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Conserved domains on  [gi|1907089802|ref|XP_036013581|]
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jun dimerization protein 2 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
128-171 2.36e-03

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05156:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 326  Bit Score: 37.99  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089802 128 GLGP-LTG----------LPSSALTTEELKYADI-RNIGAMIAPLHFLEVKLGKRP 171
Cdd:cd05156    62 GLGPkLYGifpggrleefIPSRPLTTDELSLPEIsRKIARKMARFHSLEMPISKEP 117
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
128-171 2.36e-03

Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 37.99  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089802 128 GLGP-LTG----------LPSSALTTEELKYADI-RNIGAMIAPLHFLEVKLGKRP 171
Cdd:cd05156    62 GLGPkLYGifpggrleefIPSRPLTTDELSLPEIsRKIARKMARFHSLEMPISKEP 117
 
Name Accession Description Interval E-value
ChoK_euk cd05156
Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP ...
128-171 2.36e-03

Euykaryotic Choline Kinase; ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. Along with PCho, it is involved in malignant transformation through Ras oncogenes in various human cancers such as breast, lung, colon, prostate, neuroblastoma, and hepatic lymphoma. In mammalian cells, there are three ChoK isoforms (A-1, A-2, and B) which are active in homo- or heterodimeric forms. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270705 [Multi-domain]  Cd Length: 326  Bit Score: 37.99  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907089802 128 GLGP-LTG----------LPSSALTTEELKYADI-RNIGAMIAPLHFLEVKLGKRP 171
Cdd:cd05156    62 GLGPkLYGifpggrleefIPSRPLTTDELSLPEIsRKIARKMARFHSLEMPISKEP 117
 
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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