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Conserved domains on  [gi|17533457|ref|NP_493639|]
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Snurportin-1 [Caenorhabditis elegans]

Protein Classification

Snurportin1 and Snurportin-1_C domain-containing protein( domain architecture ID 10568941)

Snurportin1 and Snurportin-1_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Snurportin-1_C cd09232
C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 ...
 96-276 9.75e-90

C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 or SNUPN) is a nuclear import adaptor for m3G-capped spliceosomal U small nucleoproteins (snRNPs), which are assembled in the cytoplasm. After capping and assembly, the U snRNPs are transported into the nucleus by SPN1 and importin beta; SPN1 is then returned to the cytoplasm by exportin 1 (CRM1), which also transports the non-capped U snRNPs. The U snRNPs are essential elements of the spliceosome, which catalyzes the excision of introns and the ligation of exons to form a mature mRNA. SPN1 contains two domains, an N-terminal importin beta-binding (IBB) domain and a C-terminal m3G cap-binding domain.


:

Pssm-ID: 185717  Cd Length: 186  Bit Score: 266.04  E-value: 9.75e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457  96 KYADKMMLSEWLVDIPESLSSDWTMVMAPVGKRTLVVASRGFTVAYNKGGREVSRFQSRLPGGNTRAKNQAWTILDCIYS 175
Cdd:cd09232   1 LYANQLMLSEWMVEVPDDLSEEWLVVPCPVGKRCLVVASKGKTVARSKNGRTLHRFSSALPGGSRKTSNSGYTILDCIYN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457 176 --NQTYYVLDLLSWNAHEYVESPYDFRQFMLKSKLEEAPELAKSTPGFRNIFSPIPSCPCSQDQMAELMKNEI---SFRL 250
Cdd:cd09232  81 edDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPCTKESLQSAYSGPLnddPYEL 160

                       170       180
                ....*....|....*....|....*.
gi 17533457 251 DGLLFYHNSVVYQPGQSPLVGWLKPW 276
Cdd:cd09232 161 DGLLFYHKESHYTPGSTPLVLWLKDY 186
Snurportin1 pfam11538
Snurportin1; Snurportin1 is a novel nuclear import receptor which contains an N-terminal ...
 26-66 5.93e-13

Snurportin1; Snurportin1 is a novel nuclear import receptor which contains an N-terminal importin beta binding domain which is essential for its function of a snRNP-specific nuclear import receptor. Snurportin1 interacts with m3G-cap where it enhances the m3G-cap dependent nuclear import of U snRNPs in Xenopus laevis oocytes and digitonin-permeabilized HeLa cells.


:

Pssm-ID: 402920  Cd Length: 40  Bit Score: 62.34  E-value: 5.93e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17533457    26 HPRYSQYKnLTKAAEQQAKRREETLERQKNGRFDTFMKLRN 66
Cdd:pfam11538   1 HPRLSQYK-KKRSALSQEERRRRLLERQKKKRLDYVNHARR 40
 
Name Accession Description Interval E-value
Snurportin-1_C cd09232
C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 ...
 96-276 9.75e-90

C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 or SNUPN) is a nuclear import adaptor for m3G-capped spliceosomal U small nucleoproteins (snRNPs), which are assembled in the cytoplasm. After capping and assembly, the U snRNPs are transported into the nucleus by SPN1 and importin beta; SPN1 is then returned to the cytoplasm by exportin 1 (CRM1), which also transports the non-capped U snRNPs. The U snRNPs are essential elements of the spliceosome, which catalyzes the excision of introns and the ligation of exons to form a mature mRNA. SPN1 contains two domains, an N-terminal importin beta-binding (IBB) domain and a C-terminal m3G cap-binding domain.


Pssm-ID: 185717  Cd Length: 186  Bit Score: 266.04  E-value: 9.75e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457  96 KYADKMMLSEWLVDIPESLSSDWTMVMAPVGKRTLVVASRGFTVAYNKGGREVSRFQSRLPGGNTRAKNQAWTILDCIYS 175
Cdd:cd09232   1 LYANQLMLSEWMVEVPDDLSEEWLVVPCPVGKRCLVVASKGKTVARSKNGRTLHRFSSALPGGSRKTSNSGYTILDCIYN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457 176 --NQTYYVLDLLSWNAHEYVESPYDFRQFMLKSKLEEAPELAKSTPGFRNIFSPIPSCPCSQDQMAELMKNEI---SFRL 250
Cdd:cd09232  81 edDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPCTKESLQSAYSGPLnddPYEL 160

                       170       180
                ....*....|....*....|....*.
gi 17533457 251 DGLLFYHNSVVYQPGQSPLVGWLKPW 276
Cdd:cd09232 161 DGLLFYHKESHYTPGSTPLVLWLKDY 186
Snurportin1 pfam11538
Snurportin1; Snurportin1 is a novel nuclear import receptor which contains an N-terminal ...
 26-66 5.93e-13

Snurportin1; Snurportin1 is a novel nuclear import receptor which contains an N-terminal importin beta binding domain which is essential for its function of a snRNP-specific nuclear import receptor. Snurportin1 interacts with m3G-cap where it enhances the m3G-cap dependent nuclear import of U snRNPs in Xenopus laevis oocytes and digitonin-permeabilized HeLa cells.


Pssm-ID: 402920  Cd Length: 40  Bit Score: 62.34  E-value: 5.93e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17533457    26 HPRYSQYKnLTKAAEQQAKRREETLERQKNGRFDTFMKLRN 66
Cdd:pfam11538   1 HPRLSQYK-KKRSALSQEERRRRLLERQKKKRLDYVNHARR 40
 
Name Accession Description Interval E-value
Snurportin-1_C cd09232
C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 ...
 96-276 9.75e-90

C-terminal m3G cap-binding domain of nuclear import adaptor snurportin-1; Snurportin-1 (SPN1 or SNUPN) is a nuclear import adaptor for m3G-capped spliceosomal U small nucleoproteins (snRNPs), which are assembled in the cytoplasm. After capping and assembly, the U snRNPs are transported into the nucleus by SPN1 and importin beta; SPN1 is then returned to the cytoplasm by exportin 1 (CRM1), which also transports the non-capped U snRNPs. The U snRNPs are essential elements of the spliceosome, which catalyzes the excision of introns and the ligation of exons to form a mature mRNA. SPN1 contains two domains, an N-terminal importin beta-binding (IBB) domain and a C-terminal m3G cap-binding domain.


Pssm-ID: 185717  Cd Length: 186  Bit Score: 266.04  E-value: 9.75e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457  96 KYADKMMLSEWLVDIPESLSSDWTMVMAPVGKRTLVVASRGFTVAYNKGGREVSRFQSRLPGGNTRAKNQAWTILDCIYS 175
Cdd:cd09232   1 LYANQLMLSEWMVEVPDDLSEEWLVVPCPVGKRCLVVASKGKTVARSKNGRTLHRFSSALPGGSRKTSNSGYTILDCIYN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457 176 --NQTYYVLDLLSWNAHEYVESPYDFRQFMLKSKLEEAPELAKSTPGFRNIFSPIPSCPCSQDQMAELMKNEI---SFRL 250
Cdd:cd09232  81 edDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPCTKESLQSAYSGPLnddPYEL 160

                       170       180
                ....*....|....*....|....*.
gi 17533457 251 DGLLFYHNSVVYQPGQSPLVGWLKPW 276
Cdd:cd09232 161 DGLLFYHKESHYTPGSTPLVLWLKDY 186
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 102-275 3.93e-18

Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent polynucleotide ligases catalyze the phosphodiester bond formation of nicked nucleic acid substrates using ATP as a cofactor in a three step reaction mechanism. This family includes ATP-dependent DNA and RNA ligases. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent DNA ligases have a highly modular architecture, consisting of a unique arrangement of two or more discrete domains, including a DNA-binding domain, an adenylation or nucleotidyltransferase (NTase) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many active site residues. Together with the C-terminal OB-fold domain, it comprises a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases including eukaryotic GRP-dependent mRNA-capping enzymes. The catalytic core contains both the active site as well as many DNA-binding residues. The RNA circularization protein from archaea and bacteria contains the minimal catalytic unit, the adenylation domain, but does not contain an OB-fold domain. This family also includes the m3G-cap binding domain of snurportin, a nuclear import adaptor that binds m3G-capped spliceosomal U small nucleoproteins (snRNPs), but doesn't have enzymatic activity.


Pssm-ID: 185704 [Multi-domain]  Cd Length: 182  Bit Score: 80.54  E-value: 3.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457 102 MLSEWLVDIPES--LSSDWTMVMAPVGKRTLVVASRGFTVAYNKGGREVSRFQSRLPGgntRAKNQAW--TILDCIYS-- 175
Cdd:cd06846   3 LLNPILEEALSEydEQDEYYVQEKYDGKRALIVALNGGVFAISRTGLEVPLPSILIPG---RELLTLKpgFILDGELVve 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533457 176 -------NQTYYVLDLLSWNAHEYVESPYDFRQFMLKSKLEEAPELAkstPGFRNIFSPIPSCPCSQDQMAELMKneiSF 248
Cdd:cd06846  80 nrevanpKPTYYAFDVVPLSGVGLRDLPYSDRFAYLKSLLKEFEGLD---PVKLVPLENAPSYDETLDDLLEKLK---KK 153

                       170       180
                ....*....|....*....|....*....
gi 17533457 249 RLDGLLFYHNSVVYQ--PGQSPLVGWLKP 275
Cdd:cd06846 154 GKEGLVFKHPDAPYKgrPGSSGNQLKLKP 182
Snurportin1 pfam11538
Snurportin1; Snurportin1 is a novel nuclear import receptor which contains an N-terminal ...
 26-66 5.93e-13

Snurportin1; Snurportin1 is a novel nuclear import receptor which contains an N-terminal importin beta binding domain which is essential for its function of a snRNP-specific nuclear import receptor. Snurportin1 interacts with m3G-cap where it enhances the m3G-cap dependent nuclear import of U snRNPs in Xenopus laevis oocytes and digitonin-permeabilized HeLa cells.


Pssm-ID: 402920  Cd Length: 40  Bit Score: 62.34  E-value: 5.93e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17533457    26 HPRYSQYKnLTKAAEQQAKRREETLERQKNGRFDTFMKLRN 66
Cdd:pfam11538   1 HPRLSQYK-KKRSALSQEERRRRLLERQKKKRLDYVNHARR 40
IBB pfam01749
Importin beta binding domain; This family consists of the importin alpha (karyopherin alpha), ...
 28-85 4.22e-03

Importin beta binding domain; This family consists of the importin alpha (karyopherin alpha), importin beta (karyopherin beta) binding domain. The domain mediates formation of the importin alpha beta complex; required for classical NLS import of proteins into the nucleus, through the nuclear pore complex and across the nuclear envelope. Also in the alignment is the NLS of importin alpha which overlaps with the IBB domain.


Pssm-ID: 460311 [Multi-domain]  Cd Length: 79  Bit Score: 35.59  E-value: 4.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17533457    28 RYSQYKNLTKAAEQQAKRREE-TLERQKNGRFDTFMKLRNLAFDDVTSDEDDEQKIETT 85
Cdd:pfam01749   1 RRKSFKNKGKDADELRRRREEvQVELRKQKREEQLLKRRNVGAPSSSSSSAESQLLESL 59
 
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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