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Conserved domains on  [gi|213385323|ref|NP_001131031|]
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anaphase-promoting complex subunit 5 isoform b [Homo sapiens]

Protein Classification

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 ...
 155-255 1.59e-34

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: 126.18  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  155 HYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESksngeegygrSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQE 234
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDYMLTQNEES----------FYQYALLNLASLHADFGHNEEAVAAIEEAIRLARE 70

                          90       100
                  ....*....|....*....|.
gi 213385323  235 SNDHVCLQHCLSWLYVLGQKR 255
Cdd:pfam12862  71 NKDTACLNHALSWLYNFLKAY 91
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 1-66 2.88e-22

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: 93.08  E-value: 2.88e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213385323   1 MAEGELKDMEQFFDDLSDSFSGTEPE-----VHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNG 66
Cdd:cd16270   73 IAEEGIDDLLDFFDSLERLLSGSEEEvepalLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYYESG 143
TPR_MalT super family cl40220
MalT-like TPR region; This entry contains a series of TPR repeats.
 340-533 5.78e-03

MalT-like TPR region; This entry contains a series of TPR repeats.


The actual alignment was detected with superfamily member pfam17874:

Pssm-ID: 436107 [Multi-domain]  Cd Length: 336  Bit Score: 39.22  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  340 EAVNAGVQQNNTESFAVALCHLAELHAEQGCFAAASEV--------LKHLKERFP----PNSQHAQL---WMLCDQKIQF 404
Cdd:pfam17874  65 EAEALARRADSPHVTLWALLQQGEILRAQGRLHQALETyqqalqlaRDHGLQHLPlhgfLLVGLADLlyeWNDLEEAEQH 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  405 -DRAMNDGKYHLADSLVTGITALnsiegvyrkAVVLQAQNQMSEAHKLLQKLlvhcQKLKNTEMVISVLLSVAE----LY 479
Cdd:pfam17874 145 aQQGIQLGRQWEPDAAVDAYVLL---------ARIALAQGELEEALTLLRRA----ELLARQSFFHVDWLANAErvrvRL 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213385323  480 WRSSSPTIALPMLLQALALSKEYRLQYLASEtVLNLAFAQLILGIPEQALSLLH 533
Cdd:pfam17874 212 WLARGDLRAAVRWLRAAEPPSDADNHFLERE-LRNLARVLLALGRFDDALSLLE 264
 
Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 155-255 1.59e-34

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: 126.18  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  155 HYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESksngeegygrSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQE 234
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDYMLTQNEES----------FYQYALLNLASLHADFGHNEEAVAAIEEAIRLARE 70

                          90       100
                  ....*....|....*....|.
gi 213385323  235 SNDHVCLQHCLSWLYVLGQKR 255
Cdd:pfam12862  71 NKDTACLNHALSWLYNFLKAY 91
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 1-66 2.88e-22

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: 93.08  E-value: 2.88e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213385323   1 MAEGELKDMEQFFDDLSDSFSGTEPE-----VHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNG 66
Cdd:cd16270   73 IAEEGIDDLLDFFDSLERLLSGSEEEvepalLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYYESG 143
TPR_MalT pfam17874
MalT-like TPR region; This entry contains a series of TPR repeats.
 340-533 5.78e-03

MalT-like TPR region; This entry contains a series of TPR repeats.


Pssm-ID: 436107 [Multi-domain]  Cd Length: 336  Bit Score: 39.22  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  340 EAVNAGVQQNNTESFAVALCHLAELHAEQGCFAAASEV--------LKHLKERFP----PNSQHAQL---WMLCDQKIQF 404
Cdd:pfam17874  65 EAEALARRADSPHVTLWALLQQGEILRAQGRLHQALETyqqalqlaRDHGLQHLPlhgfLLVGLADLlyeWNDLEEAEQH 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  405 -DRAMNDGKYHLADSLVTGITALnsiegvyrkAVVLQAQNQMSEAHKLLQKLlvhcQKLKNTEMVISVLLSVAE----LY 479
Cdd:pfam17874 145 aQQGIQLGRQWEPDAAVDAYVLL---------ARIALAQGELEEALTLLRRA----ELLARQSFFHVDWLANAErvrvRL 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213385323  480 WRSSSPTIALPMLLQALALSKEYRLQYLASEtVLNLAFAQLILGIPEQALSLLH 533
Cdd:pfam17874 212 WLARGDLRAAVRWLRAAEPPSDADNHFLERE-LRNLARVLLALGRFDDALSLLE 264
 
Name Accession Description Interval E-value
ANAPC5 pfam12862
Anaphase-promoting complex subunit 5; Apc5 is a subunit of the anaphase-promoting complex ...
 155-255 1.59e-34

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: 126.18  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  155 HYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESksngeegygrSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQE 234
Cdd:pfam12862   1 HYLSYLNALRVKDYQSALDSLHRYFDYMLTQNEES----------FYQYALLNLASLHADFGHNEEAVAAIEEAIRLARE 70

                          90       100
                  ....*....|....*....|.
gi 213385323  235 SNDHVCLQHCLSWLYVLGQKR 255
Cdd:pfam12862  71 NKDTACLNHALSWLYNFLKAY 91
Apc5_N cd16270
N-terminal domain of the anaphase-promoting complex subunit Apc5 (or Anapc5); The N-terminal ...
 1-66 2.88e-22

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: 93.08  E-value: 2.88e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213385323   1 MAEGELKDMEQFFDDLSDSFSGTEPE-----VHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNG 66
Cdd:cd16270   73 IAEEGIDDLLDFFDSLERLLSGSEEEvepalLHKSSVLGLFLRRMLLAFNKLSFSQVVKLYKSFQQYYESG 143
TPR_MalT pfam17874
MalT-like TPR region; This entry contains a series of TPR repeats.
 340-533 5.78e-03

MalT-like TPR region; This entry contains a series of TPR repeats.


Pssm-ID: 436107 [Multi-domain]  Cd Length: 336  Bit Score: 39.22  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  340 EAVNAGVQQNNTESFAVALCHLAELHAEQGCFAAASEV--------LKHLKERFP----PNSQHAQL---WMLCDQKIQF 404
Cdd:pfam17874  65 EAEALARRADSPHVTLWALLQQGEILRAQGRLHQALETyqqalqlaRDHGLQHLPlhgfLLVGLADLlyeWNDLEEAEQH 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213385323  405 -DRAMNDGKYHLADSLVTGITALnsiegvyrkAVVLQAQNQMSEAHKLLQKLlvhcQKLKNTEMVISVLLSVAE----LY 479
Cdd:pfam17874 145 aQQGIQLGRQWEPDAAVDAYVLL---------ARIALAQGELEEALTLLRRA----ELLARQSFFHVDWLANAErvrvRL 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213385323  480 WRSSSPTIALPMLLQALALSKEYRLQYLASEtVLNLAFAQLILGIPEQALSLLH 533
Cdd:pfam17874 212 WLARGDLRAAVRWLRAAEPPSDADNHFLERE-LRNLARVLLALGRFDDALSLLE 264
 
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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