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Conserved domains on  [gi|2570694211|gb|WMK02043|]
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leucine-tRNA ligase, cytoplasmic-like, partial [Losaria coon doubledayi]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02959 super family cl33607
aminoacyl-tRNA ligase
 2-114 2.79e-66

aminoacyl-tRNA ligase


The actual alignment was detected with superfamily member PLN02959:

Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 215.32  E-value: 2.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211    2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPneEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLAD 81
Cdd:PLN02959   670 YPFDLRVSGKDLIQNHLTFAIYNHTAIWA--EEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALAD 747

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2570694211   82 AGDSVEDANFVESTADAAILRLYTFIEWVKEVM 114
Cdd:PLN02959   748 AGDGVDDANFVFETANAAILRLTKEIAWMEEVL 780
 
Name Accession Description Interval E-value
PLN02959 PLN02959
aminoacyl-tRNA ligase
 2-114 2.79e-66

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 215.32  E-value: 2.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211    2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPneEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLAD 81
Cdd:PLN02959   670 YPFDLRVSGKDLIQNHLTFAIYNHTAIWA--EEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALAD 747

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2570694211   82 AGDSVEDANFVESTADAAILRLYTFIEWVKEVM 114
Cdd:PLN02959   748 AGDGVDDANFVFETANAAILRLTKEIAWMEEVL 780
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 2-93 3.61e-40

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: 135.45  E-value: 3.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPNE--EDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTL 79
Cdd:cd00812   223 YPVDIYIGGKEHAPNHLLYSRFNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYI 302

                          90
                  ....*....|....
gi 2570694211  80 ADAGDsvEDANFVE 93
Cdd:cd00812   303 LFAAP--PDADFDW 314
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 10-91 7.45e-12

Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439913 [Multi-domain]  Cd Length: 544  Bit Score: 60.13  E-value: 7.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211  10 GKDlIqnhltyyIYNHCAIWP------NEedKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLADAG 83
Cdd:COG0143   289 GKD-I-------IRFHAIIWPamlmaaGL--PLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREV 358


                  ....*...
gi 2570694211  84 DSVEDANF 91
Cdd:COG0143   359 PFGQDGDF 366
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 10-91 4.84e-11

tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 58.07  E-value: 4.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211  10 GKDLIqnhltyyiYNHCAIWP----NEEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLADAGDS 85
Cdd:pfam09334 286 GKDII--------YFHTIFWPamllGAGYRLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPE 357


                  ....*.
gi 2570694211  86 VEDANF 91
Cdd:pfam09334 358 TKDTDF 363
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 2-80 1.10e-05

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: 42.74  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAiwpnEEDKWP-KGIRANGhlMLNSA---KMSKSEGNFLTLSESIEKFSADGMRL 77
Cdd:TIGR00422 477 YPTDLLVTGYDIIFFWVARMIFRSLA----LTGQVPfKEVYIHG--LVRDEqgrKMSKSLGNVIDPLDVIEKYGADALRF 550


                  ...
gi 2570694211  78 TLA 80
Cdd:TIGR00422 551 TLA 553
 
Name Accession Description Interval E-value
PLN02959 PLN02959
aminoacyl-tRNA ligase
 2-114 2.79e-66

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 215.32  E-value: 2.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211    2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPneEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLAD 81
Cdd:PLN02959   670 YPFDLRVSGKDLIQNHLTFAIYNHTAIWA--EEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALAD 747

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2570694211   82 AGDSVEDANFVESTADAAILRLYTFIEWVKEVM 114
Cdd:PLN02959   748 AGDGVDDANFVFETANAAILRLTKEIAWMEEVL 780
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
 2-114 2.11e-43

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 150.40  E-value: 2.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPneEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLAD 81
Cdd:PRK12300  529 YPVDWRHSGKDLIPNHLTFFIFNHVAIFP--EEKWPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTS 606

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2570694211  82 AGDSVEDANFVESTADAAILRLYTFIEWVKEVM 114
Cdd:PRK12300  607 SAELLQDADWREKEVESVRRQLERFYELAKELI 639
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 2-93 3.61e-40

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: 135.45  E-value: 3.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPNE--EDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTL 79
Cdd:cd00812   223 YPVDIYIGGKEHAPNHLLYSRFNHKALFDEGlvTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYI 302

                          90
                  ....*....|....
gi 2570694211  80 ADAGDsvEDANFVE 93
Cdd:cd00812   303 LFAAP--PDADFDW 314
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 2-80 2.21e-15

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: 69.75  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAIwpnEEDKWPKGIRANGHLMLN-SAKMSKSEGNFLTLSESIEKFSADGMRLTLA 80
Cdd:cd00668   225 YPADWHLIGKDILRGWANFWITMLVAL---FGEIPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLT 301
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 10-91 7.45e-12

Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439913 [Multi-domain]  Cd Length: 544  Bit Score: 60.13  E-value: 7.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211  10 GKDlIqnhltyyIYNHCAIWP------NEedKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLADAG 83
Cdd:COG0143   289 GKD-I-------IRFHAIIWPamlmaaGL--PLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREV 358


                  ....*...
gi 2570694211  84 DSVEDANF 91
Cdd:COG0143   359 PFGQDGDF 366
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 10-91 4.84e-11

tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 58.07  E-value: 4.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211  10 GKDLIqnhltyyiYNHCAIWP----NEEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLADAGDS 85
Cdd:pfam09334 286 GKDII--------YFHTIFWPamllGAGYRLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPE 357


                  ....*.
gi 2570694211  86 VEDANF 91
Cdd:pfam09334 358 TKDTDF 363
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 10-91 7.56e-11

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 57.47  E-value: 7.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211  10 GKDLIqnhltyyiYNHCAIWP----NEEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLA-DAGD 84
Cdd:PRK00133  291 GKDII--------YFHTLFWPamleGAGYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAaKLPE 362


                  ....*..
gi 2570694211  85 SVEDANF 91
Cdd:PRK00133  363 TIDDLDF 369
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 43-113 6.21e-09

Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439985 [Multi-domain]  Cd Length: 465  Bit Score: 52.03  E-value: 6.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211  43 NGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLADAG---------DSVEDanfvestADAAILRLYTFIEWVKEV 113
Cdd:COG0215   256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHyrspldfseEALEE-------AEKALERLYNALRRLEEA 328
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
 44-109 4.32e-08

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 49.64  E-value: 4.32e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570694211  44 GHLMLNSAKMSKSEGNFLTLSESIEKFSADGMR-LTLADAGDSVedANFVESTADAAILRLYTFIEW 109
Cdd:PTZ00399  307 GHLHIKGLKMSKSLKNFITIRQALSKYTARQIRlLFLLHKWDKP--MNYSDESMDEAIEKDKVFFNF 371
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
 43-79 9.21e-08

catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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.


Pssm-ID: 173899 [Multi-domain]  Cd Length: 213  Bit Score: 47.96  E-value: 9.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2570694211  43 NGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTL 79
Cdd:cd00672   165 TGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
 2-82 2.84e-07

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 46.98  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPNEedkWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTLAD 81
Cdd:pfam01406 206 DQIDIHGGGIDLAFPHHENEIAQSEAAFDKQ---LANYWLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLS 282


                  .
gi 2570694211  82 A 82
Cdd:pfam01406 283 V 283
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 2-91 3.79e-06

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: 43.77  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAiwpnEEDKWP-KGIRANGhLMLNS--AKMSKSEGNFLTLSESIEKFSADGMRLT 78
Cdd:cd00817   295 YPTSLLVTGHDIIFFWVARMIMRGLK----LTGKLPfKEVYLHG-LVRDEdgRKMSKSLGNVIDPLDVIDGYGADALRFT 369

                          90
                  ....*....|...
gi 2570694211  79 LADAGDSVEDANF 91
Cdd:cd00817   370 LASAATQGRDINL 382
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 2-80 1.10e-05

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: 42.74  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAiwpnEEDKWP-KGIRANGhlMLNSA---KMSKSEGNFLTLSESIEKFSADGMRL 77
Cdd:TIGR00422 477 YPTDLLVTGYDIIFFWVARMIFRSLA----LTGQVPfKEVYIHG--LVRDEqgrKMSKSLGNVIDPLDVIEKYGADALRF 550


                  ...
gi 2570694211  78 TLA 80
Cdd:TIGR00422 551 TLA 553
PLN02224 PLN02224
methionine-tRNA ligase
 2-88 2.34e-05

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 42.01  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYyiynhcaiWP----NEEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMR- 76
Cdd:PLN02224  320 WPASLHLIGKDILRFHAVY--------WPamlmSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRy 391

                          90
                  ....*....|....*..
gi 2570694211  77 -----LTLADAGDSVED 88
Cdd:PLN02224  392 fflreVEFGNDGDYSED 408
Anticodon_Ia_Leu_AEc cd07959
Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This ...
 91-114 6.13e-05

Anticodon-binding domain of archaeal and eukaryotic cytoplasmic leucyl tRNA synthetases; This domain is found in leucyl tRNA synthetases (LeuRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain. In contrast to other class Ia enzymes, the anticodon is not used as an identity element in LeuRS (with exceptions such as Saccharomyces cerevisiae and some other eukaryotes). No anticodon-binding site can be defined for this family, which includes archaeal and eukaryotic cytoplasmic members. LeuRS catalyzes the transfer of leucine to the 3'-end of its tRNA.


Pssm-ID: 153413 [Multi-domain]  Cd Length: 117  Bit Score: 39.11  E-value: 6.13e-05
                          10        20
                  ....*....|....*....|....
gi 2570694211  91 FVESTADAAILRLYTFIEWVKEVM 114
Cdd:cd07959     1 FREEEANSAILRLERFYELAEELI 24
valS PRK05729
valyl-tRNA synthetase; Reviewed
 52-80 6.76e-05

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 40.47  E-value: 6.76e-05
                          10        20
                  ....*....|....*....|....*....
gi 2570694211  52 KMSKSEGNFLTLSESIEKFSADGMRLTLA 80
Cdd:PRK05729  520 KMSKSKGNVIDPLDLIDKYGADALRFTLA 548
ValS COG0525
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ...
 52-80 9.57e-05

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: 40.03  E-value: 9.57e-05
                          10        20
                  ....*....|....*....|....*....
gi 2570694211  52 KMSKSEGNFLTLSESIEKFSADGMRLTLA 80
Cdd:COG0525   522 KMSKSKGNVIDPLDLIDKYGADALRFTLA 550
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 52-91 1.72e-04

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: 39.14  E-value: 1.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2570694211  52 KMSKSEGNFLTLSESIEKFSADGMRLTLADAGDSVEDANF 91
Cdd:cd00818   299 KMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAEDLRF 338
PLN02946 PLN02946
cysteine-tRNA ligase
 2-79 1.96e-04

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 39.14  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570694211   2 YPVDLRVSGKDLIQNHLTYYIYNHCAIWPNEE-DKWPKgiraNGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTL 79
Cdd:PLN02946  276 HSFDIHGGGMDLVFPHHENEIAQSCAACCDSNiSYWIH----NGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFL 350
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 52-91 1.18e-03

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: 37.00  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2570694211  52 KMSKSEGNFLTLSESIEKFSADGMRLTLADAgDSVEDANF 91
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANS-DYGRDINL 601
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 3-80 1.27e-03

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 36.78  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570694211   3 PVDLRVSGKDLIqnhltyyiYNHCAIWP-----NEEDKwPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRL 77
Cdd:PRK11893  254 PADVHLIGKDIL--------RFHAVYWPaflmaAGLPL-PKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVRY 324


                  ...
gi 2570694211  78 TLA 80
Cdd:PRK11893  325 FLL 327
LeuS COG0495
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ...
 43-79 1.31e-03

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: 36.57  E-value: 1.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2570694211  43 NGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMRLTL 79
Cdd:COG0495   580 DGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLFE 616
cysS PRK14536
cysteinyl-tRNA synthetase; Provisional
 4-79 1.37e-03

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 184731 [Multi-domain]  Cd Length: 490  Bit Score: 36.82  E-value: 1.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570694211   4 VDLRVSGKDLIQNHLTYYIYNHCAIwpnEEDKWPKGIRANGHLMLNSAKMSKSEGNFLTLSESIEK-FSADGMRLTL 79
Cdd:PRK14536  234 CDIHIGGVDHIRVHHTNEIAQCEAA---TGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFL 307
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 52-77 1.82e-03

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: 36.21  E-value: 1.82e-03
                          10        20
                  ....*....|....*....|....*.
gi 2570694211  52 KMSKSEGNFLTLSESIEKFSADGMRL 77
Cdd:COG0060   603 KMSKSLGNVVDPQEVIDKYGADILRL 628
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 37-76 7.70e-03

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 34.39  E-value: 7.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2570694211  37 PKGIRANGHLMLNSAKMSKSEGNFLTLSESIEKFSADGMR 76
Cdd:PRK12267  284 PKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALR 323
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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