NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1022433253|ref|NP_001311015|]
View 

RNA pseudouridylate synthase domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

pseudouridine synthase family protein( domain architecture ID 10120734)

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_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
18-218 2.20e-55

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: 177.91  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  18 FLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELADPDTCYgfrFCHQLDFSTSGALCVALNKAAAGSAYRCFKERRVTK 97
Cdd:cd02869     1 LLVVNKPAGLPVHPGPGHLTGTLVNALLKLLLLLGEEFRPG---LVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  98 AYLALLRGHIQESRVTISHAIGRNSTEGRAHtmciegsqgVAGCENPKPSLTDLVVLEHGlyagDPVSKVLLKPLTGRTH 177
Cdd:cd02869    78 TYLALVDGKPPEDEGTIDAPLGRKKRKKRAR---------VVVSEDGKPAITHYKVLERF----GNVTLVELQLETGRTH 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1022433253 178 QLRVHCSALGHPVVGDLTYGEVSGREDRPFRMMLHAFYLRI 218
Cdd:cd02869   145 QIRVHLASIGHPIVGDPKYGGKASDSPGLKRLALHAYRLSF 185
 
Name Accession Description Interval E-value
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
18-218 2.20e-55

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: 177.91  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  18 FLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELADPDTCYgfrFCHQLDFSTSGALCVALNKAAAGSAYRCFKERRVTK 97
Cdd:cd02869     1 LLVVNKPAGLPVHPGPGHLTGTLVNALLKLLLLLGEEFRPG---LVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  98 AYLALLRGHIQESRVTISHAIGRNSTEGRAHtmciegsqgVAGCENPKPSLTDLVVLEHGlyagDPVSKVLLKPLTGRTH 177
Cdd:cd02869    78 TYLALVDGKPPEDEGTIDAPLGRKKRKKRAR---------VVVSEDGKPAITHYKVLERF----GNVTLVELQLETGRTH 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1022433253 178 QLRVHCSALGHPVVGDLTYGEVSGREDRPFRMMLHAFYLRI 218
Cdd:cd02869   145 QIRVHLASIGHPIVGDPKYGGKASDSPGLKRLALHAYRLSF 185
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
11-232 1.31e-47

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: 159.15  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  11 IVYRSRDFLVVNK------HwdvriDSKAWRETlTLQKQLRYRFPELADPDTCYgfrFCHQLDFSTSGALCVALNKAAAG 84
Cdd:COG0564     1 ILYEDEDLLVVNKpaglvvH-----PGSGGDDG-TLVNALRAHLGELSGVPRPG---LVHRLDRDTSGLLLVAKTRKAAR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  85 SAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTeGRAHTMCIEgsqgvagcENPKPSLTDLVVLEHGlyagDPV 164
Cdd:COG0564    72 RLSEQFREREVEKRYLALVEGKPKEDEGTIDAPLGRDPK-DRKKMAVVD--------EDGKPAVTHYRVLERF----GGY 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022433253 165 SKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevSGREDRPF---RMMLHAFYLRI--PTDTECVEVCTPDP 232
Cdd:COG0564   139 SLVEVRLETGRTHQIRVHLAHIGHPIVGDPLYG--GDRSNRLLgldRQALHAYRLGFphPVTGEPLEFEAPLP 209
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
3-232 6.78e-33

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: 123.20  E-value: 6.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   3 PGSVENLSIVYRSRDFLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELADpdTCYGFrFCHQLDFSTSGALCVALNKAA 82
Cdd:TIGR00005  66 PPQDIPLDILFEDEDIIVINKPSGLVVHPGGGNPFGTVLNALLAHCPPIAG--VERVG-IVHRLDRDTSGLMVVAKTPLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  83 AGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEgrahtmciEGSQGVAGCENPKPSLTDLVVLEHGLYAgd 162
Cdd:TIGR00005 143 LRELQRQLKNRTVTKEYVALVHGQFDSGGGTVDAPLGRVPNN--------RGLMAVHPSSEGKPAVTHFRVLERFGNA-- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253 163 pvSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevSGREDRPF--------RMMLHAFYLRI--PTDTECVEVCTPDP 232
Cdd:TIGR00005 213 --SLVECELETGRTHQIRVHLQYLGHPLAGDPLYG--NKPVPGNNlngllnfdRQALHAYELGFihPATGEILEFEAPLP 288
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
64-218 1.63e-25

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 101.61  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  64 HQLDFSTSGALCVALNKAAAGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEGRAHTMCIEGSqgvagcen 143
Cdd:PRK10158   61 HRLDMATSGVIVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETG-------- 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1022433253 144 pKPSLTDLVVLEhglYAGDPVSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGEVSGREDRPfRMMLHAFYLRI 218
Cdd:PRK10158  133 -KPAQTEYEVVE---YAADNTARVVLKPITGRSHQLRVHMLALGHPILGDRFYASPEARAMAP-RLLLHAEMLTI 202
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
60-185 3.28e-20

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: 85.15  E-value: 3.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  60 FRFCHQLDFSTSGALCVALNKAAAGSAYRCFKERRVTKAYLALLRGHIqESRVTISHAIGRNSTEGRAHTMCIEGSqgva 139
Cdd:pfam00849  38 LYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLALVDKPE-EEEGTIKSPIKKEKNKSPFRKEEELGG---- 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1022433253 140 gcenpKPSLTDLVVLEHGLYAgdPVSKVLLKPLTGRTHQLRVHCSA 185
Cdd:pfam00849 113 -----KKAVTHLKVLKSGSKG--DYSLLELELVTGRKHQIRAHLAA 151
 
Name Accession Description Interval E-value
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
18-218 2.20e-55

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: 177.91  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  18 FLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELADPDTCYgfrFCHQLDFSTSGALCVALNKAAAGSAYRCFKERRVTK 97
Cdd:cd02869     1 LLVVNKPAGLPVHPGPGHLTGTLVNALLKLLLLLGEEFRPG---LVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  98 AYLALLRGHIQESRVTISHAIGRNSTEGRAHtmciegsqgVAGCENPKPSLTDLVVLEHGlyagDPVSKVLLKPLTGRTH 177
Cdd:cd02869    78 TYLALVDGKPPEDEGTIDAPLGRKKRKKRAR---------VVVSEDGKPAITHYKVLERF----GNVTLVELQLETGRTH 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1022433253 178 QLRVHCSALGHPVVGDLTYGEVSGREDRPFRMMLHAFYLRI 218
Cdd:cd02869   145 QIRVHLASIGHPIVGDPKYGGKASDSPGLKRLALHAYRLSF 185
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
11-232 1.31e-47

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: 159.15  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  11 IVYRSRDFLVVNK------HwdvriDSKAWRETlTLQKQLRYRFPELADPDTCYgfrFCHQLDFSTSGALCVALNKAAAG 84
Cdd:COG0564     1 ILYEDEDLLVVNKpaglvvH-----PGSGGDDG-TLVNALRAHLGELSGVPRPG---LVHRLDRDTSGLLLVAKTRKAAR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  85 SAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTeGRAHTMCIEgsqgvagcENPKPSLTDLVVLEHGlyagDPV 164
Cdd:COG0564    72 RLSEQFREREVEKRYLALVEGKPKEDEGTIDAPLGRDPK-DRKKMAVVD--------EDGKPAVTHYRVLERF----GGY 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022433253 165 SKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevSGREDRPF---RMMLHAFYLRI--PTDTECVEVCTPDP 232
Cdd:COG0564   139 SLVEVRLETGRTHQIRVHLAHIGHPIVGDPLYG--GDRSNRLLgldRQALHAYRLGFphPVTGEPLEFEAPLP 209
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
3-232 6.78e-33

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: 123.20  E-value: 6.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   3 PGSVENLSIVYRSRDFLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELADpdTCYGFrFCHQLDFSTSGALCVALNKAA 82
Cdd:TIGR00005  66 PPQDIPLDILFEDEDIIVINKPSGLVVHPGGGNPFGTVLNALLAHCPPIAG--VERVG-IVHRLDRDTSGLMVVAKTPLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  83 AGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEgrahtmciEGSQGVAGCENPKPSLTDLVVLEHGLYAgd 162
Cdd:TIGR00005 143 LRELQRQLKNRTVTKEYVALVHGQFDSGGGTVDAPLGRVPNN--------RGLMAVHPSSEGKPAVTHFRVLERFGNA-- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253 163 pvSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevSGREDRPF--------RMMLHAFYLRI--PTDTECVEVCTPDP 232
Cdd:TIGR00005 213 --SLVECELETGRTHQIRVHLQYLGHPLAGDPLYG--NKPVPGNNlngllnfdRQALHAYELGFihPATGEILEFEAPLP 288
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
64-218 1.63e-25

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 101.61  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  64 HQLDFSTSGALCVALNKAAAGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEGRAHTMCIEGSqgvagcen 143
Cdd:PRK10158   61 HRLDMATSGVIVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETG-------- 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1022433253 144 pKPSLTDLVVLEhglYAGDPVSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGEVSGREDRPfRMMLHAFYLRI 218
Cdd:PRK10158  133 -KPAQTEYEVVE---YAADNTARVVLKPITGRSHQLRVHMLALGHPILGDRFYASPEARAMAP-RLLLHAEMLTI 202
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
3-214 1.64e-24

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: 98.47  E-value: 1.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   3 PGSVENLSIVYRSRDFLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPeladpdtCYGFRFCHQLDFSTSGALCVALNKAA 82
Cdd:cd02557    10 PVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYG-------LTELRPCHRLDRLTSGLLLFAKTSQT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  83 AGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEGRahtmciegsQGVAGCENPKPSLTdlvVLEHGLYAGD 162
Cdd:cd02557    83 ASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGG---------LRNDVDEKGKDART---IFKRLSYNGD 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1022433253 163 P-VSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevsgredrPFRMMLHAF 214
Cdd:cd02557   151 LnTSVVLCKPITGRTHQIRVHLQYLGHPIVNDPIYN--------NLGIYLHAL 195
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
9-219 3.75e-23

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: 95.09  E-value: 3.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   9 LSIVYRSRDFLVVNK--------HWdvrIDSKAWRETL-TLQKQL-RYRFPeladpdtcygfrfCHQLDFSTSGALCVAL 78
Cdd:cd02563     1 LEILYQDEHLVAINKpsgllvhrSE---LDRHETRFALqTLRDQLgQHVYP-------------VHRLDRPTSGVLLFAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  79 NKAAAGSAYRCFKERRVTKAYLALLRGHIQESRvTISHAIGRNSTEGrahtmcieGSQGVAGCENPKPSLTD-------L 151
Cdd:cd02563    65 SSEVARKLGEQFTEHRVHKTYLAVVRGYVPESG-TIDYPLSEELDKL--------ADKFASDDKAPQAATTHyrllaveE 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1022433253 152 VVLEHGLYAGDPVSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGEvsGREDRPF-------RMMLHAFYLRIP 219
Cdd:cd02563   136 LPVVVGKYPTSRYSLVELTPHTGRKHQLRRHLAHIRHPIIGDTTHGD--GRHNRFFrehfgchRLLLAATRLEFT 208
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
9-217 1.48e-20

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 88.95  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   9 LSIVYRSRDFLVVNK--HWDVRidsKAW---RETL----TLQKQL-RYRFPeladpdtcygfrfCHQLDFSTSGALCVAL 78
Cdd:PRK11112    2 LEILYQDEWLVAVNKpaGWLVH---RSWldrHETVfvmqTVRDQIgQHVFT-------------AHRLDRPTSGVLLMAL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  79 NKAAAGSAYRCFKERRVTKAYLALLRGHIQESRvTISHAI--------GRNSTEGRAHTMCIEGSQGVAGCENPKPSltd 150
Cdd:PRK11112   66 SSEVARLLAQQFEQHQIQKTYHAIVRGWLMEEA-VLDYPLkeeldkiaDKFAREDKAPQPAVTHYRGLATVEMPVAT--- 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1022433253 151 lvvlehGLYAGDPVSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGEvsGREDRPF-------RMMLHAFYLR 217
Cdd:PRK11112  142 ------GRYPTTRYSLVELEPKTGRKHQLRRHMAHLRHPIIGDTKHGD--LRQNRSLaehfgcsRLMLHASELS 207
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
9-259 2.98e-20

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


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 89.35  E-value: 2.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   9 LSIVYRSRDFLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELAD-PdtcygfR--FCHQLDFSTSGALCVALNKAAAGS 85
Cdd:PRK11180   84 LDIVYEDDDILVINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADvP------RagIVHRLDKDTTGLMVVAKTVPAQTR 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  86 AYRCFKERRVTKAYLALLRGHIQESRvTISHAIGRNSTEgRAHtmciegsqgVAGCENPKPSLTDLVVLEH-GLYagdpv 164
Cdd:PRK11180  158 LVEALQKREITREYEAVAIGHMTAGG-TVDEPISRHPTK-RTH---------MAVHPMGKPAVTHYRIMEHfRVH----- 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253 165 SKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevsGREdRP-------FRMM--------LHAFYLRI--PTDTECVEV 227
Cdd:PRK11180  222 TRLRLRLETGRTHQIRVHMAHITHPLVGDQVYG---GRP-RPpkgaseeFISTlrkfdrqaLHATMLRLyhPITGIEMEW 297
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1022433253 228 CTPDPflpsldacwsphtllQSLDQLVQALRA 259
Cdd:PRK11180  298 HAPLP---------------QDMVELIEALRA 314
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
60-185 3.28e-20

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: 85.15  E-value: 3.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  60 FRFCHQLDFSTSGALCVALNKAAAGSAYRCFKERRVTKAYLALLRGHIqESRVTISHAIGRNSTEGRAHTMCIEGSqgva 139
Cdd:pfam00849  38 LYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLALVDKPE-EEEGTIKSPIKKEKNKSPFRKEEELGG---- 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1022433253 140 gcenpKPSLTDLVVLEHGLYAgdPVSKVLLKPLTGRTHQLRVHCSA 185
Cdd:pfam00849 113 -----KKAVTHLKVLKSGSKG--DYSLLELELVTGRKHQIRAHLAA 151
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
64-217 3.99e-16

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 77.46  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  64 HQLDFSTSGALCVALNKAAAGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEGrahtmcieGSQGVAGCEN 143
Cdd:PRK11025  141 HRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLLKNILQS--------GERIVRVSQE 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253 144 PKPSLTDLVVLEHGLYAgdpvSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGevsgreDRPF----------RMMLHA 213
Cdd:PRK11025  213 GKPSETRFKVEERYAFA----TLVRASPVTGRTHQIRVHTQYAGHPIAFDDRYG------DREFdqqltgtglnRLFLHA 282

                  ....
gi 1022433253 214 FYLR 217
Cdd:PRK11025  283 AALK 286
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
9-212 1.91e-15

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: 74.23  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253   9 LSIVYRSRDFLVVNK-HWDVRIDSKAW-RETLTLQKQLRYRFPELAdPdtcygfrfCHQLDFSTSGALCVALNKAAAGSA 86
Cdd:cd02558    39 ETILHQDEHLLVADKpHFLPVTPRGRYvTETLLVRLRRQTGNPDLT-P--------AHRLDRLTAGLVLFSKRPETRGAY 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  87 YRCFKERRVTKAYLAL------LRGHIQ-ESRVTishaigrnSTEGRAHTMCIEGsqgvagcenPKPSLTDLVVLEH--- 156
Cdd:cd02558   110 QTLFARREVSKTYEAVapyvpaLTFPLTvRSRIV--------KGRGFFQAREVEG---------EPNAETRIELLARrgg 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433253 157 -GLYAgdpvskvlLKPLTGRTHQLRVHCSALGHPVVGDLTYGEVSGREDRPFRMMLH 212
Cdd:cd02558   173 wGLYR--------LSPHTGKTHQLRVHMAALGVPILNDPFYPVLLDKDPDDFSRPLQ 221
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
63-191 1.48e-09

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: 55.84  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433253  63 CHQLDFSTSGALCVALNKAAAgsaYRCFKERR-VTKAYLALLRGHIQESRVTISHAIGRNSTEGRAHtmciegsqgvagc 141
Cdd:cd02550    38 AGRLDKDTSGLLLLTNDGRLQ---RRLTEPRReIEKEYLVTVRGELDEEGIEDLATVRRGRLSGLVD------------- 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1022433253 142 ENPKPSLTDLVVLEHGlyagDPVSKVLLKPLTGRTHQLRVHCSALGHPVV 191
Cdd:cd02550   102 EGVPLAVTKVRVIGEH----GGTGRLRLTLKTGRTHQIRRHCAAVGFPVL 147
 
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