RecName: Full=Proline--tRNA ligase; AltName: Full=Prolyl-tRNA synthetase; Short=ProRS
Protein Classification
proline--tRNA ligase( domain architecture ID 11483602)
proline--tRNA ligase catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro)
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| PRK09194 | PRK09194 | prolyl-tRNA synthetase; Provisional |
1-570 | 0e+00 | |||||||||
prolyl-tRNA synthetase; Provisional : Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 974.95 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| PRK09194 | PRK09194 | prolyl-tRNA synthetase; Provisional |
1-570 | 0e+00 | |||||||||
prolyl-tRNA synthetase; Provisional Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 974.95 E-value: 0e+00
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| ProS | COG0442 | Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-569 | 0e+00 | |||||||||
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 916.85 E-value: 0e+00
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| proS_fam_II | TIGR00409 | prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-571 | 0e+00 | |||||||||
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273063 [Multi-domain] Cd Length: 568 Bit Score: 659.20 E-value: 0e+00
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| ProRS_core_prok | cd00779 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-456 | 1.61e-133 | |||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes. Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 389.63 E-value: 1.61e-133
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| tRNA_edit | pfam04073 | Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
258-371 | 2.17e-30 | |||||||||
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold. Pssm-ID: 427693 [Multi-domain] Cd Length: 123 Bit Score: 115.39 E-value: 2.17e-30
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| Name | Accession | Description | Interval | E-value | |||||||||
| PRK09194 | PRK09194 | prolyl-tRNA synthetase; Provisional |
1-570 | 0e+00 | |||||||||
prolyl-tRNA synthetase; Provisional Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 974.95 E-value: 0e+00
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| ProS | COG0442 | Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ... |
1-569 | 0e+00 | |||||||||
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440211 [Multi-domain] Cd Length: 564 Bit Score: 916.85 E-value: 0e+00
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| proS_fam_II | TIGR00409 | prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ... |
1-571 | 0e+00 | |||||||||
prolyl-tRNA synthetase, family II; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi. [Protein synthesis, tRNA aminoacylation] Pssm-ID: 273063 [Multi-domain] Cd Length: 568 Bit Score: 659.20 E-value: 0e+00
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| PRK12325 | PRK12325 | prolyl-tRNA synthetase; Provisional |
1-556 | 3.37e-180 | |||||||||
prolyl-tRNA synthetase; Provisional Pssm-ID: 237059 [Multi-domain] Cd Length: 439 Bit Score: 515.56 E-value: 3.37e-180
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| ProRS_core_prok | cd00779 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-456 | 1.61e-133 | |||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes. Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 389.63 E-value: 1.61e-133
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| ProRS-INS | cd04334 | INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ... |
225-385 | 1.32e-65 | |||||||||
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA synthetase (ProRS) however, this CD is not exclusively bacterial. It is also found at the N-terminus of the eukaryotic/archaea-like ProRS's of yeasts and single-celled parasites. ProRS catalyzes the attachment of proline to tRNA(Pro); proline is first activated by ATP, and then transferred to the acceptor end of tRNA(Pro). ProRS can inadvertently process noncognate amino acids such as alanine and cysteine, and to avoid such errors, in post-transfer editing, the INS domain deacylates mischarged Ala-tRNA(Pro), thus ensuring the fidelity of translation. Misacylated Cys-tRNA(Pro) is not edited by ProRS. In addition to the INS editing domain, the prokaryote-like ProRS protein contains catalytic and anticodon-binding domains which form a dimeric interface. Pssm-ID: 239826 [Multi-domain] Cd Length: 160 Bit Score: 211.22 E-value: 1.32e-65
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| ProRS_core | cd00772 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
17-250 | 3.14e-46 | |||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 163.69 E-value: 3.14e-46
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| YbaK_like | cd04332 | YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ... |
251-382 | 2.94e-39 | |||||||||
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX). Pssm-ID: 239824 [Multi-domain] Cd Length: 136 Bit Score: 139.99 E-value: 2.94e-39
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| Gly_His_Pro_Ser_Thr_tRS_core | cd00670 | Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
49-229 | 1.88e-30 | |||||||||
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 119.03 E-value: 1.88e-30
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| tRNA_edit | pfam04073 | Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ... |
258-371 | 2.17e-30 | |||||||||
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold. Pssm-ID: 427693 [Multi-domain] Cd Length: 123 Bit Score: 115.39 E-value: 2.17e-30
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| ProRS_anticodon_short | cd00861 | ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
471-566 | 2.47e-26 | |||||||||
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. Pssm-ID: 238438 [Multi-domain] Cd Length: 94 Bit Score: 102.67 E-value: 2.47e-26
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| EbsC | COG2606 | Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ... |
254-348 | 2.49e-21 | |||||||||
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis]; Pssm-ID: 442018 [Multi-domain] Cd Length: 152 Bit Score: 90.53 E-value: 2.49e-21
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| class_II_aaRS-like_core | cd00768 | Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
49-203 | 2.93e-19 | |||||||||
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ. Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 86.40 E-value: 2.93e-19
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| ProX_deacylase | cd04333 | This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ... |
253-348 | 3.84e-19 | |||||||||
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain. Pssm-ID: 239825 [Multi-domain] Cd Length: 148 Bit Score: 84.09 E-value: 3.84e-19
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| tRNA-synt_2b | pfam00587 | tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
95-205 | 4.84e-19 | |||||||||
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members. Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 85.16 E-value: 4.84e-19
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| ProRS_core_arch_euk | cd00778 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
38-188 | 1.13e-14 | |||||||||
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria. Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 74.17 E-value: 1.13e-14
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| HGTP_anticodon | pfam03129 | Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
479-556 | 9.41e-14 | |||||||||
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain. Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 67.23 E-value: 9.41e-14
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| HGTP_anticodon | cd00738 | HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
475-556 | 2.09e-13 | |||||||||
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 66.27 E-value: 2.09e-13
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| PRK12444 | PRK12444 | threonyl-tRNA synthetase; Reviewed |
36-194 | 1.44e-11 | |||||||||
threonyl-tRNA synthetase; Reviewed Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 67.08 E-value: 1.44e-11
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| ThrRS_core | cd00771 | Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
36-166 | 4.47e-11 | |||||||||
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 64.11 E-value: 4.47e-11
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| PLN02908 | PLN02908 | threonyl-tRNA synthetase |
36-192 | 7.95e-10 | |||||||||
threonyl-tRNA synthetase Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 61.71 E-value: 7.95e-10
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| HisS | COG0124 | Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
42-155 | 1.26e-09 | |||||||||
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 60.52 E-value: 1.26e-09
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| ThrS | COG0441 | Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
42-163 | 1.37e-08 | |||||||||
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 57.73 E-value: 1.37e-08
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| ProRS_anticodon_zinc | cd00862 | ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
462-571 | 6.19e-08 | |||||||||
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs. Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 53.07 E-value: 6.19e-08
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| HisRS-like_core | cd00773 | Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
47-155 | 8.02e-08 | |||||||||
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain. Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 53.76 E-value: 8.02e-08
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| YeaK | cd04336 | YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ... |
255-348 | 1.76e-07 | |||||||||
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans. Pssm-ID: 239828 [Multi-domain] Cd Length: 153 Bit Score: 50.81 E-value: 1.76e-07
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| YbaK_deacylase | cd00002 | This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ... |
265-366 | 3.26e-07 | |||||||||
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's. Pssm-ID: 237976 [Multi-domain] Cd Length: 152 Bit Score: 50.14 E-value: 3.26e-07
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| PLN02837 | PLN02837 | threonine-tRNA ligase |
17-217 | 2.00e-06 | |||||||||
threonine-tRNA ligase Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 50.67 E-value: 2.00e-06
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| PrdX_deacylase | cd04335 | This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ... |
252-356 | 8.61e-06 | |||||||||
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins. Pssm-ID: 239827 Cd Length: 156 Bit Score: 45.97 E-value: 8.61e-06
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| GlyRS-like_core | cd00774 | Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ... |
25-157 | 5.37e-05 | |||||||||
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues. Pssm-ID: 238397 [Multi-domain] Cd Length: 254 Bit Score: 44.89 E-value: 5.37e-05
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| PLN02734 | PLN02734 | glycyl-tRNA synthetase |
129-157 | 3.00e-03 | |||||||||
glycyl-tRNA synthetase Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 40.50 E-value: 3.00e-03
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