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Conserved domains on  [gi|154286672|ref|XP_001544131|]
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conserved hypothetical protein [Histoplasma mississippiense (nom. inval.)]

Protein Classification

Apc5_N and ANAPC5 domain-containing protein( domain architecture ID 11075350)

Apc5_N and ANAPC5 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 271-361 1.61e-50

Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Apc5, although it does not harbour a classical RNA binding domain, Apc5 binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC. This region of the Apc5 member proteins carries a TPR-like motif.


:

Pssm-ID: 432838  Cd Length: 91  Bit Score: 167.40  E-value: 1.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154286672  271 HYIKFLDAWKAGDYPSSFDHLHRYFDYTMQSRDRTFYQYALLNLAILQADFGCHAEAVAAMQEAISIARETHDMSCLNFC 350
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDYMLTQNEESFYQYALLNLASLHADFGHNEEAVAAIEEAIRLARENKDTACLNHA 80

                          90
                  ....*....|.
gi 154286672  351 MSWLYHFGKAF 361
Cdd:pfam12862  81 LSWLYNFLKAY 91
Apc5_N super family cl25346
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 100-172 3.02e-03

N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal domain of Apc5 interacts with subunits Apc4, Apc15, and CDC23. Apc5 is a subunit of the eukaryotic anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Although Apc5 does not contain a classical RNA binding domain, it binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC.


The actual alignment was detected with superfamily member cd16270:

Pssm-ID: 293878  Cd Length: 143  Bit Score: 37.99  E-value: 3.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154286672 100 DALDEFFAGILTMLtktredqindrnNGIAPQTGRMMISRTSLLGMFVRRAHLEYTRLQFHDAVALWRGFIKY 172
Cdd:cd16270   79 DDLLDFFDSLERLL------------SGSEEEVEPALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQY 139
 
Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 271-361 1.61e-50

Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Apc5, although it does not harbour a classical RNA binding domain, Apc5 binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC. This region of the Apc5 member proteins carries a TPR-like motif.


Pssm-ID: 432838  Cd Length: 91  Bit Score: 167.40  E-value: 1.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154286672  271 HYIKFLDAWKAGDYPSSFDHLHRYFDYTMQSRDRTFYQYALLNLAILQADFGCHAEAVAAMQEAISIARETHDMSCLNFC 350
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDYMLTQNEESFYQYALLNLASLHADFGHNEEAVAAIEEAIRLARENKDTACLNHA 80

                          90
                  ....*....|.
gi 154286672  351 MSWLYHFGKAF 361
Cdd:pfam12862  81 LSWLYNFLKAY 91
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 100-172 3.02e-03

N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal domain of Apc5 interacts with subunits Apc4, Apc15, and CDC23. Apc5 is a subunit of the eukaryotic anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Although Apc5 does not contain a classical RNA binding domain, it binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC.


Pssm-ID: 293878  Cd Length: 143  Bit Score: 37.99  E-value: 3.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154286672 100 DALDEFFAGILTMLtktredqindrnNGIAPQTGRMMISRTSLLGMFVRRAHLEYTRLQFHDAVALWRGFIKY 172
Cdd:cd16270   79 DDLLDFFDSLERLL------------SGSEEEVEPALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQY 139
 
Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 271-361 1.61e-50

Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Apc5, although it does not harbour a classical RNA binding domain, Apc5 binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC. This region of the Apc5 member proteins carries a TPR-like motif.


Pssm-ID: 432838  Cd Length: 91  Bit Score: 167.40  E-value: 1.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154286672  271 HYIKFLDAWKAGDYPSSFDHLHRYFDYTMQSRDRTFYQYALLNLAILQADFGCHAEAVAAMQEAISIARETHDMSCLNFC 350
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDYMLTQNEESFYQYALLNLASLHADFGHNEEAVAAIEEAIRLARENKDTACLNHA 80

                          90
                  ....*....|.
gi 154286672  351 MSWLYHFGKAF 361
Cdd:pfam12862  81 LSWLYNFLKAY 91
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 100-172 3.02e-03

N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal domain of Apc5 interacts with subunits Apc4, Apc15, and CDC23. Apc5 is a subunit of the eukaryotic anaphase-promoting complex/cyclosome (APC/C) which is a multi-subunit ubiquitin ligase that mediates the proteolysis of cell cycle proteins in mitosis and G1. Although Apc5 does not contain a classical RNA binding domain, it binds the poly(A) binding protein (PABP), which directly binds the internal ribosome entry site (IRES) of growth factor 2 mRNA. PABP was found to enhance IRES-mediated translation, whereas Apc5 over-expression counteracted this effect. In addition to its association with the APC/C complex, Apc5 binds much heavier complexes and co-sediments with the ribosomal fraction. The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC.


Pssm-ID: 293878  Cd Length: 143  Bit Score: 37.99  E-value: 3.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154286672 100 DALDEFFAGILTMLtktredqindrnNGIAPQTGRMMISRTSLLGMFVRRAHLEYTRLQFHDAVALWRGFIKY 172
Cdd:cd16270   79 DDLLDFFDSLERLL------------SGSEEEVEPALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQY 139
 
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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