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Conserved domains on  [gi|268607501|ref|NP_084115|]
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pseudouridylate synthase TRUB1 isoform 2 [Mus musculus]

Protein Classification

pseudouridine synthase family protein( domain architecture ID 1007)

pseudouridine synthase family protein may catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PseudoU_synth super family cl00130
Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to ...
 58-233 1.19e-88

Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi); Pseudouridine synthases contains the RsuA/RluD, TruA, TruB and TruD families. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases. Some psi sites such as psi55,13,38 and 39 in tRNA are highly conserved, being in the same position in eubacteria, archeabacteria and eukaryotes. Other psi sites occur in a more restricted fashion, for example psi2604in 23S RNA made by E.coli RluF has only been detected in E.coli. Human dyskerin with the help of guide RNAs makes the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


The actual alignment was detected with superfamily member cd02867:

Pssm-ID: 469624 [Multi-domain]  Cd Length: 312  Bit Score: 264.68  E-value: 1.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLLAEAGMPSPEWN-------------KRQKQTLKVGHGGTLDSAAQGVLVVGIGRGT 124
Cdd:cd02867    1 GVFAINKPSGITSAQVLNDLKPLFLNSALFKDKIQRavakrgkkarrrkGRKRSKLKIGHGGTLDPLATGVLVVGVGAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 125 KMLTSMLSGSKRYITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKK 204
Cdd:cd02867   81 KQLQDYLSCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDIEEVLAKFRGDIKQVPPLYSALKMDGKRLYEYARE 160

                        170       180
                 ....*....|....*....|....*....
gi 268607501 205 GKVVEARPARPVTVHSISLLKFQPPFFTL 233
Cdd:cd02867  161 GKPLPRPIERRQVVVSELLVKDWIEPGPL 189
 
Name Accession Description Interval E-value
PseudoU_synth_TruB_4 cd02867
Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to ...
 58-233 1.19e-88

Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to Saccharomyces cerevisiae Pus4. S. cerevisiae Pus4, makes psi55 in the T loop of both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211344 [Multi-domain]  Cd Length: 312  Bit Score: 264.68  E-value: 1.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLLAEAGMPSPEWN-------------KRQKQTLKVGHGGTLDSAAQGVLVVGIGRGT 124
Cdd:cd02867    1 GVFAINKPSGITSAQVLNDLKPLFLNSALFKDKIQRavakrgkkarrrkGRKRSKLKIGHGGTLDPLATGVLVVGVGAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 125 KMLTSMLSGSKRYITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKK 204
Cdd:cd02867   81 KQLQDYLSCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDIEEVLAKFRGDIKQVPPLYSALKMDGKRLYEYARE 160

                        170       180
                 ....*....|....*....|....*....
gi 268607501 205 GKVVEARPARPVTVHSISLLKFQPPFFTL 233
Cdd:cd02867  161 GKPLPRPIERRQVVVSELLVKDWIEPGPL 189
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
 58-233 1.28e-65

tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal structure and biogenesis]; tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439900 [Multi-domain]  Cd Length: 288  Bit Score: 205.28  E-value: 1.28e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKeKLLaeagmpspewnkrqkQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:COG0130    1 GILLLDKPAGMTSHDVVQKVR-RLL---------------GAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTY 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 138 ITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVT 217
Cdd:COG0130   65 RATIRLGVETDTDDAEGEVVETSPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVE-RPPRPVT 143

                        170
                 ....*....|....*.
gi 268607501 218 VHSISLLKFQPPFFTL 233
Cdd:COG0130  144 IYSLELLSFDAPELTL 159
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
 94-233 1.33e-60

TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes TruB, a pseudouridylate synthase that specifically converts uracil 55 to pseudouridine in most tRNAs. This family also includes Cbf5p that modifies rRNA.


Pssm-ID: 426297  Cd Length: 148  Bit Score: 187.69  E-value: 1.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501   94 KRQKQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYITIGELGKATDTLDSTGKVTEEkPYDKITREDIEGI 173
Cdd:pfam01509   1 KRILGAKKVGHTGTLDPLATGVLPVCVGEATKLLQYLLDADKEYVATIRLGVATDTLDAEGEIVEE-SVDHITEEKIEEV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  174 LQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVTVHSISLLKFQPPFFTL 233
Cdd:pfam01509  80 LASFTGEIEQVPPMYSAVKVNGKRLYELAREGIEVE-RPPRPVTIYSLELLEFDLPEVTF 138
TruB TIGR00431
tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to ...
 58-237 3.81e-44

tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to pseudouridine in the T loop of most tRNAs in all three domains of life. This model is built on a seed alignment of bacterial proteins only. Saccharomyces cerevisiae protein YNL292w (Pus4) has been shown to be the pseudouridine 55 synthase of both cytosolic and mitochondrial compartments, active at no other position on tRNA and the only enzyme active at that position in the species. A distinct yeast protein YLR175w, (centromere/microtubule-binding protein CBF5) is an rRNA pseudouridine synthase, and the archaeal set is much more similar to CBF5 than to Pus4. It is unclear whether the archaeal proteins found by this model are tRNA pseudouridine 55 synthases like TruB, rRNA pseudouridine synthases like CBF5, or (as suggested by the absence of paralogs in the Archaea) both. CBF5 likely has additional, eukaryotic-specific functions. The trusted cutoff is set above the scores for the archaeal homologs of unknown function, so yeast Pus4p scores between trusted and noise. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129523  Cd Length: 209  Bit Score: 147.90  E-value: 3.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501   58 GVFAVHKPKGPTSAELLNRLKeKLLaeagmpspewnkrqkQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:TIGR00431   3 GVLLLDKPQGMTSFDALAKVR-RLL---------------NVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEY 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  138 ITIGELGKATDTLDSTGKVTEEKPYDKITrEDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVT 217
Cdd:TIGR00431  67 RAEIRLGVRTDTLDPDGQIVETRPVNPTT-EDVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVE-RKARPVT 144

                         170       180
                  ....*....|....*....|
gi 268607501  218 VHSISLLKFQPPFFTLGFLC 237
Cdd:TIGR00431 145 VYDLQFLKYEGPELTLEVHC 164
truB PRK14846
tRNA pseudouridine synthase B; Provisional
 62-226 2.94e-23

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 237834 [Multi-domain]  Cd Length: 345  Bit Score: 96.25  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  62 VHKPKGPTSAELLNRLKeKLLAEagmpspewnkrqkqtLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYITIG 141
Cdd:PRK14846   8 IYKPRGISSAQLVSIVK-KILGK---------------TKIGHAGTLDVEAEGILPFAVGEATKLIHLLIDARKTYIFTV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 142 ELGKATDTLDSTGKVTEEKPYDKiTREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEARPaRPVTVHSI 221
Cdd:PRK14846  72 KFGMQTNSGDCAGKVIATKDCIP-SQEEAYAVCSKFIGNVTQIPPAFSALKVNGVRAYKLAREGKKVELKP-RNITIYDL 149


                 ....*
gi 268607501 222 SLLKF 226
Cdd:PRK14846 150 KCLNF 154
 
Name Accession Description Interval E-value
PseudoU_synth_TruB_4 cd02867
Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to ...
 58-233 1.19e-88

Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to Saccharomyces cerevisiae Pus4. S. cerevisiae Pus4, makes psi55 in the T loop of both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211344 [Multi-domain]  Cd Length: 312  Bit Score: 264.68  E-value: 1.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLLAEAGMPSPEWN-------------KRQKQTLKVGHGGTLDSAAQGVLVVGIGRGT 124
Cdd:cd02867    1 GVFAINKPSGITSAQVLNDLKPLFLNSALFKDKIQRavakrgkkarrrkGRKRSKLKIGHGGTLDPLATGVLVVGVGAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 125 KMLTSMLSGSKRYITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKK 204
Cdd:cd02867   81 KQLQDYLSCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDIEEVLAKFRGDIKQVPPLYSALKMDGKRLYEYARE 160

                        170       180
                 ....*....|....*....|....*....
gi 268607501 205 GKVVEARPARPVTVHSISLLKFQPPFFTL 233
Cdd:cd02867  161 GKPLPRPIERRQVVVSELLVKDWIEPGPL 189
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
 58-233 1.28e-65

tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal structure and biogenesis]; tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439900 [Multi-domain]  Cd Length: 288  Bit Score: 205.28  E-value: 1.28e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKeKLLaeagmpspewnkrqkQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:COG0130    1 GILLLDKPAGMTSHDVVQKVR-RLL---------------GAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTY 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 138 ITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVT 217
Cdd:COG0130   65 RATIRLGVETDTDDAEGEVVETSPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVE-RPPRPVT 143

                        170
                 ....*....|....*.
gi 268607501 218 VHSISLLKFQPPFFTL 233
Cdd:COG0130  144 IYSLELLSFDAPELTL 159
PseudoU_synth_TruB_like cd00506
Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal ...
 58-237 3.84e-62

Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruB, Saccharomyces cerevisiae Pus4, M. tuberculosis TruB, S. cerevisiae Cbf5 and human dyskerin. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E. coli TruB, M. tuberculosis TruB and S. cerevisiae Pus4, make psi55 in the T loop of tRNAs. Pus4 catalyses the formation of psi55 in both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. S. cerevisiae Cbf5 and human dyskerin are nucleolar proteins that, with the help of guide RNAs, make the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Cbf5/Dyskerin is the catalytic subunit of eukaryotic box H/ACA small nucleolar ribonucleoprotein (snoRNP) particles. Mutations in human dyskerin cause X-linked dyskeratosis congenitas.


Pssm-ID: 211323 [Multi-domain]  Cd Length: 210  Bit Score: 193.91  E-value: 3.84e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLLAEagmpspewnkrqkqtlKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:cd00506    1 GLFAVDKPQGPSSHDVVDTIRRIFLAE----------------KVGHGGTLDPFATGVLVVGIGKATKLLKHLLAATKDY 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 138 ITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEARPaRPVT 217
Cdd:cd00506   65 TAIGRLGQATDTFDATGQVIEETPYDHITHEQLERALETLTGDIQQVPPLYSAVKRQGQRAYELARRGLLVPDEA-RPPT 143

                        170       180
                 ....*....|....*....|
gi 268607501 218 VHSISLLKFQPPFFTLGFLC 237
Cdd:cd00506  144 IYELLCIRFNPPHFLLEVEV 163
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
 94-233 1.33e-60

TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes TruB, a pseudouridylate synthase that specifically converts uracil 55 to pseudouridine in most tRNAs. This family also includes Cbf5p that modifies rRNA.


Pssm-ID: 426297  Cd Length: 148  Bit Score: 187.69  E-value: 1.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501   94 KRQKQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYITIGELGKATDTLDSTGKVTEEkPYDKITREDIEGI 173
Cdd:pfam01509   1 KRILGAKKVGHTGTLDPLATGVLPVCVGEATKLLQYLLDADKEYVATIRLGVATDTLDAEGEIVEE-SVDHITEEKIEEV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  174 LQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVTVHSISLLKFQPPFFTL 233
Cdd:pfam01509  80 LASFTGEIEQVPPMYSAVKVNGKRLYELAREGIEVE-RPPRPVTIYSLELLEFDLPEVTF 138
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
 58-235 1.49e-59

Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial pseudouridine synthases similar to E. coli TruB and Mycobacterium tuberculosis TruB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruB and M. tuberculosis TruB make psi55 in the T loop of tRNAs. Psi55 is nearly universally conserved. E. coli TruB is not inhibited by RNA containing 5-fluorouridine.


Pssm-ID: 211339 [Multi-domain]  Cd Length: 213  Bit Score: 187.27  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLlaeagmpspewnkrqkQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:cd02573    1 GILLLDKPAGLTSHDVVQKVRRLL----------------GTKKVGHTGTLDPLATGVLPIALGEATKLSQYLLDADKTY 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 138 ITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVT 217
Cdd:cd02573   65 RATVRLGEATDTDDAEGEIIETSPPPRLTEEEIEAALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVE-RPPRKVT 143

                        170
                 ....*....|....*...
gi 268607501 218 VHSISLLKFQPPFFTLGF 235
Cdd:cd02573  144 IYSLELLSFDPENPEADF 161
TruB TIGR00431
tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to ...
 58-237 3.81e-44

tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to pseudouridine in the T loop of most tRNAs in all three domains of life. This model is built on a seed alignment of bacterial proteins only. Saccharomyces cerevisiae protein YNL292w (Pus4) has been shown to be the pseudouridine 55 synthase of both cytosolic and mitochondrial compartments, active at no other position on tRNA and the only enzyme active at that position in the species. A distinct yeast protein YLR175w, (centromere/microtubule-binding protein CBF5) is an rRNA pseudouridine synthase, and the archaeal set is much more similar to CBF5 than to Pus4. It is unclear whether the archaeal proteins found by this model are tRNA pseudouridine 55 synthases like TruB, rRNA pseudouridine synthases like CBF5, or (as suggested by the absence of paralogs in the Archaea) both. CBF5 likely has additional, eukaryotic-specific functions. The trusted cutoff is set above the scores for the archaeal homologs of unknown function, so yeast Pus4p scores between trusted and noise. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129523  Cd Length: 209  Bit Score: 147.90  E-value: 3.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501   58 GVFAVHKPKGPTSAELLNRLKeKLLaeagmpspewnkrqkQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:TIGR00431   3 GVLLLDKPQGMTSFDALAKVR-RLL---------------NVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEY 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  138 ITIGELGKATDTLDSTGKVTEEKPYDKITrEDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEaRPARPVT 217
Cdd:TIGR00431  67 RAEIRLGVRTDTLDPDGQIVETRPVNPTT-EDVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVE-RKARPVT 144

                         170       180
                  ....*....|....*....|
gi 268607501  218 VHSISLLKFQPPFFTLGFLC 237
Cdd:TIGR00431 145 VYDLQFLKYEGPELTLEVHC 164
truB PRK14846
tRNA pseudouridine synthase B; Provisional
 62-226 2.94e-23

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 237834 [Multi-domain]  Cd Length: 345  Bit Score: 96.25  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  62 VHKPKGPTSAELLNRLKeKLLAEagmpspewnkrqkqtLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYITIG 141
Cdd:PRK14846   8 IYKPRGISSAQLVSIVK-KILGK---------------TKIGHAGTLDVEAEGILPFAVGEATKLIHLLIDARKTYIFTV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 142 ELGKATDTLDSTGKVTEEKPYDKiTREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEARPaRPVTVHSI 221
Cdd:PRK14846  72 KFGMQTNSGDCAGKVIATKDCIP-SQEEAYAVCSKFIGNVTQIPPAFSALKVNGVRAYKLAREGKKVELKP-RNITIYDL 149


                 ....*
gi 268607501 222 SLLKF 226
Cdd:PRK14846 150 KCLNF 154
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
 58-238 1.14e-22

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 92.45  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLLaeagmpspewnKRQKQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGS--K 135
Cdd:cd02868    1 GLFAVYKPPGVHWKHVRDTIESNLL-----------KYFPEDKVLVGVHRLDAFSSGVLVLGVNHGNKLLSHLYSNHptR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 136 RYITIGELGKATDTLDSTGKVTEEKPYDKITREDIEGILQkftgnIMQVPPLYSALKKDGQRLST-----LMKKGKVvea 210
Cdd:cd02868   70 VYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLA-----VIQSGHQQKAFELCSVDDQSqqaaeLAARGLI--- 141

                        170       180       190
                 ....*....|....*....|....*....|
gi 268607501 211 RPA--RPVTVHSISLLKFQPPFFTLGFLCI 238
Cdd:cd02868  142 RPAdkSPPIIYGIRLLEFRPPEFTLEVQCI 171
truB PRK02193
tRNA pseudouridine synthase B; Provisional
 62-235 6.22e-22

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 91.35  E-value: 6.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  62 VHKPKGPTSAELLNRLKekllaeagmpspewnkRQKQTLKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRYITIG 141
Cdd:PRK02193   5 LYKPKGISSFKFIKNFA----------------KTNNIKKIGHTGTLDPLASGLLLVATDEDTKLIDYLDQKDKTYIAKI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 142 ELGKATDTLDSTGKVTEEKPYDKITREDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKKGKVVEARPArPVTVHSI 221
Cdd:PRK02193  69 KFGFISTTYDSEGQIINVSQNIKVTKENLEEALNNLVGSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPI-EIKISKI 147

                        170
                 ....*....|....
gi 268607501 222 SLLKFQPPFFTLGF 235
Cdd:PRK02193 148 ELLNFDEKLQNCVF 161
PseudoU_synth_hDyskerin cd02572
Pseudouridine synthase, human dyskerin like; This group consists of eukaryotic and archeal ...
 57-228 1.21e-20

Pseudouridine synthase, human dyskerin like; This group consists of eukaryotic and archeal pseudouridine synthases similar to human dyskerin, Saccharomyces cerevisiae Cbf5, and Drosophila melanogaster Mfl (minifly protein). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactor is required. S. cerevisiae Cbf5 and human dyskerin are nucleolar proteins that, with the help of guide RNAs, make the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Cbf5/Dyskerin is the catalytic subunit of eukaryotic box H/ACA small nucleolar ribonucleoprotein (snoRNP) particles. D. melanogaster mfl hosts in its fourth intron, a box H/AC snoRNA gene. In addition dyskerin is likely to have a structural role in the telomerase complex. Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Mutations in Drosophila Mfl results in miniflies that suffer abnormalities.


Pssm-ID: 211338  Cd Length: 182  Bit Score: 85.78  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  57 SGVFAVHKPKGPTSAELLNRLKEKLLAEagmpspewnkrqkqtlKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKR 136
Cdd:cd02572    2 YGVINLDKPSGPSSHEVVAWIKRILGVE----------------KTGHSGTLDPKVTGCLPVCIDRATRLVKSQQEAGKE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501 137 YITIGELgkatdtldstgkvteekpYDKITREDIEGILQKFTGNIMQVPPLYSALKkdgqrlstlmkkgkvveaRPARPV 216
Cdd:cd02572   66 YVCVMRL------------------HDDVDEEKVRRVLEEFTGAIFQRPPLISAVK------------------RQLRVR 109

                        170
                 ....*....|..
gi 268607501 217 TVHSISLLKFQP 228
Cdd:cd02572  110 TIYESKLLEYDG 121
PRK04270 PRK04270
RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;
58-193 3.42e-18

RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;


Pssm-ID: 179806 [Multi-domain]  Cd Length: 300  Bit Score: 81.44  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268607501  58 GVFAVHKPKGPTSAELLNRLKEKLLAEagmpspewnkrqkqtlKVGHGGTLDSAAQGVLVVGIGRGTKMLTSMLSGSKRY 137
Cdd:PRK04270  23 GVVNLDKPPGPTSHEVAAWVRDILGVE----------------KAGHGGTLDPKVTGVLPVALGKATKVVQALLESGKEY 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 268607501 138 ITIGELgkatdtldstgkvteekpYDKITREDIEGILQKFTGNIMQVPPLYSALKK 193
Cdd:PRK04270  87 VCVMHL------------------HGDVPEEDIRKVFKEFTGEIYQKPPLKSAVKR 124
 
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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