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Conserved domains on  [gi|315027653|gb|EFT39585|]
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Orf28 family protein, partial [Enterococcus faecalis TX2137]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phage_lysozyme2 super family cl40256
Phage tail lysozyme; This domain has a lysozyme like fold. It is found in the tail protein of ...
426-476 2.78e-13

Phage tail lysozyme; This domain has a lysozyme like fold. It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer.


The actual alignment was detected with superfamily member pfam18013:

Pssm-ID: 465617  Cd Length: 139  Bit Score: 66.94  E-value: 2.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 315027653  426 KRAQAVYDYLSKKGYTKEGISAILGNFSVESGINPKRAEgdYLNPPVGAHG 476
Cdd:pfam18013   1 KNAKAIYNFLKSKGYSKAAAAGILGNMQRESGFNPGAVE--DEGGGGGGYG 49
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
176-209 2.60e-03

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 cd17657:

Pssm-ID: 475123  Cd Length: 144  Bit Score: 38.25  E-value: 2.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 315027653 176 YFTKLDAQHTDDNNLFYSNIDDVLFYMNYrYDDF 209
Cdd:cd17657   11 YFASLRGPPKSTDNTHYFSIDDELVYEPF-FADF 43
 
Name Accession Description Interval E-value
Phage_lysozyme2 pfam18013
Phage tail lysozyme; This domain has a lysozyme like fold. It is found in the tail protein of ...
426-476 2.78e-13

Phage tail lysozyme; This domain has a lysozyme like fold. It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer.


Pssm-ID: 465617  Cd Length: 139  Bit Score: 66.94  E-value: 2.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 315027653  426 KRAQAVYDYLSKKGYTKEGISAILGNFSVESGINPKRAEgdYLNPPVGAHG 476
Cdd:pfam18013   1 KNAKAIYNFLKSKGYSKAAAAGILGNMQRESGFNPGAVE--DEGGGGGGYG 49
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
176-209 2.60e-03

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: 38.25  E-value: 2.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 315027653 176 YFTKLDAQHTDDNNLFYSNIDDVLFYMNYrYDDF 209
Cdd:cd17657   11 YFASLRGPPKSTDNTHYFSIDDELVYEPF-FADF 43
 
Name Accession Description Interval E-value
Phage_lysozyme2 pfam18013
Phage tail lysozyme; This domain has a lysozyme like fold. It is found in the tail protein of ...
426-476 2.78e-13

Phage tail lysozyme; This domain has a lysozyme like fold. It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer.


Pssm-ID: 465617  Cd Length: 139  Bit Score: 66.94  E-value: 2.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 315027653  426 KRAQAVYDYLSKKGYTKEGISAILGNFSVESGINPKRAEgdYLNPPVGAHG 476
Cdd:pfam18013   1 KNAKAIYNFLKSKGYSKAAAAGILGNMQRESGFNPGAVE--DEGGGGGGYG 49
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
176-209 2.60e-03

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: 38.25  E-value: 2.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 315027653 176 YFTKLDAQHTDDNNLFYSNIDDVLFYMNYrYDDF 209
Cdd:cd17657   11 YFASLRGPPKSTDNTHYFSIDDELVYEPF-FADF 43
 
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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