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Conserved domains on  [gi|2462516674|ref|XP_054220610|]
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arginyl-tRNA--protein transferase 1 isoform X5 [Homo sapiens]

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 ...
 337-461 1.96e-58

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: 190.32  E-value: 1.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 337 LYVKYQVAIHQDPPDECGKTE-----AETPpngpdcgYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLYYDPDYSFLSL 411
Cdd:pfam04377   5 LYRRYQRARHGDMPDDSSEQGykrflCDSP-------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFYDPDYAKRSL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462516674 412 GVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLC 461
Cdd:pfam04377  78 GTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 21-92 9.70e-31

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: 114.19  E-value: 9.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462516674  21 YRCGYCKNESGSRSNGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMnQTCCPQYTIRCRPLQFQPSKSHKK 92
Cdd:pfam04376   1 SPCGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-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 ...
 337-461 1.96e-58

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: 190.32  E-value: 1.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 337 LYVKYQVAIHQDPPDECGKTE-----AETPpngpdcgYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLYYDPDYSFLSL 411
Cdd:pfam04377   5 LYRRYQRARHGDMPDDSSEQGykrflCDSP-------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFYDPDYAKRSL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462516674 412 GVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLC 461
Cdd:pfam04377  78 GTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 21-92 9.70e-31

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: 114.19  E-value: 9.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462516674  21 YRCGYCKNESGSRSNGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMnQTCCPQYTIRCRPLQFQPSKSHKK 92
Cdd:pfam04376   1 SPCGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 376-471 3.91e-28

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 112.55  E-value: 3.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 376 YWLDGKIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYR 455
Cdd:COG2935   149 FRLDGRLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFR 223

                          90
                  ....*....|....*.
gi 2462516674 456 PSDLLCPEtyVWVPIE 471
Cdd:COG2935   224 PLERLIGG--GWQRLD 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 337-471 7.27e-27

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 108.76  E-value: 7.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 337 LYVKYQVAIHQDPPdecgkteaETPPNGPDcgYGSFHQQ---------YWLDGKIIAVGVIDILPNCVSSVYLYYDPDYS 407
Cdd:PRK01305  111 LYRRYLRARHADGG--------MDPPSRDQ--YAQFLEDswvntrfieFRGDGKLVAVAVTDVLDDGLSAVYTFYDPDEE 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462516674 408 FLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLCPetYVWVPIE 471
Cdd:PRK01305  181 HRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILID--GGWQRLE 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 39-96 1.63e-10

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 61.38  E-value: 1.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516674  39 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQytirCR---PL-----QFQPSKSHKKVLKK 96
Cdd:PRK01305   35 SHPIAAELYDELLQAGFRRSGNIAYRPH-----CDG----CRacvSVripvaEFVPSRSQRRVLKR 91
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 39-96 1.14e-09

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 59.01  E-value: 1.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462516674  39 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQYT----IRCRPLQFQPSKSHKKVLKK 96
Cdd:COG2935    35 SGPLAAELYDALLRAGFRRSGNILYRPH-----CPGCRacvsVRIPVADFRPSRSQRRVLKR 91
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
 337-461 1.96e-58

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: 190.32  E-value: 1.96e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 337 LYVKYQVAIHQDPPDECGKTE-----AETPpngpdcgYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLYYDPDYSFLSL 411
Cdd:pfam04377   5 LYRRYQRARHGDMPDDSSEQGykrflCDSP-------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFYDPDYAKRSL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462516674 412 GVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLC 461
Cdd:pfam04377  78 GTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 21-92 9.70e-31

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: 114.19  E-value: 9.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462516674  21 YRCGYCKNESGSRSNGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMnQTCCPQYTIRCRPLQFQPSKSHKK 92
Cdd:pfam04376   1 SPCGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 376-471 3.91e-28

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 112.55  E-value: 3.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 376 YWLDGKIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYR 455
Cdd:COG2935   149 FRLDGRLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFR 223

                          90
                  ....*....|....*.
gi 2462516674 456 PSDLLCPEtyVWVPIE 471
Cdd:COG2935   224 PLERLIGG--GWQRLD 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 337-471 7.27e-27

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 108.76  E-value: 7.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462516674 337 LYVKYQVAIHQDPPdecgkteaETPPNGPDcgYGSFHQQ---------YWLDGKIIAVGVIDILPNCVSSVYLYYDPDYS 407
Cdd:PRK01305  111 LYRRYLRARHADGG--------MDPPSRDQ--YAQFLEDswvntrfieFRGDGKLVAVAVTDVLDDGLSAVYTFYDPDEE 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462516674 408 FLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMKYKGQYRPSDLLCPetYVWVPIE 471
Cdd:PRK01305  181 HRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILID--GGWQRLE 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 39-96 1.63e-10

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 61.38  E-value: 1.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516674  39 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQytirCR---PL-----QFQPSKSHKKVLKK 96
Cdd:PRK01305   35 SHPIAAELYDELLQAGFRRSGNIAYRPH-----CDG----CRacvSVripvaEFVPSRSQRRVLKR 91
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 39-96 1.14e-09

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 59.01  E-value: 1.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462516674  39 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQYT----IRCRPLQFQPSKSHKKVLKK 96
Cdd:COG2935    35 SGPLAAELYDALLRAGFRRSGNILYRPH-----CPGCRacvsVRIPVADFRPSRSQRRVLKR 91
 
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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