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Conserved domains on  [gi|19484200|gb|AAH25917|]
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Itpk1 protein, partial [Mus musculus]

Protein Classification

ATP-grasp domain-containing protein( domain architecture ID 106900)

ATP-grasp domain-containing protein may be related to carbamoyl phosphate synthetase and predicted to be involved in the biosynthesis of a ribonucleoside involved in stress response

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 ...
 1-95 5.19e-47

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: 153.00  E-value: 5.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484200     1 DRESIFFNSHNVSKPESSSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQT-GQHAVIDVNAFPGY 79
Cdd:pfam05770 106 DRSSGSFRFSQVSNLTASADDAELDKILEIAEMPPDPFLEDLARALRRALGLRLFNFDIIRDAGTaDRYLVIDINYFPGY 185

                          90
                  ....*....|....*.
gi 19484200    80 EGVSEFFTDLLNHIAT 95
Cdd:pfam05770 186 AKMPEYETVLTDFFWS 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 ...
 1-95 5.19e-47

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: 153.00  E-value: 5.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484200     1 DRESIFFNSHNVSKPESSSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQT-GQHAVIDVNAFPGY 79
Cdd:pfam05770 106 DRSSGSFRFSQVSNLTASADDAELDKILEIAEMPPDPFLEDLARALRRALGLRLFNFDIIRDAGTaDRYLVIDINYFPGY 185

                          90
                  ....*....|....*.
gi 19484200    80 EGVSEFFTDLLNHIAT 95
Cdd:pfam05770 186 AKMPEYETVLTDFFWS 201
PLN02941 PLN02941
inositol-tetrakisphosphate 1-kinase
 11-90 2.88e-10

inositol-tetrakisphosphate 1-kinase


Pssm-ID: 215508 [Multi-domain]  Cd Length: 328  Bit Score: 58.04  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484200   11 NVSKPESSSVLTELDKIEG-VFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQH-AVIDVNAFPGYEGVSEF--- 85
Cdd:PLN02941 236 RVSNAAASADDADNGGLDPeVAELPPRPFLEDLARELRRRLGLRLFNFDMIREHGTGDRyYVIDINYFPGYAKMPGYetv 315


                 ....*
gi 19484200   86 FTDLL 90
Cdd:PLN02941 316 LTDFL 320
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 34-82 1.56e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 44.16  E-value: 1.56e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19484200  34 PSDEViRELSRALRQALGVSLFGIDIIINNqtGQHAVIDVNAFPGYEGV 82
Cdd:COG0189 222 LTDEE-RELALRAAPALGLDFAGVDLIEDD--DGPLVLEVNVTPGFRGL 267
 
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 ...
 1-95 5.19e-47

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: 153.00  E-value: 5.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484200     1 DRESIFFNSHNVSKPESSSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQT-GQHAVIDVNAFPGY 79
Cdd:pfam05770 106 DRSSGSFRFSQVSNLTASADDAELDKILEIAEMPPDPFLEDLARALRRALGLRLFNFDIIRDAGTaDRYLVIDINYFPGY 185

                          90
                  ....*....|....*.
gi 19484200    80 EGVSEFFTDLLNHIAT 95
Cdd:pfam05770 186 AKMPEYETVLTDFFWS 201
PLN02941 PLN02941
inositol-tetrakisphosphate 1-kinase
 11-90 2.88e-10

inositol-tetrakisphosphate 1-kinase


Pssm-ID: 215508 [Multi-domain]  Cd Length: 328  Bit Score: 58.04  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19484200   11 NVSKPESSSVLTELDKIEG-VFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQH-AVIDVNAFPGYEGVSEF--- 85
Cdd:PLN02941 236 RVSNAAASADDADNGGLDPeVAELPPRPFLEDLARELRRRLGLRLFNFDMIREHGTGDRyYVIDINYFPGYAKMPGYetv 315


                 ....*
gi 19484200   86 FTDLL 90
Cdd:PLN02941 316 LTDFL 320
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 34-82 1.56e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 44.16  E-value: 1.56e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19484200  34 PSDEViRELSRALRQALGVSLFGIDIIINNqtGQHAVIDVNAFPGYEGV 82
Cdd:COG0189 222 LTDEE-RELALRAAPALGLDFAGVDLIEDD--DGPLVLEVNVTPGFRGL 267
 
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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