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Conserved domains on  [gi|1907199790|ref|XP_036011109|]
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DALR anticodon-binding domain-containing protein 3 isoform X4 [Mus musculus]

Protein Classification

DALR_1 domain-containing protein( domain architecture ID 10656406)

DALR_1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DALR_1 smart00836
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
 418-479 5.40e-16

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.


:

Pssm-ID: 214846 [Multi-domain]  Cd Length: 122  Bit Score: 74.15  E-value: 5.40e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199790  418 VCKFLVQLSMDFSSYYNRVHILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPLSHI 479
Cdd:smart00836  64 LANYLYDLAAAFHSFYNRVRVLGEENPEL---RKARLALLKAVRQVLANGLRLLGISAPERM 122
 
Name Accession Description Interval E-value
DALR_1 smart00836
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
 418-479 5.40e-16

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.


Pssm-ID: 214846 [Multi-domain]  Cd Length: 122  Bit Score: 74.15  E-value: 5.40e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199790  418 VCKFLVQLSMDFSSYYNRVHILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPLSHI 479
Cdd:smart00836  64 LANYLYDLAAAFHSFYNRVRVLGEENPEL---RKARLALLKAVRQVLANGLRLLGISAPERM 122
DALR_1 pfam05746
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
 362-479 1.21e-14

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteriztic conserved amino acids.


Pssm-ID: 399042 [Multi-domain]  Cd Length: 117  Bit Score: 69.99  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199790 362 ILSVATIKFEMLSTAPQ--SQGEWLLLFNSVLPFLDLLsQTVSLAGTPglhipvrtEMVCKFLVQLSMDFSSYYNRVHIL 439
Cdd:pfam05746  11 ILRKAGELGINLDIDADllTEEEEKELLKALLQFPEVL-EEAAEELEP--------HRLANYLYELASAFHSFYNNCRVL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907199790 440 GEPRPHLFgqmfARLQLLRAVREVFHTGLAMLGLPPLSHI 479
Cdd:pfam05746  82 DEDNEERN----ARLALLKAVRQVLKNGLDLLGIEAPEKM 117
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
 418-476 5.98e-09

Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 58.24  E-value: 5.98e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199790 418 VCKFLVQLSMDFSSYYNRVHILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPL 476
Cdd:COG0018   516 IANYLYELAKAFHSFYNACRILKAEDEEL---RAARLALVAATAQVLKNGLGLLGISAP 571
Anticodon_Ia_Arg cd07956
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ...
 418-476 1.46e-08

Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA synthetases (ArgRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ArgRS catalyzes the transfer of arginine to the 3'-end of its tRNA.


Pssm-ID: 153410 [Multi-domain]  Cd Length: 156  Bit Score: 53.76  E-value: 1.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199790 418 VCKFLVQLSMDFSSYYNRVHILGEPRphlfGQMFARLQLLRAVREVFHTGLAMLGLPPL 476
Cdd:cd07956    99 IATYLFDLAHAFSKFYNACPVLGAEE----ELRNARLALVAAARQVLANGLDLLGIEAP 153
argS PRK01611
arginyl-tRNA synthetase; Reviewed
 418-476 7.62e-07

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 51.31  E-value: 7.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199790 418 VCKFLVQLSMDFSSYYNRVhILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPL 476
Cdd:PRK01611  450 IANYLYELAGAFHSFYNRV-LLKDEEEEL---RNARLALVKATAQVLKNGLDLLGISAP 504
 
Name Accession Description Interval E-value
DALR_1 smart00836
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
 418-479 5.40e-16

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.


Pssm-ID: 214846 [Multi-domain]  Cd Length: 122  Bit Score: 74.15  E-value: 5.40e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907199790  418 VCKFLVQLSMDFSSYYNRVHILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPLSHI 479
Cdd:smart00836  64 LANYLYDLAAAFHSFYNRVRVLGEENPEL---RKARLALLKAVRQVLANGLRLLGISAPERM 122
DALR_1 pfam05746
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
 362-479 1.21e-14

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteriztic conserved amino acids.


Pssm-ID: 399042 [Multi-domain]  Cd Length: 117  Bit Score: 69.99  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199790 362 ILSVATIKFEMLSTAPQ--SQGEWLLLFNSVLPFLDLLsQTVSLAGTPglhipvrtEMVCKFLVQLSMDFSSYYNRVHIL 439
Cdd:pfam05746  11 ILRKAGELGINLDIDADllTEEEEKELLKALLQFPEVL-EEAAEELEP--------HRLANYLYELASAFHSFYNNCRVL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907199790 440 GEPRPHLFgqmfARLQLLRAVREVFHTGLAMLGLPPLSHI 479
Cdd:pfam05746  82 DEDNEERN----ARLALLKAVRQVLKNGLDLLGIEAPEKM 117
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
 418-476 5.98e-09

Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 58.24  E-value: 5.98e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199790 418 VCKFLVQLSMDFSSYYNRVHILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPL 476
Cdd:COG0018   516 IANYLYELAKAFHSFYNACRILKAEDEEL---RAARLALVAATAQVLKNGLGLLGISAP 571
Anticodon_Ia_Arg cd07956
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ...
 418-476 1.46e-08

Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA synthetases (ArgRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ArgRS catalyzes the transfer of arginine to the 3'-end of its tRNA.


Pssm-ID: 153410 [Multi-domain]  Cd Length: 156  Bit Score: 53.76  E-value: 1.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199790 418 VCKFLVQLSMDFSSYYNRVHILGEPRphlfGQMFARLQLLRAVREVFHTGLAMLGLPPL 476
Cdd:cd07956    99 IATYLFDLAHAFSKFYNACPVLGAEE----ELRNARLALVAAARQVLANGLDLLGIEAP 153
argS PRK01611
arginyl-tRNA synthetase; Reviewed
 418-476 7.62e-07

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 51.31  E-value: 7.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199790 418 VCKFLVQLSMDFSSYYNRVhILGEPRPHLfgqMFARLQLLRAVREVFHTGLAMLGLPPL 476
Cdd:PRK01611  450 IANYLYELAGAFHSFYNRV-LLKDEEEEL---RNARLALVKATAQVLKNGLDLLGISAP 504
 
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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