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Conserved domains on  [gi|119617425|gb|EAW97019|]
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methionine-tRNA synthetase, isoform CRA_a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
 251-364 1.48e-73

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 245.46  E-value: 1.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 251 RPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQ 330
Cdd:PLN02610   4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119617425 331 EICDKYHIIHADIYRWFNISFDIFGRTTTPQQTK 364
Cdd:PLN02610  84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTE 117
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
 77-179 4.22e-46

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS 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. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS 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. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


:

Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 154.58  E-value: 4.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  77 QDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLaGETESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79

                         90       100
                 ....*....|....*....|...
gi 119617425 157 QDPAYLPEELSALHSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
 1-74 5.01e-29

Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing a thioredoxin fold. This domain found in methionyl-tRNA synthetase (MRS), a multi-tRNA synthetase complex (MSC) component.


:

Pssm-ID: 436537  Cd Length: 74  Bit Score: 108.25  E-value: 5.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617425    1 MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSG 74
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKCDVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 251-364 1.48e-73

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 245.46  E-value: 1.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 251 RPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQ 330
Cdd:PLN02610   4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119617425 331 EICDKYHIIHADIYRWFNISFDIFGRTTTPQQTK 364
Cdd:PLN02610  84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTE 117
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 265-364 2.72e-57

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: 190.82  E-value: 2.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 265 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIY 344
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79

                         90       100
                 ....*....|....*....|
gi 119617425 345 RWFNISFDIFGRTTTPQQTK 364
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKE 99
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 266-364 1.68e-46

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 164.39  E-value: 1.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  266 VLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 345
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79

                          90
                  ....*....|....*....
gi 119617425  346 WFNISFDIFGRTTTPQQTK 364
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHE 98
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
 77-179 4.22e-46

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS 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. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS 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. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 154.58  E-value: 4.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  77 QDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLaGETESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79

                         90       100
                 ....*....|....*....|...
gi 119617425 157 QDPAYLPEELSALHSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 266-364 4.39e-43

methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273058 [Multi-domain]  Cd Length: 530  Bit Score: 158.31  E-value: 4.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  266 VLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 345
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79

                          90
                  ....*....|....*....
gi 119617425  346 WFNISFDIFGRTTTPQQTK 364
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKE 98
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 264-364 8.99e-40

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: 149.49  E-value: 8.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 264 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADI 343
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79

                         90       100
                 ....*....|....*....|.
gi 119617425 344 YRWFNISFDIFGRTTTPQQTK 364
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKE 100
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
 1-74 5.01e-29

Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing a thioredoxin fold. This domain found in methionyl-tRNA synthetase (MRS), a multi-tRNA synthetase complex (MSC) component.


Pssm-ID: 436537  Cd Length: 74  Bit Score: 108.25  E-value: 5.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617425    1 MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSG 74
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKCDVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-187 9.37e-13

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 66.84  E-value: 9.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  47 KVPVLQlDSGNYLFSTSAICRYF--------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQG--KKGEDVLGS 116
Cdd:COG0625   52 KVPVLV-DDGLVLTESLAILEYLaerypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpAAIARARAE 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617425 117 VRRALTHIDHSLSRQncPFLAGETESLADIVLWGALYPLLQDPAYLpEELSALHSWFQTLSTQEPCQRAAE 187
Cdd:COG0625  131 LARLLAVLEARLAGG--PYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALA 198
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 111-180 1.07e-05

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 43.81  E-value: 1.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617425  111 EDVLGSVRRALTHIDHSLSrqNCPFLAGETESLADIVLWGAL-YPLLQDPAYLPEELSALHSWFQTLSTQE 180
Cdd:pfam00043  25 DEALEKVARVLSALEEVLK--GQTYLVGDKLTLADIALAPALlWLYELDPACLREKFPNLKAWFERVAARP 93
PLN02395 PLN02395
glutathione S-transferase
 47-179 2.39e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 39.08  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  47 KVPVLQldSGNY-LFSTSAICRYF----------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKG----E 111
Cdd:PLN02395  52 VVPVIV--DGDYkIFESRAIMRYYaekyrsqgpdLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHILFASKMGfpadE 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617425 112 DVLGSVRRALTHI----DHSLSRQNcpFLAGETESLADIV-------LWGALypllqDPAYLPEELSALHSWFQTLSTQ 179
Cdd:PLN02395 130 KVIKESEEKLAKVldvyEARLSKSK--YLAGDFVSLADLAhlpfteyLVGPI-----GKAYLIKDRKHVSAWWDDISSR 201
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 27-68 3.03e-03

GST_N family, unknown subfamily 3; composed of uncharacterized bacterial 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 36.08  E-value: 3.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119617425  27 EVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRY 68
Cdd:cd03049   30 LVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEY 71
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 251-364 1.48e-73

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 245.46  E-value: 1.48e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 251 RPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQ 330
Cdd:PLN02610   4 EGKSPPKLPIPGKRNILITSALPYVNNVPHLGNIIGCVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPK 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119617425 331 EICDKYHIIHADIYRWFNISFDIFGRTTTPQQTK 364
Cdd:PLN02610  84 EICDKYHAIHKEVYDWFDISFDKFGRTSTPQQTE 117
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 265-364 2.72e-57

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: 190.82  E-value: 2.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 265 NVLITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIY 344
Cdd:cd00814    1 KVLITTALPYVNGVPHLGHLYGTVL-ADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLF 79

                         90       100
                 ....*....|....*....|
gi 119617425 345 RWFNISFDIFGRTTTPQQTK 364
Cdd:cd00814   80 KWLNISFDYFIRTTSPRHKE 99
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
 266-364 1.68e-46

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


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 164.39  E-value: 1.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  266 VLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 345
Cdd:pfam09334   1 ILVTTALPYANGPPHLGHLYS-YIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFK 79

                          90
                  ....*....|....*....
gi 119617425  346 WFNISFDIFGRTTTPQQTK 364
Cdd:pfam09334  80 KFNISFDDYGRTTSERHHE 98
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
 77-179 4.22e-46

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS 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. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS 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. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 154.58  E-value: 4.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  77 QDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLaGETESLADIVLWGALYPLL 156
Cdd:cd10307    1 DDDLSNQWLEWEAWLLQPALSLALALTHVQGKKSEADLNTVLNALVHLDQSLLKKSTPLL-GDKLSSADVVVWSALYPLG 79

                         90       100
                 ....*....|....*....|...
gi 119617425 157 QDPAYLPEELSALHSWFQTLSTQ 179
Cdd:cd10307   80 TDKSALPENLDNLRRWFQNVSTL 102
metG TIGR00398
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ...
 266-364 4.39e-43

methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273058 [Multi-domain]  Cd Length: 530  Bit Score: 158.31  E-value: 4.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  266 VLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYR 345
Cdd:TIGR00398   1 ILITTALPYANGKPHLGHAY-TTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWK 79

                          90
                  ....*....|....*....
gi 119617425  346 WFNISFDIFGRTTTPQQTK 364
Cdd:TIGR00398  80 WLNISFDRFIRTTDEEHKE 98
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 264-364 8.99e-40

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: 149.49  E-value: 8.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 264 RNVLITSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADI 343
Cdd:COG0143    1 KKFLVTTAIPYANGPPHIGHLY-TYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKEL 79

                         90       100
                 ....*....|....*....|.
gi 119617425 344 YRWFNISFDIFGRTTTPQQTK 364
Cdd:COG0143   80 FEKLGISFDNFIRTTSPEHKE 100
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 264-360 1.48e-38

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 147.61  E-value: 1.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 264 RNVLITSALPYVNNVPHLGNIIGcVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADI 343
Cdd:PRK00133   2 RKILVTCALPYANGPIHLGHLVE-YIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80

                         90
                 ....*....|....*..
gi 119617425 344 YRWFNISFDIFGRTTTP 360
Cdd:PRK00133  81 FAGFGISFDNYGSTHSE 97
GST_N_5 pfam18485
Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing ...
 1-74 5.01e-29

Glutathione S-transferase, N-terminal domain; This is the N-terminal (GST-N) domain containing a thioredoxin fold. This domain found in methionyl-tRNA synthetase (MRS), a multi-tRNA synthetase complex (MSC) component.


Pssm-ID: 436537  Cd Length: 74  Bit Score: 108.25  E-value: 5.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617425    1 MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSG 74
Cdd:pfam18485   1 MKLFVSEGNPHCLKVLAAAEATGVKCDVQVQFVNHEEKVVPFLTRPVLPTLELDSGQFLFSPNAICRYLFELSG 74
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 268-358 1.59e-25

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 108.43  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 268 ITSALPYVNNVPHLGNIiGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWF 347
Cdd:PRK11893   5 ITTPIYYPNGKPHIGHA-YTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEAL 83

                         90
                 ....*....|.
gi 119617425 348 NISFDIFGRTT 358
Cdd:PRK11893  84 NISYDDFIRTT 94
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 268-358 8.40e-18

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 85.62  E-value: 8.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 268 ITSALPYVNNVPHLGN----IIgcvlsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKyhiIHADI 343
Cdd:PRK12267   8 ITTPIYYPNGKPHIGHayttIA-----ADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDE---ISAGF 79

                         90
                 ....*....|....*...
gi 119617425 344 YR-W--FNISFDIFGRTT 358
Cdd:PRK12267  80 KElWkkLDISYDKFIRTT 97
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-187 9.37e-13

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 66.84  E-value: 9.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  47 KVPVLQlDSGNYLFSTSAICRYF--------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQG--KKGEDVLGS 116
Cdd:COG0625   52 KVPVLV-DDGLVLTESLAILEYLaerypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpAAIARARAE 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617425 117 VRRALTHIDHSLSRQncPFLAGETESLADIVLWGALYPLLQDPAYLpEELSALHSWFQTLSTQEPCQRAAE 187
Cdd:COG0625  131 LARLLAVLEARLAGG--PYLAGDRFSIADIALAPVLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALA 198
PLN02224 PLN02224
methionine-tRNA ligase
 262-362 2.83e-11

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 65.51  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 262 GERNVLiTSALPYVNNVPHLGNIIgCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHA 341
Cdd:PLN02224  68 ADTFVL-TTPLYYVNAPPHMGSAY-TTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYR 145

                         90       100
                 ....*....|....*....|.
gi 119617425 342 DIYRWFNISFDIFGRTTTPQQ 362
Cdd:PLN02224 146 TLWKDLDIAYDKFIRTTDPKH 166
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 267-365 3.31e-11

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: 63.98  E-value: 3.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 267 LITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGL-------------TPQEIC 333
Cdd:cd00668    3 YVTTPPPYANGSLHLGHALTHII-ADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFV 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119617425 334 DKYHIIHADIYRWFNISFDI--FGRTTTPQQTKS 365
Cdd:cd00668   82 EEMSGEHKEDFRRLGISYDWsdEYITTEPEYSKA 115
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
 104-179 5.03e-11

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.


Pssm-ID: 198322 [Multi-domain]  Cd Length: 82  Bit Score: 58.48  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 104 VVQGKKGEDVLGSV-----RRALTHIDHSLSRQNCpFLAGETESLADIVLWGALYPLLQDPAYL-PEELSALHSWFQTLS 177
Cdd:cd10289    2 AAQVDQWLDLAGSLlkgkeLEALLKSLNSYLASRT-FLVGYSLTLADVAVFSALYPSGQKLSDKeKKKFPHVTRWFNHIQ 80


                 ..
gi 119617425 178 TQ 179
Cdd:cd10289   81 NL 82
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 83-186 5.21e-09

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; composed of uncharacterized bacterial 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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 53.82  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  83 QWLEWEATELQPALSAALYYLVVQGKKGED---VLGSVRRALTHI---DHSLSRQncPFLAGETESLADIVLWGALYPLL 156
Cdd:cd03180    8 RWMDWQTSTLNPAFRYAFWGLVRTPPEQRDpaaIAASLAACNKLMailDAQLARQ--AYLAGDRFTLADIALGCSVYRWL 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 119617425 157 QDPAYLPeELSALHSWFQTLStqepcQRAA 186
Cdd:cd03180   86 ELPIERP-ALPHLERWYARLS-----QRPA 109
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 81-150 1.92e-06

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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 active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 46.47  E-value: 1.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617425  81 TNQWLEWEATELQPALSAALYYLVVQGKKG----EDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVLWG 150
Cdd:cd03178    5 VLQWLFFQMSGLGPMFGQAGHFLYFAPEKIpyaiERYTDEVKRLYGVLDKRLSDR--PYLAGEEYSIADIALYP 76
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 81-176 2.08e-06

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of 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. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. 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. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 45.95  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  81 TNQWLEWEATELQPALSAALYY----LVVQGKKGEDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVLWGALY--P 154
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLekvpLPKDEAAVEAAREELPALLAALEQLLAGR--PYLAGDQFSLADVALAPVLArlE 78

                         90       100
                 ....*....|....*....|..
gi 119617425 155 LLQDPAYLPEELSALHSWFQTL 176
Cdd:cd00299   79 ALGPYYDLLDEYPRLKAWYDRL 100
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 83-180 4.85e-06

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.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 45.63  E-value: 4.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  83 QWLEWEATELQPALSAALYYLVvqGKKG------EDVLGSVRRALTHIDHSLsrQNCPFLAGETESLADIVLWGALYPLL 156
Cdd:cd03181    7 QWISFANSELLPAAATWVLPLL--GIAPynkkavDKAKEDLKRALGVLEEHL--LTRTYLVGERITLADIFVASALLRGF 82

                         90       100
                 ....*....|....*....|....*..
gi 119617425 157 Q---DPAYLpEELSALHSWFQTLSTQE 180
Cdd:cd03181   83 EtvlDPEFR-KKYPNVTRWFNTVVNQP 108
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 111-180 1.07e-05

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 43.81  E-value: 1.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617425  111 EDVLGSVRRALTHIDHSLSrqNCPFLAGETESLADIVLWGAL-YPLLQDPAYLPEELSALHSWFQTLSTQE 180
Cdd:pfam00043  25 DEALEKVARVLSALEEVLK--GQTYLVGDKLTLADIALAPALlWLYELDPACLREKFPNLKAWFERVAARP 93
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 273-328 4.48e-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: 45.82  E-value: 4.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  273 PYVNNVPHLGNIIGCVLSaDVFARYSRLRQWNTLYLCGTDEYGTATETK----ALEEGLT 328
Cdd:TIGR00422  42 PNVTGSLHIGHALNWSIQ-DIIARYKRMKGYNVLWLPGTDHAGIATQVKvekkLGAEGKT 100
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 268-352 5.15e-05

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: 44.93  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425 268 ITSALPYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEIcDKYHI--IHADIYR 345
Cdd:cd00812    4 ILVMFPYPSGALHVGHVRTYTI-GDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDW-TEYNIkkMKEQLKR 81


                 ....*..
gi 119617425 346 wFNISFD 352
Cdd:cd00812   82 -MGFSYD 87
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 116-177 5.04e-04

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces cerevisiae GST protein, GTT2. 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. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 39.61  E-value: 5.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119617425 116 SVRRALTHIDHSLSRQncPFLAGETESLADIVLWGAL---YPLLQDPaylPEELSALHSWFQTLS 177
Cdd:cd03182   52 RVIDFLPVLDKRLAES--PYVAGDRFSIADITAFVALdfaKNLKLPV---PEELTALRRWYERMA 111
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 273-321 7.19e-04

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: 41.46  E-value: 7.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119617425 273 PYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETK 321
Cdd:cd00817   10 PNVTGSLHMGHALNNTI-QDIIARYKRMKGYNVLWPPGTDHAGIATQVV 57
GST_C_ValRS_N cd10294
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ...
 77-179 1.16e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. 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. They typically form large stable complexes with other proteins. 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. The GST_C-like domain of ValRS 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. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain.


Pssm-ID: 198327 [Multi-domain]  Cd Length: 123  Bit Score: 38.66  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  77 QDDLTNQWLEWEATELQPALSAALYYLV----VQGKKGEDVLGSVRRALTHIDHSLSRQNcpFLAGETESLADIVLWGAL 152
Cdd:cd10294    1 ACALVWQWVSFADNELTPAACAAAFPLLglsgSDKQNQQRSLAELQRVLKVLDCYLKLRT--YLVGEAITLADIAVACAL 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 119617425 153 ---YPLLQDPAyLPEELSALHSWFQTLSTQ 179
Cdd:cd10294   79 llpFKYVLDPA-RRESLLNVTRWFLTCVNQ 107
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 273-336 1.51e-03

catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which 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.


Pssm-ID: 173901 [Multi-domain]  Cd Length: 143  Bit Score: 38.61  E-value: 1.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119617425 273 PYVNNVPHLGNIIGCVLsADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKY 336
Cdd:cd00802    6 ITPNGYLHIGHLRTIVT-FDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERW 68
PLN02395 PLN02395
glutathione S-transferase
 47-179 2.39e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 39.08  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  47 KVPVLQldSGNY-LFSTSAICRYF----------FLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKG----E 111
Cdd:PLN02395  52 VVPVIV--DGDYkIFESRAIMRYYaekyrsqgpdLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLHILFASKMGfpadE 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617425 112 DVLGSVRRALTHI----DHSLSRQNcpFLAGETESLADIV-------LWGALypllqDPAYLPEELSALHSWFQTLSTQ 179
Cdd:PLN02395 130 KVIKESEEKLAKVldvyEARLSKSK--YLAGDFVSLADLAhlpfteyLVGPI-----GKAYLIKDRKHVSAWWDDISSR 201
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 273-321 2.59e-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: 40.09  E-value: 2.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 119617425  273 PYVNNVPHLGNIIGCVLSaDVFARYSRLRQWNTLYLCGTDEYGTATETK 321
Cdd:pfam00133  32 PNATGSLHIGHALAKTLK-DIVIRYKRMKGYYVLWVPGWDHHGLPTEQV 79
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 27-68 3.03e-03

GST_N family, unknown subfamily 3; composed of uncharacterized bacterial 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 36.08  E-value: 3.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119617425  27 EVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRY 68
Cdd:cd03049   30 LVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEY 71
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 83-174 3.16e-03

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; 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. 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 37.23  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  83 QWLEWEATELQPALSAALY---YLVVQGKKG--EDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVL-----WGAL 152
Cdd:cd03188    8 EWLNFIASELHKAFGPLFYparWADDALAEEvkAAARERLERRLAYLDAQLAGG--PYLLGDQFSVADAYLfvvlrWARA 85

                         90       100
                 ....*....|....*....|..
gi 119617425 153 YPLlqDPAYLPeelsALHSWFQ 174
Cdd:cd03188   86 VGL--DLSDWP----HLAAYLA 101
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
 80-176 4.43e-03

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.


Pssm-ID: 198338 [Multi-domain]  Cd Length: 101  Bit Score: 36.50  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  80 LTNQWLEWEATELQPALSAALyylvvqgkkgedvlgsVRRALTHIDHSLsrQNCPFLAGETESLADIVLWGALYPLLQDP 159
Cdd:cd10305    6 QVDQWLEYRVTQVAPASDKAD----------------AKSLLKELNSYL--QDRTYLVGHKLTLADVVLYYGLHPIMKDL 67

                         90
                 ....*....|....*...
gi 119617425 160 AYLPEE-LSALHSWFQTL 176
Cdd:cd10305   68 SPQEKEqYLNVSRWFDHV 85
PTZ00419 PTZ00419
valyl-tRNA synthetase-like protein; Provisional
 292-332 5.49e-03

valyl-tRNA synthetase-like protein; Provisional


Pssm-ID: 240411 [Multi-domain]  Cd Length: 995  Bit Score: 39.22  E-value: 5.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119617425 292 DVFARYSRLRQWNTLYLCGTDEYGTATET---KAL--EEGLTPQEI 332
Cdd:PTZ00419  87 DSLIRYHRMKGDETLWVPGTDHAGIATQVvveKKLmkEENKTRHDL 132
ValS COG0525
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ...
 292-332 5.72e-03

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: 39.26  E-value: 5.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119617425 292 DVFARYSRLRQWNTLYLCGTDEYGTATETK----ALEEGLTPQEI 332
Cdd:COG0525   62 DILIRYKRMQGYNTLWQPGTDHAGIATQAVverqLAEEGKSRHDL 106
valS PRK05729
valyl-tRNA synthetase; Reviewed
 292-332 6.37e-03

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 38.93  E-value: 6.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119617425 292 DVFARYSRLRQWNTLYLCGTDEYGTATETK----ALEEGLTPQEI 332
Cdd:PRK05729  63 DILIRYKRMQGYNTLWLPGTDHAGIATQMVverqLAAEGKSRHDL 107
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 111-174 6.82e-03

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 34.99  E-value: 6.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119617425  111 EDVLGSVRRALTHIDHSLSRQncPFLAGETESLADIVLWGALYPLLQDPAYLP--EELSALHSWFQ 174
Cdd:pfam13410   3 ERAREQLRAALDALEARLADG--PGLLGDRPTLADIALAPVLARLDAAYPGLDlrEGYPRLRAWLE 66
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 83-164 7.91e-03

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial 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. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 35.73  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617425  83 QWLEWEATELQPAL----SAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQncPFLAGETESLADiVLWGALYPLLQD 158
Cdd:cd03207    3 RWLFFAAGTVEPPLlnkaLGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGR--PYLVGERFSAAD-LLLASVLRWARA 79


                 ....*.
gi 119617425 159 PAYLPE 164
Cdd:cd03207   80 FGLLPE 85
 
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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