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Conserved domains on  [gi|24583449|ref|NP_723594|]
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RluA pseudouridine synthase 1, isoform C [Drosophila melanogaster]

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, ...
363-547 7.31e-111

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: 334.98  E-value: 7.31e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 363 NIVHRHEVPVTCQPIKIVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPK 442
Cdd:cd02557   2 HTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTSQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 443 KARQMEQQIRNRQVEKEYICRVEGVFPDGIVECKEPIEVVSYKIGV-CKVSAKGKDCTTTFQKLSQNG--TTSVVLCKPL 519
Cdd:cd02557  82 TASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGGLrNDVDEKGKDARTIFKRLSYNGdlNTSVVLCKPI 161
                       170       180
                ....*....|....*....|....*...
gi 24583449 520 TGRMHQIRVHLQYLGYPILNDPLYNHEV 547
Cdd:cd02557 162 TGRTHQIRVHLQYLGHPIVNDPIYNNLG 189
 
Name Accession Description Interval E-value
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
363-547 7.31e-111

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: 334.98  E-value: 7.31e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 363 NIVHRHEVPVTCQPIKIVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPK 442
Cdd:cd02557   2 HTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTSQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 443 KARQMEQQIRNRQVEKEYICRVEGVFPDGIVECKEPIEVVSYKIGV-CKVSAKGKDCTTTFQKLSQNG--TTSVVLCKPL 519
Cdd:cd02557  82 TASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGGLrNDVDEKGKDARTIFKRLSYNGdlNTSVVLCKPI 161
                       170       180
                ....*....|....*....|....*...
gi 24583449 520 TGRMHQIRVHLQYLGYPILNDPLYNHEV 547
Cdd:cd02557 162 TGRTHQIRVHLQYLGHPIVNDPIYNNLG 189
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
311-560 3.67e-69

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: 229.13  E-value: 3.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   311 RWVGEKILDIFSREFRAHPAEEYERCIQTGTLTVNfEKVPIDYRLK--HNDLLANIV---HRHEVPVTCQPIKIVHMDED 385
Cdd:TIGR00005   2 EQAGQRLDDFLASLLPDLSRSRIQKLIENGQVKVN-GKVTANPKLKvkDGDRITVRVpeeEEHEVPPQDIPLDILFEDED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   386 IVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKN----LRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYI 461
Cdd:TIGR00005  81 IIVINKPSGLVVHPGGGNPFGTVLNALLAHCPPIAgverVGIVHRLDRDTSGLMVVAKTPLALRELQRQLKNRTVTKEYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   462 CRVEGVFPDGIVECKEPIEVVSYKIGVCKV--SAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYLGYPILN 539
Cdd:TIGR00005 161 ALVHGQFDSGGGTVDAPLGRVPNNRGLMAVhpSSEGKPAVTHFRVLERFGNASLVECELETGRTHQIRVHLQYLGHPLAG 240
                         250       260
                  ....*....|....*....|..
gi 24583449   540 DPLY-NHEVFGPLKGRSGDIGG 560
Cdd:TIGR00005 241 DPLYgNKPVPGNNLNGLLNFDR 262
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
379-543 1.40e-52

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: 181.49  E-value: 1.40e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 379 IVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKN----LRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNR 454
Cdd:COG0564   1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRAHLGELSgvprPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 455 QVEKEYICRVEGVFPDGIVECKEPIEVVSYKIG-VCKVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYL 533
Cdd:COG0564  81 EVEKRYLALVEGKPKEDEGTIDAPLGRDPKDRKkMAVVDEDGKPAVTHYRVLERFGGYSLVEVRLETGRTHQIRVHLAHI 160
                       170
                ....*....|
gi 24583449 534 GYPILNDPLY 543
Cdd:COG0564 161 GHPIVGDPLY 170
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
386-532 2.00e-33

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: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   386 IVVVNKPASIPVHPCG--RYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYICR 463
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDslTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24583449   464 VEGVFPDgIVECKEPIEVVSYKIGVCKVSAK-GKDCTTTFQKLSQ--NGTTSVVLCKPLTGRMHQIRVHLQY 532
Cdd:pfam00849  81 VDKPEEE-EGTIKSPIKKEKNKSPFRKEEELgGKKAVTHLKVLKSgsKGDYSLLELELVTGRKHQIRAHLAA 151
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
335-548 6.43e-25

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 105.97  E-value: 6.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  335 RCIQTGTLTVNFEKVPIDYRLKHNDLL----ANIVHRHEVPVTCQPIK-------IVHMDEDIVVVNKPASIPVHPCGRY 403
Cdd:PRK11025  40 RILRKGEVRVNKKRIKPEYKLEAGDEVrippVRVAEREEEAVSPKLQKvaaladvILYEDDHILVLNKPSGTAVHGGSGL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  404 RHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYICRVEGVFPDGIVECKEPI--EV 481
Cdd:PRK11025 120 SFGVIEGLRALRPEARFLELVHRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLlkNI 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24583449  482 VSYKIGVCKVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYLGYPILNDPLYNHEVF 548
Cdd:PRK11025 200 LQSGERIVRVSQEGKPSETRFKVEERYAFATLVRASPVTGRTHQIRVHTQYAGHPIAFDDRYGDREF 266
 
Name Accession Description Interval E-value
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
363-547 7.31e-111

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: 334.98  E-value: 7.31e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 363 NIVHRHEVPVTCQPIKIVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPK 442
Cdd:cd02557   2 HTVHRHEPPVTNDPIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTSQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 443 KARQMEQQIRNRQVEKEYICRVEGVFPDGIVECKEPIEVVSYKIGV-CKVSAKGKDCTTTFQKLSQNG--TTSVVLCKPL 519
Cdd:cd02557  82 TASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGGLrNDVDEKGKDARTIFKRLSYNGdlNTSVVLCKPI 161
                       170       180
                ....*....|....*....|....*...
gi 24583449 520 TGRMHQIRVHLQYLGYPILNDPLYNHEV 547
Cdd:cd02557 162 TGRTHQIRVHLQYLGHPIVNDPIYNNLG 189
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
311-560 3.67e-69

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: 229.13  E-value: 3.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   311 RWVGEKILDIFSREFRAHPAEEYERCIQTGTLTVNfEKVPIDYRLK--HNDLLANIV---HRHEVPVTCQPIKIVHMDED 385
Cdd:TIGR00005   2 EQAGQRLDDFLASLLPDLSRSRIQKLIENGQVKVN-GKVTANPKLKvkDGDRITVRVpeeEEHEVPPQDIPLDILFEDED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   386 IVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKN----LRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYI 461
Cdd:TIGR00005  81 IIVINKPSGLVVHPGGGNPFGTVLNALLAHCPPIAgverVGIVHRLDRDTSGLMVVAKTPLALRELQRQLKNRTVTKEYV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   462 CRVEGVFPDGIVECKEPIEVVSYKIGVCKV--SAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYLGYPILN 539
Cdd:TIGR00005 161 ALVHGQFDSGGGTVDAPLGRVPNNRGLMAVhpSSEGKPAVTHFRVLERFGNASLVECELETGRTHQIRVHLQYLGHPLAG 240
                         250       260
                  ....*....|....*....|..
gi 24583449   540 DPLY-NHEVFGPLKGRSGDIGG 560
Cdd:TIGR00005 241 DPLYgNKPVPGNNLNGLLNFDR 262
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
379-543 1.40e-52

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: 181.49  E-value: 1.40e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 379 IVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKN----LRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNR 454
Cdd:COG0564   1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRAHLGELSgvprPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 455 QVEKEYICRVEGVFPDGIVECKEPIEVVSYKIG-VCKVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYL 533
Cdd:COG0564  81 EVEKRYLALVEGKPKEDEGTIDAPLGRDPKDRKkMAVVDEDGKPAVTHYRVLERFGGYSLVEVRLETGRTHQIRVHLAHI 160
                       170
                ....*....|
gi 24583449 534 GYPILNDPLY 543
Cdd:COG0564 161 GHPIVGDPLY 170
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
386-543 1.89e-50

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: 174.45  E-value: 1.89e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 386 IVVVNKPASIPVHPCGRYRHNTVV----FILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYI 461
Cdd:cd02869   1 LLVVNKPAGLPVHPGPGHLTGTLVnallKLLLLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 462 CRVEGVFPDGIVECKEPIEVVSYKIGVC-KVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYLGYPILND 540
Cdd:cd02869  81 ALVDGKPPEDEGTIDAPLGRKKRKKRARvVVSEDGKPAITHYKVLERFGNVTLVELQLETGRTHQIRVHLASIGHPIVGD 160

                ...
gi 24583449 541 PLY 543
Cdd:cd02869 161 PKY 163
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
386-532 2.00e-33

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: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   386 IVVVNKPASIPVHPCG--RYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYICR 463
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDslTKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEYLAL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24583449   464 VEGVFPDgIVECKEPIEVVSYKIGVCKVSAK-GKDCTTTFQKLSQ--NGTTSVVLCKPLTGRMHQIRVHLQY 532
Cdd:pfam00849  81 VDKPEEE-EGTIKSPIKKEKNKSPFRKEEELgGKKAVTHLKVLKSgsKGDYSLLELELVTGRKHQIRAHLAA 151
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
386-538 1.80e-32

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: 122.87  E-value: 1.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 386 IVVVNKPASIPVHPCGRYRHNTVVFILAKEfNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQirNRQVEKEYICRVE 465
Cdd:cd02550   1 ILVLNKPSGLVCHPTDRDRDPTVVVRLDKL-HGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEP--RREIEKEYLVTVR 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24583449 466 GVFPDGIVEcKEPIevVSYKIGVCKVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYLGYPIL 538
Cdd:cd02550  78 GELDEEGIE-DLAT--VRRGRLSGLVDEGVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHCAAVGFPVL 147
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
366-543 1.35e-29

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: 117.76  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 366 HR---HEVPVTCqPIKIVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPK 442
Cdd:cd02558  26 YRelpDEPPIPF-EETILHQDEHLLVADKPHFLPVTPRGRYVTETLLVRLRRQTGNPDLTPAHRLDRLTAGLVLFSKRPE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 443 KARQMEQQIRNRQVEKEYICRVEGV----FPDGIVECKEPIE-VVSYKIGVCKVSAKgkdctTTFQKLSQNGTTSVVLCK 517
Cdd:cd02558 105 TRGAYQTLFARREVSKTYEAVAPYVpaltFPLTVRSRIVKGRgFFQAREVEGEPNAE-----TRIELLARRGGWGLYRLS 179
                       170       180
                ....*....|....*....|....*.
gi 24583449 518 PLTGRMHQIRVHLQYLGYPILNDPLY 543
Cdd:cd02558 180 PHTGKTHQLRVHMAALGVPILNDPFY 205
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
377-540 3.28e-25

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: 104.34  E-value: 3.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 377 IKIVHMDEDIVVVNKPASIPVHPCGRYRHntvvfilAKEFNLKNLR--------TIHRLDRLTSGLLLFGRSPKKARQME 448
Cdd:cd02563   1 LEILYQDEHLVAINKPSGLLVHRSELDRH-------ETRFALQTLRdqlgqhvyPVHRLDRPTSGVLLFALSSEVARKLG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 449 QQIRNRQVEKEYICRVEGVFPD-GIVECKEPIEVVSYKIGVCKVSAKGKDCTTTFQKLSQN---------GTT--SVVLC 516
Cdd:cd02563  74 EQFTEHRVHKTYLAVVRGYVPEsGTIDYPLSEELDKLADKFASDDKAPQAATTHYRLLAVEelpvvvgkyPTSrySLVEL 153
                       170       180
                ....*....|....*....|....
gi 24583449 517 KPLTGRMHQIRVHLQYLGYPILND 540
Cdd:cd02563 154 TPHTGRKHQLRRHLAHIRHPIIGD 177
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
335-548 6.43e-25

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 105.97  E-value: 6.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  335 RCIQTGTLTVNFEKVPIDYRLKHNDLL----ANIVHRHEVPVTCQPIK-------IVHMDEDIVVVNKPASIPVHPCGRY 403
Cdd:PRK11025  40 RILRKGEVRVNKKRIKPEYKLEAGDEVrippVRVAEREEEAVSPKLQKvaaladvILYEDDHILVLNKPSGTAVHGGSGL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  404 RHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEKEYICRVEGVFPDGIVECKEPI--EV 481
Cdd:PRK11025 120 SFGVIEGLRALRPEARFLELVHRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLlkNI 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24583449  482 VSYKIGVCKVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHLQYLGYPILNDPLYNHEVF 548
Cdd:PRK11025 200 LQSGERIVRVSQEGKPSETRFKVEERYAFATLVRASPVTGRTHQIRVHTQYAGHPIAFDDRYGDREF 266
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
379-540 9.15e-25

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 103.97  E-value: 9.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  379 IVHMDEDIVVVNKPASIPVHPCGRYRHNTVvfilakeFNLKNLR--------TIHRLDRLTSGLLLFGRSPKKARQMEQQ 450
Cdd:PRK11112   4 ILYQDEWLVAVNKPAGWLVHRSWLDRHETV-------FVMQTVRdqigqhvfTAHRLDRPTSGVLLMALSSEVARLLAQQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  451 IRNRQVEKEYICRVEG-VFPDGIV-----------------ECKEPIEVVSYKIGVCKVS---AKGKDCTTTFqklsqng 509
Cdd:PRK11112  77 FEQHQIQKTYHAIVRGwLMEEAVLdyplkeeldkiadkfarEDKAPQPAVTHYRGLATVEmpvATGRYPTTRY------- 149
                        170       180       190
                 ....*....|....*....|....*....|.
gi 24583449  510 ttSVVLCKPLTGRMHQIRVHLQYLGYPILND 540
Cdd:PRK11112 150 --SLVELEPKTGRKHQLRRHMAHLRHPIIGD 178
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
379-546 1.09e-20

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 91.21  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  379 IVHMDEDIVVVNKPASIPVHPcGRYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQVEK 458
Cdd:PRK10158  16 ILYQDEHIMVVNKPSGLLSVP-GRLEEHKDSVMTRIQRDYPQAESVHRLDMATSGVIVVALTKAAERELKRQFREREPKK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  459 EYICRVEGvFPD---GIVE----CKEPIEVvsyKIGVCKVSakGKDCTTTFQKLS-QNGTTSVVLCKPLTGRMHQIRVHL 530
Cdd:PRK10158  95 QYVARVWG-HPSpaeGLVDlpliCDWPNRP---KQKVCYET--GKPAQTEYEVVEyAADNTARVVLKPITGRSHQLRVHM 168
                        170
                 ....*....|....*.
gi 24583449  531 QYLGYPILNDPLYNHE 546
Cdd:PRK10158 169 LALGHPILGDRFYASP 184
RluA-like TIGR01621
pseudouridine synthase Rlu family protein, TIGR01621; This model represents a clade of ...
377-544 4.38e-20

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: 89.57  E-value: 4.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   377 IKIVHMDEDIVVVNKPASIPVHPcgRYRHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQIRNRQV 456
Cdd:TIGR01621   2 FEILFTHPDFLLINKHPGISVHK--DDGETGLLQEVATQLGVGQVWLVHRLDKMTSGILLLALNAESASELSQGFAKRKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449   457 EKEYICrvegvfpdgiVECKEPIEVVSYKIGVCKVSAKG--KDCTTT-------FQKLSQNGTTSVVLCKPLTGRMHQIR 527
Cdd:TIGR01621  80 EKTYLA----------LSSKKPKKKQGLICGDMEKSRRGswKLVNSQenpaitrFFSASAATGLRLFILKPHTGKTHQLR 149
                         170
                  ....*....|....*..
gi 24583449   528 VHLQYLGYPILNDPLYN 544
Cdd:TIGR01621 150 VAMKSLGSPILGDPLYG 166
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
376-569 1.13e-15

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


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 78.95  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  376 PIKIVHMDEDIVVVNKPASIPVHPCGRYRHNTVVFILAKEF----NLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQI 451
Cdd:PRK11180  83 PLDIVYEDDDILVINKPRDLVVHPGAGNPDGTVLNALLHYYppiaDVPRAGIVHRLDKDTTGLMVVAKTVPAQTRLVEAL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449  452 RNRQVEKEYICRVEGVF-PDGIVEckEPIEVVSYKIGVCKVSAKGKDCTTTFQKLSQNGTTSVVLCKPLTGRMHQIRVHL 530
Cdd:PRK11180 163 QKREITREYEAVAIGHMtAGGTVD--EPISRHPTKRTHMAVHPMGKPAVTHYRIMEHFRVHTRLRLRLETGRTHQIRVHM 240
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24583449  531 QYLGYPILNDPLYNhevfgplkGRSGDIGGKSDE--ELIRD 569
Cdd:PRK11180 241 AHITHPLVGDQVYG--------GRPRPPKGASEEfiSTLRK 273
RsuA COG1187
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ...
330-538 7.49e-07

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: 50.80  E-value: 7.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 330 AEEYercIQTGTLTVNFEKV-PIDYRLKHNDllanIVHRHEVPVTCQPIKIVhmdediVVVNKPASIPvhpCGRY---RH 405
Cdd:COG1187  20 AEEL---IEAGRVTVNGKVVtELGTKVDPGD----EVTVDGKPLKLPEEPVY------LLLNKPAGVV---STTKdpeGR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 406 NTVVFILAKEfNLKNLRTIHRLDRLTSGLLLF---GR------SPKKarqmeqqirnrQVEKEYICRVEGVFPDGIVE-C 475
Cdd:COG1187  84 PTVFDLLPEA-RKERLFPVGRLDKDTEGLLLLtndGElahrltHPKY-----------GVEKEYLVRVDGPVTEEDLErL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24583449 476 KEPIEVVSYKIGVCKVSAKGKDCTTTFQklsqngttsVVlckpLT-GRMHQIRVHLQYLGYPIL 538
Cdd:COG1187 152 REGVELEDGPTKPAKVEILSGEANTWLR---------IT----LTeGRNRQVRRMFEAVGLPVV 202
PseudoU_synth_RsuA_like cd02870
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ...
426-538 5.54e-04

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: 40.94  E-value: 5.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 426 RLDRLTSGLLLF---GR------SPKkarqmeqqirnRQVEKEYICRVEGVFPDGIVE-CKEPIEVVSYKIGVCKVSakg 495
Cdd:cd02870  39 RLDYDTEGLLLLtndGElanrltHPR-----------YGVEKTYLVKVRGVPSEEELRrLRAGVELDDGKTAPAKVK--- 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24583449 496 kdctttfqKLSQNGTTSVVLckpLT---GRMHQIRVHLQYLGYPIL 538
Cdd:cd02870 105 --------VLSRDPKNTLLE---VTlheGRNRQVRRMFEAVGHPVL 139
PseudoU_synth_RsuA cd02553
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ...
404-474 6.48e-04

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: 40.97  E-value: 6.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 404 RHNTVVFILAKEFNLKNLRTIHRLDRLTSGLLLF---GR------SPKKarqmeqqirnrQVEKEYICRVEGVFPDGIVE 474
Cdd:cd02553  19 HHPTVIDLLPEPDRRRDLFPVGRLDKDTTGLLLLtndGQlahrltSPKK-----------HVPKTYEVTLAGPLTEDDIE 87
PseudoU_synth_RluB cd02556
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ...
409-534 4.97e-03

Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and eukaryotic proteins similar to E. coli RluB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RluB makes psi2605 in 23S RNA. psi2605 has been detected in eubacteria but, not in eukarya and archea despite the presence of a precursor U at that site.


Pssm-ID: 211330 [Multi-domain]  Cd Length: 167  Bit Score: 38.44  E-value: 4.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583449 409 VFILAKEFNLKNLRTIHRLDRLTSGLLLFGRSPKKARQMEQQirNRQVEKEYICRVEGVFPDGIVEckepievvSYKIGV 488
Cdd:cd02556  24 VFDLLPKLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHP--SNEIEREYAVRVFGQVTDEQLK--------SLKKGV 93
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 24583449 489 ckvsaKGKDCTTTFQKLSQNGTT------SVVLCKpltGRMHQIRVHLQYLG 534
Cdd:cd02556  94 -----ELEDGFAGFKSIQLEGGEgknswyRVTLRE---GRNREVRRLWEAFG 137
 
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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