Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
187-487
7.69e-157
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It 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. SerRS synthetase is a homodimer.
:
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 448.16 E-value: 7.69e-157
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
94-138
1.47e-04
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits; the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes, there are two or more paralogous genes encoding each subunit, adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
The actual alignment was detected with superfamily member cd00584:
Pssm-ID: 471851 [Multi-domain] Cd Length: 121 Bit Score: 41.44 E-value: 1.47e-04
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
187-487
7.69e-157
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It 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. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 448.16 E-value: 7.69e-157
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
58-493
8.07e-125
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 371.26 E-value: 8.07e-125
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
161-487
2.32e-107
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 326.63 E-value: 2.32e-107
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
94-138
1.47e-04
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467468 [Multi-domain] Cd Length: 121 Bit Score: 41.44 E-value: 1.47e-04
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
187-487
7.69e-157
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It 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. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 448.16 E-value: 7.69e-157
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
58-493
8.07e-125
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 371.26 E-value: 8.07e-125
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
161-487
2.32e-107
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 326.63 E-value: 2.32e-107
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ...
237-467
5.87e-16
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: 77.43 E-value: 5.87e-16
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
246-462
2.70e-12
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: 65.99 E-value: 2.70e-12
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
94-138
1.47e-04
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467468 [Multi-domain] Cd Length: 121 Bit Score: 41.44 E-value: 1.47e-04
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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