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Conserved domains on  [gi|1907176858|ref|XP_036008503|]
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arginyl-tRNA--protein transferase 1 isoform X5 [Mus musculus]

Protein Classification

arginyl-tRNA--protein transferase( domain architecture ID 10516211)

arginyl-tRNA--protein transferase (arginyltransferase) is involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
 288-418 1.78e-61

Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyzes the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a destabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified.


:

Pssm-ID: 461282  Cd Length: 122  Bit Score: 194.94  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 288 ESYQVYKRYQMVVHKDPPDKPTVSQFTRFLCSSPleaehpadgpecgYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLY 367
Cdd:pfam04377   1 EKYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFF 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907176858 368 YDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:pfam04377  68 YDPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKA 113
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 23-92 1.69e-30

Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyzes the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a de-stabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified. In S cerevisiae, Cys20, 23, 94 and/or 95 are thought to be important for activity. Of these, only Cys 94 appears to be completely conserved in this family.


:

Pssm-ID: 461281 [Multi-domain]  Cd Length: 71  Bit Score: 112.27  E-value: 1.69e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858  23 CGYCKNKLGSRSYGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMdQTCCPQYTIRCHPLQFQPSKSHKK 92
Cdd:pfam04376   3 CGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
 288-418 1.78e-61

Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyzes the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a destabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified.


Pssm-ID: 461282  Cd Length: 122  Bit Score: 194.94  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 288 ESYQVYKRYQMVVHKDPPDKPTVSQFTRFLCSSPleaehpadgpecgYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLY 367
Cdd:pfam04377   1 EKYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFF 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907176858 368 YDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:pfam04377  68 YDPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKA 113
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 23-92 1.69e-30

Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyzes the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a de-stabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified. In S cerevisiae, Cys20, 23, 94 and/or 95 are thought to be important for activity. Of these, only Cys 94 appears to be completely conserved in this family.


Pssm-ID: 461281 [Multi-domain]  Cd Length: 71  Bit Score: 112.27  E-value: 1.69e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858  23 CGYCKNKLGSRSYGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMdQTCCPQYTIRCHPLQFQPSKSHKK 92
Cdd:pfam04376   3 CGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 268-418 1.70e-27

Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 109.47  E-value: 1.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 268 LEVRVVrssppSPQFRatfQESYQVYKRYQMVVHKDPP-DKPTVSQFTRFLCSSPLEaehpadgpecgygSFHQQYWLDG 346
Cdd:COG2935    95 LTVRVL-----PPEFT---EEHYALYRRYLAARHADGGmDPMSREQYAAFLEDSWVD-------------TRLVEFRLDG 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907176858 347 KIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:COG2935   154 RLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKA 220
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 268-418 1.85e-26

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 106.45  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 268 LEVRVVrssppSPQFRatfQESYQVYKRYQMVVHKD-PPDKPTVSQFTRFLCSSPLEaehpadgpecgygSFHQQYWLDG 346
Cdd:PRK01305   95 LVVRVL-----PPEFT---EEHYALYRRYLRARHADgGMDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDG 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907176858 347 KIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:PRK01305  154 KLVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKA 220
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
 288-418 1.78e-61

Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyzes the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a destabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified.


Pssm-ID: 461282  Cd Length: 122  Bit Score: 194.94  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 288 ESYQVYKRYQMVVHKDPPDKPTVSQFTRFLCSSPleaehpadgpecgYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLY 367
Cdd:pfam04377   1 EKYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFF 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907176858 368 YDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:pfam04377  68 YDPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKA 113
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 23-92 1.69e-30

Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyzes the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a de-stabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified. In S cerevisiae, Cys20, 23, 94 and/or 95 are thought to be important for activity. Of these, only Cys 94 appears to be completely conserved in this family.


Pssm-ID: 461281 [Multi-domain]  Cd Length: 71  Bit Score: 112.27  E-value: 1.69e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858  23 CGYCKNKLGSRSYGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMdQTCCPQYTIRCHPLQFQPSKSHKK 92
Cdd:pfam04376   3 CGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 268-418 1.70e-27

Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 109.47  E-value: 1.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 268 LEVRVVrssppSPQFRatfQESYQVYKRYQMVVHKDPP-DKPTVSQFTRFLCSSPLEaehpadgpecgygSFHQQYWLDG 346
Cdd:COG2935    95 LTVRVL-----PPEFT---EEHYALYRRYLAARHADGGmDPMSREQYAAFLEDSWVD-------------TRLVEFRLDG 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907176858 347 KIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:COG2935   154 RLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKA 220
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 268-418 1.85e-26

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 106.45  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907176858 268 LEVRVVrssppSPQFRatfQESYQVYKRYQMVVHKD-PPDKPTVSQFTRFLCSSPLEaehpadgpecgygSFHQQYWLDG 346
Cdd:PRK01305   95 LVVRVL-----PPEFT---EEHYALYRRYLRARHADgGMDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDG 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907176858 347 KIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKR 418
Cdd:PRK01305  154 KLVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKA 220
 
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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