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Conserved domains on  [gi|2462516708|ref|XP_054220627|]
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arginyl-tRNA--protein transferase 1 isoform X25 [Homo sapiens]

Protein Classification

ATE_N domain-containing protein( domain architecture ID 10516187)

ATE_N domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 44-109 6.94e-28

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: 103.79  E-value: 6.94e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516708  44 PGSTPNSDSGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMnQTCCPQYTIRCRPLQFQPSKSHKK 109
Cdd:pfam04376   7 PGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
 
Name Accession Description Interval E-value
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 44-109 6.94e-28

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: 103.79  E-value: 6.94e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516708  44 PGSTPNSDSGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMnQTCCPQYTIRCRPLQFQPSKSHKK 109
Cdd:pfam04376   7 PGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 56-113 1.19e-11

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 63.69  E-value: 1.19e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516708  56 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQytirCR---PL-----QFQPSKSHKKVLKK 113
Cdd:PRK01305   35 SHPIAAELYDELLQAGFRRSGNIAYRPH-----CDG----CRacvSVripvaEFVPSRSQRRVLKR 91
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 56-113 1.36e-10

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 60.55  E-value: 1.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462516708  56 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQYTiRCRPL-----QFQPSKSHKKVLKK 113
Cdd:COG2935    35 SGPLAAELYDALLRAGFRRSGNILYRPH-----CPGCR-ACVSVripvaDFRPSRSQRRVLKR 91
 
Name Accession Description Interval E-value
ATE_N pfam04376
Arginine-tRNA-protein transferase, N terminus; This family represents the N terminal region of ...
 44-109 6.94e-28

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: 103.79  E-value: 6.94e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516708  44 PGSTPNSDSGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMnQTCCPQYTIRCRPLQFQPSKSHKK 109
Cdd:pfam04376   7 PGRKARKLFADPSGLISPELYQELLDRGFRRSGNYLYRPDC-RTCCACYTIRLDVAEFKPSRSQRR 71
PRK01305 PRK01305
arginyl-tRNA-protein transferase; Provisional
 56-113 1.19e-11

arginyl-tRNA-protein transferase; Provisional


Pssm-ID: 234939 [Multi-domain]  Cd Length: 240  Bit Score: 63.69  E-value: 1.19e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462516708  56 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQytirCR---PL-----QFQPSKSHKKVLKK 113
Cdd:PRK01305   35 SHPIAAELYDELLQAGFRRSGNIAYRPH-----CDG----CRacvSVripvaEFVPSRSQRRVLKR 91
Ate1 COG2935
Arginyl-tRNA--protein-N-Asp/Glu arginylyltransferase [Posttranslational modification, protein ...
 56-113 1.36e-10

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


Pssm-ID: 442178 [Multi-domain]  Cd Length: 240  Bit Score: 60.55  E-value: 1.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462516708  56 AHSMTVQDYQDLIDRGWRRSGKYVYKPVmnqtcCPQYTiRCRPL-----QFQPSKSHKKVLKK 113
Cdd:COG2935    35 SGPLAAELYDALLRAGFRRSGNILYRPH-----CPGCR-ACVSVripvaDFRPSRSQRRVLKR 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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