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Conserved domains on  [gi|221316667|ref|NP_001138299|]
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pseudouridylate synthase RPUSD4, mitochondrial isoform b [Homo sapiens]

Protein Classification

RNA pseudouridine synthase( domain architecture ID 10120734)

RNA pseudouridine synthase catalyzes the isomerization of specific uridines in rRNA or tRNA to pseudouridines

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
106-298 2.62e-54

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: 176.37  E-value: 2.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 106 LVVINKPYGLPVHGGPGVQLCiTDVLPILAKMLHGHKAEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKY 185
Cdd:cd02869    1 LLVVNKPAGLPVHPGPGHLTG-TLVNALLKLLLLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 186 WAITVHVPMPSAGVVDIPI------------VEKEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHLSFgLDCPIL 253
Cdd:cd02869   80 LALVDGKPPEDEGTIDAPLgrkkrkkrarvvVSEDGKPAITHYKVLERFGNVTLVELQLETGRTHQIRVHLAS-IGHPIV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 221316667 254 GDHKYSDWnrlapqklsvgtlkklglEQSKARYIPLHLHARQLIL 298
Cdd:cd02869  159 GDPKYGGK------------------ASDSPGLKRLALHAYRLSF 185
 
Name Accession Description Interval E-value
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
106-298 2.62e-54

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: 176.37  E-value: 2.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 106 LVVINKPYGLPVHGGPGVQLCiTDVLPILAKMLHGHKAEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKY 185
Cdd:cd02869    1 LLVVNKPAGLPVHPGPGHLTG-TLVNALLKLLLLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 186 WAITVHVPMPSAGVVDIPI------------VEKEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHLSFgLDCPIL 253
Cdd:cd02869   80 LALVDGKPPEDEGTIDAPLgrkkrkkrarvvVSEDGKPAITHYKVLERFGNVTLVELQLETGRTHQIRVHLAS-IGHPIV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 221316667 254 GDHKYSDWnrlapqklsvgtlkklglEQSKARYIPLHLHARQLIL 298
Cdd:cd02869  159 GDPKYGGK------------------ASDSPGLKRLALHAYRLSF 185
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
99-324 3.52e-53

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: 174.55  E-value: 3.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLPVHGGPGVQLciTDVLPILAKMLHGHKAEP-LHLCHRLDKETTGVMVLAWDKDMAHQVQELFR 177
Cdd:COG0564    1 ILYEDEDLLVVNKPAGLVVHPGSGGDD--GTLVNALRAHLGELSGVPrPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 178 TRQVVKKYWAITVHVPMPSAGVVDIPI------------VEKEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHLS 245
Cdd:COG0564   79 EREVEKRYLALVEGKPKEDEGTIDAPLgrdpkdrkkmavVDEDGKPAVTHYRVLERFGGYSLVEVRLETGRTHQIRVHLA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221316667 246 FgLDCPILGDHKYSDWNRLAPQKLSvgtlkklgleqskaryiPLHLHARQLILPALGSGkEELNLVCKLPRFFVHSLHR 324
Cdd:COG0564  159 H-IGHPIVGDPLYGGDRSNRLLGLD-----------------RQALHAYRLGFPHPVTG-EPLEFEAPLPEDFQALLEK 218
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
72-326 3.81e-39

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: 140.54  E-value: 3.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667   72 RVQEIVRFTRQLQRVHPN-VLAKALTRGILHQDKNLVVINKPYGLPVHGGPGVQlcITDVLPILAKML-HGHKAEPLHLC 149
Cdd:TIGR00005  46 KVKDGDRITVRVPEEEEHeVPPQDIPLDILFEDEDIIVINKPSGLVVHPGGGNP--FGTVLNALLAHCpPIAGVERVGIV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  150 HRLDKETTGVMVLAwDKDMAHQV-QELFRTRQVVKKYWAITVHVPMPSAGVVDIPI-------------VEKEAQVAVTQ 215
Cdd:TIGR00005 124 HRLDRDTSGLMVVA-KTPLALRElQRQLKNRTVTKEYVALVHGQFDSGGGTVDAPLgrvpnnrglmavhPSSEGKPAVTH 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  216 YQVLSSTLSSALVELQPITGIKHQLRVHLSFgLDCPILGDHKYSDwnrlaPQKLSVGTLKKLGLEqskaRYIplhLHARQ 295
Cdd:TIGR00005 203 FRVLERFGNASLVECELETGRTHQIRVHLQY-LGHPLAGDPLYGN-----KPVPGNNLNGLLNFD----RQA---LHAYE 269
                         250       260       270
                  ....*....|....*....|....*....|.
gi 221316667  296 LILPALGSGkEELNLVCKLPRFFVHSLHRLR 326
Cdd:TIGR00005 270 LGFIHPATG-EILEFEAPLPADLVLLLEALR 299
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
106-245 3.73e-34

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: 122.90  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  106 LVVINKPYGLPVHGGPGVQLCitDVLPILAKMLHGHKaEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKY 185
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDSLTKL--LSLLALLLRRELGV-KRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEY 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221316667  186 WAItVHVPMPSAGVVDIPIV------------EKEAQVAVTQYQVLSSTLSS--ALVELQPITGIKHQLRVHLS 245
Cdd:pfam00849  78 LAL-VDKPEEEEGTIKSPIKkeknkspfrkeeELGGKKAVTHLKVLKSGSKGdySLLELELVTGRKHQIRAHLA 150
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
99-294 4.20e-24

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 99.35  E-value: 4.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLPVHGG-------PGVQLCITD-----VLPIlakmlhghkaeplhlcHRLDKETTGVMVLAWDK 166
Cdd:PRK11112   4 ILYQDEWLVAVNKPAGWLVHRSwldrhetVFVMQTVRDqigqhVFTA----------------HRLDRPTSGVLLMALSS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 167 DMAHQVQELFRTRQVVKKYWAItVHVPMPSAGVVDIPIVE-------------KEAQVAVTQYQVLS-----------ST 222
Cdd:PRK11112  68 EVARLLAQQFEQHQIQKTYHAI-VRGWLMEEAVLDYPLKEeldkiadkfaredKAPQPAVTHYRGLAtvempvatgryPT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 223 LSSALVELQPITGIKHQLRVHLSFgLDCPILGDHKYSDW--NRLAPQKLSVGtlkKLGLEQSKARYI------PLHLHAR 294
Cdd:PRK11112 147 TRYSLVELEPKTGRKHQLRRHMAH-LRHPIIGDTKHGDLrqNRSLAEHFGCS---RLMLHASELSLThpftgePLTITAG 222
 
Name Accession Description Interval E-value
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
106-298 2.62e-54

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: 176.37  E-value: 2.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 106 LVVINKPYGLPVHGGPGVQLCiTDVLPILAKMLHGHKAEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKY 185
Cdd:cd02869    1 LLVVNKPAGLPVHPGPGHLTG-TLVNALLKLLLLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERKVKKTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 186 WAITVHVPMPSAGVVDIPI------------VEKEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHLSFgLDCPIL 253
Cdd:cd02869   80 LALVDGKPPEDEGTIDAPLgrkkrkkrarvvVSEDGKPAITHYKVLERFGNVTLVELQLETGRTHQIRVHLAS-IGHPIV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 221316667 254 GDHKYSDWnrlapqklsvgtlkklglEQSKARYIPLHLHARQLIL 298
Cdd:cd02869  159 GDPKYGGK------------------ASDSPGLKRLALHAYRLSF 185
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
99-324 3.52e-53

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: 174.55  E-value: 3.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLPVHGGPGVQLciTDVLPILAKMLHGHKAEP-LHLCHRLDKETTGVMVLAWDKDMAHQVQELFR 177
Cdd:COG0564    1 ILYEDEDLLVVNKPAGLVVHPGSGGDD--GTLVNALRAHLGELSGVPrPGLVHRLDRDTSGLLLVAKTRKAARRLSEQFR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 178 TRQVVKKYWAITVHVPMPSAGVVDIPI------------VEKEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHLS 245
Cdd:COG0564   79 EREVEKRYLALVEGKPKEDEGTIDAPLgrdpkdrkkmavVDEDGKPAVTHYRVLERFGGYSLVEVRLETGRTHQIRVHLA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221316667 246 FgLDCPILGDHKYSDWNRLAPQKLSvgtlkklgleqskaryiPLHLHARQLILPALGSGkEELNLVCKLPRFFVHSLHR 324
Cdd:COG0564  159 H-IGHPIVGDPLYGGDRSNRLLGLD-----------------RQALHAYRLGFPHPVTG-EPLEFEAPLPEDFQALLEK 218
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
72-326 3.81e-39

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: 140.54  E-value: 3.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667   72 RVQEIVRFTRQLQRVHPN-VLAKALTRGILHQDKNLVVINKPYGLPVHGGPGVQlcITDVLPILAKML-HGHKAEPLHLC 149
Cdd:TIGR00005  46 KVKDGDRITVRVPEEEEHeVPPQDIPLDILFEDEDIIVINKPSGLVVHPGGGNP--FGTVLNALLAHCpPIAGVERVGIV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  150 HRLDKETTGVMVLAwDKDMAHQV-QELFRTRQVVKKYWAITVHVPMPSAGVVDIPI-------------VEKEAQVAVTQ 215
Cdd:TIGR00005 124 HRLDRDTSGLMVVA-KTPLALRElQRQLKNRTVTKEYVALVHGQFDSGGGTVDAPLgrvpnnrglmavhPSSEGKPAVTH 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  216 YQVLSSTLSSALVELQPITGIKHQLRVHLSFgLDCPILGDHKYSDwnrlaPQKLSVGTLKKLGLEqskaRYIplhLHARQ 295
Cdd:TIGR00005 203 FRVLERFGNASLVECELETGRTHQIRVHLQY-LGHPLAGDPLYGN-----KPVPGNNLNGLLNFD----RQA---LHAYE 269
                         250       260       270
                  ....*....|....*....|....*....|.
gi 221316667  296 LILPALGSGkEELNLVCKLPRFFVHSLHRLR 326
Cdd:TIGR00005 270 LGFIHPATG-EILEFEAPLPADLVLLLEALR 299
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
106-245 3.73e-34

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: 122.90  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  106 LVVINKPYGLPVHGGPGVQLCitDVLPILAKMLHGHKaEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKY 185
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDSLTKL--LSLLALLLRRELGV-KRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPERKIEKEY 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221316667  186 WAItVHVPMPSAGVVDIPIV------------EKEAQVAVTQYQVLSSTLSS--ALVELQPITGIKHQLRVHLS 245
Cdd:pfam00849  78 LAL-VDKPEEEEGTIKSPIKkeknkspfrkeeELGGKKAVTHLKVLKSGSKGdySLLELELVTGRKHQIRAHLA 150
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
99-260 7.03e-29

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: 111.27  E-value: 7.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLPVHGGPGVQLCITDVLPILAKMLHGHkaepLHLCHRLDKETTGVMVLAWDKDMAHQVQELFRT 178
Cdd:cd02563    3 ILYQDEHLVAINKPSGLLVHRSELDRHETRFALQTLRDQLGQH----VYPVHRLDRPTSGVLLFALSSEVARKLGEQFTE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 179 RQVVKKYWAItVHVPMPSAGVVDIPIVE-------------KEAQVAVTQYQVLSSTLSSA-----------LVELQPIT 234
Cdd:cd02563   79 HRVHKTYLAV-VRGYVPESGTIDYPLSEeldkladkfasddKAPQAATTHYRLLAVEELPVvvgkyptsrysLVELTPHT 157
                        170       180
                 ....*....|....*....|....*.
gi 221316667 235 GIKHQLRVHLSFgLDCPILGDHKYSD 260
Cdd:cd02563  158 GRKHQLRRHLAH-IRHPIIGDTTHGD 182
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
83-260 2.50e-25

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: 101.17  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  83 LQRVH---PNVLAKALtrGILHQDKNLVVINKPYGLPVH-GGPGVQLCITDVLpilakmLHGHKAEPLHLCHRLDKETTG 158
Cdd:cd02557    1 SHTVHrhePPVTNDPI--KIVHEDDDLLVVDKPSGIPVHpTGRYRYNTVTEIL------KSEYGLTELRPCHRLDRLTSG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 159 VMVLAWDKDMAHQVQELFRTRQVVKKYWAITVHVPMPSAGVVDIPIVEKEAQV------------AVTQYQVLSS--TLS 224
Cdd:cd02557   73 LLLFAKTSQTASRLQQQIRSREVKKEYLARVKGEFPDGEVVVDQPIGLVSPKGglrndvdekgkdARTIFKRLSYngDLN 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221316667 225 SALVELQPITGIKHQLRVHLSFgLDCPILGDHKYSD 260
Cdd:cd02557  153 TSVVLCKPITGRTHQIRVHLQY-LGHPIVNDPIYNN 187
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
99-294 4.20e-24

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 99.35  E-value: 4.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLPVHGG-------PGVQLCITD-----VLPIlakmlhghkaeplhlcHRLDKETTGVMVLAWDK 166
Cdd:PRK11112   4 ILYQDEWLVAVNKPAGWLVHRSwldrhetVFVMQTVRDqigqhVFTA----------------HRLDRPTSGVLLMALSS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 167 DMAHQVQELFRTRQVVKKYWAItVHVPMPSAGVVDIPIVE-------------KEAQVAVTQYQVLS-----------ST 222
Cdd:PRK11112  68 EVARLLAQQFEQHQIQKTYHAI-VRGWLMEEAVLDYPLKEeldkiadkfaredKAPQPAVTHYRGLAtvempvatgryPT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 223 LSSALVELQPITGIKHQLRVHLSFgLDCPILGDHKYSDW--NRLAPQKLSVGtlkKLGLEQSKARYI------PLHLHAR 294
Cdd:PRK11112 147 TRYSLVELEPKTGRKHQLRRHMAH-LRHPIIGDTKHGDLrqNRSLAEHFGCS---RLMLHASELSLThpftgePLTITAG 222
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
98-258 3.67e-22

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: 93.49  E-value: 3.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  98 GILHQDKNLVVINKPYGLPVH-GGPGVQLCItdvlpiLAKMLHGHKAEPLHLCHRLDKETTGVMVLAWDKDMAHQVQELF 176
Cdd:cd02558   40 TILHQDEHLLVADKPHFLPVTpRGRYVTETL------LVRLRRQTGNPDLTPAHRLDRLTAGLVLFSKRPETRGAYQTLF 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 177 RTRQVVKKYWAITVHVP------------MPSAGVVDIPIVEKEAQvAVTQYQVLSSTLSSALVELQPITGIKHQLRVHL 244
Cdd:cd02558  114 ARREVSKTYEAVAPYVPaltfpltvrsriVKGRGFFQAREVEGEPN-AETRIELLARRGGWGLYRLSPHTGKTHQLRVHM 192
                        170
                 ....*....|....
gi 221316667 245 SfGLDCPILGDHKY 258
Cdd:cd02558  193 A-ALGVPILNDPFY 205
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
99-303 2.49e-21

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


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 90.82  E-value: 2.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLpvHGGPGVQLCITDvlPILAKMLHGH-KAEPLHlchRLDKETTGVMVLAWDKDMAHQVQELFR 177
Cdd:PRK10158  16 ILYQDEHIMVVNKPSGL--LSVPGRLEEHKD--SVMTRIQRDYpQAESVH---RLDMATSGVIVVALTKAAERELKRQFR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 178 TRQVVKKYWAITVHVPMPSAGVVDIPIV------------EKEAQVAVTQYQVLS-STLSSALVELQPITGIKHQLRVHL 244
Cdd:PRK10158  89 EREPKKQYVARVWGHPSPAEGLVDLPLIcdwpnrpkqkvcYETGKPAQTEYEVVEyAADNTARVVLKPITGRSHQLRVHM 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221316667 245 sFGLDCPILGDHKYSDwnrlapqklsvgtlkklglEQSKARYIPLHLHARQLIL--PALGS 303
Cdd:PRK10158 169 -LALGHPILGDRFYAS-------------------PEARAMAPRLLLHAEMLTIthPAYGN 209
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
106-244 2.01e-19

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


Pssm-ID: 211325 [Multi-domain]  Cd Length: 154  Bit Score: 83.58  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 106 LVVINKPYGLPVHGGPGvqlcitDVLPILAKMLHGHKAEPLHLCHRLDKETTGVMVLAWDKDMAHQVQElfRTRQVVKKY 185
Cdd:cd02550    1 ILVLNKPSGLVCHPTDR------DRDPTVVVRLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTE--PRREIEKEY 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221316667 186 WAiTVHVPMPSAGVVDIPIVE---------KEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLRVHL 244
Cdd:cd02550   73 LV-TVRGELDEEGIEDLATVRrgrlsglvdEGVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHC 139
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
75-326 2.14e-17

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


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 81.70  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  75 EIVRF--TRQLQRVHPNVLAK-----ALTRGILHQDKNLVVINKPYGLPVHGGPGVQLCITDVLPILAKmlhghKAEPLH 147
Cdd:PRK11025  64 DEVRIppVRVAEREEEAVSPKlqkvaALADVILYEDDHILVLNKPSGTAVHGGSGLSFGVIEGLRALRP-----EARFLE 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 148 LCHRLDKETTGVMVLAWDKDMAHQVQELFRTRQVVKKYWAITVHVPMPSAGVVDIPIVEKEAQ-----VAV--------T 214
Cdd:PRK11025 139 LVHRLDRDTSGVLLVAKKRSALRSLHEQLREKGMQKDYLALVRGQWQSHVKVVQAPLLKNILQsgeriVRVsqegkpseT 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 215 QYQVLSSTLSSALVELQPITGIKHQLRVHLSFGlDCPILGDHKYSDwnRLAPQKLSvgtlkKLGLEQskaryipLHLHAR 294
Cdd:PRK11025 219 RFKVEERYAFATLVRASPVTGRTHQIRVHTQYA-GHPIAFDDRYGD--REFDQQLT-----GTGLNR-------LFLHAA 283
                        250       260       270
                 ....*....|....*....|....*....|..
gi 221316667 295 QLILPALGSGkEELNLVCKLPRFFVHSLHRLR 326
Cdd:PRK11025 284 ALKFTHPGTG-EVMRIEAPLDEQLKRCLQKLR 314
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
99-258 8.33e-17

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


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 80.11  E-value: 8.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667  99 ILHQDKNLVVINKPYGLPVHGGPGvqlciTDVLPILAKMLHGHK--AE-P-LHLCHRLDKETTGVMVLAwdKDMAHQVQ- 173
Cdd:PRK11180  86 IVYEDDDILVINKPRDLVVHPGAG-----NPDGTVLNALLHYYPpiADvPrAGIVHRLDKDTTGLMVVA--KTVPAQTRl 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221316667 174 -ELFRTRQVVKKYWAITVHVpMPSAGVVDIPI-----------VEKEAQVAVTQYQVLSSTLSSALVELQPITGIKHQLR 241
Cdd:PRK11180 159 vEALQKREITREYEAVAIGH-MTAGGTVDEPIsrhptkrthmaVHPMGKPAVTHYRIMEHFRVHTRLRLRLETGRTHQIR 237
                        170
                 ....*....|....*..
gi 221316667 242 VHLSFgLDCPILGDHKY 258
Cdd:PRK11180 238 VHMAH-ITHPLVGDQVY 253
 
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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