I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and marine bivalves, are found in various invertebrate phyla and are apparently ubiquitous in insects. Lysozymes cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. I-type enzymes share structural similarity and the conserved glutamate catalytic residue of the lysozyme family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076 185 CLGCICEVTSGCNTTIGCSGS-VCGPFAITWGYWSDAGKPTLNDEPNSADGAYPRCVNDPYCAARAIQGYMAKFGQDCTG 263
Cdd:cd16890    2 CLGCLCEAASGCNPTAGCSMGgVCGPFRISKPYWQDAGKPVLPGDDPNRGGAFERCANDPYCAARTVRNYMARYGQDCNG 81

                         90       100
                 ....*....|....*....|....
gi 861640076 264 NGVIDCDDYLRIHRLGGYGCTGPL 287
Cdd:cd16890   82 DGVIDCEDYARIHYLGPNGCKNQE 105

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 861640076 132 IAKSSIVLDVKSWGDETDMKEMENAVRSIEMDGLVWG 168
Cdd:cd00292    1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWG 37

I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and marine bivalves, are found in various invertebrate phyla and are apparently ubiquitous in insects. Lysozymes cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. I-type enzymes share structural similarity and the conserved glutamate catalytic residue of the lysozyme family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076 185 CLGCICEVTSGCNTTIGCSGS-VCGPFAITWGYWSDAGKPTLNDEPNSADGAYPRCVNDPYCAARAIQGYMAKFGQDCTG 263
Cdd:cd16890    2 CLGCLCEAASGCNPTAGCSMGgVCGPFRISKPYWQDAGKPVLPGDDPNRGGAFERCANDPYCAARTVRNYMARYGQDCNG 81

                         90       100
                 ....*....|....*....|....
gi 861640076 264 NGVIDCDDYLRIHRLGGYGCTGPL 287
Cdd:cd16890   82 DGVIDCEDYARIHYLGPNGCKNQE 105

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076   4 GDLKTDKGVEDLNTYLADRSYVDGWQPTQADVAVLEALGKIPTS-SNPHVLRWYNHIKSY 62
Cdd:cd10308   23 ADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDAtKFPHLARWYRHIASF 82

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 861640076  137 IVLDVKSWGDETDMKEMENAVRSIEMDGLVWG 168
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWG 32

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 861640076   134 KSSIVLDVKSWGDETDMKEMENAVRSI-EMDGLVWG 168
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWG 36

I-type lysozyme; Invertebrate type (I-type) lysozyme, initially identified in starfish and marine bivalves, are found in various invertebrate phyla and are apparently ubiquitous in insects. Lysozymes cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. I-type enzymes share structural similarity and the conserved glutamate catalytic residue of the lysozyme family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076 185 CLGCICEVTSGCNTTIGCSGS-VCGPFAITWGYWSDAGKPTLNDEPNSADGAYPRCVNDPYCAARAIQGYMAKFGQDCTG 263
Cdd:cd16890    2 CLGCLCEAASGCNPTAGCSMGgVCGPFRISKPYWQDAGKPVLPGDDPNRGGAFERCANDPYCAARTVRNYMARYGQDCNG 81

                         90       100
                 ....*....|....*....|....
gi 861640076 264 NGVIDCDDYLRIHRLGGYGCTGPL 287
Cdd:cd16890   82 DGVIDCEDYARIHYLGPNGCKNQE 105

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076   4 GDLKTDKGVEDLNTYLADRSYVDGWQPTQADVAVLEALGKIPTS-SNPHVLRWYNHIKSY 62
Cdd:cd10308   23 ADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDAtKFPHLARWYRHIASF 82

Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS from higher 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 CysRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 861640076  12 VEDLNTYLADRSYVDGWQPTQADVAVLEALGKIPTSSNPHVLRWYNHI 59
Cdd:cd10310   23 AEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADRLVHVLRWYRHI 70

Eukaryotic elongation factor 1 beta central acidic region;

                          10        20
                  ....*....|....*....|....*...
gi 861640076   99 LFGSD-EEEDAEAAKIREERLKAYAEKK 125
Cdd:pfam10587   1 LFGSDdEEEDEEAERLREERLAAYAAKK 28

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 861640076   134 KSSIVLDVKSWGDETDMKEMENAVRSI-EMDGLVWG 168
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWG 36

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 861640076   2 AVGDLKT-DKGVEDLNTYLADRSYVDGWQPTQADVAVLEAL-------GKIPTSSNPHVLRWYNHIKS 61
Cdd:cd10306   19 VLKDFKAlSQALEELDSHLTLRTFIVGYSLSLADIAVWGALrgngvagSLIKNKVYVNLSRWFSFLES 86

Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076  13 EDLNTYLADRSYVDG-WQPTQADVAVLEAL-----GKIPTSSN-----PHVLRWYNHIKS 61
Cdd:cd10304   28 GQLNLHLRTRTFLLGtGKPSVADVAVFEAVlpvvkEWSDEVKTgyakyRHILRWVDYVQN 87

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 861640076   7 KTDKGVEDLNTYLADRSYVDGWQPTQADVAVLEAL--------GKIPTSSNPHVLRWYNHIKSYD-FKSLPGEKK 72
Cdd:cd03181   44 DLKRALGVLEEHLLTRTYLVGERITLADIFVASALlrgfetvlDPEFRKKYPNVTRWFNTVVNQPkFKAVFGEVK 118

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 861640076  15 LNTYLADRSYVDGWQPTQADVAVLE--AL---GKIPTSSNPHVLRWYNHIksydfKSLPG 69
Cdd:cd03206   45 LDQHLAGRDWLAGDRPTIADVACYPyiALapeGGVSLEPYPAIRAWLARV-----EALPG 99