NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2210364500|ref|NP_001389571|]
View 

arginyl-tRNA--protein transferase 1 isoform 6 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
325-463 3.30e-62

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: 199.95  E-value: 3.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 325 SFSLYTKYQVAIHQEAPEICEKSEFTRFLCSSPleaehpadgpecgYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLYY 404
Cdd:pfam04377   2 KYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFY 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2210364500 405 DPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDLLC 463
Cdd:pfam04377  69 DPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
16-85 5.01e-29

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: 109.57  E-value: 5.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500  16 CGYCESREGKTSCGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMdQTCCPQYTIRCHPLQFQPSKSHKK 85
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 ...
325-463 3.30e-62

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: 199.95  E-value: 3.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 325 SFSLYTKYQVAIHQEAPEICEKSEFTRFLCSSPleaehpadgpecgYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLYY 404
Cdd:pfam04377   2 KYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFY 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2210364500 405 DPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDLLC 463
Cdd:pfam04377  69 DPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
16-85 5.01e-29

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: 109.57  E-value: 5.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500  16 CGYCESREGKTSCGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMdQTCCPQYTIRCHPLQFQPSKSHKK 85
Cdd:pfam04376   3 CGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
305-473 2.47e-28

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 112.94  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 305 QVRLVPASFeDPEFnssfnqsFSLYTKYQVAIHQE---APEicEKSEFTRFLCSSPLEaehpadgpecgygSFHQQYWLD 381
Cdd:COG2935    96 TVRVLPPEF-TEEH-------YALYRRYLAARHADggmDPM--SREQYAAFLEDSWVD-------------TRLVEFRLD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 382 GKIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDL 461
Cdd:COG2935   153 GRLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLER 227
                         170
                  ....*....|..
gi 2210364500 462 LCPEtyVWVPIE 473
Cdd:COG2935   228 LIGG--GWQRLD 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
305-475 7.80e-28

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 111.84  E-value: 7.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 305 QVRLVPASFEDpefnssfnQSFSLYTKYQVAIHQEAP-EICEKSEFTRFLCSSPLEaehpadgpecgygSFHQQYWLDGK 383
Cdd:PRK01305   96 VVRVLPPEFTE--------EHYALYRRYLRARHADGGmDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDGK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 384 IIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDLLC 463
Cdd:PRK01305  155 LVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILI 229
                         170
                  ....*....|..
gi 2210364500 464 PetYVWVPIEQC 475
Cdd:PRK01305  230 D--GGWQRLEEP 239
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
325-463 3.30e-62

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: 199.95  E-value: 3.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 325 SFSLYTKYQVAIHQEAPEICEKSEFTRFLCSSPleaehpadgpecgYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLYY 404
Cdd:pfam04377   2 KYALYRRYQRARHGDMPDDSSEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFY 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2210364500 405 DPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDLLC 463
Cdd:pfam04377  69 DPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
16-85 5.01e-29

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: 109.57  E-value: 5.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500  16 CGYCESREGKTSCGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMdQTCCPQYTIRCHPLQFQPSKSHKK 85
Cdd:pfam04376   3 CGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
305-473 2.47e-28

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 112.94  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 305 QVRLVPASFeDPEFnssfnqsFSLYTKYQVAIHQE---APEicEKSEFTRFLCSSPLEaehpadgpecgygSFHQQYWLD 381
Cdd:COG2935    96 TVRVLPPEF-TEEH-------YALYRRYLAARHADggmDPM--SREQYAAFLEDSWVD-------------TRLVEFRLD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 382 GKIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDL 461
Cdd:COG2935   153 GRLVAVALTDVLPDGLSAVYTFFDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLER 227
                         170
                  ....*....|..
gi 2210364500 462 LCPEtyVWVPIE 473
Cdd:COG2935   228 LIGG--GWQRLD 237
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
305-475 7.80e-28

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 111.84  E-value: 7.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 305 QVRLVPASFEDpefnssfnQSFSLYTKYQVAIHQEAP-EICEKSEFTRFLCSSPLEaehpadgpecgygSFHQQYWLDGK 383
Cdd:PRK01305   96 VVRVLPPEFTE--------EHYALYRRYLRARHADGGmDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDGK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2210364500 384 IIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLhektsQLSYYYMGFYIHSCPKMRYKGQYRPSDLLC 463
Cdd:PRK01305  155 LVAVAVTDVLDDGLSAVYTFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILI 229
                         170
                  ....*....|..
gi 2210364500 464 PetYVWVPIEQC 475
Cdd:PRK01305  230 D--GGWQRLEEP 239
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH