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Conserved domains on  [gi|255003740|ref|NP_080094|]
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nuclear cap-binding protein subunit 3 [Mus musculus]

Protein Classification

NCBP3 domain-containing protein( domain architecture ID 10563356)

NCBP3 domain-containing protein similar to human nuclear cap-binding protein subunit 3 (NCBP3) that associates with NCBP1/CBP80 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NCBP3 pfam10309
Nuclear cap-binding protein subunit 3; NCBP3 and NCBP1 form an alternative cap-binding complex ...
 123-175 1.71e-20

Nuclear cap-binding protein subunit 3; NCBP3 and NCBP1 form an alternative cap-binding complex in higher eukaryotes. NCBP3 binds mRNA, associates with components of the mRNA processing machinery and contributes to polyA RNA export.


:

Pssm-ID: 463048  Cd Length: 59  Bit Score: 85.28  E-value: 1.71e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255003740  123 VRLETIYICGVDEMSTQDIFSYFKEY----PPAHIEWLDDTSCNVVWLDEMTATRAL 175
Cdd:pfam10309   1 IRPEALHLRGVDNLSTDDIKAYASEYfnyePPFRIEWIDDTSANLVFKSEEDALAAL 57
 
Name Accession Description Interval E-value
NCBP3 pfam10309
Nuclear cap-binding protein subunit 3; NCBP3 and NCBP1 form an alternative cap-binding complex ...
 123-175 1.71e-20

Nuclear cap-binding protein subunit 3; NCBP3 and NCBP1 form an alternative cap-binding complex in higher eukaryotes. NCBP3 binds mRNA, associates with components of the mRNA processing machinery and contributes to polyA RNA export.


Pssm-ID: 463048  Cd Length: 59  Bit Score: 85.28  E-value: 1.71e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255003740  123 VRLETIYICGVDEMSTQDIFSYFKEY----PPAHIEWLDDTSCNVVWLDEMTATRAL 175
Cdd:pfam10309   1 IRPEALHLRGVDNLSTDDIKAYASEYfnyePPFRIEWIDDTSANLVFKSEEDALAAL 57
RRM_PARN cd12428
RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; ...
 138-189 6.26e-04

RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; The subfamily corresponds to the RRM of PARN, also termed deadenylating nuclease, or deadenylation nuclease, or polyadenylate-specific ribonuclease, a processive poly(A)-specific 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. It specifically binds both, the poly(A) tail at the 3' end and the 7-methylguanosine (m7G) cap located at the 5' end of eukaryotic mRNAs, and catalyzes the 3'- to 5'-end deadenylation of single-stranded mRNA with a free 3' hydroxyl group both in the nucleus and in the cytoplasm. PARN belongs to the DEDD superfamily of exonucleases. It contains a nuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and an R3H domain. PARN exists as a homodimer. The nuclease domain is involved in the dimerization. RRM and R3H domains are essential for the RNA-binding.


Pssm-ID: 409862 [Multi-domain]  Cd Length: 66  Bit Score: 38.44  E-value: 6.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255003740 138 TQDIFSYFKEYPPAHIEWLDDTSCNVVWLDEMTATRALiNMSSLPAQDKMRS 189
Cdd:cd12428   15 TSDLYQLFSPFGGIQVSWIDDTSAFVALSDPEQVNIAL-KTITYHPSYRIRS 65
 
Name Accession Description Interval E-value
NCBP3 pfam10309
Nuclear cap-binding protein subunit 3; NCBP3 and NCBP1 form an alternative cap-binding complex ...
 123-175 1.71e-20

Nuclear cap-binding protein subunit 3; NCBP3 and NCBP1 form an alternative cap-binding complex in higher eukaryotes. NCBP3 binds mRNA, associates with components of the mRNA processing machinery and contributes to polyA RNA export.


Pssm-ID: 463048  Cd Length: 59  Bit Score: 85.28  E-value: 1.71e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255003740  123 VRLETIYICGVDEMSTQDIFSYFKEY----PPAHIEWLDDTSCNVVWLDEMTATRAL 175
Cdd:pfam10309   1 IRPEALHLRGVDNLSTDDIKAYASEYfnyePPFRIEWIDDTSANLVFKSEEDALAAL 57
RRM_PARN cd12428
RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; ...
 138-189 6.26e-04

RNA recognition motif (RRM) found in poly(A)-specific ribonuclease PARN and similar proteins; The subfamily corresponds to the RRM of PARN, also termed deadenylating nuclease, or deadenylation nuclease, or polyadenylate-specific ribonuclease, a processive poly(A)-specific 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. It specifically binds both, the poly(A) tail at the 3' end and the 7-methylguanosine (m7G) cap located at the 5' end of eukaryotic mRNAs, and catalyzes the 3'- to 5'-end deadenylation of single-stranded mRNA with a free 3' hydroxyl group both in the nucleus and in the cytoplasm. PARN belongs to the DEDD superfamily of exonucleases. It contains a nuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and an R3H domain. PARN exists as a homodimer. The nuclease domain is involved in the dimerization. RRM and R3H domains are essential for the RNA-binding.


Pssm-ID: 409862 [Multi-domain]  Cd Length: 66  Bit Score: 38.44  E-value: 6.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255003740 138 TQDIFSYFKEYPPAHIEWLDDTSCNVVWLDEMTATRALiNMSSLPAQDKMRS 189
Cdd:cd12428   15 TSDLYQLFSPFGGIQVSWIDDTSAFVALSDPEQVNIAL-KTITYHPSYRIRS 65
 
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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