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PR00236

Identifier
HSVCAPSIDP40  [View Relations]  [View Alignment]  
Accession
PR00236
No. of Motifs
8
Creation Date
28-MAY-1993  (UPDATE 19-JUN-1999)
Title
Herpesvirus capsid protein P40 signature
Database References

INTERPRO; IPR001847
Literature References
1. WELCH, A.R., WOODS, A.S., MCNALLY, L.M., COTTER, R.J. AND GIBSON, W.
A Herpesvirus maturational proteinase, assemblin: identification of its
gene, putative active site domain and cleavage site.
PROC.NATL.ACAD.SCI.U.S.A. 88(23) 10792-10796 (1991).
 
2. LIU,F. AND ROIZMAN,B.
The herpes simplex virus 1 gene encoding a protease also contains within
its coding domain the gene encoding the more abundant substrate.
J.VIROL. 65 5149-5156 (1991).
 
3. LIU,F. AND ROIZMAN,B.
Differentiation of multiple domains in the herpes simplex virus 1 protease
encoded by the UL26 gene.
PROC.NATL.ACAD.SCI.U.S.A. 89 2076-2080 (1992).
 
4. DAVISON, M.D., RIXON, F.J. AND DAVISON, A.J.
Identification of genes encoding two capsid proteins (VP24 and VP26) of
herpes simplex virus type 1.
J.GEN.VIROL. 73 2709-2713 (1992).
 
5. CHOI, H.K., TONG, L., MINOR, W., DUMAS, P., BOEGE, U., ROSSMANN, M.G.
AND WENGLER, G.
Structure of Sindbis virus core protein reveals a chymotrypsin-like serine
proteinase and the organization of the virion.
NATURE 354 (6348) 37-43 (1991).
 
6. TONG, L., WENGLER, G. AND ROSSMANN, M.G.
Refined structure of Sindbis virus core protein and comparison with other
chymotrypsin-like serine proteinase structures.
J.MOL.BIOL. 230(1) 228-247 (1993).
 
7. PEARL, L.H. AND TAYLOR, W.R.
A structural model for the retroviral proteases.
NATURE 329 351-354 (1987).
 
8. WLODAWER, A., MILLER, M., JASKOLSKI, M., SATHYANARAYANA, B.K., BALDWIN,
E., WEBER, I.T., SELK, L.M., CLAWSON, L, SCHNEIDER, J. AND KENT, S.H.B.
Conserved folding in retroviral proteases - crystal-structure of a
synthetic HIV-1 protease.
SCIENCE 245 616-621 (1989).
 
9. BAZAN, J.F. AND FLETTERICK, R.J.
Viral cysteine proteases are homologous to the trypsin-like family of
serine proteases: structural and functional implications.
PROC.NATL.ACAD.SCI.U.S.A. 85 7872-7876 (1988).
 
10. GORBALENYA, A.E., DONCHENKO, A.P., BLINOV, V.M. AND KOONIN, E.V.
Cysteine proteases of positive strand RNA viruses and chymotrypsin-like
serine proteases. A distinct protein superfamily with a common structural 
fold.
FEBS LETT. 243(2) 103-114 (1989).

Documentation
Proteases can be grouped into 4 classes according to the prominent
functional groups at the active sites: viz., the Ser, Asp, Cys and
metalloproteases. 3D structures are known for examples from all these
classes: e.g., trypsin (Ser), pepsin (Asp), papain (Cys), and 
carboxypeptidase (Zn).
 
A number of viral proteases have been discovered and attempts have been
made to assign them to one or other of the above classes, but the extent
of the sequence similarity is very low. In a few cases, X-ray studies have
confirmed the assignment; e.g., sindbis core protein seems to belong to a
third class of the trypsin-like Ser proteases [5,6]. [nb. There are 2 
types of Ser protease: the trypsin-like and subtilisin-like, which have 
an identical spatial arrangement of catalytic His, Asp and Ser but in quite
different protein scaffolds (an example of convergent evolution). The 
family of trypsin-like Ser proteases has been subdivided into 2 classes: 
the "large" class (ca 230 residues) includes mostly mammalian enzymes (e.g.
chymotrypsin, trypsin, elastase, kallikrein, thrombin) and the "small" 
class (ca 190 residues) includes the bacterial enzymes (e.g., alpha-lytic 
protease, S.griseus proteases A and B, S.griseus trypsin, S.aureus
protease)].
 
Retrovirus proteases, such as HIV protease, are Asp proteases [7,8].
There seems to be fairly good evidence that the Cys-active-centre viral
proteases are in fact trypsin-like Ser proteases in which the active
site Ser has been replaced by Cys [9,10]. The 2a and 3c subclasses of the 
viral Cys proteases are homologous with the small and large subclasses, 
respectively, of the trypsin-like Ser proteases. All the animal and plant
viral Cys proteases have in common a +ve strand RNA genome that is 
translated into a large polyprotein.
 
Herpesviridae are large ds DNA viruses. The capsid of herpes simplex virus
type 1 is composed of 7 proteins: VP5, VP19c, VP21, VP22a, VP23, VP24 and 
VP26. The region of the genome encoding VP22a is transcribed into 2 mRNAs
which have identical 3' ends but different 5' ends. The smaller mRNA is
specified by gene UL26.5 and encodes a 329 residue protein. The larger mRNA
is transcribed from gene UL26 and encodes a 635 residue protein whose
C-terminal region is identical to the 329 residue protein. The promoter
of the UL26.5 ORF is embedded in the 5'-terminal domain of the UL26 ORF.
 
The UL26 protein can proteolytically cleave itself and the UL26.5 protein
at a position 25 residues from the C-terminus. This proteolysis is
essential for capsid maturation. Capsid protein VP22a would correspond to
the UL26.5 protein cleaved 25 residues from its C-terminus, i.e. a 304
residue protein. The product of UL26.5 ORF is devoid of enzyme activity so
that the protease domain would map to the amino-proximal domain of the
UL26 ORF.
 
Genes corresponding to UL26 have been sequenced for a number of
Herpesviruses in addition to herpes simplex virus 1, including human
cytomegalovirus (UL80), simian cytomegalovirus, Epstein-Barr virus,
infectious laryngotracheitis virus, varicella voster virus (ORF33), equine
herpes virus and herpes virus saimiri. The amino terminus is the most
conserved of the UL26 protein.
 
There is a consensus sequence VXAS (where X is a polar residue) at the C-
terminal cleavage site. A similar consensus Y(V/L)XAS exists towards the C-
terminus of the putative protease domain (Ala247 - Ser248 in herpes 
simplex) and it has been proposed that the protease also acts at this 
site to produce capsid proteins VP24 (residues 1-247) and VP21 (248-610).
 
The exact extent of the protease domain remains unclear. There is some
evidence to suggest that residues 1 to 306 are necessary in herpes simplex
virus 1, but only 1 to 249 seem to be necessary in simian cytomegalovirus.
Studies with protease inhibitors suggest that the herpesvirus protease is
a Ser protease belonging to either the trypsin-like or subtilisin-like
families; it is not inhibited by inhibitors of Cys, Asp or metallo
proteases. The Ser proteases have His, Asp, and Ser in their active
sites. In an alignment of the first 300 residues of the putative protease
there are well-conserved regions containing His or Ser, but it is a little
more difficult to find a conserved Asp or Glu. Mutagenesis studies have so
far shown that out of Asp31, Ser32, Asp34, His61, His148 and Ser215, the
only residues whose substitution abolished enzyme activity were His61 and 
His148.
 
HSVCAPSIDP40 is an 8-element fingerprint that provides a general signature 
for the herpesvirus maturational proteases. The fingerprint was derived
from an initial alignment of 8 sequences: the motifs were drawn from
conserved regions spanning the full alignment length. A single iteration 
on OWL20.0 was required to reach convergence, no further sequences being
identified beyond the starting set. A more subtle fingerprint would be
needed to pinpoint related proteases.
 
An update on SPTR37_9f identified a true set of 18 sequences, and 21
partial matches.
Summary Information
  18 codes involving  8 elements
2 codes involving 7 elements
3 codes involving 6 elements
0 codes involving 5 elements
2 codes involving 4 elements
1 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
81818181818181818
721222221
620333331
500000000
420021201
310000101
200000000
12345678
True Positives
O39278        O40637        O40922        O41936        
P88911 P89449 Q69087 Q69527
Q83417 Q85027 VP40_EBV VP40_HCMVA
VP40_HSV11 VP40_HSVBC VP40_HSVEB VP40_HSVSA
VP40_SCMVC VP40_VZVD
True Positive Partials
Codes involving 7 elements
O12271 VP40_HSVE2
Codes involving 6 elements
O36367 Q69223 VP40_ILTVT
Codes involving 4 elements
O56287 VP40_HSV6U
Codes involving 3 elements
VP40_HSV7J
Sequence Titles
O39278      COUNTERPART OF HSV-1 GENE UL26 AND VZV GENE 33 - EQUINE HERPESVIRUS 4. 
O40637 PROTEASE - SAIMIRIINE HERPESVIRUS 2.
O40922 ORF 17 - KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS (KSHV) (HUMAN HERPESVIRUS 8).
O41936 CAPSID PROTEIN - MURINE HERPESVIRUS 68.
P88911 ORF 17 - KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS (KSHV) (HUMAN HERPESVIRUS 8).
P89449 PROTEASE - HERPES SIMPLEX VIRUS (TYPE 2).
Q69087 UL26 - HUMAN HERPESVIRUS 1.
Q69527 UL26 PROTEASE - HERPES SIMPLEX VIRUS (TYPE 2).
Q83417 UL26 PROTEASE - PSEUDORABIES VIRUS.
Q85027 VIRAL PROTEINASE - PSEUDORABIES VIRUS.
VP40_EBV CAPSID PROTEIN P40 (VIRION STRUCTURAL PROTEIN BVRF2) (EC-RF3 AND EC- RF3A) [CONTAINS: CAPSID PROTEIN VP24 (PROTEASE) (EC 3.4.21.-); CAPSID PROTEIN VP22A] - EPSTEIN-BARR VIRUS (STRAIN B95-8) (HUMAN HERPESVIRUS 4).
VP40_HCMVA CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); CAPSID ASSEMBLY PROTEIN] - HUMAN CYTOMEGALOVIRUS (STRAIN AD169).
VP40_HSV11 CAPSID PROTEIN P40 (VIRION STRUCTURAL PROTEIN UL26) [CONTAINS: CAPSID PROTEIN VP24 (PROTEASE) (EC 3.4.21.-); CAPSID PROTEIN VP22A] - HERPES SIMPLEX VIRUS (TYPE 1 / STRAIN 17).
VP40_HSVBC CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); CAPSID ASSEMBLY PROTEIN] - BOVINE HERPESVIRUS TYPE 1 (STRAIN COOPER).
VP40_HSVEB CAPSID PROTEIN P40 (VIRION STRUCTURAL GENE 35 PROTEIN) [CONTAINS: CAPSID PROTEIN VP24 (PROTEASE) (EC 3.4.21.-); CAPSID PROTEIN VP22A] - EQUINE HERPESVIRUS TYPE 1 (STRAIN AB4P) (EHV-1).
VP40_HSVSA CAPSID PROTEIN P40 [CONTAINS: CAPSID PROTEIN VP24 (PROTEASE) (EC 3.4.21.-); CAPSID PROTEIN VP22A] - HERPESVIRUS SAIMIRI (STRAIN 11).
VP40_SCMVC CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); CAPSID ASSEMBLY PROTEIN] - SIMIAN CYTOMEGALOVIRUS (STRAIN COLBURN).
VP40_VZVD CAPSID PROTEIN P40 (VIRION STRUCTURAL GENE 33 PROTEIN) [CONTAINS: CAPSID PROTEIN VP24 (PROTEASE) (EC 3.4.21.-); CAPSID PROTEIN VP22A] - VARICELLA-ZOSTER VIRUS (STRAIN DUMAS) (VZV).

O12271 VIRAL CORE PROTEIN - HUMAN HERPESVIRUS 1.
VP40_HSVE2 CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); CAPSID ASSEMBLY PROTEIN] - EQUINE HERPESVIRUS TYPE 2 (STRAIN 86/87) (EHV-2).

O36367 MINOR CAPSID SCAFFOLD PROTEIN - ALCELAPHINE HERPESVIRUS 1 (WILDEBEEST HERPESVIRUS).
Q69223 NEUTRAL PROTEASE LARGE SUBUNIT - MOUSE CYTOMEGALOVIRUS 1.
VP40_ILTVT CAPSID PROTEIN P40 [CONTAINS: CAPSID PROTEIN VP24 (PROTEASE) (EC 3.4.21.-); CAPSID PROTEIN VP22A] - INFECTIOUS LARYNGOTRACHEITIS VIRUS (STRAIN THORNE V882) (ILTV).

O56287 CAPSID PROTEIN - HUMAN HERPESVIRUS 7.
VP40_HSV6U CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); CAPSID ASSEMBLY PROTEIN] - HERPES SIMPLEX VIRUS (TYPE 6 / STRAIN UGANDA-1102).

VP40_HSV7J CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); CAPSID ASSEMBLY PROTEIN] - HERPES SIMPLEX VIRUS (TYPE 7 / STRAIN JI) (HHV7).
Scan History
OWL20_0    1  100  NSINGLE    
OWL26_0 1 150 NSINGLE
SPTR37_9f 3 290 NSINGLE
Initial Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
PIYVAGFLALYD VP40_HSV11 19 19 -
PIYVAGYIALYD VP40_HSVEB 13 13 -
ALYVAGYLALYS VP40_VZVD 11 11 -
IVYVAGFVDVVA VP40_HSVSA 2 2 -
PVYVGGFLARYD VP40_HCMVA 12 12 -
PVYVGGFLVRYD VP40_SCMVC 3 3 -
SVYVCGFVERPD VP40_EBV 5 5 -
YIFVAGYLVVYD VP40_ILTVT 8 8 -

Motif 2 width=9
Element Seqn Id St Int Rpt
SGELALDPD VP40_HSV11 34 3 -
EGELNITPE VP40_VZVD 25 2 -
DPVLYLNLD VP40_HSVSA 18 4 -
EAELLLPRD VP40_HCMVA 28 4 -
EAELFLPSG VP40_SCMVC 19 4 -
DACLHLDPL VP40_EBV 21 4 -
EYELTREQS VP40_ILTVT 27 7 -
GGELTLTRE VP40_HSVEB 28 3 -

Motif 3 width=10
Element Seqn Id St Int Rpt
DHRNGCVVGE VP40_HSVEB 53 16 -
EHLPESTIGH VP40_HSVSA 43 16 -
DHESSCVVGT VP40_ILTVT 51 15 -
EHLPDAPVGS VP40_EBV 46 16 -
NHDESATVGY VP40_SCMVC 45 17 -
NHDDTAVVGH VP40_HCMVA 61 24 -
DHRAGCEVGR VP40_HSV11 59 16 -
DHRKDCVVGE VP40_VZVD 50 16 -

Motif 4 width=17
Element Seqn Id St Int Rpt
TIGLYAVTHGVFCVGVI VP40_HSVSA 53 0 -
VLTILDLPRGLFCLGVV VP40_ILTVT 61 0 -
VLAVVDDPRGPFFVGLI VP40_HSV11 69 0 -
VLSIVDDARGPFFLGII VP40_HSVEB 63 0 -
VIAIIEDIRGPFFLGIV VP40_VZVD 60 0 -
VAAMQSVRDGLFCLGCV VP40_HCMVA 71 0 -
VAGLQNVRAGLFCLGRV VP40_SCMVC 55 0 -
VFGLYQSRAGLFSAASI VP40_EBV 56 0 -

Motif 5 width=16
Element Seqn Id St Int Rpt
VVEFLSGSYAGLSLSS VP40_HCMVA 119 31 -
FLYLLSNILPSLSLSS VP40_ILTVT 110 32 -
KVEALHAWLPSLSLAS VP40_EBV 103 30 -
VLEFLSGSYSGLSLSS VP40_SCMVC 105 33 -
LLYLITNYLPSVSLAT VP40_HSV11 116 30 -
LLYLVSNYLPSASLSS VP40_HSVEB 110 30 -
ALYLVTNYLPSVSLSS VP40_VZVD 107 30 -
LLEMLHTWLPALSLSS VP40_HSVSA 100 30 -

Motif 6 width=10
Element Seqn Id St Int Rpt
KHVALCSVGR VP40_SCMVC 140 19 -
AHVALCAIGR VP40_HSV11 146 14 -
AHVSLCVIGR VP40_HSVEB 140 14 -
THVALCVVGR VP40_VZVD 137 14 -
QHVSLCALGR VP40_HSVSA 130 14 -
KHVALCSVGR VP40_HCMVA 155 20 -
DHVSICALGR VP40_EBV 137 18 -
AHVALCELGR VP40_ILTVT 140 14 -

Motif 7 width=18
Element Seqn Id St Int Rpt
AVYGTDLAWVLKHFSDLE VP40_EBV 152 5 -
VTYDTGLDAAIAPFRHLS VP40_HSV11 161 5 -
VTYDATPENAVAPFKRLS VP40_HSVEB 155 5 -
VNYDCTPESSIEPFRVLS VP40_VZVD 152 5 -
AVYSMNLEDAISQFCSIS VP40_HSVSA 145 5 -
AIYGATASEAIGAFDDLS VP40_ILTVT 155 5 -
AVYGRDPEWVTQRFPDLT VP40_HCMVA 170 5 -
AVYGRQPDWVMERFPDLT VP40_SCMVC 155 5 -

Motif 8 width=12
Element Seqn Id St Int Rpt
AGIEGHTYLQAS VP40_HSVEB 231 58 -
AGIMGHVYLQAS VP40_VZVD 225 55 -
ANIPAESYLKAS VP40_EBV 224 54 -
GVTARESYVKAS VP40_SCMVC 238 65 -
AGIAGHTYLQAS VP40_HSV11 236 57 -
AAVYNPKYLQAN VP40_ILTVT 228 55 -
AKIKKLTYLKAS VP40_HSVSA 217 54 -
GVTERESYVKAS VP40_HCMVA 245 57 -
Final Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
PIYVAGFLALYD VP40_HSV11 19 19 -
PIYVAGFLALYD Q69087 20 20 -
PIYVAGFLALYD Q69527 20 20 -
PIYVAGFLALYD P89449 20 20 -
PVYVSGYLALYD Q83417 3 3 -
PIYVAGYIALYD VP40_HSVEB 13 13 -
PVYVSGYLALYD Q85027 3 3 -
PIYVAGYIALYD O39278 14 14 -
PVYVGGYLALYG VP40_HSVBC 27 27 -
ALYVAGYLALYS VP40_VZVD 11 11 -
GLYVGGFVDVVS O40922 23 23 -
GLYVGGFVDVVS P88911 23 23 -
IVYVAGFVDVVA O40637 3 3 -
IVYVAGFVDVVA VP40_HSVSA 2 2 -
PIYVGGYVDIKK O41936 5 5 -
PVYVGGFLARYD VP40_HCMVA 12 12 -
PVYVGGFLVRYD VP40_SCMVC 3 3 -
SVYVCGFVERPD VP40_EBV 5 5 -

Motif 2 width=9
Element Seqn Id St Int Rpt
SGELALDPD VP40_HSV11 34 3 -
SGELALDPD Q69087 35 3 -
PGELALDPD Q69527 35 3 -
PGELALDPD P89449 35 3 -
GGELALTRE Q83417 17 2 -
GGELTLTRE VP40_HSVEB 28 3 -
GGELALTRE Q85027 17 2 -
GGELTLTRE O39278 29 3 -
EGELVLTRE VP40_HSVBC 42 3 -
EGELNITPE VP40_VZVD 25 2 -
EQELYLDPD O40922 39 4 -
EQELYLDPD P88911 39 4 -
DPVLYLNLD O40637 19 4 -
DPVLYLNLD VP40_HSVSA 18 4 -
EKELVLDHD O41936 21 4 -
EAELLLPRD VP40_HCMVA 28 4 -
EAELFLPSG VP40_SCMVC 19 4 -
DACLHLDPL VP40_EBV 21 4 -

Motif 3 width=10
Element Seqn Id St Int Rpt
DHRAGCEVGR VP40_HSV11 59 16 -
DHRAGCEVGR Q69087 60 16 -
DHRARCEVGR Q69527 60 16 -
DHRARCEVGR P89449 60 16 -
DHRPRCDIGA Q83417 42 16 -
DHRNGCVVGE VP40_HSVEB 53 16 -
DHRPRCDIGA Q85027 42 16 -
DHRNGCVVGE O39278 54 16 -
DHASACEVGA VP40_HSVBC 67 16 -
DHRKDCVVGE VP40_VZVD 50 16 -
EHLPETEVGW O40922 64 16 -
EHLPETEVGW P88911 64 16 -
EHLPESTIGH O40637 44 16 -
EHLPESTIGH VP40_HSVSA 43 16 -
EHLADAEVGW O41936 46 16 -
NHDDTAVVGH VP40_HCMVA 61 24 -
NHDESATVGY VP40_SCMVC 45 17 -
EHLPDAPVGS VP40_EBV 46 16 -

Motif 4 width=17
Element Seqn Id St Int Rpt
VLAVVDDPRGPFFVGLI VP40_HSV11 69 0 -
VLAVVDDPRGPFFVGLI Q69087 70 0 -
VLAVVNDPRGPFFVGLI Q69527 70 0 -
VLAVVNDPRGPFFVGLI P89449 70 0 -
VLAVVDDDRGPFFLGVV Q83417 52 0 -
VLSIVDDARGPFFLGII VP40_HSVEB 63 0 -
VLAVVDDDRGPFFLGVV Q85027 52 0 -
VLSIVDDVRGPFFLGIV O39278 64 0 -
VLALADDDAGLFFVGVI VP40_HSVBC 77 0 -
VIAIIEDIRGPFFLGIV VP40_VZVD 60 0 -
TLGLFQVSHGIFCTGAI O40922 74 0 -
TLGLFQVSHGIFCTGAI P88911 74 0 -
TIGLYAVTHGVFCVGVI O40637 54 0 -
TIGLYAVTHGVFCVGVI VP40_HSVSA 53 0 -
VQTIYPASHGLFCMGEV O41936 56 0 -
VAAMQSVRDGLFCLGCV VP40_HCMVA 71 0 -
VAGLQNVRAGLFCLGRV VP40_SCMVC 55 0 -
VFGLYQSRAGLFSAASI VP40_EBV 56 0 -

Motif 5 width=16
Element Seqn Id St Int Rpt
LLYLITNYLPSVSLAT VP40_HSV11 116 30 -
LLYLITNYLPSVSLAT Q69087 117 30 -
LLYLITNYLPSVSLST Q69527 117 30 -
LLYLITNYLPSVSLST P89449 117 30 -
LLYLLSNYLPSASLSS Q83417 97 28 -
LLYLVSNYLPSASLSS VP40_HSVEB 110 30 -
LLYLLSNYLPSRSLSS Q85027 97 28 -
LLYLVSNYLPSASLSS O39278 111 30 -
FLYLVSNYLPSVSLSS VP40_HSVBC 124 30 -
ALYLVTNYLPSVSLSS VP40_VZVD 107 30 -
LLEILHTWLPGLSLSS O40922 121 30 -
LLEILHTWLPGLSLSS P88911 121 30 -
LLEMLHTWLPALSLSS O40637 101 30 -
LLEMLHTWLPALSLSS VP40_HSVSA 100 30 -
TLQMLHTWLPELSLSS O41936 104 31 -
VVEFLSGSYAGLSLSS VP40_HCMVA 119 31 -
VLEFLSGSYSGLSLSS VP40_SCMVC 105 33 -
KVEALHAWLPSLSLAS VP40_EBV 103 30 -

Motif 6 width=10
Element Seqn Id St Int Rpt
AHVALCAIGR VP40_HSV11 146 14 -
AHVALCAIGR Q69087 147 14 -
AHVALCAIGR Q69527 147 14 -
AHVALCAIGR P89449 147 14 -
AHVALCVIGR Q83417 127 14 -
AHVSLCVIGR VP40_HSVEB 140 14 -
AHVALCVIGR Q85027 127 14 -
AHVSLCVIGR O39278 141 14 -
AHVALCVLGR VP40_HSVBC 154 14 -
THVALCVVGR VP40_VZVD 137 14 -
QHVSLCALGR O40922 152 15 -
QHVSLCALGR P88911 152 15 -
QHVSLCALGR O40637 131 14 -
QHVSLCALGR VP40_HSVSA 130 14 -
HHVALCALGK O41936 135 15 -
KHVALCSVGR VP40_HCMVA 155 20 -
KHVALCSVGR VP40_SCMVC 140 19 -
DHVSICALGR VP40_EBV 137 18 -

Motif 7 width=18
Element Seqn Id St Int Rpt
VTYDTGLDAAIAPFRHLS VP40_HSV11 161 5 -
VTYDTGLDAAIAPFRHLS Q69087 162 5 -
VTYDTSLDAAIAPFRHLD Q69527 162 5 -
VTYDTSLDAAIAPFRHLD P89449 162 5 -
VVYDASPEAAVAPFRQLS Q83417 142 5 -
VTYDATPENAVAPFKRLS VP40_HSVEB 155 5 -
VVYDASPEAAVGPFRELS Q85027 142 5 -
VTYDATPENTVAPFKRLS O39278 156 5 -
VTYDATPDACVAPFRRLS VP40_HSVBC 169 5 -
VNYDCTPESSIEPFRVLS VP40_VZVD 152 5 -
AVYGHDAEWVVSRFSSVS O40922 167 5 -
AVYGHDAEWVVSRFSSVS P88911 167 5 -
AVYSMNLEDAISQFCSIS O40637 146 5 -
AVYSMNLEDAISQFCSIS VP40_HSVSA 145 5 -
AVYGHSLDWVISKFESLK O41936 150 5 -
AVYGRDPEWVTQRFPDLT VP40_HCMVA 170 5 -
AVYGRQPDWVMERFPDLT VP40_SCMVC 155 5 -
AVYGTDLAWVLKHFSDLE VP40_EBV 152 5 -

Motif 8 width=12
Element Seqn Id St Int Rpt
AGIAGHTYLQAS VP40_HSV11 236 57 -
AGIAGHTYLQAS Q69087 237 57 -
AGIAGHTYLQAS Q69527 237 57 -
AGIAGHTYLQAS P89449 237 57 -
AGVRGHTYLQAT Q83417 215 55 -
AGIEGHTYLQAS VP40_HSVEB 231 58 -
AGVRGHTYLQAT Q85027 215 55 -
AGIEGHTYLQAS O39278 232 58 -
AGIAGHTYLQAS VP40_HSVBC 244 57 -
AGIMGHVYLQAS VP40_VZVD 225 55 -
ASILSPAYLKAS O40922 239 54 -
ASILSPAYLKAS P88911 239 54 -
AKIKKLTYLKAS O40637 218 54 -
AKIKKLTYLKAS VP40_HSVSA 217 54 -
AAVKQSAYLKAS O41936 226 58 -
GVTERESYVKAS VP40_HCMVA 245 57 -
GVTARESYVKAS VP40_SCMVC 238 65 -
ANIPAESYLKAS VP40_EBV 224 54 -