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Conserved domains on  [gi|50401628|sp|Q8WW01|]
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RecName: Full=tRNA-splicing endonuclease subunit Sen15; AltName: Full=SEN15 homolog; Short=HsSEN15; AltName: Full=tRNA-intron endonuclease Sen15

Protein Classification

Sen15 domain-containing protein( domain architecture ID 10560337)

Sen15 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sen15 pfam09631
Sen15 protein; The Sen15 subunit of the tRNA intron-splicing endonuclease is one of the two ...
 65-165 1.91e-31

Sen15 protein; The Sen15 subunit of the tRNA intron-splicing endonuclease is one of the two structural subunits of this hetero-tetrameric enzyme. Residues 36-157 of this subunit possess a novel homodimeric fold. Each monomer consists of three alpha-helices and a mixed antiparallel/parallel beta-sheet. Two monomers of Sen15 fold with two monomers of Sen34, one of the two catalytic subunits, to form an alpha2-beta2 tetramer as part of the functional endonuclease assembly.


:

Pssm-ID: 462844  Cd Length: 101  Bit Score: 108.86  E-value: 1.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50401628    65 LVYLDLMESKSWHEVNCVGLPELQLICLVGTEIEGEGLQT---VVPTPITASLSHNRIREILKasrKLQGDPDLPMSFTL 141
Cdd:pfam09631   1 LVYLNLVHAQLWTDVEILSEEELQLVLLRGRPPKKLSNDDtewVLPVPLTESLSLEQLDKIFD---ELPLPDGRPKRIVL 77

                          90       100
                  ....*....|....*....|....
gi 50401628   142 AIVESDSTIVYYKLTDGFMLPDPQ 165
Cdd:pfam09631  78 AIVDDDSTVVYYFVYDGLVKPRQN 101
 
Name Accession Description Interval E-value
Sen15 pfam09631
Sen15 protein; The Sen15 subunit of the tRNA intron-splicing endonuclease is one of the two ...
 65-165 1.91e-31

Sen15 protein; The Sen15 subunit of the tRNA intron-splicing endonuclease is one of the two structural subunits of this hetero-tetrameric enzyme. Residues 36-157 of this subunit possess a novel homodimeric fold. Each monomer consists of three alpha-helices and a mixed antiparallel/parallel beta-sheet. Two monomers of Sen15 fold with two monomers of Sen34, one of the two catalytic subunits, to form an alpha2-beta2 tetramer as part of the functional endonuclease assembly.


Pssm-ID: 462844  Cd Length: 101  Bit Score: 108.86  E-value: 1.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50401628    65 LVYLDLMESKSWHEVNCVGLPELQLICLVGTEIEGEGLQT---VVPTPITASLSHNRIREILKasrKLQGDPDLPMSFTL 141
Cdd:pfam09631   1 LVYLNLVHAQLWTDVEILSEEELQLVLLRGRPPKKLSNDDtewVLPVPLTESLSLEQLDKIFD---ELPLPDGRPKRIVL 77

                          90       100
                  ....*....|....*....|....
gi 50401628   142 AIVESDSTIVYYKLTDGFMLPDPQ 165
Cdd:pfam09631  78 AIVDDDSTVVYYFVYDGLVKPRQN 101
 
Name Accession Description Interval E-value
Sen15 pfam09631
Sen15 protein; The Sen15 subunit of the tRNA intron-splicing endonuclease is one of the two ...
 65-165 1.91e-31

Sen15 protein; The Sen15 subunit of the tRNA intron-splicing endonuclease is one of the two structural subunits of this hetero-tetrameric enzyme. Residues 36-157 of this subunit possess a novel homodimeric fold. Each monomer consists of three alpha-helices and a mixed antiparallel/parallel beta-sheet. Two monomers of Sen15 fold with two monomers of Sen34, one of the two catalytic subunits, to form an alpha2-beta2 tetramer as part of the functional endonuclease assembly.


Pssm-ID: 462844  Cd Length: 101  Bit Score: 108.86  E-value: 1.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50401628    65 LVYLDLMESKSWHEVNCVGLPELQLICLVGTEIEGEGLQT---VVPTPITASLSHNRIREILKasrKLQGDPDLPMSFTL 141
Cdd:pfam09631   1 LVYLNLVHAQLWTDVEILSEEELQLVLLRGRPPKKLSNDDtewVLPVPLTESLSLEQLDKIFD---ELPLPDGRPKRIVL 77

                          90       100
                  ....*....|....*....|....
gi 50401628   142 AIVESDSTIVYYKLTDGFMLPDPQ 165
Cdd:pfam09631  78 AIVDDDSTVVYYFVYDGLVKPRQN 101
 
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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