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PR00782

Identifier
LSHMANOLYSIN  [View Relations]  [View Alignment]  
Accession
PR00782
No. of Motifs
7
Creation Date
01-JUN-1997  (UPDATE 07-JUN-1999)
Title
Leishmanolysin (M8) metalloprotease family signature
Database References

PROSITE; PS00142 ZINC_PROTEASE
BLOCKS; BL00142
INTERPRO; IPR001577
Literature References
1. RAWLINGS, N.D. AND BARRETT, A.J.
Evolutionary families of metallopeptidases.
METHODS ENZYMOL. 248 183-228 (1995).

Documentation
Metalloproteases are the most diverse of the four main types of protease,
with more than 30 families identified to date [1]. Of these, around
half contain the HEXXH motif, which has been shown in crystallographic
studies to form part of the metal-binding site [1]. The HEXXH motif is 
relatively common, but can be more stringently defined for metallo-
proteases as abXHEbbHbc, where a is most often valine or threonine and 
forms part of the S1' subsite in thermolysin and neprilysin, b is an
uncharged residue, and c a hydrophobic residue. Proline is never found
in this site, possibly because it would break the helical structure 
adopted by this motif in metalloproteases [1].
 
Metalloproteases can be split into five groups on the basis of their metal-
binding residues: the first three contain the HEXXH motif, the other two
do not [1]. In the first group, a glutamic acid completes the active site -
these are termed HEXXH+E: all families in this group show some sequence
relationship and have been assigned to clan MA [1]. The second group, which
have a third histidine as the extra metal-binding residue, are termed
HEXXH+H and are grouped into clan MB on the basis of their inter-relation-
ship [1]. In the third group, the additional metal-binding residues are
unidentified. The fourth group is diverse - the metal-binding residues are
known but do not form the HEXXH motif. And the fifth group comprises the
remaining families where the metal-binding residues are as yet unknown [1].
 
Leishmanolysin is an enzyme found in Leishmania and related parasitic
protozoa [1]. The endopeptidase is the most abundant protein on the cell
surface during the promastigote stage of the parasite, and is attached to
the membrane by a glycosylphosphatidylinositol anchor [1]. In the amastigote
form, the parasite lives in lysosomes of host macrophages, producing a
form of the protease that has an acidic pH optimum [1]. This differs from
most other metalloproteases and may be an adaptation to the environment in
which the organism survives [1]. The protein contains a catalytic HEXXH
motif, in which the additional zinc-binding residue is unknown.
 
LSHMANOLYSIN is a 7-element fingerprint that provides a fingerprint for
the leishmanolysin (M8) metalloproteases. The fingerprint was derived from 
an initial alignment of 5 sequences: the motifs were drawn from conserved
regions spanning the central portion of the alignment - motif 3 includes the
region encoded by PROSITE pattern ZINC_PROTEASE (PS00142), which contains 
the catalytic HEXXH motif; and motif 4 contains a conserved glutamate, which
may provide the additional zinc ligand. Two iterations on OWL29.3 were
required to reach convergence, at which point a true set comprising 16
sequences was identified.
 
An update on SPTR37_9f identified a true set of 21 sequences.
Summary Information
21 codes involving  7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
721212121212121
60000000
50000000
40000000
30000000
20000000
1234567
True Positives
GP63_CRIFA    GP63_LEICH    GP63_LEIDO    GP63_LEIGU    
GP63_LEIMA GP63_LEIME O00926 O00928
O43994 O46311 O46312 Q25273
Q25274 Q25275 Q25276 Q25286
Q25287 Q25288 Q25289 Q27673
Q94593
Sequence Titles
GP63_CRIFA  LEISHMANOLYSIN HOMOLOG PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE) (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) - CRITHIDIA FASCICULATA. 
GP63_LEICH LEISHMANOLYSIN PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE) (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) - LEISHMANIA CHAGASI.
GP63_LEIDO LEISHMANOLYSIN PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE) (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) - LEISHMANIA DONOVANI.
GP63_LEIGU LEISHMANOLYSIN PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE) (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) - LEISHMANIA GUYANENSIS.
GP63_LEIMA LEISHMANOLYSIN PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE) (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) - LEISHMANIA MAJOR.
GP63_LEIME LEISHMANOLYSIN C1 PRECURSOR (EC 3.4.24.36) (CELL SURFACE PROTEASE) (MAJOR SURFACE GLYCOPROTEIN) (GP63 PROTEIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) - LEISHMANIA MEXICANA.
O00926 GP63-1 SURFACE PROTEASE HOMOLOG - TRYPANOSOMA BRUCEI RHODESIENSE.
O00928 GP63-3 SURFACE PROTEASE HOMOLOG - TRYPANOSOMA BRUCEI RHODESIENSE.
O43994 LEISHMANOLYSIN (EC 3.4.24.36) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) (GLYCOPROTEIN GP63) - LEISHMANIA MAJOR.
O46311 MAJOR SURFACE GLYCOPROTEIN (EC 3.4.24.36) (LEISHMANOLYSIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) (GLYCOPROTEIN GP63) - LEISHMANIA PANAMENSIS.
O46312 MAJOR SURFACE GLYCOPROTEIN (EC 3.4.24.36) (LEISHMANOLYSIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) (GLYCOPROTEIN GP63) - LEISHMANIA PANAMENSIS.
Q25273 SURFACE PROTEASE PRECURSOR - LEISHMANIA DONOVANI.
Q25274 SURFACE PROTEASE PRECURSOR - LEISHMANIA DONOVANI.
Q25275 GLYCOPROTEIN 63 PRECURSOR - LEISHMANIA DONOVANI.
Q25276 GLYCOPROTEIN 63 PRECURSOR - LEISHMANIA DONOVANI.
Q25286 MAJOR SURFACE GLYCOPROTEIN PRECURSOR - LEISHMANIA GUYANENSIS.
Q25287 MAJOR SURFACE GLYCOPROTEIN PRECURSOR - LEISHMANIA GUYANENSIS.
Q25288 MAJOR SURFACE GLYCOPROTEIN PRECURSOR - LEISHMANIA GUYANENSIS.
Q25289 MAJOR SURFACE GLYCOPROTEIN PRECURSOR - LEISHMANIA GUYANENSIS.
Q27673 ECTO-METALLOPROTEINASE PRECURSOR (EC 3.4.24.36) (LEISHMANOLYSIN) (PROMASTIGOTE SURFACE ENDOPEPTIDASE) (GLYCOPROTEIN GP63) - LEISHMANIA AMAZONENSIS.
Q94593 GLYCOPROTEIN GP63 - LEISHMANIA INFANTUM.
Scan History
OWL29_3    2  100  NSINGLE    
SPTR37_9f 2 21 NSINGLE
Initial Motifs
Motif 1  width=30
Element Seqn Id St Int Rpt
DILVKHLIPQALQLHTERLKVRQVQDKWKV GP63_LEICH 151 151 -
DILVKYLIPQALQLHTERLKVRQVQDKWKV GP63_LEIDO 141 141 -
DILVKHLIPQAVQLHTERLKVQQVQGKWKV GP63_LEIMA 154 154 -
DILVSYLIPQALQLHAERLKVRQVQGSWKV GP63_LEIGU 152 152 -
DTLVKHLVPQALQLHRERLKVRQVQGKWKV GP63_LEIME 156 156 -
DILMNYLIPEALQMHKDRLQVQQVQGTWKV GP63_CRIFA 166 166 -

Motif 2 width=30
Element Seqn Id St Int Rpt
VASVPSEEGVLAWATTCQVFSDGHPAVGVI GP63_LEICH 211 30 -
VASVPSEGDVLAWATTCQVFSDGHPAVGVI GP63_LEIDO 201 30 -
VASVPSEEGVLAWATTCQTFSDGHPAVGVI GP63_LEIMA 214 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI GP63_LEIGU 212 30 -
VASVPSEESVLAWATTCQVFPDGHPAVGVI GP63_LEIME 216 30 -
VASVPTSPGVLAWANTCQVFSNDQPAVGVI GP63_CRIFA 225 29 -

Motif 3 width=30
Element Seqn Id St Int Rpt
NIPAANIASRYDQLVTRVVTHEMAHALGFS GP63_LEICH 241 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS GP63_LEIDO 231 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS GP63_LEIMA 244 0 -
NIPAANIVSRYDQGATRVVTHEVAHALGFS GP63_LEIGU 242 0 -
NIPAANIASRYDQLVTRVVTHEMAHAVGFS GP63_LEIME 246 0 -
NIPAATITERYDHLMVHAVTHEIAHSLGFS GP63_CRIFA 255 0 -

Motif 4 width=30
Element Seqn Id St Int Rpt
VPVINSSTAVAKAREQYGCDTLEYLEIEDQ GP63_LEICH 293 22 -
VPVINSSTAVAKAREQYGCGTLEYLEMEDQ GP63_LEIDO 283 22 -
VPVINSSTAVAKAREQYGCDTLEYLEVEDQ GP63_LEIMA 296 22 -
APVINSSTVVAKAREQYGCPTLEYLEVEDQ GP63_LEIGU 294 22 -
VSVITSSTVVAKAREQYGCNSLEYLEIEDQ GP63_LEIME 298 22 -
VPVINSPTVVAKAREHYGCDDVTYVELEDA GP63_CRIFA 307 22 -

Motif 5 width=29
Element Seqn Id St Int Rpt
GAGSAGSHIKMRNAQDELMAPAAAAGYYS GP63_LEICH 324 1 -
GAGSAGSHIKMRNAQDELMAPASDAGYYS GP63_LEIDO 314 1 -
GAGSAGSHIKMRNAQDELMAPAAAAGYYT GP63_LEIMA 327 1 -
GSGSAGSHIKMRNAKDELMAPASAAGYYT GP63_LEIGU 325 1 -
GAGSAGSHIKMRNAKDELMAPAASAGYYT GP63_LEIME 329 1 -
GSGTMGSHWKIRNAQDELMAGISGVAYYT GP63_CRIFA 338 1 -

Motif 6 width=30
Element Seqn Id St Int Rpt
ALTMAIFQDLGFYQADFSKAEVMPWGRNAG GP63_LEICH 353 0 -
ALTMAIFQDLGFYQADFSKAEEMPWGRNAG GP63_LEIDO 343 0 -
ALTMAIFQDLGFYQADFSKAEVMPWGQNAG GP63_LEIMA 356 0 -
ALTMAVFEDLGFYKADFTKAEVMPWGRNAS GP63_LEIGU 354 0 -
ALTMAVFQDLGFYQADFSKAEEMPWGRNVG GP63_LEIME 358 0 -
SLTLSAFEDLGYYKANYSNAETMKWGKDVG GP63_CRIFA 367 0 -

Motif 7 width=30
Element Seqn Id St Int Rpt
CAFLSEKCMERNITKWPAMFCNENEVTMRC GP63_LEICH 383 0 -
CAFLSEKCMEDGITKWPAMFCNENEVTMRC GP63_LEIDO 373 0 -
CAFLTNKCMEQSVTQWPAMFCNESEDAIRC GP63_LEIMA 386 0 -
CDFLTKKCMENNITQWPEMFCNTTERRYRC GP63_LEIGU 384 0 -
CAFLSEKCMAKNVTKWPAMFCNESAATIRC GP63_LEIME 388 0 -
CAFLTGKCVVDNVTQFPSMYCDKDENVYRC GP63_CRIFA 397 0 -
Final Motifs
Motif 1  width=30
Element Seqn Id St Int Rpt
DILVKHLIPQALQLHTERLKVRQVQDKWKV GP63_LEICH 151 151 -
DILVKHLIPQALQLHTERLKVRQVQDKWKV Q25273 151 151 -
DILVKYLIPQALQLHTERLKVRQVQDKWKV GP63_LEIDO 141 141 -
DILVKHLIPQAVQLHTERLKVQQVQGKWKV GP63_LEIMA 154 154 -
DILVSYLIPQALQLHAERLKVRQVQGSWKV GP63_LEIGU 152 152 -
DILVKHLIPQAVQLHKERLKVQQVQGKWKV O43994 154 154 -
DILVKHLIPQALQLHTERLKVRQVQDKWKV Q25276 151 151 -
DILRKYLIPQALQLHTERLKARQVQGKWKV Q94593 156 156 -
DILVKYLIPQALQLHTERLKVRQVQDKWNV Q25274 151 151 -
DILVSYLIPQALQLHAERLKVRQVQGTWKV Q25287 141 141 -
DILVKHLIPQALQLHTERLKVRQVQDKWKV Q25275 151 151 -
DILVSYLIPQALQLHAERLKVRQVQGTWKV Q25286 141 141 -
DILVSYLIPQALQLHAERLKVRQVQGTWKV O46311 141 141 -
DILVSYLIPQALQLHAERLKVRQVQGTWKV O46312 141 141 -
DILVSYLIPQALQLHAERLKVRQVQGTWKV Q25288 141 141 -
DTLVKHLVPQALQLHRERLKVRQVQGKWKV GP63_LEIME 156 156 -
DILVKHLVPQALQLHRERLKVQQVQGKWKV Q27673 153 153 -
DILVNVLLRQALQLHVDRLKVKRVQGSWKV Q25289 152 152 -
DILMNYLIPEALQMHKDRLQVQQVQGTWKV GP63_CRIFA 166 166 -
KSLLDAVIPDALKMHSDRLMVQPVQGPITV O00928 114 114 -
KSLLDAVIPDALKMHSDRLMVQPVKGRITV O00926 119 119 -

Motif 2 width=30
Element Seqn Id St Int Rpt
VASVPSEEGVLAWATTCQVFSDGHPAVGVI GP63_LEICH 211 30 -
VASVPSEEGVLAWAATCQVFSDGHPAVGVI Q25273 211 30 -
VASVPSEGDVLAWATTCQVFSDGHPAVGVI GP63_LEIDO 201 30 -
VASVPSEEGVLAWATTCQTFSDGHPAVGVI GP63_LEIMA 214 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI GP63_LEIGU 212 30 -
VASVPSEEGVLAWATTCQTFSDGHPAVGVI O43994 214 30 -
VASVPSEEGVLAWAATCQVFSDGHPAVGVV Q25276 211 30 -
VASVPSEEGVLAWATTCQVFSDGHPAVGVI Q94593 216 30 -
VASVPSEEGVLAWATTCQVFSDGHPAVGVI Q25274 211 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI Q25287 201 30 -
VASVPSEGDVLAWAATCQVFSDGHPAVGVI Q25275 211 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI Q25286 201 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI O46311 201 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI O46312 201 30 -
VASVPSEPGVLAWATTCQVFSDDHPAVGVI Q25288 201 30 -
VASVPSEESVLAWATTCQVFPDGHPAVGVI GP63_LEIME 216 30 -
VASVPSEESVLAWATTCQVFADGHPAVGVI Q27673 213 30 -
VASVPSEPGVMAWAVICQVFPDGRPAVGVI Q25289 212 30 -
VASVPTSPGVLAWANTCQVFSNDQPAVGVI GP63_CRIFA 225 29 -
YGAAGPMGSPAAWAGPCSRYKDHRPTVGVF O00928 172 28 -
YGAAGPMGSPAAWAVPCAKLRNGRPVVGVF O00926 177 28 -

Motif 3 width=30
Element Seqn Id St Int Rpt
NIPAANIASRYDQLVTRVVTHEMAHALGFS GP63_LEICH 241 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS Q25273 241 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS GP63_LEIDO 231 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS GP63_LEIMA 244 0 -
NIPAANIVSRYDQGATRVVTHEVAHALGFS GP63_LEIGU 242 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS O43994 244 0 -
NIPAANIASRYNQLVTRVVTHEMAHTLGFS Q25276 241 0 -
NIPAANIASRYDQAVTRVVTHEMAHALGFS Q94593 246 0 -
NIPAANIASRYDQLVTRVVTHEMAHVGFSG Q25274 241 0 -
NIPAANIVSRYDQGTTRTVTHEVAHALGFS Q25287 231 0 -
NIPAANIASRYDQLVTRVVTHEMAHALGFS Q25275 241 0 -
NIPAANIVSRYDQGTTRTVTHEVAHALGFS Q25286 231 0 -
NIPAANIVSRYDQGATRTVTHEVAHALGFS O46311 231 0 -
NIPAANIVSRYDQGATRTVTHEVAHALGFS O46312 231 0 -
NIPAANIVSRYDQGTTRVVTHEVAHALGFS Q25288 231 0 -
NIPAANIASRYDQLVTRVVTHEMAHAVGFS GP63_LEIME 246 0 -
NIPAANIASRYDQLVTRVVAHEMAHALGFS Q27673 243 0 -
NIPAAHIRSPYDQIMVRTVAHEITHALGFD Q25289 242 0 -
NIPAATITERYDHLMVHAVTHEIAHSLGFS GP63_CRIFA 255 0 -
VFNIGPEVLTSHDSSMRVTAHEIAHALGFG O00928 200 -2 -
VFNIGPEVLTSHDSSMRVTAHEIAHALGFG O00926 205 -2 -

Motif 4 width=30
Element Seqn Id St Int Rpt
VPVINSSTAVAKAREQYGCDTLEYLEIEDQ GP63_LEICH 293 22 -
VPVINSSTAVAKAREQYGCDTLEYLEIEDQ Q25273 293 22 -
VPVINSSTAVAKAREQYGCGTLEYLEMEDQ GP63_LEIDO 283 22 -
VPVINSSTAVAKAREQYGCDTLEYLEVEDQ GP63_LEIMA 296 22 -
APVINSSTVVAKAREQYGCPTLEYLEVEDQ GP63_LEIGU 294 22 -
VPVINSSTAVAKAREQYGCDTLEYLEVEDQ O43994 296 22 -
VPVLKSRTAVAKAREQYGCDTLEYLEIEDQ Q25276 293 22 -
VPVVKSSTAVAKAREQYGCGTLEYLEIEDQ Q94593 298 22 -
VSVINSSTAVAKAREQYGCDTLEYLEIEDQ Q25274 292 21 -
APVINSSTVVAKAREQYGCPTLEYLEVEDQ Q25287 283 22 -
APVINSSTAVAKAREQYGCDTLEYLEMEDE Q25275 293 22 -
APVINSSTVVAKAREQYGCPTLEYLEVEDQ Q25286 283 22 -
APVINSSTVVAKAREQYGCPTLEYLEVEDQ O46311 283 22 -
APVINSSTVVAKAREQYGCPTLEYLEVEDQ O46312 283 22 -
APVINSSTVVAKARDEYGCPTLEYLEVEDQ Q25288 283 22 -
VSVITSSTVVAKAREQYGCNSLEYLEIEDQ GP63_LEIME 298 22 -
TPMINSSTAVAKAREQYGCNSLEYLEMEDQ Q27673 295 22 -
VPVLNSPTVVAKAREQYGCASLSFLELEDT Q25289 294 22 -
VPVINSPTVVAKAREHYGCDDVTYVELEDA GP63_CRIFA 307 22 -
VWVVKSQTVVKKAQEFYGCDKITGVELEDE O00928 251 21 -
VWVVKSPTVVKKAQEFYGCNRITGVELEDE O00926 256 21 -

Motif 5 width=29
Element Seqn Id St Int Rpt
GAGSAGSHIKMRNAQDELMAPAAAAGYYS GP63_LEICH 324 1 -
GAGSAGSHIKMRNAQDELMAPAAAAGYYS Q25273 324 1 -
GAGSAGSHIKMRNAQDELMAPASDAGYYS GP63_LEIDO 314 1 -
GAGSAGSHIKMRNAQDELMAPAAAAGYYT GP63_LEIMA 327 1 -
GSGSAGSHIKMRNAKDELMAPASAAGYYT GP63_LEIGU 325 1 -
GAGSAGSHIKMRNAQDELMAPAAAAGYYT O43994 327 1 -
GAGSAGSHIKMRNAQDELMAPAAAAGYYS Q25276 324 1 -
GAGSAGSHIKMRNAQDELMAPAAAGGYYT Q94593 329 1 -
GAGSAGSHIKMRNAKDELMAPAAAAGYYS Q25274 323 1 -
GSGSAGSHLKGRNAKDELMAPASAAGYYT Q25287 314 1 -
GAGSAGSHIKMRNAQDELMAPAAAAGYYS Q25275 324 1 -
GSGSAGSHLKGRNAKDELMAPASAAGYYT Q25286 314 1 -
GSGSAGSHLKGRNAKDELMAPASAAGYYT O46311 314 1 -
GSGSAGSHLKGRNAKDELMAPASAAGYYT O46312 314 1 -
GSGSAGSHLKGRNAKDELMAPASAAGYYT Q25288 314 1 -
GAGSAGSHIKMRNAKDELMAPAASAGYYT GP63_LEIME 329 1 -
QGSAAPGSHIKANAQDELMAPTASAGYYT Q27673 324 -1 -
GTSTAGSHLKGRNAKDELMAPAVTAGYYS Q25289 325 1 -
GSGTMGSHWKIRNAQDELMAGISGVAYYT GP63_CRIFA 338 1 -
GEGTINSHWERRIAMEEMMTGVKGSDGGR O00928 282 1 -
GRGTVRSHWERRIAMEEMMAGIKGSDGGR O00926 287 1 -

Motif 6 width=30
Element Seqn Id St Int Rpt
ALTMAIFQDLGFYQADFSKAEVMPWGRNAG GP63_LEICH 353 0 -
ALTMAIFQDLGFYQADFSKAEVMPWGRNAG Q25273 353 0 -
ALTMAIFQDLGFYQADFSKAEEMPWGRNAG GP63_LEIDO 343 0 -
ALTMAIFQDLGFYQADFSKAEVMPWGQNAG GP63_LEIMA 356 0 -
ALTMAVFEDLGFYKADFTKAEVMPWGRNAS GP63_LEIGU 354 0 -
ALTMAILQDLGFYQADFSKAEVMPWGQNAG O43994 356 0 -
ALTMAIFQDLGFYQADFSKAEVMPWGRNAG Q25276 353 0 -
ALTMAVFQDLGFYQADFSKAEVMPWGRNAG Q94593 358 0 -
ALTMAIFQDLGFYQADFSKAEVMPWGRNAG Q25274 352 0 -
ALTMAVFEDLGFYQADFAKAEVMPWGRNAS Q25287 343 0 -
ALTMAIFQDLGFYQADFSKAEVMPWGRNAG Q25275 353 0 -
ALTMAVFEDLGFYKADFAKAEVMPWGRNAS Q25286 343 0 -
ALTMAVFEDLGFYKADFAKAEMMPWANLAT O46311 343 0 -
ALTMAVFEDLGFYKADFAKAEMMPWANLAT O46312 343 0 -
ALTMAVFEDLGFYQADFAKAEVMPWGRNAS Q25288 343 0 -
ALTMAVFQDLGFYQADFSKAEEMPWGRNVG GP63_LEIME 358 0 -
ALTMAVFQDLGFYQADFSKAEAMPWGRNAA Q27673 353 0 -
ALTMAVLQDLGFYRAVFRLAEVMPWAEYSS Q25289 354 0 -
SLTLSAFEDLGYYKANYSNAETMKWGKDVG GP63_CRIFA 367 0 -
VLTMALFEDMGFYRAKWGTEEDMHFGKGRG O00928 313 2 -
VLTMALFEDMGFYKAKWGTEEDMHFGKGRG O00926 318 2 -

Motif 7 width=30
Element Seqn Id St Int Rpt
CAFLSEKCMERNITKWPAMFCNENEVTMRC GP63_LEICH 383 0 -
CAFLSEKCMERNITKWPAMFCNENEVTMRC Q25273 383 0 -
CAFLSEKCMEDGITKWPAMFCNENEVTMRC GP63_LEIDO 373 0 -
CAFLTNKCMEQSVTQWPAMFCNESEDAIRC GP63_LEIMA 386 0 -
CDFLTKKCMENNITQWPEMFCNTTERRYRC GP63_LEIGU 384 0 -
CAFLTNKCMEQSVTQWPAMFCNESEDAIRC O43994 386 0 -
CAFLSEKCMERNITKWPAMFCNENEVAMRC Q25276 383 0 -
CAFLSEKCMEQNITKWRAMFCNESEDAMRC Q94593 388 0 -
CAFLSEKCMERNITKWPAMFCNENEVTMRC Q25274 382 0 -
CDFLTKKCMENNITQWPEMFCNTTDENALR Q25287 373 0 -
CAFLSEKCMEDGITKWPAMFCNSDDALRCP Q25275 383 0 -
CDFLTKKCMENNITQWPEMFCNTTDENALR Q25286 373 0 -
CDFLTKKCMENNITQWPWMFCNTDENALRC O46311 373 0 -
CDFLTKKCMENNITQWPWMFCNTDENALRC O46312 373 0 -
CDFLTKKCMENNITQWPEMFCNTTDENALR Q25288 373 0 -
CAFLSEKCMAKNVTKWPAMFCNESAATIRC GP63_LEIME 388 0 -
CAFLSEKCMANGITKWPAMFCNESADAIRC Q27673 383 0 -
CDFITQKCMERNITQWPWMFCNTTESSYRC Q25289 384 0 -
CAFLTGKCVVDNVTQFPSMYCDKDENVYRC GP63_CRIFA 397 0 -
CDFLEKKCVENGKSNFPDVFCTSETKPGEN O00928 343 0 -
CDFLKKKCIENGRSNFPDVFCTSATKKGEN O00926 348 0 -