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Conserved domains on  [gi|1090717105|emb|SEG37765|]
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tRNA pseudouridine synthase B [Oleiphilus messinensis]

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 ...
12-300 5.46e-159

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: 444.49  E-value: 5.46e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAE 91
Cdd:COG0130     1 GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRLGVETDTDDAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 GTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMTFS 171
Cdd:COG0130    81 GEVVETSPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPRPVTIYSLELLSFDAPELTLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105 172 VRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRLqsERDQDQSLDGYLLDTDVLVAHFPKKNLSAE 251
Cdd:COG0130   161 VTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEEL--EELAEGALDALLLPVDEALADLPAVELDEE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1090717105 252 ETARILHGQDITCDQV-YSDKVRLYDEQERFIGLAEsAEAGRLKPRRLVV 300
Cdd:COG0130   239 EAKRLRNGQRLPLPGLpADGLVRVYDPDGRFLALGE-IEDGRLKPKRVFN 287
 
Name Accession Description Interval E-value
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
12-300 5.46e-159

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: 444.49  E-value: 5.46e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAE 91
Cdd:COG0130     1 GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRLGVETDTDDAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 GTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMTFS 171
Cdd:COG0130    81 GEVVETSPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPRPVTIYSLELLSFDAPELTLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105 172 VRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRLqsERDQDQSLDGYLLDTDVLVAHFPKKNLSAE 251
Cdd:COG0130   161 VTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEEL--EELAEGALDALLLPVDEALADLPAVELDEE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1090717105 252 ETARILHGQDITCDQV-YSDKVRLYDEQERFIGLAEsAEAGRLKPRRLVV 300
Cdd:COG0130   239 EAKRLRNGQRLPLPGLpADGLVRVYDPDGRFLALGE-IEDGRLKPKRVFN 287
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
12-222 1.37e-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: 344.43  E-value: 1.37e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAE 91
Cdd:cd02573     1 GILLLDKPAGLTSHDVVQKVRRLLGTKKVGHTGTLDPLATGVLPIALGEATKLSQYLLDADKTYRATVRLGEATDTDDAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 GTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDA--PDMT 169
Cdd:cd02573    81 GEIIETSPPPRLTEEEIEAALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVERPPRKVTIYSLELLSFDPenPEAD 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1090717105 170 FSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRLQSE 222
Cdd:cd02573   161 FEVHCSKGTYIRSLARDLGKALGCGAHLSALRRTRSGPFTLEQAITLEELEAL 213
TruB TIGR00431
tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to ...
10-219 2.22e-93

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: 275.40  E-value: 2.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  10 ISGVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGD 89
Cdd:TIGR00431   1 INGVLLLDKPQGMTSFDALAKVRRLLNVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEYRAEIRLGVRTDTLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  90 AEGTIIQERPVPELSDaQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMT 169
Cdd:TIGR00431  81 PDGQIVETRPVNPTTE-DVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVERKARPVTVYDLQFLKYEGPELT 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1090717105 170 FSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRL 219
Cdd:TIGR00431 160 LEVHCSKGTYIRTLARDLGEKLGCGAYVSHLRRTAVGDFPLDQSVTLEEL 209
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
32-180 9.93e-84

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: 248.55  E-value: 9.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  32 RAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAEGTIIqERPVPELSDAQICDA 111
Cdd:pfam01509   1 KRILGAKKVGHTGTLDPLATGVLPVCVGEATKLLQYLLDADKEYVATIRLGVATDTLDAEGEIV-EESVDHITEEKIEEV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1090717105 112 MAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMTFSVRCSKGTYV 180
Cdd:pfam01509  80 LASFTGEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLEFDLPEVTFRVTCSKGTYI 148
truB PRK02193
tRNA pseudouridine synthase B; Provisional
13-211 6.51e-52

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 171.86  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  13 VLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAEG 92
Cdd:PRK02193    2 IKLLYKPKGISSFKFIKNFAKTNNIKKIGHTGTLDPLASGLLLVATDEDTKLIDYLDQKDKTYIAKIKFGFISTTYDSEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  93 TIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMT--F 170
Cdd:PRK02193   82 QIINVSQNIKVTKENLEEALNNLVGSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNcvF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1090717105 171 SVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDAS 211
Cdd:PRK02193  162 MWVVSRGTYIRSLIHDLGKMLKTGAYMSDLERTKIGNLDKN 202
 
Name Accession Description Interval E-value
TruB COG0130
tRNA U55 pseudouridine synthase TruB, may also work on U342 of tmRNA [Translation, ribosomal ...
12-300 5.46e-159

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: 444.49  E-value: 5.46e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAE 91
Cdd:COG0130     1 GILLLDKPAGMTSHDVVQKVRRLLGAKKVGHTGTLDPLATGVLPICLGEATKLSQYLLDADKTYRATIRLGVETDTDDAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 GTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMTFS 171
Cdd:COG0130    81 GEVVETSPVPRLTEEEIEAALASFTGEIEQVPPMYSAIKVDGKRLYELARAGEEVERPPRPVTIYSLELLSFDAPELTLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105 172 VRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRLqsERDQDQSLDGYLLDTDVLVAHFPKKNLSAE 251
Cdd:COG0130   161 VTCSKGTYIRSLARDLGEALGCGAHLSALRRTRVGPFTLEDAVTLEEL--EELAEGALDALLLPVDEALADLPAVELDEE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1090717105 252 ETARILHGQDITCDQV-YSDKVRLYDEQERFIGLAEsAEAGRLKPRRLVV 300
Cdd:COG0130   239 EAKRLRNGQRLPLPGLpADGLVRVYDPDGRFLALGE-IEDGRLKPKRVFN 287
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
12-222 1.37e-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: 344.43  E-value: 1.37e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAE 91
Cdd:cd02573     1 GILLLDKPAGLTSHDVVQKVRRLLGTKKVGHTGTLDPLATGVLPIALGEATKLSQYLLDADKTYRATVRLGEATDTDDAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 GTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDA--PDMT 169
Cdd:cd02573    81 GEIIETSPPPRLTEEEIEAALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVERPPRKVTIYSLELLSFDPenPEAD 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1090717105 170 FSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRLQSE 222
Cdd:cd02573   161 FEVHCSKGTYIRSLARDLGKALGCGAHLSALRRTRSGPFTLEQAITLEELEAL 213
TruB TIGR00431
tRNA pseudouridine(55) synthase; TruB, the tRNA pseudouridine 55 synthase, converts uracil to ...
10-219 2.22e-93

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: 275.40  E-value: 2.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  10 ISGVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGD 89
Cdd:TIGR00431   1 INGVLLLDKPQGMTSFDALAKVRRLLNVKKVGHTGTLDPFATGVLPILVGKATKLSPYLTDLDKEYRAEIRLGVRTDTLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  90 AEGTIIQERPVPELSDaQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMT 169
Cdd:TIGR00431  81 PDGQIVETRPVNPTTE-DVEAALPTFRGEIEQIPPMYSALKVNGKRLYEYARQGIEVERKARPVTVYDLQFLKYEGPELT 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1090717105 170 FSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRL 219
Cdd:TIGR00431 160 LEVHCSKGTYIRTLARDLGEKLGCGAYVSHLRRTAVGDFPLDQSVTLEEL 209
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
32-180 9.93e-84

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: 248.55  E-value: 9.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  32 RAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAEGTIIqERPVPELSDAQICDA 111
Cdd:pfam01509   1 KRILGAKKVGHTGTLDPLATGVLPVCVGEATKLLQYLLDADKEYVATIRLGVATDTLDAEGEIV-EESVDHITEEKIEEV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1090717105 112 MAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMTFSVRCSKGTYV 180
Cdd:pfam01509  80 LASFTGEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLEFDLPEVTFRVTCSKGTYI 148
PseudoU_synth_TruB_like cd00506
Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal ...
12-219 1.18e-71

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: 220.10  E-value: 1.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAE 91
Cdd:cd00506     1 GLFAVDKPQGPSSHDVVDTIRRIFLAEKVGHGGTLDPFATGVLVVGIGKATKLLKHLLAATKDYTAIGRLGQATDTFDAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 GTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAP--DMT 169
Cdd:cd00506    81 GQVIEETPYDHITHEQLERALETLTGDIQQVPPLYSAVKRQGQRAYELARRGLLVPDEARPPTIYELLCIRFNPPhfLLE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1090717105 170 FSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRL 219
Cdd:cd00506   161 VEVVCETGTYIRTLIHDLGLELGVGAHVTELRRTRVGPFKVENAVTLHHL 210
PseudoU_synth_TruB_4 cd02867
Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to ...
12-254 5.95e-57

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: 186.10  E-value: 5.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNAS-----------------------------KAGHTGNLDPMATGLLPLCFGEAT 62
Cdd:cd02867     1 GVFAINKPSGITSAQVLNDLKPLFLNSalfkdkiqravakrgkkarrrkgrkrsklKIGHGGTLDPLATGVLVVGVGAGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  63 KFSSYLLDADKAYIATARLGLVSDTGDAEGTIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLARE 142
Cdd:cd02867    81 KQLQDYLSCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDIEEVLAKFRGDIKQVPPLYSALKMDGKRLYEYARE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105 143 GKTVER--KARAVTIFELKLLEW--DAPDMTFSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDR 218
Cdd:cd02867   161 GKPLPRpiERRQVVVSELLVKDWiePGPLFTRTVEEEGKQYERSVVKMLGKELKTFAEVTELTATAEGDPVEEVEATHEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1090717105 219 LQSERDQDQSLDGYLLDTDVLVAHFPKKNLSAEETA 254
Cdd:cd02867   241 SKRKSEVEEEANEKSLGPEARSLESDAGRGSFSPAA 276
truB PRK02193
tRNA pseudouridine synthase B; Provisional
13-211 6.51e-52

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 171.86  E-value: 6.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  13 VLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAEG 92
Cdd:PRK02193    2 IKLLYKPKGISSFKFIKNFAKTNNIKKIGHTGTLDPLASGLLLVATDEDTKLIDYLDQKDKTYIAKIKFGFISTTYDSEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  93 TIIQERPVPELSDAQICDAMAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMT--F 170
Cdd:PRK02193   82 QIINVSQNIKVTKENLEEALNNLVGSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNcvF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1090717105 171 SVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFDAS 211
Cdd:PRK02193  162 MWVVSRGTYIRSLIHDLGKMLKTGAYMSDLERTKIGNLDKN 202
truB PRK14846
tRNA pseudouridine synthase B; Provisional
18-208 7.62e-47

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 237834 [Multi-domain]  Cd Length: 345  Bit Score: 160.58  E-value: 7.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  18 KPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLGLVSDTGDAEGTIIQE 97
Cdd:PRK14846   10 KPRGISSAQLVSIVKKILGKTKIGHAGTLDVEAEGILPFAVGEATKLIHLLIDARKTYIFTVKFGMQTNSGDCAGKVIAT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  98 RP-VPELSDA-QICdamAKFLGDIEQVPPMYSALKQNGQPLYKLAREGKTVERKARAVTIFELKLLEWDAPDMT--FSVR 173
Cdd:PRK14846   90 KDcIPSQEEAyAVC---SKFIGNVTQIPPAFSALKVNGVRAYKLAREGKKVELKPRNITIYDLKCLNFDEKNATatYYTE 166
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1090717105 174 CSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGF 208
Cdd:PRK14846  167 CSKGTYIRTLAEDLALSLQSLGFVIELRRTQVGIF 201
PRK04270 PRK04270
RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;
12-209 3.75e-46

RNA-guided pseudouridylation complex pseudouridine synthase subunit Cbf5;


Pssm-ID: 179806 [Multi-domain]  Cd Length: 300  Bit Score: 157.71  E-value: 3.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLglvsdtgdae 91
Cdd:PRK04270   23 GVVNLDKPPGPTSHEVAAWVRDILGVEKAGHGGTLDPKVTGVLPVALGKATKVVQALLESGKEYVCVMHL---------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  92 gtiiqERPVPElsdAQICDAMAKFLGDIEQVPPMYSAlkqngqplyklaregktVERKARAVTIFELKLLEWDAPDMTFS 171
Cdd:PRK04270   93 -----HGDVPE---EDIRKVFKEFTGEIYQKPPLKSA-----------------VKRRLRVRTIYELEILEIDGRDVLFR 147
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1090717105 172 VRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFD 209
Cdd:PRK04270  148 VRCESGTYIRKLCHDIGLALGTGAHMQELRRTRTGPFT 185
PseudoU_synth_hDyskerin cd02572
Pseudouridine synthase, human dyskerin like; This group consists of eukaryotic and archeal ...
11-209 1.10e-40

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: 139.70  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  11 SGVLLLNKPKGISSNRALQRVRAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDADKAYIATARLglvsdtGDA 90
Cdd:cd02572     2 YGVINLDKPSGPSSHEVVAWIKRILGVEKTGHSGTLDPKVTGCLPVCIDRATRLVKSQQEAGKEYVCVMRL------HDD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  91 EgtiiqerpvpelSDAQICDAMAKFLGDIEQVPPMYSALKqngqplyklaregktveRKARAVTIFELKLLEWDAP--DM 168
Cdd:cd02572    76 V------------DEEKVRRVLEEFTGAIFQRPPLISAVK-----------------RQLRVRTIYESKLLEYDGErrLV 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1090717105 169 TFSVRCSKGTYVRTLAEDIGETLGCGAHLVMLHRTHTGGFD 209
Cdd:cd02572   127 LFRVSCEAGTYIRTLCVHIGLLLGVGAHMQELRRTRSGPFS 167
TruB-C_2 pfam09157
Pseudouridine synthase II TruB, C-terminal; Members of this family adopt a secondary structure ...
244-299 6.11e-16

Pseudouridine synthase II TruB, C-terminal; Members of this family adopt a secondary structure consisting of a four-stranded beta sheet and one alpha helix. They are predominantly RNA-binding domains, mostly found in Pseudouridine synthase II TruB.


Pssm-ID: 462695  Cd Length: 57  Bit Score: 70.67  E-value: 6.11e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1090717105 244 PKKNLSAEETARILHGQDITCDQVYSD-KVRLYDEQERFIGLAESAEAGRLKPRRLV 299
Cdd:pfam09157   1 PEVNLSEESAAYFLQGQPVRVDGAPIEgLVRVYGEEGRFLGIGEIDDDGRLAPKRLV 57
PUA_TruB_bacterial cd21152
PUA RNA-binding domain of bacterial pseudouridine synthase TruB and similar proteins; The ...
241-299 3.75e-14

PUA RNA-binding domain of bacterial pseudouridine synthase TruB and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this bacterial subfamily of pseudouridine synthases, including TruB and similar proteins, are modules that assist in the binding and positioning (guide and/or substrate) of RNA to the pseudouridine synthase complex. Pseudouridine synthases are enzymes that are responsible for post-translational modifications of RNAs by specifically isomerizing uracil residues. The pseudouridine synthase TruB (also called tRNA pseudouridylate synthase B or Psi55 synthase) is responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of elongator tRNAs.


Pssm-ID: 409294  Cd Length: 60  Bit Score: 65.68  E-value: 3.75e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105 241 AHFPKKNLSAEETARILHGQDI-TCDQVYSDKVRLYDEQERFIGLAESAEAGRLKPRRLV 299
Cdd:cd21152     1 AHLPEVNLDAEEAARFLQGQPVpVPGAPIEGLVRVYDGEGRFIGLGEIDDDGRLAPKRLV 60
TruB_C_2 pfam16198
tRNA pseudouridylate synthase B C-terminal domain; This C-terminal region is found on a subset ...
181-240 7.94e-13

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: 62.49  E-value: 7.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1090717105 181 RTLAEDIGETLGCGAHLVMLHRTHTGGFDASGMLEFDRLQ-----SERDQDQSLDGYLLDTDVLV 240
Cdd:pfam16198   1 RTLCEDIGEALGCGAHMAELRRTRVGPFDEADMVTLHDLLdayllYKEGDESYLRRVLLPLESAL 65
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
12-209 1.99e-05

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: 45.07  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  12 GVLLLNKPKGISSNRALQRV-----RAMFNASKAGHTGNLDPMATGLLPLCFGEATKFSSYLLDAD--KAYIATARLGLV 84
Cdd:cd02868     1 GLFAVYKPPGVHWKHVRDTIesnllKYFPEDKVLVGVHRLDAFSSGVLVLGVNHGNKLLSHLYSNHptRVYTIRGLLGKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090717105  85 SDTGDAEGTIIQERPVPELSDAQIcdamAKFLGDIE-----QVPPMYSALKQNGQPlYKLAREGKTVERKARAVTIFELK 159
Cdd:cd02868    81 TENFFHTGRVIEKTTYDHITREKI----ERLLAVIQsghqqKAFELCSVDDQSQQA-AELAARGLIRPADKSPPIIYGIR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1090717105 160 LLEWDAPDMTFSVRCSKGT--YVRTLAEDIGETLGCGAHLVMLHRTHTGGFD 209
Cdd:cd02868   156 LLEFRPPEFTLEVQCINETqeYLRKLIHEIGLELRSSAVCTQVRRTRDGPFT 207
PUA_TruB_thermotogae cd21905
PUA RNA-binding domain of the thermotogae tRNA pseudouridine synthase B; The RNA-binding PUA ...
243-287 1.06e-03

PUA RNA-binding domain of the thermotogae tRNA pseudouridine synthase B; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of the thermotogae subfamily of pseudouridine synthases TruB are modules that assist in the binding and positioning (guide and/or substrate) of RNA to the pseudouridine synthase complex. Pseudouridine synthases are enzymes that are responsible for post-translational modifications of RNAs by specifically isomerizing uracil residues. The pseudouridine synthase TruB (also called tRNA pseudouridylate synthase B or Psi55 synthase) is responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of elongator tRNAs.


Pssm-ID: 409300 [Multi-domain]  Cd Length: 78  Bit Score: 37.22  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1090717105 243 FPKKNLSAEETARILHGQDITCDQVYS-------DKVRLYDEQERFIGLAES 287
Cdd:cd21905     1 LPKVVVNEESSKRVLNGSQIHLEDVIEvegffkgELVRIFDEEGNLLAIARA 52
 
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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