Identifier | TRNASYNTHASP  [View Relations]  [View Alignment]  
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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).
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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.
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Summary Information | 44 codes involving 4 elements 1 codes involving 3 elements 19 codes involving 2 elements
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Composite Feature Index | 4 | 44 | 44 | 44 | 44 | 3 | 1 | 0 | 1 | 1 | 2 | 0 | 19 | 0 | 19 | | 1 | 2 | 3 | 4 |
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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).
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Scan History | OWL31_1 3 38 NSINGLE SPTR37_9f 4 70 NSINGLE
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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 -
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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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