RPS-BLAST 2.2.9 [May-01-2004]
Query= local sequence: lcl|tmpseq_0 unnamed protein product
(315 letters)
Database: cdd.v2.00
 .. This CD alignment includes 3D structure. To display structure, download
Cn3D!
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PSSMs producing significant alignments: |
Score
(bits) |
E
value |
| |
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gnl|CDD|27665 |
cd00733, GlyRS_alpha_core, Class II Glycyl-tRNA synthetase (Gl... |
515 |
4e-147 |
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gnl|CDD|27666 |
cd00768, class_II_aaRS-like_core, Class II tRNA amino-acyl syn... |
55.8 |
7e-09 |
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gnl|CDD|6639 |
pfam02091, tRNA_synt_2e, Glycyl-tRNA synthetase alpha subunit |
526 |
1e-150 |
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gnl|CDD|10620 |
COG0752, GlyQ, Glycyl-tRNA synthetase, alpha subunit [Translat... |
568 |
3e-163 |
gnl|CDD|27665, cd00733, GlyRS_alpha_core, Class II Glycyl-tRNA synthetase (GlyRS) alpha subunit core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes and in arabidopsis. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. This alignment contains only sequences from the GlyRS form which heterotetramerizes. The homodimer form of GlyRS is in a different family of class II aaRS. Class II assignment is based upon structure and the presence of three characteristic sequence motifs.
CD-Length = 279 residues, 100.0% aligned
Score = 515 bits (1327), Expect = 4e-147
Query: 10 TFQDLILALQNYWAEQGCVVLQPYDMEVGAGTFHTATFLRAIGPETWNAAYVQPSRRPTD 69
Sbjct: 1 TFQDLILKLQKFWASQGCLIIQPYDMEVGAGTFHPATFLRALGPEPWNVAYVEPSRRPTD 60
Query: 70 GRYGENPNRLQHYYQFQVVLKPNPENFQELYLGSLKAIGIDPLVHDIRFVEDNWESPTLG 129
Sbjct: 61 GRYGENPNRLQHYYQFQVIIKPSPDNIQELYLESLEALGINPKEHDIRFVEDNWESPTLG 120
Query: 130 AWGLGWEIWLNGMEVTQFTYFQQVGGIECYPVTGEITYGLERLAMYLQGVDSVYDLVWTD 189
Sbjct: 121 AWGLGWEVWLDGMEVTQFTYFQQVGGIPCKPISVEITYGLERIAMYLQGVDNVYDIEWNK 180
Query: 190 GPFGKVTYGDVFHQNEVEQSTFNFEHANVPKLFELFDFYESEANRLIALELPLPTYEMVL 249
Sbjct: 181 ----KITYGDVFLQNEIEQSVYNFEYANVDMLFQLFEDYEKEAKRLLELGLPLPAYDYVL 236
Query: 250 KASHTFNLLDARRAISVTERQRYILRVRTLARAVAQSYLQARA 292
Sbjct: 237 KCSHTFNLLDARGAISVTERQRYILRIRNLAREIAKLYVEQRE 279
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gnl|CDD|27666, cd00768, class_II_aaRS-like_core, Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
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CD-Length = 211 residues, only 71.6% aligned
Score = 55.8 bits (134), Expect = 7e-09
Query: 41 TFHTATFLRAIGPETWNAAYVQPSRRPTDGRYGENPNRLQHYYQFQVVLKPNP------- 93
Sbjct: 61 PGLVRLFVSHIRKLPLRLAEIGPAFRNEGGRRG--LRRVREFTQLEGEVFGEDGEEASEF 118
Query: 94 ENFQELYLGSLKAIGIDPLVHDIRFVEDNWESPTLGAWGLGWEIWLN-----GMEVTQFT 148
Sbjct: 119 EELIELTEELLRALGIK---LDIVFVEKTPGEFSPGGAGPGFEIEVDHPEGRGLEIGSGG 175
Query: 149 YFQQVG------------GIECYPVTGEITYGLERL 172
Sbjct: 176 YRQDEQARAADLYFLDEALEYRYPPTIGFGLGLERL 211
gnl|CDD|6639, pfam02091, tRNA_synt_2e, Glycyl-tRNA synthetase alpha subunit.
CD-Length = 285 residues, 100.0% aligned
Score = 526 bits (1357), Expect = 1e-150
Query: 11 FQDLILALQNYWAEQGCVVLQPYDMEVGAGTFHTATFLRAIGPETWNAAYVQPSRRPTDG 70
Sbjct: 1 FQQMILTLQEYWASQGCVVMQPYDMEVGAGTFHPATFLRSLGPEPWNVAYVEPSRRPTDG 60
Query: 71 RYGENPNRLQHYYQFQVVLKPNPENFQELYLGSLKAIGIDPLVHDIRFVEDNWESPTLGA 130
Sbjct: 61 RYGENPNRLQHYYQFQVVLKPSPDNIQELYLGSLKALGIDPLDHDIRFVEDNWESPTLGA 120
Query: 131 WGLGWEIWLNGMEVTQFTYFQQVGGIECYPVTGEITYGLERLAMYLQGVDSVYDLVWTDG 190
Sbjct: 121 WGLGWEVWLDGMEITQFTYFQQVGGLECKPVSGEITYGLERLAMYLQGVDNVYDLVWADG 180
Query: 191 PFGKVTYGDVFHQNEVEQSTFNFEHANVPKLFELFDFYESEANRLIALELPLPTYEMVLK 250
Sbjct: 181 P---VTYGDIFLQNEVEQSTYNFETANVDRLFKLFDFYEKEALQLLENGLPLPAYDFVLK 237
Query: 251 ASHTFNLLDARRAISVTERQRYILRVRTLARAVAQSYLQARARLGFPM 298
Sbjct: 238 ASHAFNLLDARGAISVTERQRYILRIRTLARAVAELYYAQREKLGFPL 285
gnl|CDD|10620, COG0752, GlyQ, Glycyl-tRNA synthetase, alpha subunit [Translation, ribosomal structure and biogenesis]
CD-Length = 298 residues, 100.0% aligned
Score = 568 bits (1465), Expect = 3e-163
Query: 5 TPAVRTFQDLILALQNYWAEQGCVVLQPYDMEVGAGTFHTATFLRAIGPETWNAAYVQPS 64
Sbjct: 1 MNKKLTFQGLILTLQNYWAEQGCTILQPYDMEVGAGTFHPATFLRALGPEPWNAAYVQPS 60
Query: 65 RRPTDGRYGENPNRLQHYYQFQVVLKPNPENFQELYLGSLKAIGIDPLVHDIRFVEDNWE 124
Sbjct: 61 RRPTDGRYGENPNRLQHYYQFQVIIKPSPDNIQELYLGSLEALGIDPLEHDIRFVEDNWE 120
Query: 125 SPTLGAWGLGWEIWLNGMEVTQFTYFQQVGGIECYPVTGEITYGLERLAMYLQGVDSVYD 184
Sbjct: 121 NPTLGAWGLGWEVWLDGMEVTQFTYFQQVGGLECKPVSGEITYGLERLAMYIQGVDNVYD 180
Query: 185 LVWTDGPFGKVTYGDVFHQNEVEQSTFNFEHANVPKLFELFDFYESEANRLIALELPLPT 244
Sbjct: 181 LEWNDGPGGKVTYGDVFLQNEVEQSKYNFEYADVDMLFRHFDDYEKEAKRLLELGLVLPA 240
Query: 245 YEMVLKASHTFNLLDARRAISVTERQRYILRVRTLARAVAQSYLQARARLGFPMATPE 302
Sbjct: 241 YDYVLKASHTFNLLDARGAISVTERQRYILRIRNLARAVAEAYLESREALGFPLLKKE 298
Citing CD-Search:
Marchler-Bauer A, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR,
Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler GH, Mazumder R, Nikolskaya AN, Panchenko AR, Rao BS, Shoemaker BA,
Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, and Bryant SH (2003),
"CDD: a curated Entrez database of conserved domain alignments",
Nucleic Acids Res. 31:383-387.
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