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Conserved domains on  [gi|569006197|ref|XP_006526642|]
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tRNA 2'-phosphotransferase 1 isoform X3 [Mus musculus]

Protein Classification

RNA 2'-phosphotransferase family protein( domain architecture ID 140195)

RNA 2'-phosphotransferase family protein may transfer the splice junction 2'-phosphate from ligated tRNA to NAD, to produce ADP-ribose 1"-2"-cyclic phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTS_2-RNA super family cl19470
RNA 2'-phosphotransferase, Tpt1 / KptA family; Tpt1 catalyzes the last step of tRNA splicing ...
 5-83 3.96e-12

RNA 2'-phosphotransferase, Tpt1 / KptA family; Tpt1 catalyzes the last step of tRNA splicing in yeast. It transfers the splice junction 2'-phosphate from ligated tRNA to NAD, to produce ADP-ribose 1"-2"-cyclic phosphate. This is presumed to be followed by a transesterification step to release the RNA. The first step of this reaction is similar to that catalyzed by some bacterial toxins. E. coli KptA and mouse Tpt1 are likely to use the same reaction mechanism.


The actual alignment was detected with superfamily member pfam01885:

Pssm-ID: 473172  Cd Length: 168  Bit Score: 59.86  E-value: 3.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006197    5 GGRRKEGRrTHrpreqdrnVQLSKALSyalrhgalklGLPMRAGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPG 83
Cdd:pfam01885 109 GGLKRMGR-NH--------IHLATGLP----------GEAVISGMRHSSPVLIYIDVRKALADGIKFYRSENGVILTEG 168
 
Name Accession Description Interval E-value
PTS_2-RNA pfam01885
RNA 2'-phosphotransferase, Tpt1 / KptA family; Tpt1 catalyzes the last step of tRNA splicing ...
 5-83 3.96e-12

RNA 2'-phosphotransferase, Tpt1 / KptA family; Tpt1 catalyzes the last step of tRNA splicing in yeast. It transfers the splice junction 2'-phosphate from ligated tRNA to NAD, to produce ADP-ribose 1"-2"-cyclic phosphate. This is presumed to be followed by a transesterification step to release the RNA. The first step of this reaction is similar to that catalyzed by some bacterial toxins. E. coli KptA and mouse Tpt1 are likely to use the same reaction mechanism.


Pssm-ID: 460371  Cd Length: 168  Bit Score: 59.86  E-value: 3.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006197    5 GGRRKEGRrTHrpreqdrnVQLSKALSyalrhgalklGLPMRAGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPG 83
Cdd:pfam01885 109 GGLKRMGR-NH--------IHLATGLP----------GEAVISGMRHSSPVLIYIDVRKALADGIKFYRSENGVILTEG 168
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 47-93 1.31e-06

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 46.04  E-value: 1.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006197  47 AGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPGNAEGFLLP-KY 93
Cdd:PTZ00315 519 SGMRNNVQLFLYLDVAAVLADGVALYESSNGVILTPGVGHTRQLPlKY 566
KptA COG1859
RNA:NAD 2'-phosphotransferase, TPT1/KptA family [Translation, ribosomal structure and ...
 20-48 5.97e-03

RNA:NAD 2'-phosphotransferase, TPT1/KptA family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441464  Cd Length: 181  Bit Score: 34.77  E-value: 5.97e-03
                         10        20
                 ....*....|....*....|....*....
gi 569006197  20 QDRNVQLSKALSYALRHGALKLGLPMRAG 48
Cdd:COG1859    3 DKRLERLSKFLSYILRHFPEEIGLELDEE 31
 
Name Accession Description Interval E-value
PTS_2-RNA pfam01885
RNA 2'-phosphotransferase, Tpt1 / KptA family; Tpt1 catalyzes the last step of tRNA splicing ...
 5-83 3.96e-12

RNA 2'-phosphotransferase, Tpt1 / KptA family; Tpt1 catalyzes the last step of tRNA splicing in yeast. It transfers the splice junction 2'-phosphate from ligated tRNA to NAD, to produce ADP-ribose 1"-2"-cyclic phosphate. This is presumed to be followed by a transesterification step to release the RNA. The first step of this reaction is similar to that catalyzed by some bacterial toxins. E. coli KptA and mouse Tpt1 are likely to use the same reaction mechanism.


Pssm-ID: 460371  Cd Length: 168  Bit Score: 59.86  E-value: 3.96e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569006197    5 GGRRKEGRrTHrpreqdrnVQLSKALSyalrhgalklGLPMRAGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPG 83
Cdd:pfam01885 109 GGLKRMGR-NH--------IHLATGLP----------GEAVISGMRHSSPVLIYIDVRKALADGIKFYRSENGVILTEG 168
PTZ00315 PTZ00315
2'-phosphotransferase; Provisional
 47-93 1.31e-06

2'-phosphotransferase; Provisional


Pssm-ID: 240356 [Multi-domain]  Cd Length: 582  Bit Score: 46.04  E-value: 1.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 569006197  47 AGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPGNAEGFLLP-KY 93
Cdd:PTZ00315 519 SGMRNNVQLFLYLDVAAVLADGVALYESSNGVILTPGVGHTRQLPlKY 566
KptA COG1859
RNA:NAD 2'-phosphotransferase, TPT1/KptA family [Translation, ribosomal structure and ...
 20-48 5.97e-03

RNA:NAD 2'-phosphotransferase, TPT1/KptA family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441464  Cd Length: 181  Bit Score: 34.77  E-value: 5.97e-03
                         10        20
                 ....*....|....*....|....*....
gi 569006197  20 QDRNVQLSKALSYALRHGALKLGLPMRAG 48
Cdd:COG1859    3 DKRLERLSKFLSYILRHFPEEIGLELDEE 31
 
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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