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Conserved domains on  [gi|21410537|gb|AAH31182|]
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Itpk1 protein, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CPSase_L_D2 super family cl17255
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
1-23 1.42e-05

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


The actual alignment was detected with superfamily member pfam05770:

Pssm-ID: 473076  Cd Length: 201  Bit Score: 42.45  E-value: 1.42e-05
                          10        20
                  ....*....|....*....|...
gi 21410537     1 VNAFPGYEGVSEFFTDLLNHIAT 23
Cdd:pfam05770 179 INYFPGYAKMPEYETVLTDFFWS 201
 
Name Accession Description Interval E-value
Ins134_P3_kin pfam05770
Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several ...
1-23 1.42e-05

Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several inositol 1, 3, 4-trisphosphate 5/6-kinase proteins. Inositol 1,3,4-trisphosphate is at a branch point in inositol phosphate metabolism. It is dephosphorylated by specific phosphatases to either inositol 3,4-bisphosphate or inositol 1,3-bisphosphate. Alternatively, it is phosphorylated to inositol 1,3,4,6-tetrakisphosphate or inositol 1,3,4,5-tetrakisphosphate by inositol trisphosphate 5/6-kinase. This entry represents the ATP-grasp domain.


Pssm-ID: 368606  Cd Length: 201  Bit Score: 42.45  E-value: 1.42e-05
                          10        20
                  ....*....|....*....|...
gi 21410537     1 VNAFPGYEGVSEFFTDLLNHIAT 23
Cdd:pfam05770 179 INYFPGYAKMPEYETVLTDFFWS 201
 
Name Accession Description Interval E-value
Ins134_P3_kin pfam05770
Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several ...
1-23 1.42e-05

Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several inositol 1, 3, 4-trisphosphate 5/6-kinase proteins. Inositol 1,3,4-trisphosphate is at a branch point in inositol phosphate metabolism. It is dephosphorylated by specific phosphatases to either inositol 3,4-bisphosphate or inositol 1,3-bisphosphate. Alternatively, it is phosphorylated to inositol 1,3,4,6-tetrakisphosphate or inositol 1,3,4,5-tetrakisphosphate by inositol trisphosphate 5/6-kinase. This entry represents the ATP-grasp domain.


Pssm-ID: 368606  Cd Length: 201  Bit Score: 42.45  E-value: 1.42e-05
                          10        20
                  ....*....|....*....|...
gi 21410537     1 VNAFPGYEGVSEFFTDLLNHIAT 23
Cdd:pfam05770 179 INYFPGYAKMPEYETVLTDFFWS 201
 
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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