NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|740841778|ref|WP_038627031|]
View 

MULTISPECIES: pseudouridine synthase [Corynebacterium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
60-325 8.35e-102

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 cd02558:

Pssm-ID: 469624 [Multi-domain]  Cd Length: 246  Bit Score: 299.57  E-value: 8.35e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  60 GLVVRANSVPYSPDDMVKPGAEMWFYRTPAPERTIAGPMPIVFQDDNLVVVDKPSFLATMPRGRHITETAVVRLRRELGN 139
Cdd:cd02558    1 GLVVDADGEPLDPDSPYRPGTFVWYYRELPDEPPIPFEETILHQDEHLLVADKPHFLPVTPRGRYVTETLLVRLRRQTGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 140 PELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGEVTKRYHALTSPTPiagatseALPeTPLELRTRQHKVAGQMQAY 219
Cdd:cd02558   81 PDLTPAHRLDRLTAGLVLFSKRPETRGAYQTLFARREVSKTYEAVAPYVP-------ALT-FPLTVRSRIVKGRGFFQAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 220 TLEGEPNAHTIIEhislvdvpsdaddLAADSGRVALWQLKPITGRTHQLRLHLSELGFPILGDQYYPEILPLEAENTSEP 299
Cdd:cd02558  153 EVEGEPNAETRIE-------------LLARRGGWGLYRLSPHTGKTHQLRVHMAALGVPILNDPFYPVLLDKDPDDFSRP 219
                        250       260
                 ....*....|....*....|....*.
gi 740841778 300 LHLVCVEMSFADPVTGEQRTFHSRRS 325
Cdd:cd02558  220 LQLLAKELEFTDPLTGRPRRFESGRS 245
 
Name Accession Description Interval E-value
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
60-325 8.35e-102

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: 299.57  E-value: 8.35e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  60 GLVVRANSVPYSPDDMVKPGAEMWFYRTPAPERTIAGPMPIVFQDDNLVVVDKPSFLATMPRGRHITETAVVRLRRELGN 139
Cdd:cd02558    1 GLVVDADGEPLDPDSPYRPGTFVWYYRELPDEPPIPFEETILHQDEHLLVADKPHFLPVTPRGRYVTETLLVRLRRQTGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 140 PELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGEVTKRYHALTSPTPiagatseALPeTPLELRTRQHKVAGQMQAY 219
Cdd:cd02558   81 PDLTPAHRLDRLTAGLVLFSKRPETRGAYQTLFARREVSKTYEAVAPYVP-------ALT-FPLTVRSRIVKGRGFFQAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 220 TLEGEPNAHTIIEhislvdvpsdaddLAADSGRVALWQLKPITGRTHQLRLHLSELGFPILGDQYYPEILPLEAENTSEP 299
Cdd:cd02558  153 EVEGEPNAETRIE-------------LLARRGGWGLYRLSPHTGKTHQLRVHMAALGVPILNDPFYPVLLDKDPDDFSRP 219
                        250       260
                 ....*....|....*....|....*.
gi 740841778 300 LHLVCVEMSFADPVTGEQRTFHSRRS 325
Cdd:cd02558  220 LQLLAKELEFTDPLTGRPRRFESGRS 245
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
100-322 1.91e-40

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: 141.43  E-value: 1.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 100 IVFQDDNLVVVDKPSFLATMPRGRHITETAVVRLR----RELGNPELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASG 175
Cdd:COG0564    1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRahlgELSGVPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 176 EVTKRYHALTSPTPiagATSEALPETPLElrtRQHKVAGQMQAYTLEGEPnAHTiieHISLVDVpsdaddlaadSGRVAL 255
Cdd:COG0564   81 EVEKRYLALVEGKP---KEDEGTIDAPLG---RDPKDRKKMAVVDEDGKP-AVT---HYRVLER----------FGGYSL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740841778 256 WQLKPITGRTHQLRLHLSELGFPILGDQYY--PEILPLEAENtsePLHLVCVEMSFADPVTGEQRTFHS 322
Cdd:COG0564  141 VEVRLETGRTHQIRVHLAHIGHPIVGDPLYggDRSNRLLGLD---RQALHAYRLGFPHPVTGEPLEFEA 206
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
52-322 2.51e-34

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: 127.82  E-value: 2.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778   52 AVAKRFADGLVVRANSVPYSPDDMVKPGAEMwFYRTPAPER----TIAGPMPIVFQDDNLVVVDKPSFLATMPRGRHITE 127
Cdd:TIGR00005  23 RIQKLIENGQVKVNGKVTANPKLKVKDGDRI-TVRVPEEEEhevpPQDIPLDILFEDEDIIVINKPSGLVVHPGGGNPFG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  128 TAVVRLRRELGNPELV----PAHRLDRLTSGLLIFT----ARREVRGAyqglFASGEVTKRYHALTSPTPiagATSEALP 199
Cdd:TIGR00005 102 TVLNALLAHCPPIAGVervgIVHRLDRDTSGLMVVAktplALRELQRQ----LKNRTVTKEYVALVHGQF---DSGGGTV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  200 ETPLElrtrqhKVAGQMQAYTLEGEPNAHTIIEHISLVdvpsdaddlaADSGRVALWQLKPITGRTHQLRLHLSELGFPI 279
Cdd:TIGR00005 175 DAPLG------RVPNNRGLMAVHPSSEGKPAVTHFRVL----------ERFGNASLVECELETGRTHQIRVHLQYLGHPL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 740841778  280 LGDQYY---PEILPLEAENTSEP---LHLvcVEMSFADPVTGEQRTFHS 322
Cdd:TIGR00005 239 AGDPLYgnkPVPGNNLNGLLNFDrqaLHA--YELGFIHPATGEILEFEA 285
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
107-273 7.40e-21

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: 87.46  E-value: 7.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  107 LVVVDKPSFLATMPRGRHITETAVVR--LRRELGNPELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGEVTKRYHAL 184
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDSLTKLLSLLAllLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  185 TSptpiAGATSEALPETPLELRtrqHKVAGQMQAYTLeGEPNAHTIIEHISlvdvpsdaddlAADSGRVALWQLKPITGR 264
Cdd:pfam00849  81 VD----KPEEEEGTIKSPIKKE---KNKSPFRKEEEL-GGKKAVTHLKVLK-----------SGSKGDYSLLELELVTGR 141

                  ....*....
gi 740841778  265 THQLRLHLS 273
Cdd:pfam00849 142 KHQIRAHLA 150
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
100-323 2.14e-20

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 88.95  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 100 IVFQDDNLVVVDKP-------SFLAtmprgRHITETAVVRLRRELGNpELVPAHRLDRLTSGLLIFTARREVRGAYQGLF 172
Cdd:PRK11112   4 ILYQDEWLVAVNKPagwlvhrSWLD-----RHETVFVMQTVRDQIGQ-HVFTAHRLDRPTSGVLLMALSSEVARLLAQQF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 173 ASGEVTKRYHALtsptpIAGATSEAlPETPLELRTRQHKVAGQMQAYTLEGEPnAHTIIEHISLVDVPSDADDLAadSGR 252
Cdd:PRK11112  78 EQHQIQKTYHAI-----VRGWLMEE-AVLDYPLKEELDKIADKFAREDKAPQP-AVTHYRGLATVEMPVATGRYP--TTR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740841778 253 VALWQLKPITGRTHQLRLHLSELGFPILGDQYYPEILP--LEAENTSEP-LHLVCVEMSFADPVTGEQRTFHSR 323
Cdd:PRK11112 149 YSLVELEPKTGRKHQLRRHMAHLRHPIIGDTKHGDLRQnrSLAEHFGCSrLMLHASELSLTHPFTGEPLTITAG 222
 
Name Accession Description Interval E-value
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
60-325 8.35e-102

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: 299.57  E-value: 8.35e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  60 GLVVRANSVPYSPDDMVKPGAEMWFYRTPAPERTIAGPMPIVFQDDNLVVVDKPSFLATMPRGRHITETAVVRLRRELGN 139
Cdd:cd02558    1 GLVVDADGEPLDPDSPYRPGTFVWYYRELPDEPPIPFEETILHQDEHLLVADKPHFLPVTPRGRYVTETLLVRLRRQTGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 140 PELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGEVTKRYHALTSPTPiagatseALPeTPLELRTRQHKVAGQMQAY 219
Cdd:cd02558   81 PDLTPAHRLDRLTAGLVLFSKRPETRGAYQTLFARREVSKTYEAVAPYVP-------ALT-FPLTVRSRIVKGRGFFQAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 220 TLEGEPNAHTIIEhislvdvpsdaddLAADSGRVALWQLKPITGRTHQLRLHLSELGFPILGDQYYPEILPLEAENTSEP 299
Cdd:cd02558  153 EVEGEPNAETRIE-------------LLARRGGWGLYRLSPHTGKTHQLRVHMAALGVPILNDPFYPVLLDKDPDDFSRP 219
                        250       260
                 ....*....|....*....|....*.
gi 740841778 300 LHLVCVEMSFADPVTGEQRTFHSRRS 325
Cdd:cd02558  220 LQLLAKELEFTDPLTGRPRRFESGRS 245
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
100-322 1.91e-40

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: 141.43  E-value: 1.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 100 IVFQDDNLVVVDKPSFLATMPRGRHITETAVVRLR----RELGNPELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASG 175
Cdd:COG0564    1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRahlgELSGVPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFRER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 176 EVTKRYHALTSPTPiagATSEALPETPLElrtRQHKVAGQMQAYTLEGEPnAHTiieHISLVDVpsdaddlaadSGRVAL 255
Cdd:COG0564   81 EVEKRYLALVEGKP---KEDEGTIDAPLG---RDPKDRKKMAVVDEDGKP-AVT---HYRVLER----------FGGYSL 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740841778 256 WQLKPITGRTHQLRLHLSELGFPILGDQYY--PEILPLEAENtsePLHLVCVEMSFADPVTGEQRTFHS 322
Cdd:COG0564  141 VEVRLETGRTHQIRVHLAHIGHPIVGDPLYggDRSNRLLGLD---RQALHAYRLGFPHPVTGEPLEFEA 206
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
107-309 4.15e-35

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: 126.30  E-value: 4.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 107 LVVVDKPSFLATMPRGRHITETAVVRL----RRELGNPELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGEVTKRYH 182
Cdd:cd02869    1 LLVVNKPAGLPVHPGPGHLTGTLVNALlkllLLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 183 ALTSPTPIAGATSEALPETPLELRTRQHKVagqmqayTLEGEPNAHTiieHISLVDVpsdaddlaadSGRVALWQLKPIT 262
Cdd:cd02869   81 ALVDGKPPEDEGTIDAPLGRKKRKKRARVV-------VSEDGKPAIT---HYKVLER----------FGNVTLVELQLET 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 740841778 263 GRTHQLRLHLSELGFPILGDQYYpeILPLEAENTSEPLHLVCVEMSF 309
Cdd:cd02869  141 GRTHQIRVHLASIGHPIVGDPKY--GGKASDSPGLKRLALHAYRLSF 185
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
52-322 2.51e-34

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: 127.82  E-value: 2.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778   52 AVAKRFADGLVVRANSVPYSPDDMVKPGAEMwFYRTPAPER----TIAGPMPIVFQDDNLVVVDKPSFLATMPRGRHITE 127
Cdd:TIGR00005  23 RIQKLIENGQVKVNGKVTANPKLKVKDGDRI-TVRVPEEEEhevpPQDIPLDILFEDEDIIVINKPSGLVVHPGGGNPFG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  128 TAVVRLRRELGNPELV----PAHRLDRLTSGLLIFT----ARREVRGAyqglFASGEVTKRYHALTSPTPiagATSEALP 199
Cdd:TIGR00005 102 TVLNALLAHCPPIAGVervgIVHRLDRDTSGLMVVAktplALRELQRQ----LKNRTVTKEYVALVHGQF---DSGGGTV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  200 ETPLElrtrqhKVAGQMQAYTLEGEPNAHTIIEHISLVdvpsdaddlaADSGRVALWQLKPITGRTHQLRLHLSELGFPI 279
Cdd:TIGR00005 175 DAPLG------RVPNNRGLMAVHPSSEGKPAVTHFRVL----------ERFGNASLVECELETGRTHQIRVHLQYLGHPL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 740841778  280 LGDQYY---PEILPLEAENTSEP---LHLvcVEMSFADPVTGEQRTFHS 322
Cdd:TIGR00005 239 AGDPLYgnkPVPGNNLNGLLNFDrqaLHA--YELGFIHPATGEILEFEA 285
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
97-307 1.62e-31

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: 117.73  E-value: 1.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  97 PMPIVFQDDNLVVVDKPSFLATMPRGRHITETAVVRLRRELGNPELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGE 176
Cdd:cd02557   15 PIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTSQTASRLQQQIRSRE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 177 VTKRYHALtsptpIAGATSEALPET--PLELRTRQHKVAGQMqaytLEGEPNAHTIIEHISlvdvpSDADDlaaDSGRVa 254
Cdd:cd02557   95 VKKEYLAR-----VKGEFPDGEVVVdqPIGLVSPKGGLRNDV----DEKGKDARTIFKRLS-----YNGDL---NTSVV- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 740841778 255 lwQLKPITGRTHQLRLHLSELGFPILGDQYY-PEILPLEAENTSEPLHLVCVEM 307
Cdd:cd02557  157 --LCKPITGRTHQIRVHLQYLGHPIVNDPIYnNLGIYLHALRYEGPDWSYETEL 208
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
98-316 2.36e-28

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: 109.73  E-value: 2.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  98 MPIVFQDDNLVVVDKPS--FLATMPRGRHITETAVVRLRRELGNpELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASG 175
Cdd:cd02563    1 LEILYQDEHLVAINKPSglLVHRSELDRHETRFALQTLRDQLGQ-HVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 176 EVTKRYHALTSP-TPIAGATSEALPEtplELRTRQHKVAGQmqaytlEGEPNAHTIieHISLVDVPS-DADDLAADSGRV 253
Cdd:cd02563   80 RVHKTYLAVVRGyVPESGTIDYPLSE---ELDKLADKFASD------DKAPQAATT--HYRLLAVEElPVVVGKYPTSRY 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 254 ALWQLKPITGRTHQLRLHLSELGFPILGDQYYPEilplEAEN-------TSEPLHLVCVEMSFADPVTGE 316
Cdd:cd02563  149 SLVELTPHTGRKHQLRRHLAHIRHPIIGDTTHGD----GRHNrffrehfGCHRLLLAATRLEFTHPVTGE 214
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
107-273 7.40e-21

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: 87.46  E-value: 7.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  107 LVVVDKPSFLATMPRGRHITETAVVR--LRRELGNPELVPAHRLDRLTSGLLIFTARREVRGAYQGLFASGEVTKRYHAL 184
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDSLTKLLSLLAllLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  185 TSptpiAGATSEALPETPLELRtrqHKVAGQMQAYTLeGEPNAHTIIEHISlvdvpsdaddlAADSGRVALWQLKPITGR 264
Cdd:pfam00849  81 VD----KPEEEEGTIKSPIKKE---KNKSPFRKEEEL-GGKKAVTHLKVLK-----------SGSKGDYSLLELELVTGR 141

                  ....*....
gi 740841778  265 THQLRLHLS 273
Cdd:pfam00849 142 KHQIRAHLA 150
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
100-323 2.14e-20

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 88.95  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 100 IVFQDDNLVVVDKP-------SFLAtmprgRHITETAVVRLRRELGNpELVPAHRLDRLTSGLLIFTARREVRGAYQGLF 172
Cdd:PRK11112   4 ILYQDEWLVAVNKPagwlvhrSWLD-----RHETVFVMQTVRDQIGQ-HVFTAHRLDRPTSGVLLMALSSEVARLLAQQF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 173 ASGEVTKRYHALtsptpIAGATSEAlPETPLELRTRQHKVAGQMQAYTLEGEPnAHTIIEHISLVDVPSDADDLAadSGR 252
Cdd:PRK11112  78 EQHQIQKTYHAI-----VRGWLMEE-AVLDYPLKEELDKIADKFAREDKAPQP-AVTHYRGLATVEMPVATGRYP--TTR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740841778 253 VALWQLKPITGRTHQLRLHLSELGFPILGDQYYPEILP--LEAENTSEP-LHLVCVEMSFADPVTGEQRTFHSR 323
Cdd:PRK11112 149 YSLVELEPKTGRKHQLRRHMAHLRHPIIGDTKHGDLRQnrSLAEHFGCSrLMLHASELSLTHPFTGEPLTITAG 222
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
107-280 7.70e-19

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: 82.04  E-value: 7.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 107 LVVVDKPSFLATMPRGRHITETAVVRLRRELGnPELVPAHRLDRLTSGLLIFTarREVRGAYQGLFASGEVTKRYHAlTS 186
Cdd:cd02550    1 ILVLNKPSGLVCHPTDRDRDPTVVVRLDKLHG-PRVHAAGRLDKDTSGLLLLT--NDGRLQRRLTEPRREIEKEYLV-TV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 187 PTPIAGATSEALPEtplelrtrqhKVAGQMQAYTLEGEPNAHTIIEHIslvdvpsdaddlaADSGRVALWQLKPITGRTH 266
Cdd:cd02550   77 RGELDEEGIEDLAT----------VRRGRLSGLVDEGVPLAVTKVRVI-------------GEHGGTGRLRLTLKTGRTH 133
                        170
                 ....*....|....
gi 740841778 267 QLRLHLSELGFPIL 280
Cdd:cd02550  134 QIRRHCAAVGFPVL 147
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
100-320 1.36e-17

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 80.42  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 100 IVFQDDNLVVVDKPSFLATMP-RGRHITETAVVRLRRELGNPELVpaHRLDRLTSGLLIFTARREVRGAYQGLFASGEVT 178
Cdd:PRK10158  16 ILYQDEHIMVVNKPSGLLSVPgRLEEHKDSVMTRIQRDYPQAESV--HRLDMATSGVIVVALTKAAERELKRQFREREPK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 179 KRYHALT--SPTPIAGATSEAL----PETPlelrtrqhkvagqMQAYTLEGEPNAHTIIEhisLVDVPSDaddlaaDSGR 252
Cdd:PRK10158  94 KQYVARVwgHPSPAEGLVDLPLicdwPNRP-------------KQKVCYETGKPAQTEYE---VVEYAAD------NTAR 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740841778 253 ValwQLKPITGRTHQLRLHLSELGFPILGDQYYPEIlplEAENTSEPLHLVCVEMSFADPVTGEQRTF 320
Cdd:PRK10158 152 V---VLKPITGRSHQLRVHMLALGHPILGDRFYASP---EARAMAPRLLLHAEMLTITHPAYGNSMTF 213
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
97-321 1.73e-07

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


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 51.99  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778  97 PMPIVFQDDNLVVVDKPSFL-----ATMPRG-------RHITETAVVrlrrelgnPELVPAHRLDRLTSGLLIfTAR--- 161
Cdd:PRK11180  83 PLDIVYEDDDILVINKPRDLvvhpgAGNPDGtvlnallHYYPPIADV--------PRAGIVHRLDKDTTGLMV-VAKtvp 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 162 ---REVRgAYQglfaSGEVTKRYHALTSPTPIAGAT-SEALPETPLElrtRQHKVAGQMqaytleGEPnAHT---IIEHI 234
Cdd:PRK11180 154 aqtRLVE-ALQ----KREITREYEAVAIGHMTAGGTvDEPISRHPTK---RTHMAVHPM------GKP-AVThyrIMEHF 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 235 slvdvpsdaddlaadsgRV-ALWQLKPITGRTHQLRLHLSELGFPILGDQYY---PEILPLEAENTSEPLH------LVC 304
Cdd:PRK11180 219 -----------------RVhTRLRLRLETGRTHQIRVHMAHITHPLVGDQVYggrPRPPKGASEEFISTLRkfdrqaLHA 281
                        250
                 ....*....|....*..
gi 740841778 305 VEMSFADPVTGEQRTFH 321
Cdd:PRK11180 282 TMLRLYHPITGIEMEWH 298
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
100-285 2.41e-06

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 48.57  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 100 IVFQDDNLVVVDKPSFLATmpRGRHITETAVVR----LRRELGNPELVpaHRLDRLTSG-LLIFTARREVRGAYQGLFAS 174
Cdd:PRK11025  95 ILYEDDHILVLNKPSGTAV--HGGSGLSFGVIEglraLRPEARFLELV--HRLDRDTSGvLLVAKKRSALRSLHEQLREK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740841778 175 GeVTKRYHALtsptpiagatsealpetplelrtrqhkVAGQMQAYT-------LEGEPNAHTIIEHISLVDVPSDADDLA 247
Cdd:PRK11025 171 G-MQKDYLAL---------------------------VRGQWQSHVkvvqaplLKNILQSGERIVRVSQEGKPSETRFKV 222
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 740841778 248 ADSGRVA-LWQLKPITGRTHQLRLHLSELGFPILGDQYY 285
Cdd:PRK11025 223 EERYAFAtLVRASPVTGRTHQIRVHTQYAGHPIAFDDRY 261
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH