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Conserved domains on  [gi|1720432277|ref|XP_030100348|]
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snurportin-1 isoform X3 [Mus musculus]

Protein Classification

snurportin-1( domain architecture ID 10173991)

snurportin-1 functions as an U snRNP-specific nuclear import adapter that is Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs

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 ...
 11-131 9.59e-64

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: 195.55  E-value: 9.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432277  11 KSPYRGLQDYTILDCIYSEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKINPFKFVGLKNFPCTP 90
Cdd:cd09232    63 GSRKTSNSGYTILDCIYNEDDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPCTK 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720432277  91 ESLCEVLS---MDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPY 131
Cdd:cd09232   143 ESLQSAYSgplNDDPYELDGLLFYHKESHYTPGSTPLVLWLKDY 186
 
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 ...
 11-131 9.59e-64

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: 195.55  E-value: 9.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432277  11 KSPYRGLQDYTILDCIYSEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKINPFKFVGLKNFPCTP 90
Cdd:cd09232    63 GSRKTSNSGYTILDCIYNEDDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPCTK 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720432277  91 ESLCEVLS---MDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPY 131
Cdd:cd09232   143 ESLQSAYSgplNDDPYELDGLLFYHKESHYTPGSTPLVLWLKDY 186
 
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 ...
 11-131 9.59e-64

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: 195.55  E-value: 9.59e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432277  11 KSPYRGLQDYTILDCIYSEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKINPFKFVGLKNFPCTP 90
Cdd:cd09232    63 GSRKTSNSGYTILDCIYNEDDRTYYVLDVLCWNGHPLYDCETEFRFFWLRSKLEELPELDEPSEKNPFRFVPLPYFPCTK 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720432277  91 ESLCEVLS---MDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPY 131
Cdd:cd09232   143 ESLQSAYSgplNDDPYELDGLLFYHKESHYTPGSTPLVLWLKDY 186
Adenylation_DNA_ligase_like cd06846
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ...
 17-130 3.59e-32

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: 114.82  E-value: 3.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432277  17 LQDYTILDCIYSEVN-------QTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGlgektkINPFKFVGLKNFPCT 89
Cdd:cd06846    66 LKPGFILDGELVVENrevanpkPTYYAFDVVPLSGVGLRDLPYSDRFAYLKSLLKEFEG------LDPVKLVPLENAPSY 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720432277  90 PESLCEVLSMDFPFEVDGLLFYHKQTHY--SPGSTPLVGWLRP 130
Cdd:cd06846   140 DETLDDLLEKLKKKGKEGLVFKHPDAPYkgRPGSSGNQLKLKP 182
 
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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