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Conserved domains on  [gi|45550537|ref|NP_647837|]
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imaginal discs arrested [Drosophila melanogaster]

Protein Classification

Apc5_N and ANAPC5 domain-containing protein( domain architecture ID 10888568)

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 ...
 295-386 1.04e-31

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: 118.48  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537   295 YFLGYMNQLRVRDYYNALSALHRALDRspVRLMSQEKGYQYFCVNLAVLHATFGHRDEALAALRESIMLAQEHGDKRSLN 374
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDY--MLTQNEESFYQYALLNLASLHADFGHNEEAVAAIEEAIRLARENKDTACLN 78

                          90
                  ....*....|..
gi 45550537   375 LANTWYCLLRDE 386
Cdd:pfam12862  79 HALSWLYNFLKA 90
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 48-191 2.15e-19

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: 85.37  E-value: 2.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  48 HKITVLILLKQYVINKKNcldtGISMRTQRRRMFYMLVFKLIQEQDKSYNELHSLLTTGKYklDTLMLESFEKAMSEFCA 127
Cdd:cd16270   2 HKIAVLVLIKEYCRLKDS----AWTLSPKERRDFCILLLKLIQGPDMTLKELIKLIEEVCY--LPQLLDSFLERLKLIAE 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537 128 GSIEALFDFseIQNIDEILNEN------YGISQFSMVGVYVRRVGVVLERLSFPEMMDMYKNVCSYYERG 191
Cdd:cd16270  76 EGIDDLLDF--FDSLERLLSGSeeevepALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYYESG 143
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
294-505 1.88e-03

Predicted ATPase [General function prediction only];


The actual alignment was detected with superfamily member COG3899:

Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.77  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  294 PYFLGYMNQLRVRDYYNALSALHRALDRSPVRLMSQEKGYQYFcvNLAVLHATFGHRDEALAALRESIMLAQEHGDKRSL 373
Cdd:COG3899  792 ARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALF--NLGFILHWLGPLREALELLREALEAGLETGDAALA 869

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  374 NLANTWYCLLRDELPLSAVQKSVQDANEVD-GSLLQNYTLALHFAVKLGTVAGYQPLRLFDLLQHSDNLTNRNNFADHAS 452
Cdd:COG3899  870 LLALAAAAAAAAAAAALAAAAAAAARLLAAaAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45550537  453 EALALRSAVWSAYGRHELAALYSQVLLTGRDRFGSGSAGLGSALASFALWLQL 505
Cdd:COG3899  950 AAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALL 1002
 
Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 295-386 1.04e-31

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: 118.48  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537   295 YFLGYMNQLRVRDYYNALSALHRALDRspVRLMSQEKGYQYFCVNLAVLHATFGHRDEALAALRESIMLAQEHGDKRSLN 374
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDY--MLTQNEESFYQYALLNLASLHADFGHNEEAVAAIEEAIRLARENKDTACLN 78

                          90
                  ....*....|..
gi 45550537   375 LANTWYCLLRDE 386
Cdd:pfam12862  79 HALSWLYNFLKA 90
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 48-191 2.15e-19

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: 85.37  E-value: 2.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  48 HKITVLILLKQYVINKKNcldtGISMRTQRRRMFYMLVFKLIQEQDKSYNELHSLLTTGKYklDTLMLESFEKAMSEFCA 127
Cdd:cd16270   2 HKIAVLVLIKEYCRLKDS----AWTLSPKERRDFCILLLKLIQGPDMTLKELIKLIEEVCY--LPQLLDSFLERLKLIAE 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537 128 GSIEALFDFseIQNIDEILNEN------YGISQFSMVGVYVRRVGVVLERLSFPEMMDMYKNVCSYYERG 191
Cdd:cd16270  76 EGIDDLLDF--FDSLERLLSGSeeevepALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYYESG 143
COG3899 COG3899
Predicted ATPase [General function prediction only];
294-505 1.88e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.77  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  294 PYFLGYMNQLRVRDYYNALSALHRALDRSPVRLMSQEKGYQYFcvNLAVLHATFGHRDEALAALRESIMLAQEHGDKRSL 373
Cdd:COG3899  792 ARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALF--NLGFILHWLGPLREALELLREALEAGLETGDAALA 869

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  374 NLANTWYCLLRDELPLSAVQKSVQDANEVD-GSLLQNYTLALHFAVKLGTVAGYQPLRLFDLLQHSDNLTNRNNFADHAS 452
Cdd:COG3899  870 LLALAAAAAAAAAAAALAAAAAAAARLLAAaAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45550537  453 EALALRSAVWSAYGRHELAALYSQVLLTGRDRFGSGSAGLGSALASFALWLQL 505
Cdd:COG3899  950 AAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALL 1002
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
398-530 5.76e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.05  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  398 DANEVDGSLLQNYTLALHfavkLGTVAGYQPLrLFDLLQHSDNLTNRNNFADHASEALALRSAVWSAYGRHELAalysqv 477
Cdd:PRK13837  40 DAIDMAEASLQRDVLRAR----AGLLRNYDPL-VRRLGALRDALADLRRLADGDAELDQLLDRLKASVDRTDAA------ 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 45550537  478 lltgRDRFGSGSAGLGSALASF-----ALWLQLQGEPQLSKVL-LHHAKQRFPRLPSAE 530
Cdd:PRK13837 109 ----VEAFKSQNALLQNSLAYFnslssALPRSDSTDAPARAASeLASAMLRFSLDPSPA 163
 
Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 295-386 1.04e-31

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: 118.48  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537   295 YFLGYMNQLRVRDYYNALSALHRALDRspVRLMSQEKGYQYFCVNLAVLHATFGHRDEALAALRESIMLAQEHGDKRSLN 374
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDY--MLTQNEESFYQYALLNLASLHADFGHNEEAVAAIEEAIRLARENKDTACLN 78

                          90
                  ....*....|..
gi 45550537   375 LANTWYCLLRDE 386
Cdd:pfam12862  79 HALSWLYNFLKA 90
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 48-191 2.15e-19

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: 85.37  E-value: 2.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  48 HKITVLILLKQYVINKKNcldtGISMRTQRRRMFYMLVFKLIQEQDKSYNELHSLLTTGKYklDTLMLESFEKAMSEFCA 127
Cdd:cd16270   2 HKIAVLVLIKEYCRLKDS----AWTLSPKERRDFCILLLKLIQGPDMTLKELIKLIEEVCY--LPQLLDSFLERLKLIAE 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537 128 GSIEALFDFseIQNIDEILNEN------YGISQFSMVGVYVRRVGVVLERLSFPEMMDMYKNVCSYYERG 191
Cdd:cd16270  76 EGIDDLLDF--FDSLERLLSGSeeevepALLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYYESG 143
COG3899 COG3899
Predicted ATPase [General function prediction only];
294-505 1.88e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.77  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  294 PYFLGYMNQLRVRDYYNALSALHRALDRSPVRLMSQEKGYQYFcvNLAVLHATFGHRDEALAALRESIMLAQEHGDKRSL 373
Cdd:COG3899  792 ARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALF--NLGFILHWLGPLREALELLREALEAGLETGDAALA 869

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  374 NLANTWYCLLRDELPLSAVQKSVQDANEVD-GSLLQNYTLALHFAVKLGTVAGYQPLRLFDLLQHSDNLTNRNNFADHAS 452
Cdd:COG3899  870 LLALAAAAAAAAAAAALAAAAAAAARLLAAaAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45550537  453 EALALRSAVWSAYGRHELAALYSQVLLTGRDRFGSGSAGLGSALASFALWLQL 505
Cdd:COG3899  950 AAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALL 1002
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
398-530 5.76e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.05  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550537  398 DANEVDGSLLQNYTLALHfavkLGTVAGYQPLrLFDLLQHSDNLTNRNNFADHASEALALRSAVWSAYGRHELAalysqv 477
Cdd:PRK13837  40 DAIDMAEASLQRDVLRAR----AGLLRNYDPL-VRRLGALRDALADLRRLADGDAELDQLLDRLKASVDRTDAA------ 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 45550537  478 lltgRDRFGSGSAGLGSALASF-----ALWLQLQGEPQLSKVL-LHHAKQRFPRLPSAE 530
Cdd:PRK13837 109 ----VEAFKSQNALLQNSLAYFnslssALPRSDSTDAPARAASeLASAMLRFSLDPSPA 163
 
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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