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Conserved domains on  [gi|504426962|ref|WP_014614064|]
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tRNA pseudouridine(55) synthase TruB [Staphylococcus pseudintermedius]

Protein Classification

tRNA pseudouridine synthase B( domain architecture ID 11414791)

tRNA pseudouridine synthase B (TruB) catalyzes the isomerization of uridine to pseudouridine at position 55 in the psi GC loop of transfer RNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
4-305 1.42e-141

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: 400.58  E-value: 1.42e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:COG0130    1 GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRLGVETDTDDAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 GDVLAReiVTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFEND 163
Cdd:COG0130   81 GEVVET--SPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPRPVTIYSLELLS---FDAP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 164 ivRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTLALIEQsHHDDTLQNQLLPLAYGLKGLPS 243
Cdd:COG0130  156 --ELTLEVTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEELEE-LAEGALDALLLPVDEALADLPA 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426962 244 FHVqNESDKMKIKNGQKFAKGYFNVPfeqQLVMVDSDNDDVLAIYEVHPSRqdeIKPKKVFN 305
Cdd:COG0130  233 VEL-DEEEAKRLRNGQRLPLPGLPAD---GLVRVYDPDGRFLALGEIEDGR---LKPKRVFN 287
 
Name Accession Description Interval E-value
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
4-305 1.42e-141

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: 400.58  E-value: 1.42e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:COG0130    1 GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRLGVETDTDDAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 GDVLAReiVTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFEND 163
Cdd:COG0130   81 GEVVET--SPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPRPVTIYSLELLS---FDAP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 164 ivRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTLALIEQsHHDDTLQNQLLPLAYGLKGLPS 243
Cdd:COG0130  156 --ELTLEVTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEELEE-LAEGALDALLLPVDEALADLPA 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426962 244 FHVqNESDKMKIKNGQKFAKGYFNVPfeqQLVMVDSDNDDVLAIYEVHPSRqdeIKPKKVFN 305
Cdd:COG0130  233 VEL-DEEEAKRLRNGQRLPLPGLPAD---GLVRVYDPDGRFLALGEIEDGR---LKPKRVFN 287
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
4-220 5.36e-120

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: 342.89  E-value: 5.36e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:cd02573    1 GILLLDKPAGLTSHDVVQKVRRLLGTKKVGHTGTLDPLATGVLPIALGEATKLSQYLLDADKTYRATVRLGEATDTDDAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 GDVLAREivTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFEND 163
Cdd:cd02573   81 GEIIETS--PPPRLTEEEIEAALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVERPPRKVTIYSLELLS---FDPE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504426962 164 IVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTLALIEQ 220
Cdd:cd02573  156 NPEADFEVHCSKGTYIRSLARDLGKALGCGAHLSALRRTRSGPFTLEQAITLEELEA 212
TruB TIGR00431
tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to ...
4-215 8.24e-89

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: 263.85  E-value: 8.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962    4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:TIGR00431   3 GVLLLDKPQGMTSFDALAKVRRLLNVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEYRAEIRLGVRTDTLDPD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   84 GDVLAREIVTvdqFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdlifeND 163
Cdd:TIGR00431  83 GQIVETRPVN---PTTEDVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVERKARPVTVYDLQFLK-----YE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504426962  164 IVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL 215
Cdd:TIGR00431 155 GPELTLEVHCSKGTYIRTLARDLGEKLGCGAYVSHLRRTAVGDFPLDQSVTL 206
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
24-179 5.21e-75

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: 226.59  E-value: 5.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   24 RKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQTGDVLAReivTVDQFDANQVD 103
Cdd:pfam01509   1 KRILGAKKVGHTGTLDPLATGVLPVCVGEATKLLQYLLDADKEYVATIRLGVATDTLDAEGEIVEE---SVDHITEEKIE 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504426962  104 AVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFENDivRFSIEVTCGKGTYI 179
Cdd:pfam01509  78 EVLASFTGEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLE---FDLP--EVTFRVTCSKGTYI 148
PRK04270 PRK04270
RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;
3-243 6.73e-40

RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;


Pssm-ID: 179806 [Multi-domain]  Cd Length: 300  Bit Score: 141.15  E-value: 6.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   3 HGILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYraevtlgfstttedq 82
Cdd:PRK04270  22 FGVVNLDKPPGPTSHEVAAWVRDILGVEKAGHGGTLDPKVTGVLPVALGKATKVVQALLESGKEY--------------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  83 tgdvlareiVTVDQF----DANQVDAVLHSFKGWTTQIPPMYSSVkvngkklyeyarngetverpKRQIHISHIARISDL 158
Cdd:PRK04270  87 ---------VCVMHLhgdvPEEDIRKVFKEFTGEIYQKPPLKSAV--------------------KRRLRVRTIYELEIL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 159 IFENDIVRFSieVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL-----ALIEQSHHDDT--LQNQL 231
Cdd:PRK04270 138 EIDGRDVLFR--VRCESGTYIRKLCHDIGLALGTGAHMQELRRTRTGPFTEEDLVTLqdladAYYFWKEDGDEeeLRRVI 215
                        250
                 ....*....|..
gi 504426962 232 LPLAYGLKGLPS 243
Cdd:PRK04270 216 LPMEYALSHLPK 227
 
Name Accession Description Interval E-value
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
4-305 1.42e-141

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: 400.58  E-value: 1.42e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:COG0130    1 GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRLGVETDTDDAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 GDVLAReiVTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFEND 163
Cdd:COG0130   81 GEVVET--SPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPRPVTIYSLELLS---FDAP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 164 ivRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTLALIEQsHHDDTLQNQLLPLAYGLKGLPS 243
Cdd:COG0130  156 --ELTLEVTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEELEE-LAEGALDALLLPVDEALADLPA 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426962 244 FHVqNESDKMKIKNGQKFAKGYFNVPfeqQLVMVDSDNDDVLAIYEVHPSRqdeIKPKKVFN 305
Cdd:COG0130  233 VEL-DEEEAKRLRNGQRLPLPGLPAD---GLVRVYDPDGRFLALGEIEDGR---LKPKRVFN 287
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
4-220 5.36e-120

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: 342.89  E-value: 5.36e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:cd02573    1 GILLLDKPAGLTSHDVVQKVRRLLGTKKVGHTGTLDPLATGVLPIALGEATKLSQYLLDADKTYRATVRLGEATDTDDAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 GDVLAREivTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFEND 163
Cdd:cd02573   81 GEIIETS--PPPRLTEEEIEAALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVERPPRKVTIYSLELLS---FDPE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504426962 164 IVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTLALIEQ 220
Cdd:cd02573  156 NPEADFEVHCSKGTYIRSLARDLGKALGCGAHLSALRRTRSGPFTLEQAITLEELEA 212
TruB TIGR00431
tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to ...
4-215 8.24e-89

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: 263.85  E-value: 8.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962    4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:TIGR00431   3 GVLLLDKPQGMTSFDALAKVRRLLNVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEYRAEIRLGVRTDTLDPD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   84 GDVLAREIVTvdqFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdlifeND 163
Cdd:TIGR00431  83 GQIVETRPVN---PTTEDVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVERKARPVTVYDLQFLK-----YE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504426962  164 IVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL 215
Cdd:TIGR00431 155 GPELTLEVHCSKGTYIRTLARDLGEKLGCGAYVSHLRRTAVGDFPLDQSVTL 206
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
24-179 5.21e-75

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: 226.59  E-value: 5.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   24 RKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQTGDVLAReivTVDQFDANQVD 103
Cdd:pfam01509   1 KRILGAKKVGHTGTLDPLATGVLPVCVGEATKLLQYLLDADKEYVATIRLGVATDTLDAEGEIVEE---SVDHITEEKIE 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504426962  104 AVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFENDivRFSIEVTCGKGTYI 179
Cdd:pfam01509  78 EVLASFTGEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLE---FDLP--EVTFRVTCSKGTYI 148
PseudoU_synth_TruB_like cd00506
Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal ...
4-215 3.44e-65

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: 203.54  E-value: 3.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQT 83
Cdd:cd00506    1 GLFAVDKPQGPSSHDVVDTIRRIFLAEKVGHGGTLDPFATGVLVVGIGKATKLLKHLLAATKDYTAIGRLGQATDTFDAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 GDVLarEIVTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFEND 163
Cdd:cd00506   81 GQVI--EETPYDHITHEQLERALETLTGDIQQVPPLYSAVKRQGQRAYELARRGLLVPDEARPPTIYELLCIR---FNPP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504426962 164 IVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL 215
Cdd:cd00506  156 HFLLEVEVVCETGTYIRTLIHDLGLELGVGAHVTELRRTRVGPFKVENAVTL 207
PseudoU_synth_TruB_4 cd02867
Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to ...
4-235 2.02e-42

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: 148.35  E-value: 2.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKIL----------------------KTK-------KVGHTGTLDPEVDGVLPICIGQAT 54
Cdd:cd02867    1 GVFAINKPSGITSAQVLNDLKPLFlnsalfkdkiqravakrgkkarRRKgrkrsklKIGHGGTLDPLATGVLVVGVGAGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  55 KVSDYVMEMGKTYRAEVTLGFSTTTEDQTGDVLarEIVTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYA 134
Cdd:cd02867   81 KQLQDYLSCSKTYEATGLFGASTTTYDREGKIL--KKKPYSHITREDIEEVLAKFRGDIKQVPPLYSALKMDGKRLYEYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 135 RNGETVERP-KRQIHISHIARISDLIFENDivRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQAL 213
Cdd:cd02867  159 REGKPLPRPiERRQVVVSELLVKDWIEPGP--LFTRTVEEEGKQYERSVVKMLGKELKTFAEVTELTATAEGDPVEEVEA 236
                        250       260
                 ....*....|....*....|..
gi 504426962 214 TlALIEQSHHDDTLQNQLLPLA 235
Cdd:cd02867  237 T-HEESKRKSEVEEEANEKSLG 257
PRK04270 PRK04270
RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;
3-243 6.73e-40

RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;


Pssm-ID: 179806 [Multi-domain]  Cd Length: 300  Bit Score: 141.15  E-value: 6.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   3 HGILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYraevtlgfstttedq 82
Cdd:PRK04270  22 FGVVNLDKPPGPTSHEVAAWVRDILGVEKAGHGGTLDPKVTGVLPVALGKATKVVQALLESGKEY--------------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  83 tgdvlareiVTVDQF----DANQVDAVLHSFKGWTTQIPPMYSSVkvngkklyeyarngetverpKRQIHISHIARISDL 158
Cdd:PRK04270  87 ---------VCVMHLhgdvPEEDIRKVFKEFTGEIYQKPPLKSAV--------------------KRRLRVRTIYELEIL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 159 IFENDIVRFSieVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL-----ALIEQSHHDDT--LQNQL 231
Cdd:PRK04270 138 EIDGRDVLFR--VRCESGTYIRKLCHDIGLALGTGAHMQELRRTRTGPFTEEDLVTLqdladAYYFWKEDGDEeeLRRVI 215
                        250
                 ....*....|..
gi 504426962 232 LPLAYGLKGLPS 243
Cdd:PRK04270 216 LPMEYALSHLPK 227
truB PRK02193
tRNA pseudouridine synthase B; Provisional
5-267 9.59e-40

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 140.27  E-value: 9.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   5 ILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQTG 84
Cdd:PRK02193   2 IKLLYKPKGISSFKFIKNFAKTNNIKKIGHTGTLDPLASGLLLVATDEDTKLIDYLDQKDKTYIAKIKFGFISTTYDSEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  85 dvlarEIVTVDQ---FDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFE 161
Cdd:PRK02193  82 -----QIINVSQnikVTKENLEEALNNLVGSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLN---FD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962 162 NDIVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFS---LDQALT-LALI--EQSHHDdtlQNQLLPLA 235
Cdd:PRK02193 154 EKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTGAYMSDLERTKIGNLDknfLNQSLNpLDLIdlEQVKLD---KEELELLL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 504426962 236 YGLKgLPSFHVQNES-----DKM----KIKNGQKFAKGYFN 267
Cdd:PRK02193 231 QGKK-ISFFANSEEYalifkDEIvgigKIINNVLKSKKLFG 270
PseudoU_synth_hDyskerin cd02572
Pseudouridine synthase, human dyskerin like; This group consists of eukaryotic and archeal ...
4-208 7.26e-35

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: 124.68  E-value: 7.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGfstttedqt 83
Cdd:cd02572    3 GVINLDKPSGPSSHEVVAWIKRILGVEKTGHSGTLDPKVTGCLPVCIDRATRLVKSQQEAGKEYVCVMRLH--------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  84 gdvlareivtvDQFDANQVDAVLHSFKGWTTQIPPMYSSVkvngkklyeyarngetverpKRQIHISHIARISDLIFEND 163
Cdd:cd02572   74 -----------DDVDEEKVRRVLEEFTGAIFQRPPLISAV--------------------KRQLRVRTIYESKLLEYDGE 122
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504426962 164 IVRFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFS 208
Cdd:cd02572  123 RRLVLFRVSCEAGTYIRTLCVHIGLLLGVGAHMQELRRTRSGPFS 167
truB PRK14846
tRNA pseudouridine synthase B; Provisional
6-215 2.71e-34

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 237834 [Multi-domain]  Cd Length: 345  Bit Score: 127.84  E-value: 2.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   6 LPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGFSTTTEDQTGD 85
Cdd:PRK14846   6 LNIYKPRGISSAQLVSIVKKILGKTKIGHAGTLDVEAEGILPFAVGEATKLIHLLIDARKTYIFTVKFGMQTNSGDCAGK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  86 VLAREIVTVDQFDANqvdAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGETVERPKRQIHISHIARISdliFENDIV 165
Cdd:PRK14846  86 VIATKDCIPSQEEAY---AVCSKFIGNVTQIPPAFSALKVNGVRAYKLAREGKKVELKPRNITIYDLKCLN---FDEKNA 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504426962 166 RFSIEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL 215
Cdd:PRK14846 160 TATYYTECSKGTYIRTLAEDLALSLQSLGFVIELRRTQVGIFKEENAIRI 209
CBF5 TIGR00425
rRNA pseudouridine synthase, putative; This family, found in archaea and eukaryotes, includes ...
4-242 6.46e-34

rRNA pseudouridine synthase, putative; This family, found in archaea and eukaryotes, includes the only archaeal proteins markedly similar to bacterial TruB, the tRNA pseudouridine 55 synthase. However, among two related yeast proteins, the archaeal set matches yeast YLR175w far better than YNL292w. The first, termed centromere/microtubule binding protein 5 (CBF5), is an apparent rRNA pseudouridine synthase, while the second is the exclusive tRNA pseudouridine 55 synthase for both cytosolic and mitochondrial compartments. It is unclear whether archaeal proteins found by this model modify tRNA, rRNA, or both. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273073 [Multi-domain]  Cd Length: 322  Bit Score: 126.04  E-value: 6.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962    4 GILPVYKERGLTSHDVVFKLRKILKTKKVGHTGTLDPEVDGVLPICIGQATKVSDYVMEMGKTYRAEVTLGfstttedqt 83
Cdd:TIGR00425  35 GVVNLDKPSGPSSHEVVAWVRRILNVEKTGHGGTLDPKVTGVLPVCIERATRLVKSQQEAPKEYVCLMRLH--------- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   84 gdvlareivtvDQFDANQVDAVLHSFKGWTTQIPPMYSSVKvngkklyeyarngetverpkRQIHISHIARISDLIFEND 163
Cdd:TIGR00425 106 -----------RDAKEEDILRVLKEFTGRIFQRPPLKSAVK--------------------RQLRVRTIYESELLEKDGK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  164 IVRFsiEVTCGKGTYIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL-----ALIEQSHHDDT--LQNQLLPLAY 236
Cdd:TIGR00425 155 DVLF--RVSCEAGTYIRKLCVDIGEALGTGAHMQELRRTRSGCFGEDDMVTLhdlldAYVFWKEDGDEsyLRRIIKPMEY 232

                  ....*.
gi 504426962  237 GLKGLP 242
Cdd:TIGR00425 233 LLRHLK 238
TruB_C_2 pfam16198
tRNA pseudouridylate synthase B C-terminal domain; This C-terminal region is found on a subset ...
180-238 3.17e-10

tRNA pseudouridylate synthase B C-terminal domain; This C-terminal region is found on a subset of TruB_B protein family members pfam01509. It is found from bacteria and archaea to fungi, plants and human.


Pssm-ID: 465060 [Multi-domain]  Cd Length: 65  Bit Score: 55.17  E-value: 3.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504426962  180 RTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALTL-----ALIEQSHHDDT-LQNQLLPLAYGL 238
Cdd:pfam16198   1 RTLCEDIGEALGCGAHMAELRRTRVGPFDEADMVTLhdlldAYLLYKEGDESyLRRVLLPLESAL 65
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
4-214 1.24e-07

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: 51.61  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962   4 GILPVYKERGLTSHDV----VFKLRKILKTKKVgHTGT--LDPEVDGVLPICIGQATKVSDYVME--MGKTYRAEVTLGF 75
Cdd:cd02868    1 GLFAVYKPPGVHWKHVrdtiESNLLKYFPEDKV-LVGVhrLDAFSSGVLVLGVNHGNKLLSHLYSnhPTRVYTIRGLLGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426962  76 STTTEDQTGDVLAREivTVDQFDANQVDAVLHSFKGWTTQIPPMYSSVKVNGKKLYEYARNGetVERP--KRQIHISHIA 153
Cdd:cd02868   80 ATENFFHTGRVIEKT--TYDHITREKIERLLAVIQSGHQQKAFELCSVDDQSQQAAELAARG--LIRPadKSPPIIYGIR 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504426962 154 risdlIFENDIVRFSIEVTCGKGT--YIRTLATDIGRALHVPAHMSLLTRTMSGGFSLDQALT 214
Cdd:cd02868  156 -----LLEFRPPEFTLEVQCINETqeYLRKLIHEIGLELRSSAVCTQVRRTRDGPFTVDDALL 213
 
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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