| Identifier | TRNASYNTHASP [View Relations] [View Alignment]
|
| Accession | PR01042 |
| No. of Motifs | 4 |
| Creation Date | 11-DEC-1998 (UPDATE 28-JUN-1999) |
| Title | Aspartyl-tRNA synthetase signature |
| Database References | PRINTS; PR90000 TRNASYNTH; PR90002 TRNASYNTHCLII
PROSITE; PS00179 AA_TRNA_LIGASE_II_1; PS00339 AA_TRNA_LIGASE_II_2
BLOCKS; BL00179
PFAM; PF01336 Aspartyl_tRNA_N
INTERPRO; IPR002312
PDB; 1ASY; 1ASZ
SCOP; 1ASY; 1ASZ
CATH; 1ASY |
| Literature References | 1. LODISH, H., BALTIMORE, D., BERK, A., ZIPURSKY, S.L., MATSUDAIRA, P.
AND DARNELL, J.
Nucleic Acids, the Genetic Code, and Protein Synthesis.
IN MOLECULAR CELL BIOLOGY, SCIENTIFIC AMERICAN BOOKS (NEW YORK), 1995,
PP.126-128.
2. DELARUE, M.
Aminoacyl-tRNA synthetases.
CURR.OPIN.STRUCT.BIOL. 5 48-55 (1995).
3. PERONA, J.J., ROULD, M. AND STEITZ, T.A.
Structural Basis for Transfer RNA Aminoacylation by Escherichia coli
Glutaminyl-tRNA Synthetase.
BIOCHEMISTRY 32 8758-8771 (1993).
|
| Documentation | Appropriate attachment of an amino acid to its cognate tRNA is the key to
faithful translation of the genetic code. The family of enzymes responsible
for this is the aminoacyl-tRNA synthetases (AATRSs) (EC 6.1.1.-).
AATRSs catalyse a two-step reaction:
(1) Enzyme + amino acid + ATP ---> Enzyme(aminoacyl-AMP) + PPi
(2) tRNA + Enzyme(aminoacyl-AMP) ---> aminoacyl-tRNA + AMP + Enzyme
In the first step, they form an aminoacyl-adenylate, in which the carboxyl
of the amino acid is linked to the alpha-phosphate of ATP, by displacing
the pyrophosphate. When the correct tRNA is bound, the aminoacyl group is
transferred to the 2'- or 3'-terminal OH of the tRNA at the expense of AMP
[1].
Based on structural and sequence comparisons, this group of at least 20
proteins (in prokaryotes there are approximately 20, but in eukaryotes
there are usually 2 forms for each amino acid; namely, the cytosolic and
mitochondrial forms) can be divided into two classes.
Class I AATRSs contain a characteristic Rossman fold and are mostly
monomeric. At the primary structure level, two highly-conserved motifs
are observed, `HIGH' and `KMSKS' [2,3]; these are associated with the ATP-
binding site.
Class II AATRSs share an anti-parallel beta-sheet formation, flanked by
alpha-helices [3], and are mostly dimeric or multimeric.
Further distinction between the two classes is evident when the reaction
mechanisms are investigated. In reactions catalysed by the class I AATRSs,
the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in
class II reactions, the 3'-hydroxyl site is preferred.
Aspartyl-tRNA synthetase (EC 6.1.1.12) is specific to aspartate and belongs
to class II.
TRNASYNTHASP is a 4-element fingerprint that provides a signature for the
aspartyl-tRNA synthetase family. The fingerprint was derived from an initial
alignment of 6 sequences: the motifs were drawn from conserved regions
spanning the full alignment length - motif 1 includes helix 8; motifs 2 and
3 span the region encoded by PROSITE pattern AA_TRNA_LIGASE_II_1 (PS00179),
motif 2 including beta-strand 11 and motif 3 including strands 15 and 16;
and motif 4 spans the C-terminus of helix 14 and the N-terminus of strand
17. Three iterations on OWL31.1 were required to reach convergence, at which
point a true set comprising 34 sequences was identified. A single partial
match was found, SYD_PSEAE, a fragment that lacks the portion of sequence
bearing motifs 1 and 2.
An update on SPTR37_9f identified a true set of 44 sequences, and 20
partial matches.
|
| Summary Information | 44 codes involving 4 elements
1 codes involving 3 elements
19 codes involving 2 elements
|
| Composite Feature Index | | 4 | 44 | 44 | 44 | 44 | | 3 | 1 | 0 | 1 | 1 | | 2 | 0 | 19 | 0 | 19 | | 1 | 2 | 3 | 4 |
|
| True Positives | O57980 O58776 O74407 O81892
O84546 P90831 SYDC_YEAST SYDM_YEAST
SYD_AQUAE SYD_ARCFU SYD_BACSU SYD_BORBU
SYD_BUCAP SYD_CAEEL SYD_ECOLI SYD_HAEIN
SYD_HALSA SYD_HELPY SYD_HUMAN SYD_METJA
SYD_METTH SYD_MYCGE SYD_MYCLE SYD_MYCPN
SYD_MYCTU SYD_PYRKO SYD_RAT SYD_SYNY3
SYD_THETH SYD_TREPA SYNC_YEAST SYNM_YEAST
SYN_BACSU SYN_BORBU SYN_CAEEL SYN_ECOLI
SYN_HAEIN SYN_HUMAN SYN_LACDE SYN_MYCGE
SYN_MYCPN SYN_SYNY3 SYN_THETH SYN_TREPA |
| True Positive Partials | |
| Sequence Titles | O57980 434AA LONG HYPOTHETICAL ASPARAGINYL-TRNA SYNTHETASE - PYROCOCCUS HORIKOSHII.
O58776 438AA LONG HYPOTHETICAL ASPARTYL-TRNA SYNTHETASE - PYROCOCCUS HORIKOSHII.
O74407 ASPARTYL-TRNA SYNTHETASE - SCHIZOSACCHAROMYCES POMBE (FISSION YEAST).
O81892 PUTATIVE ASPARTATE--TRNA LIGASE - ARABIDOPSIS THALIANA (MOUSE-EAR CRESS).
O84546 ASPARTYL TRNA SYNTHETASE - CHLAMYDIA TRACHOMATIS.
P90831 HYPOTHETICAL PROTEIN F10C2.6 - CAENORHABDITIS ELEGANS.
SYDC_YEAST ASPARTYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
SYDM_YEAST ASPARTYL-TRNA SYNTHETASE, MITOCHONDRIAL (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
SYD_AQUAE ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - AQUIFEX AEOLICUS.
SYD_ARCFU ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - ARCHAEOGLOBUS FULGIDUS.
SYD_BACSU ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - BACILLUS SUBTILIS.
SYD_BORBU ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE).
SYD_BUCAP ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - BUCHNERA APHIDICOLA.
SYD_CAEEL PROBABLE ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - CAENORHABDITIS ELEGANS.
SYD_ECOLI ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - ESCHERICHIA COLI.
SYD_HAEIN ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - HAEMOPHILUS INFLUENZAE.
SYD_HALSA ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - HALOBACTERIUM SALINARIUM.
SYD_HELPY ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - HELICOBACTER PYLORI (CAMPYLOBACTER PYLORI).
SYD_HUMAN ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - HOMO SAPIENS (HUMAN).
SYD_METJA ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - METHANOCOCCUS JANNASCHII.
SYD_METTH ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - METHANOBACTERIUM THERMOAUTOTROPHICUM.
SYD_MYCGE ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - MYCOPLASMA GENITALIUM.
SYD_MYCLE ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) (ANTIGEN T5) - MYCOBACTERIUM LEPRAE.
SYD_MYCPN ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - MYCOPLASMA PNEUMONIAE.
SYD_MYCTU ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - MYCOBACTERIUM TUBERCULOSIS.
SYD_PYRKO ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - PYROCOCCUS KODAKARAENSIS.
SYD_RAT ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - RATTUS NORVEGICUS (RAT).
SYD_SYNY3 ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
SYD_THETH ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - THERMUS AQUATICUS (SUBSP. THERMOPHILUS).
SYD_TREPA ASPARTYL-TRNA SYNTHETASE (EC 6.1.1.12) (ASPARTATE--TRNA LIGASE) (ASPRS) - TREPONEMA PALLIDUM.
SYNC_YEAST ASPARAGINYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.22) (ASPARAGINE-- TRNA LIGASE) (ASNRS) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
SYNM_YEAST ASPARAGINYL-TRNA SYNTHETASE, MITOCHONDRIAL PRECURSOR (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
SYN_BACSU ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - BACILLUS SUBTILIS.
SYN_BORBU ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE).
SYN_CAEEL PROBABLE ASPARAGINYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - CAENORHABDITIS ELEGANS.
SYN_ECOLI ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - ESCHERICHIA COLI.
SYN_HAEIN ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - HAEMOPHILUS INFLUENZAE.
SYN_HUMAN ASPARAGINYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.22) (ASPARAGINE-- TRNA LIGASE) (ASNRS) - HOMO SAPIENS (HUMAN).
SYN_LACDE ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - LACTOBACILLUS DELBRUECKII (SUBSP. BULGARICUS).
SYN_MYCGE ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - MYCOPLASMA GENITALIUM.
SYN_MYCPN ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - MYCOPLASMA PNEUMONIAE.
SYN_SYNY3 PROBABLE ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
SYN_THETH ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - THERMUS AQUATICUS (SUBSP. THERMOPHILUS).
SYN_TREPA ASPARAGINYL-TRNA SYNTHETASE (EC 6.1.1.22) (ASPARAGINE--TRNA LIGASE) (ASNRS) - TREPONEMA PALLIDUM.
SYN_BRUMA ASPARAGINYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.22) (ASPARAGINE-- TRNA LIGASE) (ASNRS) (POTENTIALLY PROTECTIVE 63 KD ANTIGEN) - BRUGIA MALAYI.
O84786 LYSYL TRNA SYNTHETASE - CHLAMYDIA TRACHOMATIS.
O87821 LYSYL-TRNA SYNTHETASE - SINORHIZOBIUM MELILOTI.
SYK2_ECOLI LYSYL-TRNA SYNTHETASE, HEAT INDUCIBLE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - ESCHERICHIA COLI.
SYKC_YEAST LYSYL-TRNA SYNTHETASE, CYTOPLASMIC (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
SYKM_YEAST LYSYL-TRNA SYNTHETASE, MITOCHONDRIAL PRECURSOR (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
SYK_ACICA LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - ACINETOBACTER CALCOACETICUS.
SYK_BACSU LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - BACILLUS SUBTILIS.
SYK_CAEEL PROBABLE LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - CAENORHABDITIS ELEGANS.
SYK_CAMJE LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - CAMPYLOBACTER JEJUNI.
SYK_CRILO LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - CRICETULUS LONGICAUDATUS (LONG-TAILED HAMSTER) (CHINESE HAMSTER).
SYK_HUMAN LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) (KIAA0070) - HOMO SAPIENS (HUMAN).
SYK_LYCES LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - LYCOPERSICON ESCULENTUM (TOMATO).
SYK_MYCFE LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - MYCOPLASMA FERMENTANS.
SYK_MYCHO LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - MYCOPLASMA HOMINIS.
SYK_MYCTU LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - MYCOBACTERIUM TUBERCULOSIS.
SYK_STAAU LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - STAPHYLOCOCCUS AUREUS.
SYK_SULSO LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - SULFOLOBUS SOLFATARICUS.
SYK_SYNY3 LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
SYK_THETH LYSYL-TRNA SYNTHETASE (EC 6.1.1.6) (LYSINE--TRNA LIGASE) (LYSRS) - THERMUS AQUATICUS (SUBSP. THERMOPHILUS).
|
| Scan History | OWL31_1 3 38 NSINGLE
SPTR37_9f 4 70 NSINGLE
|
| Initial Motifs | Motif 1 width=13
Element Seqn Id St Int Rpt
LPQSPQLFKQLLM SYD_MYCLE 189 189 -
LAQSPQLYKQMAI SYD_CAEEL 276 276 -
LPQSPQLFKQLLM SYD_MYCCA 147 147 -
LAQSPQLYKQMCI SYD_HUMAN 245 245 -
LPQSPQLFKQLLM SYD_ECOLI 190 190 -
LPQSPQLFKQLLM SYD_HAEIN 191 191 -
Motif 2 width=14
Element Seqn Id St Int Rpt
EKVYTIGPVFRAED SYD_CAEEL 293 4 -
DRYYQIVRCFRDED SYD_MYCCA 164 4 -
DRYYQIVKCFRDED SYD_ECOLI 207 4 -
DRYYQIVKCFRDED SYD_HAEIN 208 4 -
ERYYQIAHCYRDED SYD_MYCLE 206 4 -
EKVFSIGPVFRAED SYD_HUMAN 262 4 -
Motif 3 width=17
Element Seqn Id St Int Rpt
YDLVMNGFEIGGGSQRI SYD_MYCCA 423 245 -
YDMVINGYEVGGGSVRI SYD_ECOLI 474 253 -
YDMVINGYEVGGGSVRI SYD_HAEIN 475 253 -
YDIVCNGHEIGSGSVRI SYD_MYCLE 474 254 -
YDMFMRGEEILSGAQRI SYD_CAEEL 446 139 -
YDMFMRGEEILSGAQRI SYD_HUMAN 415 139 -
Motif 4 width=15
Element Seqn Id St Int Rpt
IDSFKYGCPPHAGGG SYD_CAEEL 486 23 -
IDSFRFGAPPHAGGG SYD_HUMAN 455 23 -
LDALKYGTPPHAGLA SYD_ECOLI 518 27 -
MNAYKYGAPYHAGIA SYD_MYCCA 467 27 -
LDALKFGTPPHAGLA SYD_HAEIN 519 27 -
LEAFTFGAPPHGGIA SYD_MYCLE 518 27 -
|
| Final Motifs | Motif 1 width=13
Element Seqn Id St Int Rpt
LPQSPQLFKQLLM SYD_SYNY3 197 197 -
LPQSPQLFKQLLM SYD_BACSU 196 196 -
LPQSPQLFKQMLM SYD_THETH 196 196 -
LPQSPQLFKQLLM SYD_HELPY 190 190 -
LPQSPQLFKQILM SYD_AQUAE 201 201 -
LPQSPQLFKQMLM O81892 248 248 -
LPQSPQLFKQILM SYD_BUCAP 188 188 -
LPQSPQLFKQLLM SYD_ECOLI 190 190 -
LPQSPQLFKQILM O84546 196 196 -
LPQSPQLFKQLLM SYD_MYCTU 194 194 -
LPQSPQLFKQLLM SYD_HAEIN 191 191 -
LPQSPQLYKQLLM SYD_TREPA 210 210 -
LPQSPQLFKQLLM SYD_MYCLE 189 189 -
LPQSPQLYKQLIM SYD_BORBU 111 111 -
LGQSPQLYKQMLM SYD_METJA 193 193 -
LAQSPQLYKQIMM SYD_PYRKO 187 187 -
LAQSPQLYKQMMM O58776 187 187 -
LAQSPQLYKQMAI SYD_CAEEL 276 276 -
LPQSPQQFKQLLM P90831 186 186 -
LDQSPQQYKQLLM SYDM_YEAST 221 221 -
LVQSPQIYKQLLM SYD_MYCGE 181 181 -
LNQSPQLYKQVLM SYD_ARCFU 185 185 -
LSQSPQLYKQMLI O74407 304 304 -
LAQSPQLYKQMCI SYD_HUMAN 245 245 -
LAQSPQLYKQMCI SYD_RAT 246 246 -
LPQSPQIYKQLLM SYD_MYCPN 187 187 -
LGQSPQLYKQIMM SYD_METTH 192 192 -
LSQSPQLYKQILV SYD_HALSA 186 186 -
LAQSPQFNKQQLI SYDC_YEAST 297 297 -
LSQSGQLYAEAGA SYN_THETH 182 182 -
LTVSGQLEAEVMA SYN_SYNY3 255 255 -
LSQSGQLYMEAAA SYN_BACSU 180 180 -
LSQSGQLYGEVGA SYN_LACDE 182 182 -
LTQSSQLYLETCL SYNC_YEAST 301 301 -
LTVSGQLNGETYA SYN_HAEIN 219 219 -
LTVSGQLNGETYA SYN_ECOLI 207 207 -
LTVSGQLQGEAYA SYN_TREPA 239 239 -
LSQSAQLYLEAAI O57980 185 185 -
LTQSSQLYLETCL SYN_HUMAN 296 296 -
LTQSSQLYLETCN SYN_CAEEL 292 292 -
LSVTGQLHGEAYA SYN_BORBU 208 208 -
LTVSTQLHLEILA SYNM_YEAST 213 213 -
LTVSGQFGAEAFA SYN_MYCGE 191 191 -
LTVSGQFGAECYA SYN_MYCPN 190 190 -
Motif 2 width=14
Element Seqn Id St Int Rpt
DRYYQIARCFRDED SYD_SYNY3 214 4 -
ERYYQIARCFRDED SYD_BACSU 213 4 -
DRYFQIARCFRDED SYD_THETH 213 4 -
DRYFQIARCFRDED SYD_HELPY 207 4 -
DRYFQIVKCFRDED SYD_AQUAE 218 4 -
DKYYQIARCFRDED O81892 265 4 -
DKYYQIVKCFRDED SYD_BUCAP 205 4 -
DRYYQIVKCFRDED SYD_ECOLI 207 4 -
DRYFQIATCFRDED O84546 213 4 -
ERYYQIARCYRDED SYD_MYCTU 211 4 -
DRYYQIVKCFRDED SYD_HAEIN 208 4 -
DRYFQLARCYRDED SYD_TREPA 227 4 -
ERYYQIAHCYRDED SYD_MYCLE 206 4 -
DKYFQIARCYRDED SYD_BORBU 128 4 -
DRVFEIAPIFRAEE SYD_METJA 210 4 -
DRVYEIAPIFRAEE SYD_PYRKO 204 4 -
DKVFEIAPIFRAEE O58776 204 4 -
EKVYTIGPVFRAED SYD_CAEEL 293 4 -
DRYFQIARCYRDEG P90831 203 4 -
NKYYQMARCFRDED SYDM_YEAST 238 4 -
EKYFQIARVYRDED SYD_MYCGE 198 4 -
EKVFEIGPIFRAEE SYD_ARCFU 202 4 -
ERVFEIGPVFRAED O74407 321 4 -
EKVFSIGPVFRAED SYD_HUMAN 262 4 -
EKVFCIGPVFRAED SYD_RAT 263 4 -
EKYFQIAHVYRDED SYD_MYCPN 204 4 -
DRVYEIAPIFRAEE SYD_METTH 209 4 -
DRLFEVGHAFRAED SYD_HALSA 203 4 -
ERVYEIGPVFRAEN SYDC_YEAST 314 4 -
AKVYTFGPTFRAER SYN_THETH 198 3 -
QNVYTFGPTFRAEN SYN_SYNY3 271 3 -
GKVFSFGPTFRAEK SYN_BACSU 196 3 -
GKIFTFGPTFRAEA SYN_LACDE 198 3 -
GDVYTIQESFRAEK SYNC_YEAST 317 3 -
SKIYTFGPTFRAEN SYN_HAEIN 235 3 -
SKIYTFGPTFRAEN SYN_ECOLI 223 3 -
TRIYTFGPTFRAEN SYN_TREPA 255 3 -
EKVWSLTPSFRAEK O57980 201 3 -
GDVFCIAQSYRAEQ SYN_HUMAN 312 3 -
GDVYCISQSYRAEK SYN_CAEEL 308 3 -
SKIYTFGPTFRAEN SYN_BORBU 224 3 -
SRCWTLSPCFRAEK SYNM_YEAST 229 3 -
KKVFTFGPTFRAEK SYN_MYCGE 207 3 -
KKVFTFGPTFRAEK SYN_MYCPN 206 3 -
Motif 3 width=17
Element Seqn Id St Int Rpt
YDLVMNGVEIGGGSLRI SYD_SYNY3 480 252 -
YDLVLNGYELGGGSIRI SYD_BACSU 477 250 -
YDLVLNGVEVGGGSIRI SYD_THETH 468 241 -
YDVVLNGVELGGGSIRI SYD_HELPY 466 245 -
YDMVLNGEEIGGGSIRI SYD_AQUAE 492 260 -
YDMVYNGVEIGGGSLRI O81892 526 247 -
YDLVINGYEIGGGSVRI SYD_BUCAP 472 253 -
YDMVINGYEVGGGSVRI SYD_ECOLI 474 253 -
YDLVLNGYEIASGSQRI O84546 473 246 -
YDIVCNGHEIGGGSVRI SYD_MYCTU 479 254 -
YDMVINGYEVGGGSVRI SYD_HAEIN 475 253 -
YDLVLNGYELASGSIRI SYD_TREPA 491 250 -
YDIVCNGHEIGSGSVRI SYD_MYCLE 474 254 -
YDLVLNGVELGSGSIRI SYD_BORBU 392 250 -
FDLMYKDLEISSGAQRI SYD_METJA 353 129 -
FDLEYRGVEISSGGQRE SYD_PYRKO 353 135 -
FDLEYRGVEISSGGQRE O58776 353 135 -
YDMFMRGEEILSGAQRI SYD_CAEEL 446 139 -
YDLVINGVEMGGGSIRI P90831 454 237 -
YDLVVNGVELGGGSTRI SYDM_YEAST 545 293 -
FDLVLNGFEIGSGSIRI SYD_MYCGE 443 231 -
FDLMHGWLELSSGAQRI SYD_ARCFU 345 129 -
YDFFMKGQEIMSGAQRI O74407 494 159 -
YDMFMRGEEILSGAQRI SYD_HUMAN 415 139 -
YDMFMRGEEILSGAQRI SYD_RAT 416 139 -
YDLVLNGFELGSGSIRI SYD_MYCPN 449 231 -
FDLMYRDLEISSGAMRV SYD_METTH 352 129 -
FDLLYRGQELSSGGQRE SYD_HALSA 351 134 -
YDFFMRGEEILSGAQRI SYDC_YEAST 469 141 -
LLRPEGYGEIIGGSQRI SYN_THETH 353 141 -
DILAPKIGEIIGGSQRE SYN_SYNY3 428 143 -
LIAPEGYGEIIGGSERI SYN_BACSU 345 135 -
VEAPEGYGEIMGGSERE SYN_LACDE 347 135 -
DVLMPNVGEITGGSMRI SYNC_YEAST 469 138 -
DVLAPGIGEIIGGSQRE SYN_HAEIN 392 143 -
DVLAPGIGEIIGGSQRE SYN_ECOLI 380 143 -
DLLVPGLGEIMGGSERE SYN_TREPA 438 169 -
MLAPEGYGEIIGGSQRE O57980 349 134 -
DVLMPNVGEIVGGSMRI SYN_HUMAN 463 137 -
DLLMPGVGEIVGGSMRI SYN_CAEEL 460 138 -
DILVPKIGEIIGGSERE SYN_BORBU 381 143 -
DLLVPGMGEIIGGSLRE SYNM_YEAST 405 162 -
DLLLPKIGEICGGSERE SYN_MYCGE 371 150 -
DLLFPQIGEICGGSERE SYN_MYCPN 370 150 -
Motif 4 width=15
Element Seqn Id St Int Rpt
LDAFEYGTPPHGGIA SYD_SYNY3 524 27 -
LEAFEYGAPPHGGIA SYD_BACSU 521 27 -
LEALEYGAPPHGGIA SYD_THETH 512 27 -
LEALKFGAPPHGGFA SYD_HELPY 510 27 -
LEALKYGAPPHGGLA SYD_AQUAE 536 27 -
LEALDMGAPPHGGIA O81892 570 27 -
IEALKYGPPPHAGIA SYD_BUCAP 516 27 -
LDALKYGTPPHAGLA SYD_ECOLI 518 27 -
IDALSFGTPPHLGIA O84546 517 27 -
LEAFMFGAPPHGGIA SYD_MYCTU 523 27 -
LDALKFGTPPHAGLA SYD_HAEIN 519 27 -
TEAFKYGAPPHGGIA SYD_TREPA 535 27 -
LEAFTFGAPPHGGIA SYD_MYCLE 518 27 -
LKALEYGAPNHGGIA SYD_BORBU 436 27 -
LEAFKYGMPPHAGWG SYD_METJA 393 23 -
LKAFRYGMPPHGGFG SYD_PYRKO 393 23 -
LKAFEYGMPPHGGFG O58776 393 23 -
IDSFKYGCPPHAGGG SYD_CAEEL 486 23 -
LNALSHGAPPHGGFA P90831 494 23 -
LNAFDMGTPPHAGFA SYDM_YEAST 588 26 -
LEAYQYGAPVHGGMG SYD_MYCGE 483 23 -
LEAFRYGMPPHAGWG SYD_ARCFU 385 23 -
IDAFAIGCPPHAGGG O74407 535 24 -
IDSFRFGAPPHAGGG SYD_HUMAN 455 23 -
IDSFRFGAPPHAGGG SYD_RAT 456 23 -
MEAYQYGAPVHAGMG SYD_MYCPN 489 23 -
LSAFEYGMPPHAGWG SYD_METTH 392 23 -
LDAFRYGVPPHGGYG SYD_HALSA 391 23 -
CDGFSYGCPPHAGGG SYDC_YEAST 511 25 -
LDLRRFGSVPHSGFG SYN_THETH 393 23 -
LDLRRYGSVPHAGFG SYN_SYNY3 468 23 -
AELRKYGSVPHSGFG SYN_BACSU 385 23 -
LDLRKYGSVPHSGFG SYN_LACDE 387 23 -
IDQRKYGTCPHGGYG SYNC_YEAST 509 23 -
RDLRKYGSVPHSGFG SYN_HAEIN 432 23 -
RDLRRYGTVPHSGFG SYN_ECOLI 420 23 -
TDLRRFGTAPHAGFG SYN_TREPA 478 23 -
LDLRRYGSVPHSGFG O57980 389 23 -
TDQRKYGTCPHGGYG SYN_HUMAN 503 23 -
MDQRKYGSVPHGGYG SYN_CAEEL 500 23 -
LDLRRFGSAPHSGFG SYN_BORBU 421 23 -
VSLRKEGSAPHGGFG SYNM_YEAST 446 24 -
LDMRKWGYFASAGFG SYN_MYCGE 411 23 -
LDMRKWGYFASAGFG SYN_MYCPN 410 23 -
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