q12581 271 95 -
VHKFADYYVEKALELTPDQLE CP5B_CANTR 267 95 -
VHKFTDYYVQKALDATPEELE CP5I_CANMA 266 95 -
VHKFADFYVQKALSLTEADLE Q12582 283 95 -
VHKFADFYVQKALSLTDDDLE CP5D_CANMA 283 95 -
VHKFSDYYVNKALNATPEELE O74626 264 95 -
VHKFADHYVQKALELTDEDLE CP5A_CANTR 285 95 -
VHKFTNYYVQRALDATPEELE CP5H_CANTR 262 95 -
VHKLAQYFVNTALNATEKEVE CP5C_CANMA 267 94 -
VHKLAQYFVNTALNATEKEVE O94080 265 92 -
VHKFSDYYIKKALTATPEELE CP5K_CANMA 264 95 -
VHKLAQYFVNKALDASEDEVA CP5E_CANMA 267 94 -
VHKFTNYYVQKALDATPEELE CP5G_CANTR 255 92 -
VHKFSDYYIKKALTATPEELE CP5J_CANMA 264 95 -
VHYLAKYFVNKALNFTPEEIE CP5F_CANTR 268 94 -
VHAFVDHYVEKALANSDEEKS O74128 258 96 -
VHDFTDFYVSKALAARKEKFQ O74132 270 109 -
VHAFVDHYVKKALEESEKHVD O74127 262 95 -
IHDYVDRYVDKALLARKEKSE O74129 253 94 -
VKDFSQFFVDKALNTSKEKLK O74130 263 102 -
VQDFSQRCVDKVLNMSNSEID CP5T_CANMA 245 84 -
CHNFIDYFVYKALATPMEKDQ CP5V_CANAP 261 95 -
IKTFVDFFAAKALKARKEKDM O74131 271 110 -
CHNFIDYFVYKALATPMEKGQ CP5W_CANAP 261 95 -
VKTFVDHYAAKAIKARNEKNT O74133 271 110 -
QHEFVSYFVQKAISMSDEELN CP5Q_CANMA 261 97 -
VQAFCDYLVQKSLENTCNDKF CP5N_CANTR 256 81 -
VHAFSNHFVNQALKLTPQELQ O74134 331 160 -
QKDFVDVYIDRVVGMSEEELN CP5P_CANTR 258 95 -

Motif 4 width=17
Element Seqn Id St Int Rpt
LPRGGGKDGLSPILVRK Q12581 405 113 -
LPRGGGKDGLSPVLVRK CP5B_CANTR 401 113 -
LPRGGGPDGKDPIFIKK CP5I_CANMA 400 113 -
LPRGGGKDGMSPIAIKK Q12582 417 113 -
LPRGGGKDGMSPIAIKK CP5D_CANMA 417 113 -
LPRGGGPDGMSTILIKQ O74626 394 109 -
LPRGGGEGGLSPIAIKK CP5A_CANTR 419 113 -
LPRGGGSDGNSPVLVKK CP5H_CANTR 396 113 -
LPRGGGKDGNSPIFVPK CP5C_CANMA 403 115 -
LPRGGGKDGNSPIFVPK O94080 401 115 -
LPHGGGPDGMSPILVRK CP5K_CANMA 398 113 -
LPRGGGKDGTSPIFVPK CP5E_CANMA 403 115 -
LPRGGGPDGKDPILVRK CP5G_CANTR 389 113 -
LPHGGGPDGMSPILVRK CP5J_CANMA 398 113 -
LPRGGGPNGTDPIFIPK CP5F_CANTR 404 115 -
LPRGGGPDESKPILVRK O74128 389 110 -
LPKGGGPDLDQPIFIPK O74132 403 112 -
LPRGGGPDGMQPIVVRK O74127 393 110 -
LPRGGGPQGDKPIFVAK O74129 386 112 -
LPRGGGPDGKQPVFVYK O74130 396 112 -
LPHGGGVDGMSPILIKK CP5T_CANMA 376 110 -
LPTGGGPNGDQPVFVPK CP5V_CANAP 392 110 -
LPRGGGPDQSQPIFIPK O74131 404 112 -
FPTGGGPNGDQPIFVPK CP5W_CANAP 392 110 -
LPRGGGPDGSQPIFVPK O74133 404 112 -
LPRGGGEDCSHPILVKK CP5Q_CANMA 391 109 -
LPKGGGPDGQDPILVKK CP5N_CANTR 382 105 -
LPTGGGKNHDEPIFVAK O74134 463 111 -
IPRGGGKSCTDPILVHK CP5P_CANTR 388 109 -