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Conserved domains on  [gi|79455290|ref|NP_191700|]
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U-box kinase family protein [Arabidopsis thaliana]

Protein Classification

argininosuccinate synthase; FAD synthase( domain architecture ID 10113151)

argininosuccinate synthase reversibly catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate| FAD (Flavin adenine dinucleotide) synthase catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 13-166 7.62e-62

N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model represents the N-terminal domain found in some plant serine threonine kinases (STK, EC 2.7.11.-) and U-box domain-containing proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. These enzymes belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. U-box domain-containing proteins function as E3 ubiquitin ligases (EC 2.3.2.27), mediating the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin. The N-terminal domain of these proteins is homologous to the universal stress protein (USP) family which has an ATP binding fold. The N-terminal domain is predicted to be involved in ATP binding.


:

Pssm-ID: 467493  Cd Length: 154  Bit Score: 192.89  E-value: 7.62e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79455290  13 RIYVALGREIANNKSNLAWVLDNCQ--GNKICIVLVHRPPQMIPVLGTKFDAATVDEELVRAYREKQKAKTDKILDEYLR 90
Cdd:cd01989   1 KVAVAVDGDDKKSKSALKWALDNLAprGAKIVLVHVHPPVTMIPTPSGKVPPIQLREEEVSAYRKQEREKTEKMLLPYLD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79455290  91 ICLRKGVQAEKLCVEMNSIEKGIVQMISENKVRKFIMGAASDKHFStkMEDLRSKKAIFVCQQASATCHIRFTCKG 166
Cdd:cd01989  81 MCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFS--MKLKKSDVASSVMKAAPDFCTVWVVCKG 154
 
Name Accession Description Interval E-value
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 13-166 7.62e-62

N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model represents the N-terminal domain found in some plant serine threonine kinases (STK, EC 2.7.11.-) and U-box domain-containing proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. These enzymes belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. U-box domain-containing proteins function as E3 ubiquitin ligases (EC 2.3.2.27), mediating the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin. The N-terminal domain of these proteins is homologous to the universal stress protein (USP) family which has an ATP binding fold. The N-terminal domain is predicted to be involved in ATP binding.


Pssm-ID: 467493  Cd Length: 154  Bit Score: 192.89  E-value: 7.62e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79455290  13 RIYVALGREIANNKSNLAWVLDNCQ--GNKICIVLVHRPPQMIPVLGTKFDAATVDEELVRAYREKQKAKTDKILDEYLR 90
Cdd:cd01989   1 KVAVAVDGDDKKSKSALKWALDNLAprGAKIVLVHVHPPVTMIPTPSGKVPPIQLREEEVSAYRKQEREKTEKMLLPYLD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79455290  91 ICLRKGVQAEKLCVEMNSIEKGIVQMISENKVRKFIMGAASDKHFStkMEDLRSKKAIFVCQQASATCHIRFTCKG 166
Cdd:cd01989  81 MCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFS--MKLKKSDVASSVMKAAPDFCTVWVVCKG 154
 
Name Accession Description Interval E-value
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 13-166 7.62e-62

N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model represents the N-terminal domain found in some plant serine threonine kinases (STK, EC 2.7.11.-) and U-box domain-containing proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. These enzymes belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. U-box domain-containing proteins function as E3 ubiquitin ligases (EC 2.3.2.27), mediating the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin. The N-terminal domain of these proteins is homologous to the universal stress protein (USP) family which has an ATP binding fold. The N-terminal domain is predicted to be involved in ATP binding.


Pssm-ID: 467493  Cd Length: 154  Bit Score: 192.89  E-value: 7.62e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79455290  13 RIYVALGREIANNKSNLAWVLDNCQ--GNKICIVLVHRPPQMIPVLGTKFDAATVDEELVRAYREKQKAKTDKILDEYLR 90
Cdd:cd01989   1 KVAVAVDGDDKKSKSALKWALDNLAprGAKIVLVHVHPPVTMIPTPSGKVPPIQLREEEVSAYRKQEREKTEKMLLPYLD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79455290  91 ICLRKGVQAEKLCVEMNSIEKGIVQMISENKVRKFIMGAASDKHFStkMEDLRSKKAIFVCQQASATCHIRFTCKG 166
Cdd:cd01989  81 MCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFS--MKLKKSDVASSVMKAAPDFCTVWVVCKG 154
 
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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