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Conserved domains on  [gi|7661556|ref|NP_056494|]
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pseudouridylate synthase TRUB2, mitochondrial isoform 1 [Homo sapiens]

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 2.56e-122

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: 350.53  E-value: 2.56e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   11 GLFAVYKPPGLKWKHLRDTVELQLLKglnarkppapkqrvrfllgpmegseekeltltatsvpsfinhplvcgpAFAHLK 90
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK------------------------------------------------YFPEDK 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   91 VGVG-HRLDAQASGVLVLGVGHGCRLLTDMYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQ 169
Cdd:cd02868  33 VLVGvHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556  170 GSHQ-KALVMYSNLDLKTQEAYEMAvRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKT 248
Cdd:cd02868 113 SGHQqKAFELCSVDDQSQQAAELAA-RGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7661556  249 TAVCTQVRRTRDGFFTLDSALLRTQWDLTNIQDAI 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 2.56e-122

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: 350.53  E-value: 2.56e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   11 GLFAVYKPPGLKWKHLRDTVELQLLKglnarkppapkqrvrfllgpmegseekeltltatsvpsfinhplvcgpAFAHLK 90
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK------------------------------------------------YFPEDK 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   91 VGVG-HRLDAQASGVLVLGVGHGCRLLTDMYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQ 169
Cdd:cd02868  33 VLVGvHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556  170 GSHQ-KALVMYSNLDLKTQEAYEMAvRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKT 248
Cdd:cd02868 113 SGHQqKAFELCSVDDQSQQAAELAA-RGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7661556  249 TAVCTQVRRTRDGFFTLDSALLRTQWDLTNIQDAI 283
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
90-227 2.03e-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: 117.97  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556     90 KVGVGHRLDAQASGVLVLGVGHGCRLLTDMYNAhlTKDYTVRGLLGKATDDFREDGRLVEkTTYDHVTREKLDRILAVIQ 169
Cdd:pfam01509   8 KVGHTGTLDPLATGVLPVCVGEATKLLQYLLDA--DKEYVATIRLGVATDTLDAEGEIVE-ESVDHITEEKIEEVLASFT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7661556    170 GSHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQC 227
Cdd:pfam01509  85 GEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLEFDLPEVTFRVTC 142
truB PRK02193
tRNA pseudouridine synthase B; Provisional
90-263 4.95e-12

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 65.16  E-value: 4.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556    90 KVGVGHRLDAQASGVLVLGVGHGCRLLTdmYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQ 169
Cdd:PRK02193  28 KIGHTGTLDPLASGLLLVATDEDTKLID--YLDQKDKTYIAKIKFGFISTTYDSEGQIINVSQNIKVTKENLEEALNNLV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   170 GSHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKTT 249
Cdd:PRK02193 106 GSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTG 185
                        170
                 ....*....|....
gi 7661556   250 AVCTQVRRTRDGFF 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 2.56e-122

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: 350.53  E-value: 2.56e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   11 GLFAVYKPPGLKWKHLRDTVELQLLKglnarkppapkqrvrfllgpmegseekeltltatsvpsfinhplvcgpAFAHLK 90
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK------------------------------------------------YFPEDK 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   91 VGVG-HRLDAQASGVLVLGVGHGCRLLTDMYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQ 169
Cdd:cd02868  33 VLVGvHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVIQ 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556  170 GSHQ-KALVMYSNLDLKTQEAYEMAvRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKT 248
Cdd:cd02868 113 SGHQqKAFELCSVDDQSQQAAELAA-RGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 7661556  249 TAVCTQVRRTRDGFFTLDSALLRTQWDLTNIQDAI 283
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
PseudoU_synth_TruB_like cd00506
Pseudouridine synthase, TruB family; This group consists of eukaryotic, bacterial and archeal ...
11-274 3.36e-58

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: 186.59  E-value: 3.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   11 GLFAVYKPPGLKWKHLRDTVELQLLKGlnarkppapkqrvrfllgpmegseekeltltatsvpsfinhplvcgpafahlK 90
Cdd:cd00506   1 GLFAVDKPQGPSSHDVVDTIRRIFLAE----------------------------------------------------K 28
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   91 VGVGHRLDAQASGVLVLGVGHGCRLLTDMYNAhlTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQG 170
Cdd:cd00506  29 VGHGGTLDPFATGVLVVGIGKATKLLKHLLAA--TKDYTAIGRLGQATDTFDATGQVIEETPYDHITHEQLERALETLTG 106
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556  171 SHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKTTA 250
Cdd:cd00506 107 DIQQVPPLYSAVKRQGQRAYELARRGLLVPDEARPPTIYELLCIRFNPPHFLLEVEVVCETGTYIRTLIHDLGLELGVGA 186
                       250       260
                ....*....|....*....|....
gi 7661556  251 VCTQVRRTRDGFFTLDSALLRTQW 274
Cdd:cd00506 187 HVTELRRTRVGPFKVENAVTLHHL 210
TruB_N pfam01509
TruB family pseudouridylate synthase (N terminal domain); Members of this family are involved ...
90-227 2.03e-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: 117.97  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556     90 KVGVGHRLDAQASGVLVLGVGHGCRLLTDMYNAhlTKDYTVRGLLGKATDDFREDGRLVEkTTYDHVTREKLDRILAVIQ 169
Cdd:pfam01509   8 KVGHTGTLDPLATGVLPVCVGEATKLLQYLLDA--DKEYVATIRLGVATDTLDAEGEIVE-ESVDHITEEKIEEVLASFT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7661556    170 GSHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQC 227
Cdd:pfam01509  85 GEIEQVPPMYSAVKVNGKRLYELAREGIEVERPPRPVTIYSLELLEFDLPEVTFRVTC 142
PseudoU_synth_TruB_4 cd02867
Pseudouridine synthase homolog 4; This group consists of Eukaryotic TruB proteins similar to ...
89-272 2.92e-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: 92.11  E-value: 2.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   89 LKVGVGHRLDAQASGVLVLGVGHGCRLLTDMYnaHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVI 168
Cdd:cd02867  56 LKIGHGGTLDPLATGVLVVGVGAGTKQLQDYL--SCSKTYEATGLFGASTTTYDREGKILKKKPYSHITREDIEEVLAKF 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556  169 QGSHQKALVMYSNLDLKTQEAYEMAVRGLirpmnKSPMLITGIRCLYF---------APPEFLLEVQCMHETQKelRKLV 239
Cdd:cd02867 134 RGDIKQVPPLYSALKMDGKRLYEYAREGK-----PLPRPIERRQVVVSellvkdwiePGPLFTRTVEEEGKQYE--RSVV 206
                       170       180       190
                ....*....|....*....|....*....|...
gi 7661556  240 HEIGLELKTTAVCTQVRRTRDGFFTLDSALLRT 272
Cdd:cd02867 207 KMLGKELKTFAEVTELTATAEGDPVEEVEATHE 239
PseudoU_synth_EcTruB cd02573
Pseudouridine synthase, Escherichia coli TruB like; This group consists of bacterial ...
93-269 4.91e-18

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: 81.34  E-value: 4.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   93 VGH--RLDAQASGVLVLGVGHGCRLLTDMYNAhlTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQG 170
Cdd:cd02573  29 VGHtgTLDPLATGVLPIALGEATKLSQYLLDA--DKTYRATVRLGEATDTDDAEGEIIETSPPPRLTEEEIEAALKAFTG 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556  171 SHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAP--PEFLLEVQCMHETQkeLRKLVHEIGLELKT 248
Cdd:cd02573 107 EIEQVPPMYSAVKVDGKRLYELARAGEEVERPPRKVTIYSLELLSFDPenPEADFEVHCSKGTY--IRSLARDLGKALGC 184
                       170       180
                ....*....|....*....|.
gi 7661556  249 TAVCTQVRRTRDGFFTLDSAL 269
Cdd:cd02573 185 GAHLSALRRTRSGPFTLEQAI 205
truB PRK02193
tRNA pseudouridine synthase B; Provisional
90-263 4.95e-12

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 65.16  E-value: 4.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556    90 KVGVGHRLDAQASGVLVLGVGHGCRLLTdmYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQ 169
Cdd:PRK02193  28 KIGHTGTLDPLASGLLLVATDEDTKLID--YLDQKDKTYIAKIKFGFISTTYDSEGQIINVSQNIKVTKENLEEALNNLV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661556   170 GSHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKTT 249
Cdd:PRK02193 106 GSQKQVPPVFSAKKVNGKRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTG 185
                        170
                 ....*....|....
gi 7661556   250 AVCTQVRRTRDGFF 263
Cdd:PRK02193 186 AYMSDLERTKIGNL 199
 
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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