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Conserved domains on  [gi|1958711623|ref|XP_038951773|]
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dual specificity protein phosphatase CDC14B isoform X16 [Rattus norvegicus]

Protein Classification

dual-specificity protein phosphatase CDC14 family protein( domain architecture ID 13026109)

dual-specificity protein phosphatase CDC14 family protein similar to Saccharomyces cerevisiae Cdc14p that orchestrates various events essential for mitotic exit

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 52-190 2.04e-74

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


:

Pssm-ID: 350495  Cd Length: 144  Bit Score: 223.15  E-value: 2.04e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958711623  52 ITDRLCFAILYSRPKSASNEHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIIHFTGTDQRKQAN 131
Cdd:cd17657     6 IPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSLDPKKRAN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958711623 132 AAFLIGCYMVIYLGRAPEDAYRTLIFGDTAYIPFRDAAYGSCSFYITLLDCFHAVKKAI 190
Cdd:cd17657    86 AAFLIGAYAVIYLGKTPEEAYRPLESGEPPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 199-243 1.19e-20

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


The actual alignment was detected with superfamily member cd14499:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 174  Bit Score: 85.97  E-value: 1.19e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958711623 199 SFNLDEYEHYEKAENGDFNWIIPERFLAFCGPHSRSRLESGETAF 243
Cdd:cd14499     1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTH 45
 
Name Accession Description Interval E-value
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 52-190 2.04e-74

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


Pssm-ID: 350495  Cd Length: 144  Bit Score: 223.15  E-value: 2.04e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958711623  52 ITDRLCFAILYSRPKSASNEHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIIHFTGTDQRKQAN 131
Cdd:cd17657     6 IPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSLDPKKRAN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958711623 132 AAFLIGCYMVIYLGRAPEDAYRTLIFGDTAYIPFRDAAYGSCSFYITLLDCFHAVKKAI 190
Cdd:cd17657    86 AAFLIGAYAVIYLGKTPEEAYRPLESGEPPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
DSPn pfam14671
Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity ...
 52-189 1.28e-64

Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This family represents the N-terminal half of the core. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole. The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, family DSPc, pfam00782. Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity.


Pssm-ID: 464252  Cd Length: 140  Bit Score: 198.15  E-value: 1.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958711623  52 ITDRLCFAILYSRPKSASNEHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIIHFTGTDQRKQAN 131
Cdd:pfam14671   3 IPDRLYFATLKSKPKNTPNYHYFSIDDELVYEPFYFDFGPLNLAHLYRFCIKLNKKLKSPELKKKKIVHYTSQDKQKRAN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958711623 132 AAFLIGCYMVIYLGRAPEDAYRTLIFGDTAYIPFRDAAYGSCSFYITLLDCFHAVKKA 189
Cdd:pfam14671  83 AAFLIGAYMVLYLNMSPEEALSPLSSISPPFIPFRDASYGPCTYTLTLLDCLKGLEKA 140
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 199-243 1.19e-20

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 85.97  E-value: 1.19e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958711623 199 SFNLDEYEHYEKAENGDFNWIIPERFLAFCGPHSRSRLESGETAF 243
Cdd:cd14499     1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTH 45
 
Name Accession Description Interval E-value
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 52-190 2.04e-74

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


Pssm-ID: 350495  Cd Length: 144  Bit Score: 223.15  E-value: 2.04e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958711623  52 ITDRLCFAILYSRPKSASNEHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIIHFTGTDQRKQAN 131
Cdd:cd17657     6 IPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSLDPKKRAN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958711623 132 AAFLIGCYMVIYLGRAPEDAYRTLIFGDTAYIPFRDAAYGSCSFYITLLDCFHAVKKAI 190
Cdd:cd17657    86 AAFLIGAYAVIYLGKTPEEAYRPLESGEPPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
DSPn pfam14671
Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity ...
 52-189 1.28e-64

Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This family represents the N-terminal half of the core. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole. The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, family DSPc, pfam00782. Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity.


Pssm-ID: 464252  Cd Length: 140  Bit Score: 198.15  E-value: 1.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958711623  52 ITDRLCFAILYSRPKSASNEHYFSIDNELEYENFYADFGPLNLAMVYRYCCKINKKLKSITMLRKKIIHFTGTDQRKQAN 131
Cdd:pfam14671   3 IPDRLYFATLKSKPKNTPNYHYFSIDDELVYEPFYFDFGPLNLAHLYRFCIKLNKKLKSPELKKKKIVHYTSQDKQKRAN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958711623 132 AAFLIGCYMVIYLGRAPEDAYRTLIFGDTAYIPFRDAAYGSCSFYITLLDCFHAVKKA 189
Cdd:pfam14671  83 AAFLIGAYMVLYLNMSPEEALSPLSSISPPFIPFRDASYGPCTYTLTLLDCLKGLEKA 140
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 199-243 1.19e-20

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 85.97  E-value: 1.19e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958711623 199 SFNLDEYEHYEKAENGDFNWIIPERFLAFCGPHSRSRLESGETAF 243
Cdd:cd14499     1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTH 45
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 92-184 5.17e-08

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 50.04  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958711623  92 LNLAMVYRYCCKINKKLKsitmLRKKIIHFTgtdQRKQANAAFLIGCYMVIYLGRAPEDAYRTLIFGDTAYIPfrdaayg 171
Cdd:cd14494    37 LTLAMVDRFLEVLDQAEK----PGEPVLVHC---KAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIP------- 102

                          90
                  ....*....|...
gi 1958711623 172 scsFYITLLDCFH 184
Cdd:cd14494   103 ---QTIEQLDFLI 112
 
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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