|
Name |
Accession |
Description |
Interval |
E-value |
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
1-151 |
1.24e-126 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 373.62 E-value: 1.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYR 80
Cdd:COG0495 55 NYTIGDVVARYKRMQGYNVLHPMGWDAFGLPAENAAIKNGVHPAEWTYENIANMRRQLKRLGLSYDWSREIATCDPEYYK 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDTKVERKEIPQWFIKITAYADQLLND 151
Cdd:COG0495 135 WTQWIFLQLYEKGLAYRKEAPVNWCPVDQTVLANEQVIDGRCWRCGAPVEKKELPQWFLKITDYADELLDD 205
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
1-151 |
2.26e-106 |
|
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 321.70 E-value: 2.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYR 80
Cdd:TIGR00396 51 NYTITDVLSRYYRMKGYNVLHPIGWDAFGLPAENAAIKRGIHPAKWTYENIANMKKQLQALGFSYDWDREIATCDPEYYK 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI-DGCCWRCDTKVERKEIPQWFIKITAYADQLLND 151
Cdd:TIGR00396 131 WTQWIFLELFEKGLAYVKEADVNWCPNDGTVLANEQVDsDGRSWRGDTPVEKKELKQWFLKITAYAEELLND 202
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
2-151 |
1.38e-67 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 220.08 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYRW 81
Cdd:PLN02563 134 YTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSYDWDREISTTEPEYYKW 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 82 EQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDTKVERKEIPQWFIKITAYADQLLND 151
Cdd:PLN02563 214 TQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDGLSERGGHPVIRKPMRQWMLKITAYADRLLED 283
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
1-151 |
9.35e-65 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 199.78 E-value: 9.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYR 80
Cdd:cd00812 22 TYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFSYDWRREFTTCDPEYYK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCpndqtvlaneqvidgccwrcdtkverKEIPQWFIKI--TAYADQLLND 151
Cdd:cd00812 102 FTQWLFLKLYEKGLAYKKEAPVNWC--------------------------KLLDQWFLKYseTEWKEKLLKD 148
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
1-118 |
1.03e-19 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 84.38 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAP---------------WTYA--NIDYMKNQLKLLGF 63
Cdd:pfam00133 45 AKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKKLGIKEKktrhkygreefrekcREWKmeYADEIRKQFRRLGR 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1596061470 64 GYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI 118
Cdd:pfam00133 125 SIDWDREYFTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVE 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
1-151 |
1.24e-126 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 373.62 E-value: 1.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYR 80
Cdd:COG0495 55 NYTIGDVVARYKRMQGYNVLHPMGWDAFGLPAENAAIKNGVHPAEWTYENIANMRRQLKRLGLSYDWSREIATCDPEYYK 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDTKVERKEIPQWFIKITAYADQLLND 151
Cdd:COG0495 135 WTQWIFLQLYEKGLAYRKEAPVNWCPVDQTVLANEQVIDGRCWRCGAPVEKKELPQWFLKITDYADELLDD 205
|
|
| leuS_bact |
TIGR00396 |
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases ... |
1-151 |
2.26e-106 |
|
leucyl-tRNA synthetase, eubacterial and mitochondrial family; The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273057 [Multi-domain] Cd Length: 842 Bit Score: 321.70 E-value: 2.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYR 80
Cdd:TIGR00396 51 NYTITDVLSRYYRMKGYNVLHPIGWDAFGLPAENAAIKRGIHPAKWTYENIANMKKQLQALGFSYDWDREIATCDPEYYK 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI-DGCCWRCDTKVERKEIPQWFIKITAYADQLLND 151
Cdd:TIGR00396 131 WTQWIFLELFEKGLAYVKEADVNWCPNDGTVLANEQVDsDGRSWRGDTPVEKKELKQWFLKITAYAEELLND 202
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
2-151 |
1.38e-67 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 220.08 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYRW 81
Cdd:PLN02563 134 YTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRSQLKSLGFSYDWDREISTTEPEYYKW 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 82 EQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDTKVERKEIPQWFIKITAYADQLLND 151
Cdd:PLN02563 214 TQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVDGLSERGGHPVIRKPMRQWMLKITAYADRLLED 283
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
1-151 |
9.35e-65 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 199.78 E-value: 9.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDWDREVATCKPDYYR 80
Cdd:cd00812 22 TYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGFSYDWRREFTTCDPEYYK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCpndqtvlaneqvidgccwrcdtkverKEIPQWFIKI--TAYADQLLND 151
Cdd:cd00812 102 FTQWLFLKLYEKGLAYKKEAPVNWC--------------------------KLLDQWFLKYseTEWKEKLLKD 148
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
1-149 |
5.88e-38 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 132.76 E-value: 5.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAP----------------WTYANIDYMKNQLKLLGFG 64
Cdd:cd00817 23 NNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKKLGIEGKtrhdlgreeflekcweWKEESGGKIREQLKRLGAS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 65 YDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVidgcCWRCDTKVERKEIPQWFIKITAY 144
Cdd:cd00817 103 VDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV----CSRSGDVIEPLLKPQWFVKVKDL 178
|
....*
gi 1596061470 145 ADQLL 149
Cdd:cd00817 179 AKKAL 183
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
1-113 |
1.06e-27 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 107.20 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEgaaVK----NNTAPAP------------WTYANIDYMKNQLKLLGFG 64
Cdd:PRK13208 60 SYTHTDFIARYQRMRGYNVFFPQGWDDNGLPTE---RKvekyYGIRKDDisreefielcreLTDEDEKKFRELWRRLGLS 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1596061470 65 YDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLA 113
Cdd:PRK13208 137 VDWSLEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCETAIA 185
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
1-118 |
3.79e-26 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 102.83 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAP----------------WTYANIDYMKNQLKLLGFG 64
Cdd:TIGR00422 55 NWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEKKLGAEGKtkhdlgreefrekiweWKEESGGTIKNQIKRLGAS 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1596061470 65 YDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI 118
Cdd:TIGR00422 135 LDWSRERFTMDEGLSKAVKEAFVRLYEKGLIYRGEYLVNWDPKLNTAISDIEVE 188
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
2-111 |
3.83e-25 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 99.94 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAA--VKNNTAPAPWTYANI------------------DY----MKNQ 57
Cdd:PRK12300 9 YTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAerIARGDPETIELYKSLygipeeelekfkdpeyivEYfseeAKED 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1596061470 58 LKLLGFGYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTV 111
Cdd:PRK12300 89 MKRIGYSIDWRREFTTTDPEYSKFIEWQFRKLKEKGLIVKGSHPVRYCPNDNNP 142
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
1-149 |
4.61e-24 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 94.79 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAA-------------VKNNTAPAPWTYANIDYMKNQLKLLGFGYDW 67
Cdd:cd00668 22 THIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAerkggrkkktiwiEEFREDPKEFVEEMSGEHKEDFRRLGISYDW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 68 DREVATCKPDYYRWEQWFFTKLYEKGLVYKktsavnwcpndqtvlaneqvidgccwrcDTKVERKEiPQWFIKITAYADQ 147
Cdd:cd00668 102 SDEYITTEPEYSKAVELIFSRLYEKGLIYR----------------------------GTHPVRIT-EQWFFDMPKFKEK 152
|
..
gi 1596061470 148 LL 149
Cdd:cd00668 153 LL 154
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
2-150 |
4.29e-21 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 88.02 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYDwdREVATCKPDYYRW 81
Cdd:PRK11893 24 TLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNISYD--DFIRTTDPRHKEA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1596061470 82 EQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDG--CCWRCDTKVERKEIPQWFIKITAYADQLLN 150
Cdd:PRK11893 102 VQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIEDgyRCPPTGAPVEWVEEESYFFRLSKYQDKLLE 172
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
1-118 |
1.03e-19 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 84.38 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAP---------------WTYA--NIDYMKNQLKLLGF 63
Cdd:pfam00133 45 AKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKKLGIKEKktrhkygreefrekcREWKmeYADEIRKQFRRLGR 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1596061470 64 GYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI 118
Cdd:pfam00133 125 SIDWDREYFTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVE 179
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
2-150 |
7.26e-17 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 75.26 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYD-WDRevaTCKPDYYR 80
Cdd:cd00814 23 TVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNISFDyFIR---TTSPRHKE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLAneqvidgccwrcdtkvERKEIPQWFIKITAYADQLLN 150
Cdd:cd00814 100 IVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP----------------EWREEEHYFFRLSKFQDRLLE 153
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
2-149 |
1.19e-16 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 75.02 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYANIDYMKNQLKLLGFGYD-WDRevaTCKPDYYR 80
Cdd:pfam09334 22 YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKKFNISFDdYGR---TTSERHHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 81 WEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGC-----------------------------CWRCDTKVER 131
Cdd:pfam09334 99 LVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCphcgsedargdqcencgrhleptelinpkCVICGTTPEV 178
|
170
....*....|....*...
gi 1596061470 132 KEIPQWFIKITAYADQLL 149
Cdd:pfam09334 179 KETEHYFFDLSKFQDKLR 196
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
1-114 |
1.94e-16 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 75.12 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVL-QPiGWDAFGLPAEGAAVKN---------NTAPAPW-----TYA--NIDYMKNQLKLLGF 63
Cdd:COG0060 68 NKILKDIIVRYKTMRGFDVPyVP-GWDCHGLPIELKVEKElgikkkdieKVGIAEFrekcrEYAlkYVDEQREDFKRLGV 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1596061470 64 GYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLAN 114
Cdd:COG0060 147 WGDWDNPYLTMDPEYEESIWWALKKLYEKGLLYKGLKPVPWCPRCGTALAE 197
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
1-118 |
2.53e-16 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 74.76 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVL-QPiGWDAFG----------LPAEG------------AAVKNntapapWT--YANIdyMK 55
Cdd:PRK05729 58 NNTLQDILIRYKRMQGYNTLwLP-GTDHAGiatqmvverqLAAEGksrhdlgrekflEKVWE------WKeeSGGT--IT 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1596061470 56 NQLKLLGFGYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI 118
Cdd:PRK05729 129 NQLRRLGASCDWSRERFTMDEGLSKAVREVFVRLYEKGLIYRGKRLVNWDPKLQTALSDLEVE 191
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
1-149 |
9.52e-15 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 69.57 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTY-----------------ANIDYMKNQLKLLGF 63
Cdd:cd00818 23 NKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDIekmgiaefnakcrefalRYVDEQEEQFQRLGV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 64 GYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWcPndqtvlaneqVIdgccwrcdtkveRKEIPQWFIKITA 143
Cdd:cd00818 103 WVDWENPYKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPW-P----------LI------------YRATPQWFIRVTK 159
|
....*.
gi 1596061470 144 YADQLL 149
Cdd:cd00818 160 IKDRLL 165
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
1-118 |
4.54e-14 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 68.15 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVL-QPiGWDAFG----------LPAEG------------AAVknntapapW----TYANIdy 53
Cdd:COG0525 57 NNTLQDILIRYKRMQGYNTLwQP-GTDHAGiatqavverqLAEEGksrhdlgrekflERV--------WewkeESGGT-- 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1596061470 54 MKNQLKLLGFGYDWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVI 118
Cdd:COG0525 126 ITNQLRRLGASCDWSRERFTMDEGLSKAVREVFVRLYEKGLIYRGKRLVNWDPKLKTALSDLEVE 190
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
3-144 |
2.53e-12 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 63.10 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 3 TIGDVISRYQRMLGKNVLQPIGWDAFGLpAEGAAV------KNNtaPAPWTYANIDYMK--------------NQLKLLG 62
Cdd:PTZ00419 84 AIQDSLIRYHRMKGDETLWVPGTDHAGI-ATQVVVekklmkEEN--KTRHDLGREEFLKkvwewkdkhgnnicNQLRRLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 63 FGYDWDREVATCkpDYYRWE--QWFFTKLYEKGLVYKKTSAVNWCPNDQTVLAneqvidgccwrcDTKVERKEIPQ-WFI 139
Cdd:PTZ00419 161 SSLDWSREVFTM--DEQRSKavKEAFVRLYEDGLIYRDTRLVNWCCYLKTAIS------------DIEVEFEEIEKpTKI 226
|
....*
gi 1596061470 140 KITAY 144
Cdd:PTZ00419 227 TIPGY 231
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
2-149 |
4.29e-11 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 59.43 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 2 YT--IGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPApwTYAniDYM----KNQLKLLGFGYdwDREVATCK 75
Cdd:PRK12267 25 YTtiAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQ--EYV--DEIsagfKELWKKLDISY--DKFIRTTD 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1596061470 76 PDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGC-CWRCDTKVERKEIPQWFIKITAYADQLL 149
Cdd:PRK12267 99 ERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVDGGkCPDCGREVELVKEESYFFRMSKYQDRLL 173
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
3-117 |
2.92e-10 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 57.31 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 3 TIGDVISRYQRMLGKNVLQPIGWDAFGLP-----------AEGAAVKNNTAPA------PWTYANIDYMKNQLKLLGFGY 65
Cdd:PRK14900 72 TLQDVLIRWKRMSGFNTLWLPGTDHAGIAtqmivekelkkTEKKSRHDLGREAflervwAWKEQYGSRIGEQHKALGASL 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1596061470 66 DWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQV 117
Cdd:PRK14900 152 DWQRERFTMDEGLSRAVREVFVRLHEEGLIYREKKLINWCPDCRTALSDLEV 203
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
3-117 |
5.09e-10 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 56.49 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 3 TIGDVISRYQRMLGKNVLQPIGWDAFG----------LPAEGAAVKNNTAPA------PWTYANIDYMKNQLKLLGFGYD 66
Cdd:PLN02943 112 TLEDIMVRYNRMKGRPTLWIPGTDHAGiatqlvvekmLASEGIKRTDLGRDEftkrvwEWKEKYGGTITNQIKRLGASCD 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1596061470 67 WDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQV 117
Cdd:PLN02943 192 WSRERFTLDEQLSRAVVEAFVRLHEKGLIYQGSYMVNWSPNLQTAVSDLEV 242
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
1-113 |
9.73e-10 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 55.93 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 1 NYTIGDVISRYQRMLGKNVLQPIGWDAFGLPAE-------GAAVKNNTAP-------APWTYANIDYMKNQLKLLGFGYD 66
Cdd:PLN02843 54 NKILKDFINRYQLLQGKKVHYVPGWDCHGLPIElkvlqslDQEARKELTPiklrakaAKFAKKTVDTQRESFKRYGVWGD 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1596061470 67 WDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLA 113
Cdd:PLN02843 134 WENPYLTLDPEYEAAQIEVFGQMFLNGYIYRGRKPVHWSPSSRTALA 180
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
5-148 |
1.97e-09 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 54.77 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 5 GDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPApwtyANIDYMKNQLK--LLGFGYDWDREVATCKPDYYRWE 82
Cdd:PRK00133 28 ADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPE----ELIARYHAEHKrdFAGFGISFDNYGSTHSEENRELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 83 QWFFTKLYEKGLVYKKTSAVNWCPNDQTVL-------------ANEQVIDGC--CWR--------------CDTKVERKE 133
Cdd:PRK00133 104 QEIYLKLKENGYIYEKTIEQLYDPEKGMFLpdrfvkgtcpkcgAEDQYGDNCevCGAtysptelinpksaiSGATPVLKE 183
|
170
....*....|....*
gi 1596061470 134 IPQWFIKITAYADQL 148
Cdd:PRK00133 184 SEHFFFKLPRFEEFL 198
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
3-97 |
4.66e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 48.18 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 3 TIGDVISRYQRMLGKNVLQPIGWDAFGLPAE------------------GAAVKNNTAPAPWTYANIDYMKNqLKLLGFG 64
Cdd:PLN02882 62 TIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEyeidkklgikrrddvlkmGIDKYNEECRSIVTRYSKEWEKT-VTRTGRW 140
|
90 100 110
....*....|....*....|....*....|...
gi 1596061470 65 YDWDREVATCKPDYYRWEQWFFTKLYEKGLVYK 97
Cdd:PLN02882 141 IDFENDYKTMDPKFMESVWWVFKQLFEKGLVYK 173
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
122-149 |
4.72e-05 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 41.99 E-value: 4.72e-05
10 20
....*....|....*....|....*...
gi 1596061470 122 CWRCDTKVERKEIPQWFIKITAYADQLL 149
Cdd:COG0060 404 CWRCKTPLIYRATPQWFISMDKLRDRAL 431
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
5-148 |
1.44e-04 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 40.85 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 5 GDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPApwtyANIDYMKNQLKLLGFGYD--WDREVATCKPDYYRWE 82
Cdd:PLN02224 95 ADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPP----EHCDIISQSYRTLWKDLDiaYDKFIRTTDPKHEAIV 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 83 QWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCwrCDTK----VERKEiPQWFIKITAYADQL 148
Cdd:PLN02224 171 KEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLENNC--CPVHqmpcVARKE-DNYFFALSKYQKPL 237
|
|
| ileS |
TIGR00392 |
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ... |
120-149 |
1.59e-04 |
|
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273054 [Multi-domain] Cd Length: 861 Bit Score: 40.44 E-value: 1.59e-04
10 20 30
....*....|....*....|....*....|
gi 1596061470 120 GCCWRCDTKVERKEIPQWFIKITAYADQLL 149
Cdd:TIGR00392 407 PHCWRTKTPVIYRATEQWFIKTKDIKDQML 436
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
4-117 |
2.20e-04 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 40.27 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 4 IGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKN---------------NTAPAPWTYANiDY---MKNQLKLLGFGY 65
Cdd:PLN02381 153 IEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKlmrerhltrhdigreEFVSEVWKWKD-EYggtILNQLRRLGASL 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1596061470 66 DWDREVATCKPDYYRWEQWFFTKLYEKGLVYKKTSAVNWCPNDQTVLANEQV 117
Cdd:PLN02381 232 DWSRECFTMDEQRSKAVTEAFVRLYKEGLIYRDIRLVNWDCTLRTAISDVEV 283
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
4-97 |
2.70e-03 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 37.25 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596061470 4 IGDVISRYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNtapapwtyaNIDYMKNQLKL-------------LGFGYDWDRE 70
Cdd:PTZ00427 127 IKDCVTRYFYQCGFSVERKFGWDCHGLPIEYEIEKEN---------NINKKEDILKMgidvynekcrgivLKYSNEWVKT 197
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1596061470 71 V-------------ATCKPDYYRWEQWFFTKLYEKGLVYK 97
Cdd:PTZ00427 198 VerigrwidfkndyKTMDKTFMESVWWVFSELYKNNYVYK 237
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
122-149 |
7.43e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 35.86 E-value: 7.43e-03
10 20
....*....|....*....|....*...
gi 1596061470 122 CWRCDTKVERKEIPQWFIKITAYADQLL 149
Cdd:PLN02882 412 CWRSDTPLIYRAVPSWFVKVEEIKDRLL 439
|
|
| |
