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Conserved domains on  [gi|62079245|ref|NP_001014279|]
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pseudouridylate synthase TRUB2, mitochondrial [Rattus norvegicus]

Protein Classification

pseudouridine synthase family protein; rRNA pseudouridine synthase( domain architecture ID 10120731)

pseudouridine synthase family protein may catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines| rRNA pseudouridine synthase catalyzes the formation of pseudouridine at position 516 in 16S or position 2605 in 23S rRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
11-283 6.51e-110

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


:

Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 318.56  E-value: 6.51e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  11 GLFAVYKPPGLKWLHVRETVELQLLKglnaqqpsapeqhvrfllgpvegseekkltltatsvpsltthrlvrgpAFRNLK 90
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK------------------------------------------------YFPEDK 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  91 IGVG-HRLDVQASGVLVLAVGHGRSLLTDMYDAHLTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERLDRILAMIQ 169
Cdd:cd02868  33 VLVGvHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245 170 GSHQ-KALVMYSNLDLKSQEAYErAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMHETQQQLRRLVHEIGLELKT 248
Cdd:cd02868 113 SGHQqKAFELCSVDDQSQQAAEL-AARGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 62079245 249 TAVCMQVRRTRDGFFGLDDALLRTQWDLHSIQDAI 283
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
 
Name Accession Description Interval E-value
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
11-283 6.51e-110

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 318.56  E-value: 6.51e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  11 GLFAVYKPPGLKWLHVRETVELQLLKglnaqqpsapeqhvrfllgpvegseekkltltatsvpsltthrlvrgpAFRNLK 90
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK------------------------------------------------YFPEDK 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  91 IGVG-HRLDVQASGVLVLAVGHGRSLLTDMYDAHLTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERLDRILAMIQ 169
Cdd:cd02868  33 VLVGvHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245 170 GSHQ-KALVMYSNLDLKSQEAYErAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMHETQQQLRRLVHEIGLELKT 248
Cdd:cd02868 113 SGHQqKAFELCSVDDQSQQAAEL-AARGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 62079245 249 TAVCMQVRRTRDGFFGLDDALLRTQWDLHSIQDAI 283
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
90-227 7.28e-32

TruB family pseudouridylate synthase (N terminal domain); 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 TruB, a pseudouridylate synthase that specifically converts uracil 55 to pseudouridine in most tRNAs. This family also includes Cbf5p that modifies rRNA.


Pssm-ID: 426297  Cd Length: 148  Bit Score: 116.04  E-value: 7.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245    90 KIGVGHRLDVQASGVLVLAVGHGRSLLTDMYDAhlTKDYTVRGLLGKATDNFCEDGQLIEkTTYDHVTRERLDRILAMIQ 169
Cdd:pfam01509   8 KVGHTGTLDPLATGVLPVCVGEATKLLQYLLDA--DKEYVATIRLGVATDTLDAEGEIVE-ESVDHITEEKIEEVLASFT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62079245   170 GSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQC 227
Cdd:pfam01509  85 GEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLEFDLPEVTFRVTC 142
truB PRK02193
tRNA pseudouridine synthase B; Provisional
90-263 7.72e-14

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 70.55  E-value: 7.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245   90 KIGVGHRLDVQASGVLVLAVGHGRSLLTdmYDAHLTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERLDRILAMIQ 169
Cdd:PRK02193  28 KIGHTGTLDPLASGLLLVATDEDTKLID--YLDQKDKTYIAKIKFGFISTTYDSEGQIINVSQNIKVTKENLEEALNNLV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  170 GSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMHETQQQLRRLVHEIGLELKTT 249
Cdd:PRK02193 106 GSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTG 185
                        170
                 ....*....|....
gi 62079245  250 AVCMQVRRTRDGFF 263
Cdd:PRK02193 186 AYMSDLERTKIGNL 199
 
Name Accession Description Interval E-value
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
11-283 6.51e-110

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 318.56  E-value: 6.51e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  11 GLFAVYKPPGLKWLHVRETVELQLLKglnaqqpsapeqhvrfllgpvegseekkltltatsvpsltthrlvrgpAFRNLK 90
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK------------------------------------------------YFPEDK 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  91 IGVG-HRLDVQASGVLVLAVGHGRSLLTDMYDAHLTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERLDRILAMIQ 169
Cdd:cd02868  33 VLVGvHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245 170 GSHQ-KALVMYSNLDLKSQEAYErAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMHETQQQLRRLVHEIGLELKT 248
Cdd:cd02868 113 SGHQqKAFELCSVDDQSQQAAEL-AARGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 62079245 249 TAVCMQVRRTRDGFFGLDDALLRTQWDLHSIQDAI 283
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
PseudoU_synth_TruB_like cd00506
Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal ...
73-274 1.62e-54

Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruB, Saccharomyces cerevisiae Pus4, M. tuberculosis TruB, S. cerevisiae Cbf5 and human dyskerin. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E. coli TruB, M. tuberculosis TruB and S. cerevisiae Pus4, make psi55 in the T loop of tRNAs. Pus4 catalyses the formation of psi55 in both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. S. cerevisiae Cbf5 and human dyskerin are nucleolar proteins that, with the help of guide RNAs, make the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Cbf5/Dyskerin is the catalytic subunit of eukaryotic box H/ACA small nucleolar ribonucleoprotein (snoRNP) particles. Mutations in human dyskerin cause X-linked dyskeratosis congenitas.


Pssm-ID: 211323 [Multi-domain]  Cd Length: 210  Bit Score: 176.96  E-value: 1.62e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  73 PSLTTHRLVRGPAFRNL---KIGVGHRLDVQASGVLVLAVGHGRSLLTDMYDAhlTKDYTVRGLLGKATDNFCEDGQLIE 149
Cdd:cd00506   8 PQGPSSHDVVDTIRRIFlaeKVGHGGTLDPFATGVLVVGIGKATKLLKHLLAA--TKDYTAIGRLGQATDTFDATGQVIE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245 150 KTTYDHVTRERLDRILAMIQGSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMH 229
Cdd:cd00506  86 ETPYDHITHEQLERALETLTGDIQQVPPLYSAVKRQGQRAYELARRGLLVPDEARPPTIYELLCIRFNPPHFLLEVEVVC 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 62079245 230 ETQQQLRRLVHEIGLELKTTAVCMQVRRTRDGFFGLDDALLRTQW 274
Cdd:cd00506 166 ETGTYIRTLIHDLGLELGVGAHVTELRRTRVGPFKVENAVTLHHL 210
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
90-227 7.28e-32

TruB family pseudouridylate synthase (N terminal domain); 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 TruB, a pseudouridylate synthase that specifically converts uracil 55 to pseudouridine in most tRNAs. This family also includes Cbf5p that modifies rRNA.


Pssm-ID: 426297  Cd Length: 148  Bit Score: 116.04  E-value: 7.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245    90 KIGVGHRLDVQASGVLVLAVGHGRSLLTDMYDAhlTKDYTVRGLLGKATDNFCEDGQLIEkTTYDHVTRERLDRILAMIQ 169
Cdd:pfam01509   8 KVGHTGTLDPLATGVLPVCVGEATKLLQYLLDA--DKEYVATIRLGVATDTLDAEGEIVE-ESVDHITEEKIEEVLASFT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62079245   170 GSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQC 227
Cdd:pfam01509  85 GEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLEFDLPEVTFRVTC 142
PseudoU_synth_TruB_4 cd02867
Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to ...
11-250 1.17e-21

Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to Saccharomyces cerevisiae Pus4. S. cerevisiae Pus4, makes psi55 in the T loop of both cytoplasmic and mitochondrial tRNAs. Psi55 is almost universally conserved. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211344 [Multi-domain]  Cd Length: 312  Bit Score: 93.27  E-value: 1.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  11 GLFAVYKPPG---------LKWLhvretvelqLLKGLNAQQPSAPEQHVRfllgpveGSEEKKltltatsvpsltTHRLV 81
Cdd:cd02867   1 GVFAINKPSGitsaqvlndLKPL---------FLNSALFKDKIQRAVAKR-------GKKARR------------RKGRK 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  82 RGPafrnLKIGVGHRLDVQASGVLVLAVGHGRSLLTDMYdaHLTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERL 161
Cdd:cd02867  53 RSK----LKIGHGGTLDPLATGVLVVGVGAGTKQLQDYL--SCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDI 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245 162 DRILAMIQGSHQKALVMYSNLDLKSQEAYERAVQGVirpmnKSPMLIAGIRC------LHFAP---PEFLLEVQCmhETQ 232
Cdd:cd02867 127 EEVLAKFRGDIKQVPPLYSALKMDGKRLYEYAREGK-----PLPRPIERRQVvvsellVKDWIepgPLFTRTVEE--EGK 199
                       250
                ....*....|....*...
gi 62079245 233 QQLRRLVHEIGLELKTTA 250
Cdd:cd02867 200 QYERSVVKMLGKELKTFA 217
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
87-269 1.93e-19

Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial pseudouridine synthases similar to E. coli TruB and Mycobacterium tuberculosis TruB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruB and M. tuberculosis TruB make psi55 in the T loop of tRNAs. Psi55 is nearly universally conserved. E. coli TruB is not inhibited by RNA containing 5-fluorouridine.


Pssm-ID: 211339 [Multi-domain]  Cd Length: 213  Bit Score: 84.80  E-value: 1.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  87 RNLKIG-VGH--RLDVQASGVLVLAVGHGRSLLTDMYDAhlTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERLDR 163
Cdd:cd02573  22 RLLGTKkVGHtgTLDPLATGVLPIALGEATKLSQYLLDA--DKTYRATVRLGEATDTDDAEGEIIETSPPPRLTEEEIEA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245 164 ILAMIQGSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAP--PEFLLEVQCMHETqqQLRRLVHE 241
Cdd:cd02573 100 ALKAFTGEIEQVPPMYSAVKVDGKRLYELARAGEEVERPPRKVTIYSLELLSFDPenPEADFEVHCSKGT--YIRSLARD 177
                       170       180
                ....*....|....*....|....*...
gi 62079245 242 IGLELKTTAVCMQVRRTRDGFFGLDDAL 269
Cdd:cd02573 178 LGKALGCGAHLSALRRTRSGPFTLEQAI 205
truB PRK02193
tRNA pseudouridine synthase B; Provisional
90-263 7.72e-14

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 70.55  E-value: 7.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245   90 KIGVGHRLDVQASGVLVLAVGHGRSLLTdmYDAHLTKDYTVRGLLGKATDNFCEDGQLIEKTTYDHVTRERLDRILAMIQ 169
Cdd:PRK02193  28 KIGHTGTLDPLASGLLLVATDEDTKLID--YLDQKDKTYIAKIKFGFISTTYDSEGQIINVSQNIKVTKENLEEALNNLV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  170 GSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMHETQQQLRRLVHEIGLELKTT 249
Cdd:PRK02193 106 GSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTG 185
                        170
                 ....*....|....
gi 62079245  250 AVCMQVRRTRDGFF 263
Cdd:PRK02193 186 AYMSDLERTKIGNL 199
truB PRK14846
tRNA pseudouridine synthase B; Provisional
90-269 3.03e-08

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 237834 [Multi-domain]  Cd Length: 345  Bit Score: 54.27  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245   90 KIGVGH--RLDVQASGVLVLAVGHGRSLLTDMYDAHLTKDYTVRglLGKATDNFCEDGQLIekTTYDHV-TRERLDRILA 166
Cdd:PRK14846  29 KTKIGHagTLDVEAEGILPFAVGEATKLIHLLIDARKTYIFTVK--FGMQTNSGDCAGKVI--ATKDCIpSQEEAYAVCS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62079245  167 MIQGSHQKALVMYSNLDLKSQEAYERAVQGVIRPMNKSPMLIAGIRCLHFAPPEFLLEVQCMHETQQQLRRLVHEIGLEL 246
Cdd:PRK14846 105 KFIGNVTQIPPAFSALKVNGVRAYKLAREGKKVELKPRNITIYDLKCLNFDEKNATATYYTECSKGTYIRTLAEDLALSL 184
                        170       180
                 ....*....|....*....|...
gi 62079245  247 KTTAVCMQVRRTRDGFFGLDDAL 269
Cdd:PRK14846 185 QSLGFVIELRRTQVGIFKEENAI 207
 
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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