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Conserved domains on  [gi|570359588|ref|NP_001275663|]
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arginyl-tRNA--protein transferase 1 isoform 3 [Homo sapiens]

Protein Classification

arginyl-tRNA--protein transferase( domain architecture ID 10516218)

arginyl-tRNA--protein transferase such as arginyl-tRNA--protein transferase 1, which 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 ...
175-314 4.58e-69

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: 213.82  E-value: 4.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588  175 ESYQVYKRYQMVIHKNPPDTPTESQFTRFLCSSPleaetppngpdcgYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLY 254
Cdd:pfam04377   1 EKYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFF 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588  255 YDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLC 314
Cdd:pfam04377  68 YDPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
175-314 4.58e-69

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: 213.82  E-value: 4.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588  175 ESYQVYKRYQMVIHKNPPDTPTESQFTRFLCSSPleaetppngpdcgYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLY 254
Cdd:pfam04377   1 EKYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFF 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588  255 YDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLC 314
Cdd:pfam04377  68 YDPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
155-324 4.01e-33

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 124.11  E-value: 4.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 155 LEVRVVRSSPPSSQfkatllesYQVYKRYQMVIHKNPP-DTPTESQFTRFLCSSPLEaetppngpdcgygSFHQQYWLDG 233
Cdd:COG2935   95 LTVRVLPPEFTEEH--------YALYRRYLAARHADGGmDPMSREQYAAFLEDSWVD-------------TRLVEFRLDG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 234 KIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLL 313
Cdd:COG2935  154 RLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLERL 228
                        170
                 ....*....|.
gi 570359588 314 CPEtyVWVPIE 324
Cdd:COG2935  229 IGG--GWQRLD 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
155-324 5.20e-32

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 121.08  E-value: 5.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 155 LEVRVVRSSPPSSQfkatllesYQVYKRYQMVIHKN-PPDTPTESQFTRFLCSSPLEaetppngpdcgygSFHQQYWLDG 233
Cdd:PRK01305  95 LVVRVLPPEFTEEH--------YALYRRYLRARHADgGMDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 234 KIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLL 313
Cdd:PRK01305 154 KLVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEIL 228
                        170
                 ....*....|.
gi 570359588 314 CPetYVWVPIE 324
Cdd:PRK01305 229 ID--GGWQRLE 237
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
175-314 4.58e-69

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: 213.82  E-value: 4.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588  175 ESYQVYKRYQMVIHKNPPDTPTESQFTRFLCSSPleaetppngpdcgYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLY 254
Cdd:pfam04377   1 EKYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFF 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588  255 YDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLC 314
Cdd:pfam04377  68 YDPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
155-324 4.01e-33

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 124.11  E-value: 4.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 155 LEVRVVRSSPPSSQfkatllesYQVYKRYQMVIHKNPP-DTPTESQFTRFLCSSPLEaetppngpdcgygSFHQQYWLDG 233
Cdd:COG2935   95 LTVRVLPPEFTEEH--------YALYRRYLAARHADGGmDPMSREQYAAFLEDSWVD-------------TRLVEFRLDG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 234 KIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLL 313
Cdd:COG2935  154 RLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLERL 228
                        170
                 ....*....|.
gi 570359588 314 CPEtyVWVPIE 324
Cdd:COG2935  229 IGG--GWQRLD 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
155-324 5.20e-32

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 121.08  E-value: 5.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 155 LEVRVVRSSPPSSQfkatllesYQVYKRYQMVIHKN-PPDTPTESQFTRFLCSSPLEaetppngpdcgygSFHQQYWLDG 233
Cdd:PRK01305  95 LVVRVLPPEFTEEH--------YALYRRYLRARHADgGMDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570359588 234 KIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLL 313
Cdd:PRK01305 154 KLVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEIL 228
                        170
                 ....*....|.
gi 570359588 314 CPetYVWVPIE 324
Cdd:PRK01305 229 ID--GGWQRLE 237
 
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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