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Conserved domains on  [gi|1143463356|ref|NP_001335528|]
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Arginyl-tRNA--protein transferase 1 [Caenorhabditis elegans]

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 ...
179-313 6.51e-63

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: 198.03  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 179 ESFELYKNYQHTIHKD--EDCRLAGFRRFLCDSPLkkeqrggielGSFHLWFLLDDKLIAVCVVDILPKCFSAKYMYYNP 256
Cdd:pfam04377   1 EKYALYRRYQRARHGDmpDDSSEQGYKRFLCDSPV----------GTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFYDP 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1143463356 257 EYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLC 313
Cdd:pfam04377  71 DYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
5-45 5.73e-15

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: 69.12  E-value: 5.73e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1143463356   5 EAGWSTSGRYLYKPDNRvTCCPQYTIRLDVTKFKMSRSQKR 45
Cdd:pfam04376  32 DRGFRRSGNYLYRPDCR-TCCACYTIRLDVAEFKPSRSQRR 71
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
179-313 6.51e-63

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: 198.03  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 179 ESFELYKNYQHTIHKD--EDCRLAGFRRFLCDSPLkkeqrggielGSFHLWFLLDDKLIAVCVVDILPKCFSAKYMYYNP 256
Cdd:pfam04377   1 EKYALYRRYQRARHGDmpDDSSEQGYKRFLCDSPV----------GTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFYDP 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1143463356 257 EYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLC 313
Cdd:pfam04377  71 DYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
177-322 2.59e-33

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 124.88  E-value: 2.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 177 DNESFELYKNYQHTIHKDEDCRLAG---FRRFLCDSPLKkeqrggielgSFHLWFLLDDKLIAVCVVDILPKCFSAKYMY 253
Cdd:COG2935   105 TEEHYALYRRYLAARHADGGMDPMSreqYAAFLEDSWVD----------TRLVEFRLDGRLVAVALTDVLPDGLSAVYTF 174
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463356 254 YNPEYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLCDQsfRWVDF 322
Cdd:COG2935   175 FDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLERLIGG--GWQRL 236
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
175-325 2.60e-31

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 119.54  E-value: 2.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 175 TRDNESFELYKNYQHTIHKDEDCRLAG---FRRFLCDSPLKkeqrggielgSFHLWFLLDDKLIAVCVVDILPKCFSAKY 251
Cdd:PRK01305  103 EFTEEHYALYRRYLRARHADGGMDPPSrdqYAQFLEDSWVN----------TRFIEFRGDGKLVAVAVTDVLDDGLSAVY 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143463356 252 MYYNPEYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLCDQsfRWVDFNSC 325
Cdd:PRK01305  173 TFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILIDG--GWQRLEEP 239
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
5-45 5.73e-15

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: 69.12  E-value: 5.73e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1143463356   5 EAGWSTSGRYLYKPDNRvTCCPQYTIRLDVTKFKMSRSQKR 45
Cdd:pfam04376  32 DRGFRRSGNYLYRPDCR-TCCACYTIRLDVAEFKPSRSQRR 71
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
179-313 6.51e-63

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: 198.03  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 179 ESFELYKNYQHTIHKD--EDCRLAGFRRFLCDSPLkkeqrggielGSFHLWFLLDDKLIAVCVVDILPKCFSAKYMYYNP 256
Cdd:pfam04377   1 EKYALYRRYQRARHGDmpDDSSEQGYKRFLCDSPV----------GTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFYDP 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1143463356 257 EYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLC 313
Cdd:pfam04377  71 DYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
177-322 2.59e-33

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 124.88  E-value: 2.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 177 DNESFELYKNYQHTIHKDEDCRLAG---FRRFLCDSPLKkeqrggielgSFHLWFLLDDKLIAVCVVDILPKCFSAKYMY 253
Cdd:COG2935   105 TEEHYALYRRYLAARHADGGMDPMSreqYAAFLEDSWVD----------TRLVEFRLDGRLVAVALTDVLPDGLSAVYTF 174
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463356 254 YNPEYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLCDQsfRWVDF 322
Cdd:COG2935   175 FDPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLERLIGG--GWQRL 236
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
175-325 2.60e-31

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 119.54  E-value: 2.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463356 175 TRDNESFELYKNYQHTIHKDEDCRLAG---FRRFLCDSPLKkeqrggielgSFHLWFLLDDKLIAVCVVDILPKCFSAKY 251
Cdd:PRK01305  103 EFTEEHYALYRRYLRARHADGGMDPPSrdqYAQFLEDSWVN----------TRFIEFRGDGKLVAVAVTDVLDDGLSAVY 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143463356 252 MYYNPEYSFLSLGTYTALREIEQTQRLhaiysNLKYYYMGYYIHSCPKMRYKAKFRPSDLLCDQsfRWVDFNSC 325
Cdd:PRK01305  173 TFYDPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILIDG--GWQRLEEP 239
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
5-45 5.73e-15

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: 69.12  E-value: 5.73e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1143463356   5 EAGWSTSGRYLYKPDNRvTCCPQYTIRLDVTKFKMSRSQKR 45
Cdd:pfam04376  32 DRGFRRSGNYLYRPDCR-TCCACYTIRLDVAEFKPSRSQRR 71
 
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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