blastp_kegg |
lcl|vvi:100242505
|
4 |
142 |
+ |
139 |
none |
22.42 |
620 |
72.66 |
1e-62 |
lysyl-tRNA synthetase-like
|
blastp_kegg |
lcl|vvi:100262532
|
4 |
142 |
+ |
139 |
none |
22.46 |
619 |
72.66 |
3e-62 |
lysyl-tRNA synthetase-like
|
blastp_kegg |
lcl|eus:EUTSA_v10020276mg
|
10 |
142 |
+ |
133 |
none |
21.56 |
617 |
73.68 |
2e-60 |
hypothetical protein
|
blastp_kegg |
lcl|brp:103846034
|
12 |
142 |
+ |
131 |
none |
21.20 |
618 |
74.81 |
4e-60 |
lysine--tRNA ligase
|
blastp_kegg |
lcl|pper:PRUPE_ppa016996mg
|
1 |
142 |
+ |
142 |
none |
24.27 |
585 |
68.31 |
1e-59 |
hypothetical protein
|
blastp_kegg |
lcl|cit:102615402
|
3 |
142 |
+ |
140 |
Gaps:1 |
21.35 |
651 |
70.50 |
5e-59 |
lysine--tRNA ligase-like
|
blastp_kegg |
lcl|tcc:TCM_019889
|
10 |
142 |
+ |
133 |
none |
21.70 |
613 |
72.18 |
6e-59 |
Lysyl-tRNA synthetase 1 isoform 1
|
blastp_kegg |
lcl|rcu:RCOM_0435350
|
13 |
142 |
+ |
130 |
none |
21.42 |
607 |
73.85 |
8e-59 |
lysyl-tRNA synthetase putative (EC:6.1.1.6)
|
blastp_kegg |
lcl|crb:CARUB_v10013215mg
|
5 |
142 |
+ |
138 |
none |
22.04 |
626 |
69.57 |
1e-58 |
hypothetical protein
|
blastp_kegg |
lcl|gmx:100809106
|
3 |
142 |
+ |
140 |
none |
23.49 |
596 |
67.14 |
2e-58 |
lysine--tRNA ligase-like
|
blastp_pdb |
3bju_D
|
23 |
142 |
+ |
120 |
Gaps:1 |
22.84 |
521 |
46.22 |
1e-31 |
mol:protein length:521 Lysyl-tRNA synthetase
|
blastp_pdb |
3bju_C
|
23 |
142 |
+ |
120 |
Gaps:1 |
22.84 |
521 |
46.22 |
1e-31 |
mol:protein length:521 Lysyl-tRNA synthetase
|
blastp_pdb |
3bju_B
|
23 |
142 |
+ |
120 |
Gaps:1 |
22.84 |
521 |
46.22 |
1e-31 |
mol:protein length:521 Lysyl-tRNA synthetase
|
blastp_pdb |
3bju_A
|
23 |
142 |
+ |
120 |
Gaps:1 |
22.84 |
521 |
46.22 |
1e-31 |
mol:protein length:521 Lysyl-tRNA synthetase
|
blastp_uniprot_sprot |
sp|Q9ZPI1|SYK_ARATH
|
3 |
142 |
+ |
140 |
none |
22.36 |
626 |
65.71 |
2e-55 |
Lysine--tRNA ligase OS Arabidopsis thaliana GN At3g11710 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q6F2U9|SYK_ORYSJ
|
14 |
142 |
+ |
129 |
none |
21.43 |
602 |
62.02 |
9e-49 |
Lysine--tRNA ligase OS Oryza sativa subsp. japonica GN Os03g0586800 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q43776|SYK_SOLLC
|
3 |
142 |
+ |
140 |
none |
23.81 |
588 |
50.00 |
5e-45 |
Lysine--tRNA ligase OS Solanum lycopersicum GN LYSRS PE 2 SV 1
|
blastp_uniprot_sprot |
sp|Q99MN1|SYK_MOUSE
|
3 |
142 |
+ |
140 |
Gaps:1 |
23.36 |
595 |
43.88 |
6e-34 |
Lysine--tRNA ligase OS Mus musculus GN Kars PE 1 SV 1
|
blastp_uniprot_sprot |
sp|P37879|SYK_CRIGR
|
19 |
142 |
+ |
124 |
Gaps:1 |
20.60 |
597 |
45.53 |
4e-32 |
Lysine--tRNA ligase OS Cricetulus griseus GN KARS PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q15046|SYK_HUMAN
|
19 |
142 |
+ |
124 |
Gaps:1 |
20.60 |
597 |
45.53 |
2e-31 |
Lysine--tRNA ligase OS Homo sapiens GN KARS PE 1 SV 3
|
blastp_uniprot_sprot |
sp|Q9UUE6|SYKC_SCHPO
|
12 |
142 |
+ |
131 |
Gaps:3 |
22.00 |
591 |
42.31 |
5e-31 |
Lysine--tRNA ligase cytoplasmic OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN krs1 PE 3 SV 1
|
blastp_uniprot_sprot |
sp|P15180|SYKC_YEAST
|
22 |
142 |
+ |
121 |
Gaps:2 |
20.47 |
591 |
46.28 |
6e-28 |
Lysine--tRNA ligase cytoplasmic OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN KRS1 PE 1 SV 2
|
blastp_uniprot_sprot |
sp|Q22099|SYK_CAEEL
|
24 |
139 |
+ |
116 |
Gaps:2 |
19.93 |
572 |
46.49 |
6e-26 |
Lysine--tRNA ligase OS Caenorhabditis elegans GN krs-1 PE 3 SV 1
|
blastp_uniprot_sprot |
sp|Q9X231|SYK_THEMA
|
27 |
141 |
+ |
115 |
Gaps:3 |
22.31 |
502 |
37.50 |
1e-14 |
Lysine--tRNA ligase OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) GN lysS PE 3 SV 1
|
rpsblast_cdd |
gnl|CDD|178118
|
4 |
142 |
+ |
139 |
Gaps:1 |
24.95 |
553 |
61.59 |
6e-56 |
PLN02502 PLN02502 lysyl-tRNA synthetase.
|
rpsblast_cdd |
gnl|CDD|173607
|
12 |
142 |
+ |
131 |
none |
22.39 |
585 |
44.27 |
2e-32 |
PTZ00417 PTZ00417 lysine-tRNA ligase Provisional.
|
rpsblast_cdd |
gnl|CDD|188056
|
24 |
141 |
+ |
118 |
Gaps:4 |
23.39 |
496 |
34.48 |
2e-24 |
TIGR00499 lysS_bact lysyl-tRNA synthetase eukaryotic and non-spirochete bacterial. This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme but not archaeal or spirochete forms.
|
rpsblast_cdd |
gnl|CDD|179044
|
23 |
141 |
+ |
119 |
Gaps:5 |
23.63 |
491 |
32.76 |
3e-21 |
PRK00484 lysS lysyl-tRNA synthetase Reviewed.
|
rpsblast_cdd |
gnl|CDD|31383
|
19 |
142 |
+ |
124 |
Gaps:4 |
24.30 |
502 |
32.79 |
3e-21 |
COG1190 LysU Lysyl-tRNA synthetase (class II) [Translation ribosomal structure and biogenesis].
|
rpsblast_cdd |
gnl|CDD|58592
|
77 |
142 |
+ |
66 |
Gaps:3 |
58.33 |
108 |
50.79 |
1e-16 |
cd04322 LysRS_N LysRS_N: N-terminal anticodon recognition domain of lysyl-tRNA synthetases (LysRS). These enzymes are homodimeric class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs the activated AA is attached to the 3'OH of the terminal ribose. Included in this group are E. coli LysS and LysU. These two isoforms of LysRS are encoded by distinct genes which are differently regulated. Eukaryotes contain 2 sets of aaRSs both of which encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis whereas the other exclusively with mitochondrial protein synthesis. Saccharomyces cerevisiae cytoplasmic and mitochondrial LysRSs have been shown to participate in the mitochondrial import of the only nuclear-encoded tRNA of S. cerevisiae (tRNAlysCUU). The gene for human LysRS encodes both the cytoplasmic and the mitochondrial isoforms of LysRS. In addition to their housekeeping role human lysRS may function as a signaling molecule that activates immune cells and tomato LysRS may participate in a root-specific process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging..
|