Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 104 EKAQILEWTTKAFSP---IETQSIVEQLDEFLKSSTFIAqDSGISVADLAVYARIHSYICGLSAKEGYKLNNVCRWFDFI 180
Cdd:cd10289   1 EAAQVDQWLDLAGSLlkgKELEALLKSLNSYLASRTFLV-GYSLTLADVAVFSALYPSGQKLSDKEKKKFPHVTRWFNHI 79

                ...
gi 19115568 181 QHQ 183
Cdd:cd10289  80 QNL 82

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 277 PVPSMIDFRIGFIEKAVKHPNADSLYVSTIHCGDaEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVF 356
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGE-EEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVL 79

                        90       100
                ....*....|....*....|....*.
gi 19115568 357 CASSPDKSVVEFVLPPENAEIGDRLT 382
Cdd:cd02799  80 CASNADHEKVELLEPPEGAKPGERVT 105

Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 104 EKAQILEWTTKAFSP---IETQSIVEQLDEFLKSSTFIAqDSGISVADLAVYARIHSYICGLSAKEGYKLNNVCRWFDFI 180
Cdd:cd10289   1 EAAQVDQWLDLAGSLlkgKELEALLKSLNSYLASRTFLV-GYSLTLADVAVFSALYPSGQKLSDKEKKKFPHVTRWFNHI 79

                ...
gi 19115568 181 QHQ 183
Cdd:cd10289  80 QNL 82

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 276 TPVPSMIDFRIGFIEKAVKHPNADSLYVSTIHCGdaEGPRTVCSGLVKY----IPLEQMQQRKVIVVANLKPVNMRSVKS 351
Cdd:COG0073  36 EKVGGLDGLRVGKVLEAEPHPNADKLLVLQVDVG--EETRQIVCGAPNVyagdKVPEALVGAQVPGVVNLKPRKIRGVES 113

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19115568 352 QAMVFCAS--SPDKSVVEFVLPPENAEIG-DRLTFEGFDTEEPEAQLNPKR 399
Cdd:COG0073 114 EGMLCSAEelGLGEDHDGILELPEDAPPGdDAEYLLLLDDVIIEILTTPNR 164

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 277 PVPSMIDFRIGFIEKAVKHPNADSLYVSTIHCGDaEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVF 356
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGE-EEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVL 79

                        90       100
                ....*....|....*....|....*.
gi 19115568 357 CASSPDKSVVEFVLPPENAEIGDRLT 382
Cdd:cd02799  80 CASNADHEKVELLEPPEGAKPGERVT 105

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568   284 FRIGFIEKAVKHPNADSLYVSTIHCGDAEgPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFCASSPDK 363
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEE-PRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDG 79

                          90
                  ....*....|....*..
gi 19115568   364 SVVEFVLPPENAEIGDR 380
Cdd:pfam01588  80 GSVGLLEPPADVPPGTK 96

tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 282 IDFRIGFIEKAVKHPNADSLYVSTIHCGdaEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFCASSP 361
Cdd:cd02800   9 VDLRVGKVLEAERVEGSDKLLKLTVDLG--EEERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAEDG 86

                        90       100
                ....*....|....*....|
gi 19115568 362 DKsvVEFVLPPENAEIGDRL 381
Cdd:cd02800  87 GK--LKLLTPDEEVEPGSRV 104

methionyl-tRNA synthetase; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568  267 APKEPPKAATPVPSMIDF--------RIGFIEKAVKHPNADSLYVSTIHCGdaEGPRTVCSGLVKYIPLEQMQQRKVIVV 338
Cdd:PRK00133 553 AAAAAPLAEEPIAETISFddfakvdlRVAKIVEAEKVEGADKLLKLTLDLG--EETRQVFSGIKSAYDPEELVGKLVVMV 630

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19115568  339 ANLKPVNMRSVKSQAMVFCASSPDKSVveFVL-PPENAEIGDR 380
Cdd:PRK00133 631 ANLAPRKMKFGVSEGMVLAAGPGGGDL--FLLePDEGAKPGMR 671

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568   282 IDFRIGFIEKAVKHPNADSLYVSTIHCGDAEgpRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFcASSP 361
Cdd:TIGR00399  40 VDLRVGKILKAERVEKSDKLLKLKLDLGDEK--RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMIL-AAED 116

                          90       100
                  ....*....|....*....|
gi 19115568   362 DKSVVEFVLPPENAEIGDRL 381
Cdd:TIGR00399 117 DGKVLFLLSPDQEAIAGERI 136

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 104 EKAQILEWT-------TKAFSPIETQSIVEQLDEFLKSSTFIAQDSgISVADLAVYARIHSYICGLSAKEGYKLNNVCRW 176
Cdd:cd10305   3 ERAQVDQWLeyrvtqvAPASDKADAKSLLKELNSYLQDRTYLVGHK-LTLADVVLYYGLHPIMKDLSPQEKEQYLNVSRW 81

                        90
                ....*....|
gi 19115568 177 FDFIQHQESV 186
Cdd:cd10305  82 FDHVQHLPGI 91

chaperone CsaA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568  281 MIDFRIGFIEKAVKHPNADSL-YVSTIHCGDAEGPRTVCSGLVKYIPLEQMQQRKVIVVANLKPVNMRSVKSQAMVFCAS 359
Cdd:PRK10089  11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGEEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGFE 90

                 ....*..
gi 19115568  360 SPDKSVV 366
Cdd:PRK10089  91 DEDGEVV 97

Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 104 EKAQILEWTTKAFSPI------ETQSIVEQLDEFLKSSTFIAQDSgISVADLAVYARIHSYICGLSAKEGYKLNNVCRWF 177
Cdd:cd10306   3 DKEQVAEWIDFATTLLvlkdfkALSQALEELDSHLTLRTFIVGYS-LSLADIAVWGALRGNGVAGSLIKNKVYVNLSRWF 81

                ...
gi 19115568 178 DFI 180
Cdd:cd10306  82 SFL 84

tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115568 284 FRIGFIEKAVKHPNADSLYVSTIHCGDAEgPRTVCSG--LVKyipleqmqQRKVIVVAN----------LKPVNMRSVKS 351
Cdd:cd02796   1 VVVGKVLEVEPHPNADKLNVCKVDIGENK-PLQIVCGapNVR--------AGDKVVVALpgavlpgglkIKKRKLRGVES 71

                        90       100       110
                ....*....|....*....|....*....|....
gi 19115568 352 QAMvFCA------SSPDKSVVEFvlpPENAEIGD 379
Cdd:cd02796  72 EGM-LCSakelglGEDSDGIIEL---PEDAPVGT 101