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Conserved domains on  [gi|15241389|ref|NP_199927|]
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Pseudouridine synthase family protein [Arabidopsis thaliana]

Protein Classification

pseudouridine synthase family protein( domain architecture ID 10118721)

pseudouridine synthase family protein may catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines; similar to Saccharomyces cerevisiae tRNA pseudouridine(31) synthase that catalyzes the formation of pseudouridine at position 31 in the psi GC loop of tRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
121-394 1.00e-103

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: 305.32  E-value: 1.00e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 121 THFLHRHEPPVMIDDVVILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTA 200
Cdd:cd02557   1 SHTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 201 AKADFFRQQIEGGMVKKRYIAKVIGVFPEDEMIVDANINYNGSEGRstaedansSGDDKKVKGKPACTKFTRIDTNG--T 278
Cdd:cd02557  81 QTASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGG--------LRNDVDEKGKDARTIFKRLSYNGdlN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 279 HSLVSCEPVTGRTHQIRVHLQYTGHPIANDPLYLNqhidnletyiakridagerkivspddyvyssedfsidpmctncpk 358
Cdd:cd02557 153 TSVVLCKPITGRTHQIRVHLQYLGHPIVNDPIYNN--------------------------------------------- 187
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15241389 359 lipqgyeehdEALWLHCVQYCGTGWEYECPYPSWAS 394
Cdd:cd02557 188 ----------LGIYLHALRYEGPDWSYETELPDWAS 213
 
Name Accession Description Interval E-value
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
121-394 1.00e-103

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: 305.32  E-value: 1.00e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 121 THFLHRHEPPVMIDDVVILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTA 200
Cdd:cd02557   1 SHTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 201 AKADFFRQQIEGGMVKKRYIAKVIGVFPEDEMIVDANINYNGSEGRstaedansSGDDKKVKGKPACTKFTRIDTNG--T 278
Cdd:cd02557  81 QTASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGG--------LRNDVDEKGKDARTIFKRLSYNGdlN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 279 HSLVSCEPVTGRTHQIRVHLQYTGHPIANDPLYLNqhidnletyiakridagerkivspddyvyssedfsidpmctncpk 358
Cdd:cd02557 153 TSVVLCKPITGRTHQIRVHLQYLGHPIVNDPIYNN--------------------------------------------- 187
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15241389 359 lipqgyeehdEALWLHCVQYCGTGWEYECPYPSWAS 394
Cdd:cd02557 188 ----------LGIYLHALRYEGPDWSYETELPDWAS 213
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
69-311 2.92e-66

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: 212.57  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389    69 KRWTGKTIVDLFADEFKGRPRDYYVGAVKSGRIKVDGEIVP-VSYIVKSSQKIT---HFLHRHEPPVMIDDVVILHQEPD 144
Cdd:TIGR00005   1 EEQAGQRLDDFLASLLPDLSRSRIQKLIENGQVKVNGKVTAnPKLKVKDGDRITvrvPEEEEHEVPPQDIPLDILFEDED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   145 VVTVCKPASVPVHPCGQYRKNTIVGILDAE--HDLGT--LFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYI 220
Cdd:TIGR00005  81 IIVINKPSGLVVHPGGGNPFGTVLNALLAHcpPIAGVerVGIVHRLDRDTSGLMVVAKTPLALRELQRQLKNRTVTKEYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   221 AKVIGVFPEDEMIVDANInyngsegrstAEDANSSGDDK---KVKGKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVH 297
Cdd:TIGR00005 161 ALVHGQFDSGGGTVDAPL----------GRVPNNRGLMAvhpSSEGKPAVTHFRVLERFGNASLVECELETGRTHQIRVH 230
                         250
                  ....*....|....
gi 15241389   298 LQYTGHPIANDPLY 311
Cdd:TIGR00005 231 LQYLGHPLAGDPLY 244
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
138-311 5.34e-50

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: 167.62  E-value: 5.34e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 138 ILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGIL----DAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGG 213
Cdd:COG0564   1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALrahlGELSGVPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 214 MVKKRYIAKVIGVFPEDEMIVDANInyngseGRStaedansSGDDKKV-----KGKPACTKFTRIDTNGTHSLVSCEPVT 288
Cdd:COG0564  81 EVEKRYLALVEGKPKEDEGTIDAPL------GRD-------PKDRKKMavvdeDGKPAVTHYRVLERFGGYSLVEVRLET 147
                       170       180
                ....*....|....*....|...
gi 15241389 289 GRTHQIRVHLQYTGHPIANDPLY 311
Cdd:COG0564 148 GRTHQIRVHLAHIGHPIVGDPLY 170
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
145-300 1.66e-26

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: 103.64  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   145 VVTVCKPASVPVHPCG--QYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAK 222
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDslTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   223 VIGvFPEDEMIVDANINYNGSEGRstaedansSGDDKKVKGKPACTKFTRI--DTNGTHSLVSCEPVTGRTHQIRVHLQY 300
Cdd:pfam00849  81 VDK-PEEEEGTIKSPIKKEKNKSP--------FRKEEELGGKKAVTHLKVLksGSKGDYSLLELELVTGRKHQIRAHLAA 151
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
96-317 6.21e-19

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 86.71  E-value: 6.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   96 VKSGRIKVD-----GEIV---PVSYIVKSSQKITHFLHRheppVMIDDVVILHQEPDVVTVCKPASVPVHPCGQYRKNTI 167
Cdd:PRK11025  49 VNKKRIKPEykleaGDEVripPVRVAEREEEAVSPKLQK----VAALADVILYEDDHILVLNKPSGTAVHGGSGLSFGVI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  168 VGILDAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAKVIGVFPEDEMIVDANINYNGSEGRS 247
Cdd:PRK11025 125 EGLRALRPEARFLELVHRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLLKNILQSGE 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  248 TAEDANSsgddkkvKGKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVHLQYTGHPIANDPLYLNQHID 317
Cdd:PRK11025 205 RIVRVSQ-------EGKPSETRFKVEERYAFATLVRASPVTGRTHQIRVHTQYAGHPIAFDDRYGDREFD 267
 
Name Accession Description Interval E-value
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
121-394 1.00e-103

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: 305.32  E-value: 1.00e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 121 THFLHRHEPPVMIDDVVILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTA 200
Cdd:cd02557   1 SHTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 201 AKADFFRQQIEGGMVKKRYIAKVIGVFPEDEMIVDANINYNGSEGRstaedansSGDDKKVKGKPACTKFTRIDTNG--T 278
Cdd:cd02557  81 QTASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGG--------LRNDVDEKGKDARTIFKRLSYNGdlN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 279 HSLVSCEPVTGRTHQIRVHLQYTGHPIANDPLYLNqhidnletyiakridagerkivspddyvyssedfsidpmctncpk 358
Cdd:cd02557 153 TSVVLCKPITGRTHQIRVHLQYLGHPIVNDPIYNN--------------------------------------------- 187
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15241389 359 lipqgyeehdEALWLHCVQYCGTGWEYECPYPSWAS 394
Cdd:cd02557 188 ----------LGIYLHALRYEGPDWSYETELPDWAS 213
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
69-311 2.92e-66

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: 212.57  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389    69 KRWTGKTIVDLFADEFKGRPRDYYVGAVKSGRIKVDGEIVP-VSYIVKSSQKIT---HFLHRHEPPVMIDDVVILHQEPD 144
Cdd:TIGR00005   1 EEQAGQRLDDFLASLLPDLSRSRIQKLIENGQVKVNGKVTAnPKLKVKDGDRITvrvPEEEEHEVPPQDIPLDILFEDED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   145 VVTVCKPASVPVHPCGQYRKNTIVGILDAE--HDLGT--LFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYI 220
Cdd:TIGR00005  81 IIVINKPSGLVVHPGGGNPFGTVLNALLAHcpPIAGVerVGIVHRLDRDTSGLMVVAKTPLALRELQRQLKNRTVTKEYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   221 AKVIGVFPEDEMIVDANInyngsegrstAEDANSSGDDK---KVKGKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVH 297
Cdd:TIGR00005 161 ALVHGQFDSGGGTVDAPL----------GRVPNNRGLMAvhpSSEGKPAVTHFRVLERFGNASLVECELETGRTHQIRVH 230
                         250
                  ....*....|....
gi 15241389   298 LQYTGHPIANDPLY 311
Cdd:TIGR00005 231 LQYLGHPLAGDPLY 244
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
138-311 5.34e-50

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: 167.62  E-value: 5.34e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 138 ILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGIL----DAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGG 213
Cdd:COG0564   1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALrahlGELSGVPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 214 MVKKRYIAKVIGVFPEDEMIVDANInyngseGRStaedansSGDDKKV-----KGKPACTKFTRIDTNGTHSLVSCEPVT 288
Cdd:COG0564  81 EVEKRYLALVEGKPKEDEGTIDAPL------GRD-------PKDRKKMavvdeDGKPAVTHYRVLERFGGYSLVEVRLET 147
                       170       180
                ....*....|....*....|...
gi 15241389 289 GRTHQIRVHLQYTGHPIANDPLY 311
Cdd:COG0564 148 GRTHQIRVHLAHIGHPIVGDPLY 170
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
150-311 4.35e-46

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: 156.34  E-value: 4.35e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 150 KPASVPVHPCGQYRKNTIVGILDAEHDLGT----LFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAKVIG 225
Cdd:cd02869   6 KPAGLPVHPGPGHLTGTLVNALLKLLLLLGeefrPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTYLALVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 226 VFPEDEMIVDANINYNGSEGRSTAEDANssgddkkvKGKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVHLQYTGHPI 305
Cdd:cd02869  86 KPPEDEGTIDAPLGRKKRKKRARVVVSE--------DGKPAITHYKVLERFGNVTLVELQLETGRTHQIRVHLASIGHPI 157

                ....*.
gi 15241389 306 ANDPLY 311
Cdd:cd02869 158 VGDPKY 163
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
104-311 1.15e-26

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: 106.59  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 104 DGEIVPVSYIVKSSQKIthFLHR---HEPPVMIDdVVILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGILDAEHDLGTL 180
Cdd:cd02558   7 DGEPLDPDSPYRPGTFV--WYYRelpDEPPIPFE-ETILHQDEHLLVADKPHFLPVTPRGRYVTETLLVRLRRQTGNPDL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 181 FPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAkVIGVFPEDEMIVDAninyngsegRSTAEDANSSGDDKK 260
Cdd:cd02558  84 TPAHRLDRLTAGLVLFSKRPETRGAYQTLFARREVSKTYEA-VAPYVPALTFPLTV---------RSRIVKGRGFFQARE 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15241389 261 VKGKP-ACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVHLQYTGHPIANDPLY 311
Cdd:cd02558 154 VEGEPnAETRIELLARRGGWGLYRLSPHTGKTHQLRVHMAALGVPILNDPFY 205
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
145-300 1.66e-26

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: 103.64  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   145 VVTVCKPASVPVHPCG--QYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAK 222
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDslTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   223 VIGvFPEDEMIVDANINYNGSEGRstaedansSGDDKKVKGKPACTKFTRI--DTNGTHSLVSCEPVTGRTHQIRVHLQY 300
Cdd:pfam00849  81 VDK-PEEEEGTIKSPIKKEKNKSP--------FRKEEELGGKKAVTHLKVLksGSKGDYSLLELELVTGRKHQIRAHLAA 151
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
150-305 3.05e-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: 100.14  E-value: 3.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 150 KPASVPVHPCGQYRKNTIVGILDaEHDLGTLFPIHRLDRLVSGLLIIARTAAKADffRQQIEGGMVKKRYIAKVIGVFPE 229
Cdd:cd02550   6 KPSGLVCHPTDRDRDPTVVVRLD-KLHGPRVHAAGRLDKDTSGLLLLTNDGRLQR--RLTEPRREIEKEYLVTVRGELDE 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241389 230 DEMIVDANINYNGSEGRSTAedanssgddkkvKGKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVHLQYTGHPI 305
Cdd:cd02550  83 EGIEDLATVRRGRLSGLVDE------------GVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHCAAVGFPV 146
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
138-308 4.86e-21

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: 90.47  E-value: 4.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 138 ILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGILDAEHDLGT-LFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVK 216
Cdd:cd02563   3 ILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQhVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEHRVH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 217 KRYIAKVIGVFPEdemivDANINYNGSEGRSTAEDANSSGDDKKvkgKPACTKFTRIDT-----------NGTHSLVSCE 285
Cdd:cd02563  83 KTYLAVVRGYVPE-----SGTIDYPLSEELDKLADKFASDDKAP---QAATTHYRLLAVeelpvvvgkypTSRYSLVELT 154
                       170       180
                ....*....|....*....|...
gi 15241389 286 PVTGRTHQIRVHLQYTGHPIAND 308
Cdd:cd02563 155 PHTGRKHQLRRHLAHIRHPIIGD 177
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
96-317 6.21e-19

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 86.71  E-value: 6.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   96 VKSGRIKVD-----GEIV---PVSYIVKSSQKITHFLHRheppVMIDDVVILHQEPDVVTVCKPASVPVHPCGQYRKNTI 167
Cdd:PRK11025  49 VNKKRIKPEykleaGDEVripPVRVAEREEEAVSPKLQK----VAALADVILYEDDHILVLNKPSGTAVHGGSGLSFGVI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  168 VGILDAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAKVIGVFPEDEMIVDANINYNGSEGRS 247
Cdd:PRK11025 125 EGLRALRPEARFLELVHRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLLKNILQSGE 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  248 TAEDANSsgddkkvKGKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVHLQYTGHPIANDPLYLNQHID 317
Cdd:PRK11025 205 RIVRVSQ-------EGKPSETRFKVEERYAFATLVRASPVTGRTHQIRVHTQYAGHPIAFDDRYGDREFD 267
RluA-like TIGR01621
pseudouridine synthase Rlu family protein, TIGR01621; This model represents a clade of ...
132-311 7.22e-17

pseudouridine synthase Rlu family protein, TIGR01621; This model represents a clade of sequences within the pseudouridine synthase superfamily (pfam00849). The superfamily includes E. coli proteins: RluA, RluB, RluC, RluD, and RsuA. The sequences modeled here are most closely related to RluA. Neisseria, among those species hitting this model, does not appear to have an RluA homolog. It is presumed that these sequences function as pseudouridine synthases, although perhaps with different specificity. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 130682 [Multi-domain]  Cd Length: 217  Bit Score: 78.79  E-value: 7.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   132 MIDdvvILHQEPDVVTVCKPASVPVHPcgQYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIE 211
Cdd:TIGR01621   1 MFE---ILFTHPDFLLINKHPGISVHK--DDGETGLLQEVATQLGVGQVWLVHRLDKMTSGILLLALNAESASELSQGFA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   212 GGMVKKRYIAKvigvfpedemivdaninyngSEGRSTAEDANSSGDDKKV----------KGKPACTKFTRIDTNGTHSL 281
Cdd:TIGR01621  76 KRKIEKTYLAL--------------------SSKKPKKKQGLICGDMEKSrrgswklvnsQENPAITRFFSASAATGLRL 135
                         170       180       190
                  ....*....|....*....|....*....|
gi 15241389   282 VSCEPVTGRTHQIRVHLQYTGHPIANDPLY 311
Cdd:TIGR01621 136 FILKPHTGKTHQLRVAMKSLGSPILGDPLY 165
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
138-308 8.85e-17

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 79.32  E-value: 8.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  138 ILHQEPDVVTVCKPASVPVHPCGQYRKNTIVGILDAEHDLGT-LFPIHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVK 216
Cdd:PRK11112   4 ILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQhVFTAHRLDRPTSGVLLMALSSEVARLLAQQFEQHQIQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  217 KRYIAKVIGVFPEDemivdANINYNGSEGRSTAEDANSSGDdkkVKGKPACTKFT------------RIDTNgTHSLVSC 284
Cdd:PRK11112  84 KTYHAIVRGWLMEE-----AVLDYPLKEELDKIADKFARED---KAPQPAVTHYRglatvempvatgRYPTT-RYSLVEL 154
                        170       180
                 ....*....|....*....|....
gi 15241389  285 EPVTGRTHQIRVHLQYTGHPIAND 308
Cdd:PRK11112 155 EPKTGRKHQLRRHMAHLRHPIIGD 178
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
136-311 1.78e-14

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 71.95  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  136 VVILHQEPDVVTVCKPA---SVPvhpcGQYRKNTIVGILDAEHDLGTLFPIHRLDRLVSGLLIIARTAAKADFFRQQIEG 212
Cdd:PRK10158  14 LVILYQDEHIMVVNKPSgllSVP----GRLEEHKDSVMTRIQRDYPQAESVHRLDMATSGVIVVALTKAAERELKRQFRE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  213 GMVKKRYIAKVIGVFPEDEMIVDANInyngsegrsTAEDANSSgdDKKV---KGKPACTKFTRIDTNGTHSL-VSCEPVT 288
Cdd:PRK10158  90 REPKKQYVARVWGHPSPAEGLVDLPL---------ICDWPNRP--KQKVcyeTGKPAQTEYEVVEYAADNTArVVLKPIT 158
                        170       180
                 ....*....|....*....|...
gi 15241389  289 GRTHQIRVHLQYTGHPIANDPLY 311
Cdd:PRK10158 159 GRSHQLRVHMLALGHPILGDRFY 181
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
74-311 2.10e-11

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


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 64.31  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389   74 KTIVDLFADEFKGRPRDYyvgaVKSGRIKVDGEIV--PVSYIVKSSQ-KITHFLH---RHEP-PVMIDdvvILHQEPDVV 146
Cdd:PRK11180  22 QALAELFPDYSRSRIKEW----ILDQRVLVNGKVInkPKEKVLGGEQvAIDAEIEeeaRFEPqDIPLD---IVYEDDDIL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  147 TVCKPASVPVHPCGQYRKNTIVGILDAEHDLGTLFP----IHRLDRLVSGLLIIARTAAKADFFRQQIEGGMVKKRYIAK 222
Cdd:PRK11180  95 VINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADVPragiVHRLDKDTTGLMVVAKTVPAQTRLVEALQKREITREYEAV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  223 VIGVFPEDEMiVDANINYNGSegRSTAEDANSSGddkkvkgKPACTKFTRIDTNGTHSLVSCEPVTGRTHQIRVHLQYTG 302
Cdd:PRK11180 175 AIGHMTAGGT-VDEPISRHPT--KRTHMAVHPMG-------KPAVTHYRIMEHFRVHTRLRLRLETGRTHQIRVHMAHIT 244

                 ....*....
gi 15241389  303 HPIANDPLY 311
Cdd:PRK11180 245 HPLVGDQVY 253
RsuA COG1187
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ...
96-295 2.18e-06

Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ribosomal structure and biogenesis]; Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440800 [Multi-domain]  Cd Length: 226  Bit Score: 48.11  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389  96 VKSGRIKVDGEIV-PVSYIVKSSQKIT---HFLHRHEPPVmiddVVILHQEPDVVTVCKPasvpvhpcGQYRKnTIVGIL 171
Cdd:COG1187  24 IEAGRVTVNGKVVtELGTKVDPGDEVTvdgKPLKLPEEPV----YLLLNKPAGVVSTTKD--------PEGRP-TVFDLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 172 DAEHDLGtLFPIHRLDRLVSGLLI------IAR--TAAKADffrqqieggmVKKRYIAKVIGVFPEDEMivdaninyngs 243
Cdd:COG1187  91 PEARKER-LFPVGRLDKDTEGLLLltndgeLAHrlTHPKYG----------VEKEYLVRVDGPVTEEDL----------- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241389 244 egrstaeDANSSG---DDKKVkgKPActKFTRIDTNGTHSLVscepVT---GRTHQIR 295
Cdd:COG1187 149 -------ERLREGvelEDGPT--KPA--KVEILSGEANTWLR----ITlteGRNRQVR 191
PseudoU_synth_RsuA cd02553
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ...
137-196 6.90e-03

Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and bacterial proteins similar to Escherichia coli RsuA. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RsuA makes psi516 in 16S RNA. Psi at this position is not generally conserved in other organisms.


Pssm-ID: 211327 [Multi-domain]  Cd Length: 167  Bit Score: 37.11  E-value: 6.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241389 137 VILHQEPDVVTVCKPasvPVHPcgqyrknTIVGILDAEHDLGTLFPIHRLDRLVSGLLII 196
Cdd:cd02553   3 LMLNKPAGVVCATKD---PHHP-------TVIDLLPEPDRRRDLFPVGRLDKDTTGLLLL 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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