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Conserved domains on  [gi|515628145|ref|WP_017060745|]
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MULTISPECIES: tRNA pseudouridine(65) synthase TruC [Vibrio]

Protein Classification

tRNA pseudouridine(65) synthase TruC( domain architecture ID 10013734)

tRNA pseudouridine(65) synthase TruC catalyzes the isomerization of uridines at positions 65 in tRNA to pseudouridines

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
1-246 0e+00

tRNA pseudouridine synthase C; Provisional


:

Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 498.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   1 MLEIIYQDEYFVAVNKPAGMLVHRSWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANH 80
Cdd:PRK11112   1 MLEILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQHVFTAHRLDRPTSGVLLMALSSEVARLLAQQFEQH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  81 EMQKTYHAIVRGWIEEGDTLDYALKVELDKIADKFAKEDKEAQEAVTVYEPLAKVEVPYSTGRFPTSRYCLVEMMPKTGR 160
Cdd:PRK11112  81 QIQKTYHAIVRGWLMEEAVLDYPLKEELDKIADKFAREDKAPQPAVTHYRGLATVEMPVATGRYPTTRYSLVELEPKTGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145 161 KHQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDLDSHRLLLHASELRFIHPFTKEELVMKANLDETWLRLFETFEWDTNL 240
Cdd:PRK11112 161 KHQLRRHMAHLRHPIIGDTKHGDLRQNRSLAEHFGCSRLMLHASELSLTHPFTGEPLTITAGLDETWQQLLSQFGWRGLL 240

                 ....*.
gi 515628145 241 IDAQTC 246
Cdd:PRK11112 241 PENERV 246
 
Name Accession Description Interval E-value
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
1-246 0e+00

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 498.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   1 MLEIIYQDEYFVAVNKPAGMLVHRSWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANH 80
Cdd:PRK11112   1 MLEILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQHVFTAHRLDRPTSGVLLMALSSEVARLLAQQFEQH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  81 EMQKTYHAIVRGWIEEGDTLDYALKVELDKIADKFAKEDKEAQEAVTVYEPLAKVEVPYSTGRFPTSRYCLVEMMPKTGR 160
Cdd:PRK11112  81 QIQKTYHAIVRGWLMEEAVLDYPLKEELDKIADKFAREDKAPQPAVTHYRGLATVEMPVATGRYPTTRYSLVELEPKTGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145 161 KHQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDLDSHRLLLHASELRFIHPFTKEELVMKANLDETWLRLFETFEWDTNL 240
Cdd:PRK11112 161 KHQLRRHMAHLRHPIIGDTKHGDLRQNRSLAEHFGCSRLMLHASELSLTHPFTGEPLTITAGLDETWQQLLSQFGWRGLL 240

                 ....*.
gi 515628145 241 IDAQTC 246
Cdd:PRK11112 241 PENERV 246
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
2-224 1.35e-129

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: 365.50  E-value: 1.35e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   2 LEIIYQDEYFVAVNKPAGMLVHRSWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANHE 81
Cdd:cd02563    1 LEILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQHVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEHR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  82 MQKTYHAIVRGWIEEGDTLDYALKVELDKIADKFAKEDKEAQEAVTVYEPLAKVEVPYSTGRFPTSRYCLVEMMPKTGRK 161
Cdd:cd02563   81 VHKTYLAVVRGYVPESGTIDYPLSEELDKLADKFASDDKAPQAATTHYRLLAVEELPVVVGKYPTSRYSLVELTPHTGRK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515628145 162 HQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDLDSHRLLLHASELRFIHPFTKEELVMKANLD 224
Cdd:cd02563  161 HQLRRHLAHIRHPIIGDTTHGDGRHNRFFREHFGCHRLLLAATRLEFTHPVTGERLLIEAPLD 223
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
4-232 2.29e-79

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: 237.73  E-value: 2.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   4 IIYQDEYFVAVNKPAGMLVHRSWLDKHETqfVMQTLRDQIG-----QHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFA 78
Cdd:COG0564    1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGT--LVNALRAHLGelsgvPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  79 NHEMQKTYHAIVRGWI-EEGDTLDYALKVELDKIAdKFAKEDKEAQEAVTVYEPLAKVEvpystgrfptsRYCLVEMMPK 157
Cdd:COG0564   79 EREVEKRYLALVEGKPkEDEGTIDAPLGRDPKDRK-KMAVVDEDGKPAVTHYRVLERFG-----------GYSLVEVRLE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515628145 158 TGRKHQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDldshRLLLHASELRFIHPFTKEELVMKANLDETWLRLFE 232
Cdd:COG0564  147 TGRTHQIRVHLAHIGHPIVGDPLYGGDRSNRLLGLD----RQALHAYRLGFPHPVTGEPLEFEAPLPEDFQALLE 217
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
2-234 4.16e-44

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: 150.55  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145    2 LEIIYQDEYFVAVNKPAGMLVHRSwlDKHETQFVMQTLRDQIGQH-----VFPLHRLDRPTSGVLVFALSSEVASQVMPM 76
Cdd:TIGR00005  72 LDILFEDEDIIVINKPSGLVVHPG--GGNPFGTVLNALLAHCPPIagverVGIVHRLDRDTSGLMVVAKTPLALRELQRQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   77 FANHEMQKTYHAIVRG-WIEEGDTLDYAL-KVELDKIadKFA-KEDKEAQEAVTVYEPLAkvevpystgRFPtsRYCLVE 153
Cdd:TIGR00005 150 LKNRTVTKEYVALVHGqFDSGGGTVDAPLgRVPNNRG--LMAvHPSSEGKPAVTHFRVLE---------RFG--NASLVE 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  154 MMPKTGRKHQLRRHMAHLRHPIVGDTSHGDG---KHNRLFRDDLDshRLLLHASELRFIHPFTKEELVMKANLDETWLRL 230
Cdd:TIGR00005 217 CELETGRTHQIRVHLQYLGHPLAGDPLYGNKpvpGNNLNGLLNFD--RQALHAYELGFIHPATGEILEFEAPLPADLVLL 294

                  ....
gi 515628145  231 FETF 234
Cdd:TIGR00005 295 LEAL 298
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
11-170 3.55e-36

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: 125.60  E-value: 3.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   11 FVAVNKPAGMLVHR-SWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANHEMQKTYHAI 89
Cdd:pfam00849   1 YIVVNKPAGVPVHPtDSLTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   90 VRGWIEEGDTLDYALKVELDKIAdKFAKEDKEAQEAVTVYEPLAkvevpystgRFPTSRYCLVEMMPKTGRKHQLRRHMA 169
Cdd:pfam00849  81 VDKPEEEEGTIKSPIKKEKNKSP-FRKEEELGGKKAVTHLKVLK---------SGSKGDYSLLELELVTGRKHQIRAHLA 150

                  .
gi 515628145  170 H 170
Cdd:pfam00849 151 A 151
 
Name Accession Description Interval E-value
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
1-246 0e+00

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 498.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   1 MLEIIYQDEYFVAVNKPAGMLVHRSWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANH 80
Cdd:PRK11112   1 MLEILYQDEWLVAVNKPAGWLVHRSWLDRHETVFVMQTVRDQIGQHVFTAHRLDRPTSGVLLMALSSEVARLLAQQFEQH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  81 EMQKTYHAIVRGWIEEGDTLDYALKVELDKIADKFAKEDKEAQEAVTVYEPLAKVEVPYSTGRFPTSRYCLVEMMPKTGR 160
Cdd:PRK11112  81 QIQKTYHAIVRGWLMEEAVLDYPLKEELDKIADKFAREDKAPQPAVTHYRGLATVEMPVATGRYPTTRYSLVELEPKTGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145 161 KHQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDLDSHRLLLHASELRFIHPFTKEELVMKANLDETWLRLFETFEWDTNL 240
Cdd:PRK11112 161 KHQLRRHMAHLRHPIIGDTKHGDLRQNRSLAEHFGCSRLMLHASELSLTHPFTGEPLTITAGLDETWQQLLSQFGWRGLL 240

                 ....*.
gi 515628145 241 IDAQTC 246
Cdd:PRK11112 241 PENERV 246
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
2-224 1.35e-129

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: 365.50  E-value: 1.35e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   2 LEIIYQDEYFVAVNKPAGMLVHRSWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANHE 81
Cdd:cd02563    1 LEILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQHVYPVHRLDRPTSGVLLFALSSEVARKLGEQFTEHR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  82 MQKTYHAIVRGWIEEGDTLDYALKVELDKIADKFAKEDKEAQEAVTVYEPLAKVEVPYSTGRFPTSRYCLVEMMPKTGRK 161
Cdd:cd02563   81 VHKTYLAVVRGYVPESGTIDYPLSEELDKLADKFASDDKAPQAATTHYRLLAVEELPVVVGKYPTSRYSLVELTPHTGRK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515628145 162 HQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDLDSHRLLLHASELRFIHPFTKEELVMKANLD 224
Cdd:cd02563  161 HQLRRHLAHIRHPIIGDTTHGDGRHNRFFREHFGCHRLLLAATRLEFTHPVTGERLLIEAPLD 223
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
4-232 2.29e-79

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: 237.73  E-value: 2.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   4 IIYQDEYFVAVNKPAGMLVHRSWLDKHETqfVMQTLRDQIG-----QHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFA 78
Cdd:COG0564    1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGT--LVNALRAHLGelsgvPRPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  79 NHEMQKTYHAIVRGWI-EEGDTLDYALKVELDKIAdKFAKEDKEAQEAVTVYEPLAKVEvpystgrfptsRYCLVEMMPK 157
Cdd:COG0564   79 EREVEKRYLALVEGKPkEDEGTIDAPLGRDPKDRK-KMAVVDEDGKPAVTHYRVLERFG-----------GYSLVEVRLE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515628145 158 TGRKHQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDDldshRLLLHASELRFIHPFTKEELVMKANLDETWLRLFE 232
Cdd:COG0564  147 TGRTHQIRVHLAHIGHPIVGDPLYGGDRSNRLLGLD----RQALHAYRLGFPHPVTGEPLEFEAPLPEDFQALLE 217
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
11-208 2.57e-52

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


Pssm-ID: 211346 [Multi-domain]  Cd Length: 185  Bit Score: 167.90  E-value: 2.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  11 FVAVNKPAGMLVHRSWLDKHET--QFVMQTLRDQ-IGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANHEMQKTYH 87
Cdd:cd02869    1 LLVVNKPAGLPVHPGPGHLTGTlvNALLKLLLLLgEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  88 AIVRGWIEEGDTLDYALKVELDKIADKFAKEDKEAQEAVTVYEPLAkvevpystgrfPTSRYCLVEMMPKTGRKHQLRRH 167
Cdd:cd02869   81 ALVDGKPPEDEGTIDAPLGRKKRKKRARVVVSEDGKPAITHYKVLE-----------RFGNVTLVELQLETGRTHQIRVH 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 515628145 168 MAHLRHPIVGDTSHGDGKHNRLFrddldSHRLLLHASELRF 208
Cdd:cd02869  150 LASIGHPIVGDPKYGGKASDSPG-----LKRLALHAYRLSF 185
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
2-234 4.16e-44

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: 150.55  E-value: 4.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145    2 LEIIYQDEYFVAVNKPAGMLVHRSwlDKHETQFVMQTLRDQIGQH-----VFPLHRLDRPTSGVLVFALSSEVASQVMPM 76
Cdd:TIGR00005  72 LDILFEDEDIIVINKPSGLVVHPG--GGNPFGTVLNALLAHCPPIagverVGIVHRLDRDTSGLMVVAKTPLALRELQRQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   77 FANHEMQKTYHAIVRG-WIEEGDTLDYAL-KVELDKIadKFA-KEDKEAQEAVTVYEPLAkvevpystgRFPtsRYCLVE 153
Cdd:TIGR00005 150 LKNRTVTKEYVALVHGqFDSGGGTVDAPLgRVPNNRG--LMAvHPSSEGKPAVTHFRVLE---------RFG--NASLVE 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  154 MMPKTGRKHQLRRHMAHLRHPIVGDTSHGDG---KHNRLFRDDLDshRLLLHASELRFIHPFTKEELVMKANLDETWLRL 230
Cdd:TIGR00005 217 CELETGRTHQIRVHLQYLGHPLAGDPLYGNKpvpGNNLNGLLNFD--RQALHAYELGFIHPATGEILEFEAPLPADLVLL 294

                  ....
gi 515628145  231 FETF 234
Cdd:TIGR00005 295 LEAL 298
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
12-176 6.68e-38

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: 129.80  E-value: 6.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  12 VAVNKPAGMLVHRSWLDKHETQFVMqtLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPmfANHEMQKTYHAIVR 91
Cdd:cd02550    2 LVLNKPSGLVCHPTDRDRDPTVVVR--LDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTE--PRREIEKEYLVTVR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  92 GWIEEGDTLDYALKVeldkIADKFAKEDKEAQEAVTVYEPLAkvevpystgrfPTSRYCLVEMMPKTGRKHQLRRHMAHL 171
Cdd:cd02550   78 GELDEEGIEDLATVR----RGRLSGLVDEGVPLAVTKVRVIG-----------EHGGTGRLRLTLKTGRTHQIRRHCAAV 142

                 ....*
gi 515628145 172 RHPIV 176
Cdd:cd02550  143 GFPVL 147
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
11-170 3.55e-36

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: 125.60  E-value: 3.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   11 FVAVNKPAGMLVHR-SWLDKHETQFVMQTLRDQIGQHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANHEMQKTYHAI 89
Cdd:pfam00849   1 YIVVNKPAGVPVHPtDSLTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   90 VRGWIEEGDTLDYALKVELDKIAdKFAKEDKEAQEAVTVYEPLAkvevpystgRFPTSRYCLVEMMPKTGRKHQLRRHMA 169
Cdd:pfam00849  81 VDKPEEEEGTIKSPIKKEKNKSP-FRKEEELGGKKAVTHLKVLK---------SGSKGDYSLLELELVTGRKHQIRAHLA 150

                  .
gi 515628145  170 H 170
Cdd:pfam00849 151 A 151
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
2-178 3.40e-30

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: 111.95  E-value: 3.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   2 LEIIYQDEYFVAVNKPAGMLVHRSWLDKHETqfVMQTLRDQIG-QHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANH 80
Cdd:cd02557   16 IKIVHEDDDLLVVDKPSGIPVHPTGRYRYNT--VTEILKSEYGlTELRPCHRLDRLTSGLLLFAKTSQTASRLQQQIRSR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  81 EMQKTYHAIVRGWIEEGdtldyalKVELDK----IADKFAKEDKE---AQEAVTVYEPLAkvevpYstgrFPTSRYCLVE 153
Cdd:cd02557   94 EVKKEYLARVKGEFPDG-------EVVVDQpiglVSPKGGLRNDVdekGKDARTIFKRLS-----Y----NGDLNTSVVL 157
                        170       180
                 ....*....|....*....|....*
gi 515628145 154 MMPKTGRKHQLRRHMAHLRHPIVGD 178
Cdd:cd02557  158 CKPITGRTHQIRVHLQYLGHPIVND 182
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
2-224 1.88e-25

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 99.68  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   2 LEIIYQDEYFVAVNKPAGMLVHRSWLDKHETQFVMQTLRDqigqhvFP----LHRLDRPTSGVLVFALSSEVASQVMPMF 77
Cdd:PRK10158  14 LVILYQDEHIMVVNKPSGLLSVPGRLEEHKDSVMTRIQRD------YPqaesVHRLDMATSGVIVVALTKAAERELKRQF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  78 ANHEMQKTYHAIVRGWIEEGDTLdyalkVELDKIADkFAKEDKEAqeavTVYEPLAKVEVPYSTGRFPTSRYCLVEMMPK 157
Cdd:PRK10158  88 REREPKKQYVARVWGHPSPAEGL-----VDLPLICD-WPNRPKQK----VCYETGKPAQTEYEVVEYAADNTARVVLKPI 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515628145 158 TGRKHQLRRHMAHLRHPIVGDTSHGDGKHNRLfrddldSHRLLLHASELRFIHPFTKEELVMKANLD 224
Cdd:PRK10158 158 TGRSHQLRVHMLALGHPILGDRFYASPEARAM------APRLLLHAEMLTITHPAYGNSMTFKAPAD 218
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
4-226 8.85e-25

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 99.80  E-value: 8.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   4 IIYQDEYFVAVNKPAGMLVHR-SWLDkhetqF-VMQTLRDQIGQHVFP--LHRLDRPTSGVLVFALSSEVASQVMPMFAN 79
Cdd:PRK11025  95 ILYEDDHILVLNKPSGTAVHGgSGLS-----FgVIEGLRALRPEARFLelVHRLDRDTSGVLLVAKKRSALRSLHEQLRE 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  80 HEMQKTYHAIVRG-WIEEGDTLDYAL-KVELDKiADKFAKEDKEAQEAVTVYeplaKVEvpystGRFPTSryCLVEMMPK 157
Cdd:PRK11025 170 KGMQKDYLALVRGqWQSHVKVVQAPLlKNILQS-GERIVRVSQEGKPSETRF----KVE-----ERYAFA--TLVRASPV 237
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515628145 158 TGRKHQLRRHMAHLRHPIVGDTSHGDGKHNRLFRDdLDSHRLLLHASELRFIHPFTKEELVMKANLDET 226
Cdd:PRK11025 238 TGRTHQIRVHTQYAGHPIAFDDRYGDREFDQQLTG-TGLNRLFLHAAALKFTHPGTGEVMRIEAPLDEQ 305
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
2-223 8.78e-24

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: 95.80  E-value: 8.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   2 LEIIYQDEYFVAVNKPAGMLVHRSwlDKHETQFVMQTLRDQIGQ-HVFPLHRLDRPTSGVLVFALSSEVASQVMPMFANH 80
Cdd:cd02558   39 ETILHQDEHLLVADKPHFLPVTPR--GRYVTETLLVRLRRQTGNpDLTPAHRLDRLTAGLVLFSKRPETRGAYQTLFARR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  81 EMQKTYHAIVRgwIEEGDTLDYALKVELDKIADKFAKEDKEAQ-EAVTVYEPLAKVEvpystgrfptsRYCLVEMMPKTG 159
Cdd:cd02558  117 EVSKTYEAVAP--YVPALTFPLTVRSRIVKGRGFFQAREVEGEpNAETRIELLARRG-----------GWGLYRLSPHTG 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145 160 RKHQLRRHMAHLRHPIVGDtshgdgkhnRLFRDDLD------SHRLLLHASELRFIHPFTKEELVMKANL 223
Cdd:cd02558  184 KTHQLRVHMAALGVPILND---------PFYPVLLDkdpddfSRPLQLLAKELEFTDPLTGRPRRFESGR 244
RluA-like TIGR01621
pseudouridine synthase Rlu family protein, TIGR01621; This model represents a clade of ...
1-208 2.06e-23

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: 94.20  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145    1 MLEIIYQDEYFVAVNKPAGMLVHRswlDKHETQfVMQTLRDQIG-QHVFPLHRLDRPTSGVLVFALSSEVASQVMPMFAN 79
Cdd:TIGR01621   1 MFEILFTHPDFLLINKHPGISVHK---DDGETG-LLQEVATQLGvGQVWLVHRLDKMTSGILLLALNAESASELSQGFAK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   80 HEMQKTYHAIV-------RGWIeEGDTldyalkveldKIADKFAKEDKEAQE--AVTVYEPLAKVevpystgrfPTSRYC 150
Cdd:TIGR01621  77 RKIEKTYLALSskkpkkkQGLI-CGDM----------EKSRRGSWKLVNSQEnpAITRFFSASAA---------TGLRLF 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 515628145  151 LVEmmPKTGRKHQLRRHMAHLRHPIVGDTSHGDGKhnrlfrddlDSHRLLLHASELRF 208
Cdd:TIGR01621 137 ILK--PHTGKTHQLRVAMKSLGSPILGDPLYGTTD---------ESDRGYLHAFALRF 183
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
2-240 1.26e-18

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


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 83.19  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145   2 LEIIYQDEYFVAVNKPAGMLVHRSWLDKHETqfVMQTLrdqigQHVFP----------LHRLDRPTSGVLVFALSSEVAS 71
Cdd:PRK11180  84 LDIVYEDDDILVINKPRDLVVHPGAGNPDGT--VLNAL-----LHYYPpiadvpragiVHRLDKDTTGLMVVAKTVPAQT 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  72 QVMPMFANHEMQKTYHAIVRGWIEEGDTLDyalkvelDKIADKFAKEDKEA-----QEAVTVYEPLAKVEVpystgrfpt 146
Cdd:PRK11180 157 RLVEALQKREITREYEAVAIGHMTAGGTVD-------EPISRHPTKRTHMAvhpmgKPAVTHYRIMEHFRV--------- 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145 147 srYCLVEMMPKTGRKHQLRRHMAHLRHPIVGDTSHG------DGKHNRLFRDDLDSHRLLLHASELRFIHPFTKEELVMK 220
Cdd:PRK11180 221 --HTRLRLRLETGRTHQIRVHMAHITHPLVGDQVYGgrprppKGASEEFISTLRKFDRQALHATMLRLYHPITGIEMEWH 298
                        250       260
                 ....*....|....*....|
gi 515628145 221 ANLDETWLRLFETFEWDTNL 240
Cdd:PRK11180 299 APLPQDMVELIEALRADFEE 318
PseudoU_synth_RsuA_like cd02870
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ...
11-176 9.56e-09

Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the synthesis of pseudouridine from uracil in ribosomal RNA. The RsuA subfamily includes Pseudouridine Synthase similar to Ribosomal small subunit pseudouridine 516 synthase. Most of the proteins in this family are bacterial proteins.


Pssm-ID: 211347 [Multi-domain]  Cd Length: 146  Bit Score: 52.88  E-value: 9.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  11 FVAVNKPAGMLVHRSwlDKHETQFVMQTLRDqIGQHVFPLHRLDRPTSGVLVFALSSEVASQVM-PmfaNHEMQKTYHAI 89
Cdd:cd02870    1 YLLLNKPRGVVSTVR--DPEGRPTVLDLLKD-VGERLFPVGRLDYDTEGLLLLTNDGELANRLThP---RYGVEKTYLVK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628145  90 VRGwieegdtldyalkveldkiadKFAKEDKEAQEAVTVYE--PLAKVEVPYSTGRFPTSrycLVEMMPKTGRKHQLRRH 167
Cdd:cd02870   75 VRG---------------------VPSEEELRRLRAGVELDdgKTAPAKVKVLSRDPKNT---LLEVTLHEGRNRQVRRM 130

                 ....*....
gi 515628145 168 MAHLRHPIV 176
Cdd:cd02870  131 FEAVGHPVL 139
 
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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