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Conserved domains on  [gi|1082860117|gb|OGB73115|]
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pseudouridine synthase [Burkholderiales bacterium RIFOXYC12_FULL_65_23]

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 ...
2-220 3.16e-106

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 cd02563:

Pssm-ID: 469624 [Multi-domain]  Cd Length: 223  Bit Score: 305.80  E-value: 3.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERGE 81
Cdd:cd02563     1 LEILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQHVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEHR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  82 aMRKSYRAVVRGWPPESGVIDHPLKRMPDDM----RTEREEVQDALTHYRLLERYELPLAQGAFTSTRCALVELQPVTGR 157
Cdd:cd02563    81 -VHKTYLAVVRGYVPESGTIDYPLSEELDKLadkfASDDKAPQAATTHYRLLAVEELPVVVGKYPTSRYSLVELTPHTGR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 158 RHQLRRHMKHIAHPIIGDATHGKGPLNRALAELLGLQRLWLHAGRLELTHPVTGQPLLIEAAP 220
Cdd:cd02563   160 KHQLRRHLAHIRHPIIGDTTHGDGRHNRFFREHFGCHRLLLAATRLEFTHPVTGERLLIEAPL 222
 
Name Accession Description Interval E-value
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
2-220 3.16e-106

tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved.


Pssm-ID: 211333 [Multi-domain]  Cd Length: 223  Bit Score: 305.80  E-value: 3.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERGE 81
Cdd:cd02563     1 LEILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQHVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEHR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  82 aMRKSYRAVVRGWPPESGVIDHPLKRMPDDM----RTEREEVQDALTHYRLLERYELPLAQGAFTSTRCALVELQPVTGR 157
Cdd:cd02563    81 -VHKTYLAVVRGYVPESGTIDYPLSEELDKLadkfASDDKAPQAATTHYRLLAVEELPVVVGKYPTSRYSLVELTPHTGR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 158 RHQLRRHMKHIAHPIIGDATHGKGPLNRALAELLGLQRLWLHAGRLELTHPVTGQPLLIEAAP 220
Cdd:cd02563   160 KHQLRRHLAHIRHPIIGDTTHGDGRHNRFFREHFGCHRLLLAATRLEFTHPVTGERLLIEAPL 222
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
1-224 4.83e-100

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 291.57  E-value: 4.83e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   1 MLTILYRDDYLVSVAKPPGLLVHRTGLDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERG 80
Cdd:PRK11112    1 MLEILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQHVFTAHRLDRPTSGVLLMALSSEVARLLAQQFEQH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  81 EaMRKSYRAVVRGWPPESGVIDHPLK----RMPDDMRTEREEVQDALTHYRLLERYELPLAQGAFTSTRCALVELQPVTG 156
Cdd:PRK11112   81 Q-IQKTYHAIVRGWLMEEAVLDYPLKeeldKIADKFAREDKAPQPAVTHYRGLATVEMPVATGRYPTTRYSLVELEPKTG 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082860117 157 RRHQLRRHMKHIAHPIIGDATHGKGPLNRALAELLGLQRLWLHAGRLELTHPVTGQPLLIEAAPGEEW 224
Cdd:PRK11112  160 RKHQLRRHMAHLRHPIIGDTKHGDLRQNRSLAEHFGCSRLMLHASELSLTHPFTGEPLTITAGLDETW 227
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
4-227 3.55e-77

Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and biogenesis]; Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440330 [Multi-domain]  Cd Length: 218  Bit Score: 231.95  E-value: 3.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   4 ILYRDDYLVSVAKPPGLLVHRTGLDAGETrfALQLLRDQIG-----RPVWPVHRLDKGTSGVLLFALDAATARALGLAFE 78
Cdd:COG0564     1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGT--LVNALRAHLGelsgvPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  79 RGEaMRKSYRAVVRGWPPE-SGVIDHPLKRMPDD---MRTEREEVQDALTHYRLLERYElplaqgaftstRCALVELQPV 154
Cdd:COG0564    79 ERE-VEKRYLALVEGKPKEdEGTIDAPLGRDPKDrkkMAVVDEDGKPAVTHYRVLERFG-----------GYSLVEVRLE 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 155 TGRRHQLRRHMKHIAHPIIGDATHGKGPLNRalaeLLGLQRLWLHAGRLELTHPVTGQPLLIEAAPGEEWARW 227
Cdd:COG0564   147 TGRTHQIRVHLAHIGHPIVGDPLYGGDRSNR----LLGLDRQALHAYRLGFPHPVTGEPLEFEAPLPEDFQAL 215
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
2-218 9.48e-50

pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161659 [Multi-domain]  Cd Length: 299  Bit Score: 164.42  E-value: 9.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETRF-ALQLLRDQIG--RPVWPVHRLDKGTSGVLLFALDAATARALGLAFE 78
Cdd:TIGR00005  72 LDILFEDEDIIVINKPSGLVVHPGGGNPFGTVLnALLAHCPPIAgvERVGIVHRLDRDTSGLMVVAKTPLALRELQRQLK 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  79 RGEaMRKSYRAVVRG-WPPESGVIDHPLKRMPDDmRTER-----EEVQDALTHYRLLERYElplaqgaftstRCALVELQ 152
Cdd:TIGR00005 152 NRT-VTKEYVALVHGqFDSGGGTVDAPLGRVPNN-RGLMavhpsSEGKPAVTHFRVLERFG-----------NASLVECE 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082860117 153 PVTGRRHQLRRHMKHIAHPIIGDATHGKGPLNRALAE-LLGLQRLWLHAGRLELTHPVTGQPLLIEA 218
Cdd:TIGR00005 219 LETGRTHQIRVHLQYLGHPLAGDPLYGNKPVPGNNLNgLLNFDRQALHAYELGFIHPATGEILEFEA 285
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
10-167 7.00e-34

RNA pseudouridylate synthase; 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 RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.


Pssm-ID: 459961 [Multi-domain]  Cd Length: 151  Bit Score: 119.05  E-value: 7.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  10 YLVsVAKPPGLLVHRTG-LDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERGEaMRKSYR 88
Cdd:pfam00849   1 YIV-VNKPAGVPVHPTDsLTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERK-IEKEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  89 AVVRGWPPESGVIDHPLKRMPDDMRTEREEVQD---ALTHYRLLERyelplaqgaFTSTRCALVELQPVTGRRHQLRRHM 165
Cdd:pfam00849  79 ALVDKPEEEEGTIKSPIKKEKNKSPFRKEEELGgkkAVTHLKVLKS---------GSKGDYSLLELELVTGRKHQIRAHL 149

                  ..
gi 1082860117 166 KH 167
Cdd:pfam00849 150 AA 151
 
Name Accession Description Interval E-value
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
2-220 3.16e-106

tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved.


Pssm-ID: 211333 [Multi-domain]  Cd Length: 223  Bit Score: 305.80  E-value: 3.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERGE 81
Cdd:cd02563     1 LEILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQHVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEHR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  82 aMRKSYRAVVRGWPPESGVIDHPLKRMPDDM----RTEREEVQDALTHYRLLERYELPLAQGAFTSTRCALVELQPVTGR 157
Cdd:cd02563    81 -VHKTYLAVVRGYVPESGTIDYPLSEELDKLadkfASDDKAPQAATTHYRLLAVEELPVVVGKYPTSRYSLVELTPHTGR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 158 RHQLRRHMKHIAHPIIGDATHGKGPLNRALAELLGLQRLWLHAGRLELTHPVTGQPLLIEAAP 220
Cdd:cd02563   160 KHQLRRHLAHIRHPIIGDTTHGDGRHNRFFREHFGCHRLLLAATRLEFTHPVTGERLLIEAPL 222
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
1-224 4.83e-100

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 291.57  E-value: 4.83e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   1 MLTILYRDDYLVSVAKPPGLLVHRTGLDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERG 80
Cdd:PRK11112    1 MLEILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQHVFTAHRLDRPTSGVLLMALSSEVARLLAQQFEQH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  81 EaMRKSYRAVVRGWPPESGVIDHPLK----RMPDDMRTEREEVQDALTHYRLLERYELPLAQGAFTSTRCALVELQPVTG 156
Cdd:PRK11112   81 Q-IQKTYHAIVRGWLMEEAVLDYPLKeeldKIADKFAREDKAPQPAVTHYRGLATVEMPVATGRYPTTRYSLVELEPKTG 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082860117 157 RRHQLRRHMKHIAHPIIGDATHGKGPLNRALAELLGLQRLWLHAGRLELTHPVTGQPLLIEAAPGEEW 224
Cdd:PRK11112  160 RKHQLRRHMAHLRHPIIGDTKHGDLRQNRSLAEHFGCSRLMLHASELSLTHPFTGEPLTITAGLDETW 227
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
4-227 3.55e-77

Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and biogenesis]; Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440330 [Multi-domain]  Cd Length: 218  Bit Score: 231.95  E-value: 3.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   4 ILYRDDYLVSVAKPPGLLVHRTGLDAGETrfALQLLRDQIG-----RPVWPVHRLDKGTSGVLLFALDAATARALGLAFE 78
Cdd:COG0564     1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGT--LVNALRAHLGelsgvPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  79 RGEaMRKSYRAVVRGWPPE-SGVIDHPLKRMPDD---MRTEREEVQDALTHYRLLERYElplaqgaftstRCALVELQPV 154
Cdd:COG0564    79 ERE-VEKRYLALVEGKPKEdEGTIDAPLGRDPKDrkkMAVVDEDGKPAVTHYRVLERFG-----------GYSLVEVRLE 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 155 TGRRHQLRRHMKHIAHPIIGDATHGKGPLNRalaeLLGLQRLWLHAGRLELTHPVTGQPLLIEAAPGEEWARW 227
Cdd:COG0564   147 TGRTHQIRVHLAHIGHPIVGDPLYGGDRSNR----LLGLDRQALHAYRLGFPHPVTGEPLEFEAPLPEDFQAL 215
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
10-205 2.88e-52

Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli.


Pssm-ID: 211346 [Multi-domain]  Cd Length: 185  Bit Score: 167.51  E-value: 2.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  10 YLVsVAKPPGLLVHRTGLDAGETRFALQLLRDQI---GRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERGEaMRKS 86
Cdd:cd02869     1 LLV-VNKPAGLPVHPGPGHLTGTLVNALLKLLLLlgeEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERK-VKKT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  87 YRAVVRG-WPPESGVIDHPLKRMPDD---MRTEREEVQDALTHYRLLERYElplaqgaftstRCALVELQPVTGRRHQLR 162
Cdd:cd02869    79 YLALVDGkPPEDEGTIDAPLGRKKRKkraRVVVSEDGKPAITHYKVLERFG-----------NVTLVELQLETGRTHQIR 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1082860117 163 RHMKHIAHPIIGDATHGKGPLNRalaelLGLQRLWLHAGRLEL 205
Cdd:cd02869   148 VHLASIGHPIVGDPKYGGKASDS-----PGLKRLALHAYRLSF 185
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
2-218 9.48e-50

pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161659 [Multi-domain]  Cd Length: 299  Bit Score: 164.42  E-value: 9.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETRF-ALQLLRDQIG--RPVWPVHRLDKGTSGVLLFALDAATARALGLAFE 78
Cdd:TIGR00005  72 LDILFEDEDIIVINKPSGLVVHPGGGNPFGTVLnALLAHCPPIAgvERVGIVHRLDRDTSGLMVVAKTPLALRELQRQLK 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  79 RGEaMRKSYRAVVRG-WPPESGVIDHPLKRMPDDmRTER-----EEVQDALTHYRLLERYElplaqgaftstRCALVELQ 152
Cdd:TIGR00005 152 NRT-VTKEYVALVHGqFDSGGGTVDAPLGRVPNN-RGLMavhpsSEGKPAVTHFRVLERFG-----------NASLVECE 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082860117 153 PVTGRRHQLRRHMKHIAHPIIGDATHGKGPLNRALAE-LLGLQRLWLHAGRLELTHPVTGQPLLIEA 218
Cdd:TIGR00005 219 LETGRTHQIRVHLQYLGHPLAGDPLYGNKPVPGNNLNgLLNFDRQALHAYELGFIHPATGEILEFEA 285
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
10-167 7.00e-34

RNA pseudouridylate synthase; 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 RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.


Pssm-ID: 459961 [Multi-domain]  Cd Length: 151  Bit Score: 119.05  E-value: 7.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  10 YLVsVAKPPGLLVHRTG-LDAGETRFALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFERGEaMRKSYR 88
Cdd:pfam00849   1 YIV-VNKPAGVPVHPTDsLTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERK-IEKEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  89 AVVRGWPPESGVIDHPLKRMPDDMRTEREEVQD---ALTHYRLLERyelplaqgaFTSTRCALVELQPVTGRRHQLRRHM 165
Cdd:pfam00849  79 ALVDKPEEEEGTIKSPIKKEKNKSPFRKEEELGgkkAVTHLKVLKS---------GSKGDYSLLELELVTGRKHQIRAHL 149

                  ..
gi 1082860117 166 KH 167
Cdd:pfam00849 150 AA 151
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
4-218 9.22e-34

23S rRNA pseudouridine(955/2504/2580) synthase RluC;


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 123.69  E-value: 9.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   4 ILYRDDYLVSVAKPPGLLVHR-TGLDAGETRfALQLLRDQiGRPVWPVHRLDKGTSGVLLFALDAATARALGLAFeRGEA 82
Cdd:PRK11025   95 ILYEDDHILVLNKPSGTAVHGgSGLSFGVIE-GLRALRPE-ARFLELVHRLDRDTSGVLLVAKKRSALRSLHEQL-REKG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  83 MRKSYRAVVRG-WPPESGVIDHPLKR--MPDDMRTER--EEVQDALTHYRLLERYELplaqgaftstrCALVELQPVTGR 157
Cdd:PRK11025  172 MQKDYLALVRGqWQSHVKVVQAPLLKniLQSGERIVRvsQEGKPSETRFKVEERYAF-----------ATLVRASPVTGR 240
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082860117 158 RHQLRRHMKHIAHPIIGDATHGKGPLNRALAElLGLQRLWLHAGRLELTHPVTGQPLLIEA 218
Cdd:PRK11025  241 THQIRVHTQYAGHPIAFDDRYGDREFDQQLTG-TGLNRLFLHAAALKFTHPGTGEVMRIEA 300
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
4-207 1.01e-32

Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, Saccharomyces cerevisiae RIB2_like. This group is comprised of eukaryotic and bacterial proteins similar to Saccharomyces cerevisiae RIB2, S. cerevisiae Pus6p and human hRPUDSD2. S. cerevisiae RIB2 displays two distinct catalytic activities. The N-terminal domain of RIB2 is RNA:psi-synthase which makes psi32 on cytoplasmic tRNAs. Psi32 is highly phylogenetically conserved. The C-terminal domain of RIB2 has a DRAP deaminase activity which catalyses the formation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate from 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate during riboflavin biosynthesis. S. cerevisiae Pus6p makes the psi31 of cytoplasmic and mitochondrial tRNAs.


Pssm-ID: 211331 [Multi-domain]  Cd Length: 213  Bit Score: 118.12  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   4 ILYRDDYLVSVAKPPGLLVHRTGldagetRFA----LQLLRDQIG-RPVWPVHRLDKGTSGVLLFALDAATARALGLAFE 78
Cdd:cd02557    18 IVHEDDDLLVVDKPSGIPVHPTG------RYRyntvTEILKSEYGlTELRPCHRLDRLTSGLLLFAKTSQTASRLQQQIR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  79 RGEaMRKSYRAVVRG-WPPESGVIDHP--LKRMPDDMR-TEREEVQDALTHYRLLeRYELPLAQgaftstrcALVELQPV 154
Cdd:cd02557    92 SRE-VKKEYLARVKGeFPDGEVVVDQPigLVSPKGGLRnDVDEKGKDARTIFKRL-SYNGDLNT--------SVVLCKPI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 155 TGRRHQLRRHMKHIAHPIIGDathgkgPLNRALAellglqrLWLHAGRLELTH 207
Cdd:cd02557   162 TGRTHQIRVHLQYLGHPIVND------PIYNNLG-------IYLHALRYEGPD 201
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
2-218 2.19e-28

bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 107.00  E-value: 2.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETRFALQLLRDqigrpvWP----VHRLDKGTSGVLLFALDAATARALGLAF 77
Cdd:PRK10158   14 LVILYQDEHIMVVNKPSGLLSVPGRLEEHKDSVMTRIQRD------YPqaesVHRLDMATSGVIVVALTKAAERELKRQF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  78 ERGEAmRKSYRAVVRGWP-PESGVIDHPLkrMPDDMRTEREEV-----QDALTHYRLLEryelplaqgaFTSTRCALVEL 151
Cdd:PRK10158   88 REREP-KKQYVARVWGHPsPAEGLVDLPL--ICDWPNRPKQKVcyetgKPAQTEYEVVE----------YAADNTARVVL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082860117 152 QPVTGRRHQLRRHMKHIAHPIIGDATHGKgPLNRALAEllglqRLWLHAGRLELTHPVTGQPLLIEA 218
Cdd:PRK10158  155 KPITGRSHQLRVHMLALGHPILGDRFYAS-PEARAMAP-----RLLLHAEMLTITHPAYGNSMTFKA 215
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
2-211 1.57e-26

23S rRNA pseudouridine(1911/1915/1917) synthase RluD;


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 104.37  E-value: 1.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVH-------RTGLDAgetrfalqLL----------RDQIgrpvwpVHRLDKGTSGVLLFA 64
Cdd:PRK11180   84 LDIVYEDDDILVINKPRDLVVHpgagnpdGTVLNA--------LLhyyppiadvpRAGI------VHRLDKDTTGLMVVA 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  65 LDAATARALGLAFERGEAMRKsYRAVVRGWPPESGVIDHPLKRMPddmrTEREEV------QDALTHYRLLERYElplaq 138
Cdd:PRK11180  150 KTVPAQTRLVEALQKREITRE-YEAVAIGHMTAGGTVDEPISRHP----TKRTHMavhpmgKPAVTHYRIMEHFR----- 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082860117 139 gAFTSTRcalveLQPVTGRRHQLRRHMKHIAHPIIGDATHG------KGPLNRALAELLGLQRLWLHAGRLELTHPVTG 211
Cdd:PRK11180  220 -VHTRLR-----LRLETGRTHQIRVHMAHITHPLVGDQVYGgrprppKGASEEFISTLRKFDRQALHATMLRLYHPITG 292
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
11-172 1.05e-25

Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli.


Pssm-ID: 211325 [Multi-domain]  Cd Length: 154  Bit Score: 98.21  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  11 LVSVAKPPGLLVHRTGLDAGETrfALQLLRDQIGRPVWPVHRLDKGTSGVLLFALDAATARALGlafERGEAMRKSYRAV 90
Cdd:cd02550     1 ILVLNKPSGLVCHPTDRDRDPT--VVVRLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLT---EPRREIEKEYLVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  91 VRGWPPESGVIDHPLKRMPDDMRTEREEVQDALTHYRLLERYElplaqgaftstRCALVELQPVTGRRHQLRRHMKHIAH 170
Cdd:cd02550    76 VRGELDEEGIEDLATVRRGRLSGLVDEGVPLAVTKVRVIGEHG-----------GTGRLRLTLKTGRTHQIRRHCAAVGF 144

                  ..
gi 1082860117 171 PI 172
Cdd:cd02550   145 PV 146
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
2-219 9.16e-22

Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial proteins assigned to the RluA family of pseudouridine synthases. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. The RluA family is comprised of proteins related to Escherichia coli RluA.


Pssm-ID: 211332 [Multi-domain]  Cd Length: 246  Bit Score: 90.02  E-value: 9.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117   2 LTILYRDDYLVSVAKPPGLLVHRTGLDAGETrfALQLLRDQIGRP-VWPVHRLDKGTSGVLLFALDAATARALGLAFERG 80
Cdd:cd02558    39 ETILHQDEHLLVADKPHFLPVTPRGRYVTET--LLVRLRRQTGNPdLTPAHRLDRLTAGLVLFSKRPETRGAYQTLFARR 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860117  81 EAmRKSYRAVVRgWPPESG----VIDHPLKRMPDDMRTEREEVQDALTHYRLLERyelplaqgaftSTRCALVELQPVTG 156
Cdd:cd02558   117 EV-SKTYEAVAP-YVPALTfpltVRSRIVKGRGFFQAREVEGEPNAETRIELLAR-----------RGGWGLYRLSPHTG 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860117 157 RRHQLRRHMKHIAHPIIGDATHgkgPLNRALAELLGLQRLWLHAGRLELTHPVTGQPLLIEAA 219
Cdd:cd02558   184 KTHQLRVHMAALGVPILNDPFY---PVLLDKDPDDFSRPLQLLAKELEFTDPLTGRPRRFESG 243
 
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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