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Conserved domains on  [gi|45445455|gb|AAF57496|]
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arginyltransferase 1, isoform A [Drosophila melanogaster]

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 ...
249-385 2.20e-60

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: 193.40  E-value: 2.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455   249 SFALYKKYQISIHNDPPKD--QDAYKEHLQATPlqnekpwdgpemgYGSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:pfam04377   2 KYALYRRYQRARHGDMPDDssEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFY 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45445455   327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLC 385
Cdd:pfam04377  69 DPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
14-85 1.19e-21

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: 88.38  E-value: 1.19e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45445455    14 SKCGYCAGANCSLSHGMHAYQLDCRDYQDLIDRGWRRCGYYCYKLRNQeTCCPCYTIKCNGLEFKLSKSNKR 85
Cdd:pfam04376   1 SPCGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDCR-TCCACYTIRLDVAEFKPSRSQRR 71
Rib_recp_KP_reg super family cl25527
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
98-182 4.39e-03

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


The actual alignment was detected with superfamily member pfam05104:

Pssm-ID: 461548 [Multi-domain]  Cd Length: 140  Bit Score: 37.41  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455    98 KRESKP-----EAGDG----DGEADADYAIVAPEVtASEPQPQLPDKSPPVINVEQVASLATA------QRKPTKQATAA 162
Cdd:pfam05104  41 KKEEKPngklpESEQAdeseEEPREFKTPDEAPSA-ALEPEPVPTPVPAPVEPEPAPPSESPApspkekKKKEKKSAKVE 119
                          90       100
                  ....*....|....*....|
gi 45445455   163 AVEAPTLGSNKSAAPISNKP 182
Cdd:pfam05104 120 PAETPEAVQPKPALEKEEPP 139
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
249-385 2.20e-60

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: 193.40  E-value: 2.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455   249 SFALYKKYQISIHNDPPKD--QDAYKEHLQATPlqnekpwdgpemgYGSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:pfam04377   2 KYALYRRYQRARHGDMPDDssEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFY 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45445455   327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLC 385
Cdd:pfam04377  69 DPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
250-396 1.65e-29

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 115.63  E-value: 1.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455 250 FALYKKYQISIHND---PPKDQDAYKEHLQATPLQnekpwdgpemgygSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:COG2935 109 YALYRRYLAARHADggmDPMSREQYAAFLEDSWVD-------------TRLVEFRLDGRLVAVALTDVLPDGLSAVYTFF 175
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455 327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLCPEtyEWLPLTD 396
Cdd:COG2935 176 DPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLERLIGG--GWQRLDP 238
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
250-396 6.62e-27

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 108.37  E-value: 6.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455  250 FALYKKYQISIHND---PPKDQDAYKEHLQATPLQnekpwdgpemgygSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:PRK01305 109 YALYRRYLRARHADggmDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDGKLVAVAVTDVLDDGLSAVYTFY 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455  327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLCPetYEWLPLTD 396
Cdd:PRK01305 176 DPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILID--GGWQRLEE 238
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
14-85 1.19e-21

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: 88.38  E-value: 1.19e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45445455    14 SKCGYCAGANCSLSHGMHAYQLDCRDYQDLIDRGWRRCGYYCYKLRNQeTCCPCYTIKCNGLEFKLSKSNKR 85
Cdd:pfam04376   1 SPCGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDCR-TCCACYTIRLDVAEFKPSRSQRR 71
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
98-182 4.39e-03

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 461548 [Multi-domain]  Cd Length: 140  Bit Score: 37.41  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455    98 KRESKP-----EAGDG----DGEADADYAIVAPEVtASEPQPQLPDKSPPVINVEQVASLATA------QRKPTKQATAA 162
Cdd:pfam05104  41 KKEEKPngklpESEQAdeseEEPREFKTPDEAPSA-ALEPEPVPTPVPAPVEPEPAPPSESPApspkekKKKEKKSAKVE 119
                          90       100
                  ....*....|....*....|
gi 45445455   163 AVEAPTLGSNKSAAPISNKP 182
Cdd:pfam05104 120 PAETPEAVQPKPALEKEEPP 139
 
Name Accession Description Interval E-value
ATE_C pfam04377
Arginine-tRNA-protein transferase, C terminus; This family represents the C terminal region of ...
249-385 2.20e-60

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: 193.40  E-value: 2.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455   249 SFALYKKYQISIHNDPPKD--QDAYKEHLQATPlqnekpwdgpemgYGSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:pfam04377   2 KYALYRRYQRARHGDMPDDssEQGYKRFLCDSP-------------VGTYHQEYRLDGKLIAVGVIDILPDGLSSVYFFY 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45445455   327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLC 385
Cdd:pfam04377  69 DPDYAKRSLGTYSILREIELAREL-----GLPYYYLGYYIHDCPKMRYKARFRPLELLC 122
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
250-396 1.65e-29

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 115.63  E-value: 1.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455 250 FALYKKYQISIHND---PPKDQDAYKEHLQATPLQnekpwdgpemgygSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:COG2935 109 YALYRRYLAARHADggmDPMSREQYAAFLEDSWVD-------------TRLVEFRLDGRLVAVALTDVLPDGLSAVYTFF 175
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455 327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLCPEtyEWLPLTD 396
Cdd:COG2935 176 DPDLARRSLGTYAILWQIELARRL-----GLPYLYLGYWIEGSRKMAYKARFRPLERLIGG--GWQRLDP 238
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
250-396 6.62e-27

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 108.37  E-value: 6.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455  250 FALYKKYQISIHND---PPKDQDAYKEHLQATPLQnekpwdgpemgygSFHQQYWLDDKLIAVGVIDILPGCVSSVYFFY 326
Cdd:PRK01305 109 YALYRRYLRARHADggmDPPSRDQYAQFLEDSWVN-------------TRFIEFRGDGKLVAVAVTDVLDDGLSAVYTFY 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455  327 DPDYSFLSLGTYGSLREIELVQSLaekvpSLKYYYMGFYIHSCPKMRYKGKLSPSYLLCPetYEWLPLTD 396
Cdd:PRK01305 176 DPDEEHRSLGTFAILWQIELAKRL-----GLPYVYLGYWIKGSRKMNYKARFRPLEILID--GGWQRLEE 238
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
14-85 1.19e-21

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: 88.38  E-value: 1.19e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45445455    14 SKCGYCAGANCSLSHGMHAYQLDCRDYQDLIDRGWRRCGYYCYKLRNQeTCCPCYTIKCNGLEFKLSKSNKR 85
Cdd:pfam04376   1 SPCGYCPGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDCR-TCCACYTIRLDVAEFKPSRSQRR 71
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
98-182 4.39e-03

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 461548 [Multi-domain]  Cd Length: 140  Bit Score: 37.41  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45445455    98 KRESKP-----EAGDG----DGEADADYAIVAPEVtASEPQPQLPDKSPPVINVEQVASLATA------QRKPTKQATAA 162
Cdd:pfam05104  41 KKEEKPngklpESEQAdeseEEPREFKTPDEAPSA-ALEPEPVPTPVPAPVEPEPAPPSESPApspkekKKKEKKSAKVE 119
                          90       100
                  ....*....|....*....|
gi 45445455   163 AVEAPTLGSNKSAAPISNKP 182
Cdd:pfam05104 120 PAETPEAVQPKPALEKEEPP 139
 
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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