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Conserved domains on  [gi|440212877|gb|AGB92245|]
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glu-/pro-tRNA synthetase, partial [Prolimacodes badia]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
1-68 1.79e-31

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.


The actual alignment was detected with superfamily member cd00778:

Pssm-ID: 444800 [Multi-domain]  Cd Length: 261  Bit Score: 112.30  E-value: 1.79e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440212877   1 GGSYTTTVEAYVPaSGRAIQGATSHHLGQNFSKIFDVIYDDPEtQEKKYVYQNSWGMTTRTIGVMVLV 68
Cdd:cd00778  196 GADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-GQKEYVHQTSWGISTRLIGAIIMI 261
HGTP_anticodon super family cl00266
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
74-134 2.70e-21

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).


The actual alignment was detected with superfamily member cd00862:

Pssm-ID: 469699 [Multi-domain]  Cd Length: 202  Bit Score: 84.66  E-value: 2.70e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440212877  74 GLVLPPRIADIQVIVVPCGItassTPEDRKSLYDSCKGLVDDLITAGLRAEGDYRENYSPG 134
Cdd:cd00862    1 GLVLPPRVAPIQVVIVPIGI----KDEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPG 57
 
Name Accession Description Interval E-value
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
1-68 1.79e-31

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: 112.30  E-value: 1.79e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440212877   1 GGSYTTTVEAYVPaSGRAIQGATSHHLGQNFSKIFDVIYDDPEtQEKKYVYQNSWGMTTRTIGVMVLV 68
Cdd:cd00778  196 GADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-GQKEYVHQTSWGISTRLIGAIIMI 261
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
74-134 2.70e-21

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: 84.66  E-value: 2.70e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440212877  74 GLVLPPRIADIQVIVVPCGItassTPEDRKSLYDSCKGLVDDLITAGLRAEGDYRENYSPG 134
Cdd:cd00862    1 GLVLPPRVAPIQVVIVPIGI----KDEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPG 57
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
85-134 8.36e-03

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: 33.33  E-value: 8.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 440212877   85 QVIVVPCGitasstpEDRKSLYDSCKGLVDDLITAGLRAEGDYReNYSPG 134
Cdd:pfam03129   1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIG 42
 
Name Accession Description Interval E-value
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
1-68 1.79e-31

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: 112.30  E-value: 1.79e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440212877   1 GGSYTTTVEAYVPaSGRAIQGATSHHLGQNFSKIFDVIYDDPEtQEKKYVYQNSWGMTTRTIGVMVLV 68
Cdd:cd00778  196 GADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-GQKEYVHQTSWGISTRLIGAIIMI 261
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
74-134 2.70e-21

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: 84.66  E-value: 2.70e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440212877  74 GLVLPPRIADIQVIVVPCGItassTPEDRKSLYDSCKGLVDDLITAGLRAEGDYRENYSPG 134
Cdd:cd00862    1 GLVLPPRVAPIQVVIVPIGI----KDEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPG 57
ProRS_core cd00772
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
1-67 1.07e-06

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: 46.21  E-value: 1.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440212877   1 GGSYTTTVEAYVpASGRAIQGATSHHLGQNFSKIFDVI--YDDPETQEkKYVYQNSWGMT-TRTIGVMVL 67
Cdd:cd00772  196 GASKSREFEALM-EDGKAKQAETGHIFGEGFARAFDLKakFLDKDGKE-KFFEMGCWGIGiSRFIGAIIE 263
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
85-134 8.36e-03

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: 33.33  E-value: 8.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 440212877   85 QVIVVPCGitasstpEDRKSLYDSCKGLVDDLITAGLRAEGDYReNYSPG 134
Cdd:pfam03129   1 QVVVIPLG-------EKAEELEEYAQKLAEELRAAGIRVELDDR-NESIG 42
 
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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