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Conserved domains on  [gi|2217291292|ref|XP_047285582|]
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pseudouridylate synthase PUS7L isoform X5 [Homo sapiens]

Protein Classification

pseudouridine synthase family protein( domain architecture ID 1007)

pseudouridine synthase family protein may catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PseudoU_synth super family cl00130
Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to ...
 310-466 2.70e-62

Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi); Pseudouridine synthases contains the RsuA/RluD, TruA, TruB and TruD families. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases. Some psi sites such as psi55,13,38 and 39 in tRNA are highly conserved, being in the same position in eubacteria, archeabacteria and eukaryotes. Other psi sites occur in a more restricted fashion, for example psi2604in 23S RNA made by E.coli RluF has only been detected in E.coli. Human dyskerin with the help of guide RNAs makes the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


The actual alignment was detected with superfamily member cd02576:

Pssm-ID: 469624 [Multi-domain]  Cd Length: 371  Bit Score: 207.08  E-value: 2.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 310 GKVI----YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKeiEKKRMNVF 385
Cdd:cd02576    22 GSVVhltdYLHFTLYKENKDTMEAINKIAKLLRVKPSDFSYAGTKDKRAVTVQRVSVKKVTASRLKALNS--KLRGIRVG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 386 NIRSVDDSLRLGQLKGNHFDIVIRNLKkqindsANLRERIMEAIENVKKKGFVNYYGPQRFGKgRKVHTDQIGLALLKNE 465
Cdd:cd02576   100 NFEYKDEPLKLGDLKGNEFTIVIRNVK------ADSEELIKQALESLKEKGFINYYGLQRFGT-FSIPTHEIGIAILKEN 172


                  .
gi 2217291292 466 M 466
Cdd:cd02576   173 W 173
PseudoU_synth super family cl00130
Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to ...
 34-61 1.78e-04

Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi); Pseudouridine synthases contains the RsuA/RluD, TruA, TruB and TruD families. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases. Some psi sites such as psi55,13,38 and 39 in tRNA are highly conserved, being in the same position in eubacteria, archeabacteria and eukaryotes. Other psi sites occur in a more restricted fashion, for example psi2604in 23S RNA made by E.coli RluF has only been detected in E.coli. Human dyskerin with the help of guide RNAs makes the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


The actual alignment was detected with superfamily member cd02576:

Pssm-ID: 469624 [Multi-domain]  Cd Length: 371  Bit Score: 43.75  E-value: 1.78e-04
                          10        20
                  ....*....|....*....|....*...
gi 2217291292  34 GFHGTIKSSPSDFIVIEIDEQGQLVNKT 61
Cdd:cd02576     1 GFRGIIKQRYSDFVVNEIDLDGSVVHLT 28
 
Name Accession Description Interval E-value
PseudoU_synth_ScPUS7 cd02576
Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases ...
 310-466 2.70e-62

Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). Saccharomyces cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA), psi13 in cytoplasmic tRNAs and psi35 in pre-tRNATyr. Psi35 in yeast U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35.


Pssm-ID: 211341 [Multi-domain]  Cd Length: 371  Bit Score: 207.08  E-value: 2.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 310 GKVI----YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKeiEKKRMNVF 385
Cdd:cd02576    22 GSVVhltdYLHFTLYKENKDTMEAINKIAKLLRVKPSDFSYAGTKDKRAVTVQRVSVKKVTASRLKALNS--KLRGIRVG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 386 NIRSVDDSLRLGQLKGNHFDIVIRNLKkqindsANLRERIMEAIENVKKKGFVNYYGPQRFGKgRKVHTDQIGLALLKNE 465
Cdd:cd02576   100 NFEYKDEPLKLGDLKGNEFTIVIRNVK------ADSEELIKQALESLKEKGFINYYGLQRFGT-FSIPTHEIGIAILKEN 172


                  .
gi 2217291292 466 M 466
Cdd:cd02576   173 W 173
TruD COG0585
tRNA(Glu) U13 pseudouridine synthase TruD [Translation, ribosomal structure and biogenesis]; ...
 303-465 6.29e-33

tRNA(Glu) U13 pseudouridine synthase TruD [Translation, ribosomal structure and biogenesis]; tRNA(Glu) U13 pseudouridine synthase TruD is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440350 [Multi-domain]  Cd Length: 349  Bit Score: 127.62  E-value: 6.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 303 PLSECQEGKviYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVR-KVTPERLKNIE-KEIEkk 380
Cdd:COG0585    34 GFEPSGEGE--HLLLRIEKRGWNTLDVARRLARALGISRRRVGYAGLKDRHAVTTQWFSVHlGKDEPDLSALElEGVE-- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 381 rmnVFNIRSVDDSLRLGQLKGNHFDIVIRNLKKQindsanlRERIMEAIENVKKKGFVNYYGPQRFGKGRkvHTDQIGLA 460
Cdd:COG0585   110 ---VLEVGRHRRKLRRGDLKGNRFTIVLRDVDGD-------RERLEARLEEIAAQGVPNYFGEQRFGSDG--PNLFVAKA 177


                  ....*
gi 2217291292 461 LLKNE 465
Cdd:COG0585   178 LLRGD 182
TruD pfam01142
tRNA pseudouridine synthase D (TruD); TruD is responsible for synthesis of pseudouridine from ...
 314-465 3.45e-30

tRNA pseudouridine synthase D (TruD); TruD is responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. The structure of TruD reveals an overall V-shaped molecule which contains an RNA-binding cleft.


Pssm-ID: 426077 [Multi-domain]  Cd Length: 414  Bit Score: 121.53  E-value: 3.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 314 YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNiekeIEKKRMNVFNIRSVDDS 393
Cdd:pfam01142  44 YLILRLEKRNWDTNDAVRELARALGISRKRIGFAGTKDKRAVTTQYISIYGVDPEELEA----LNLKDIEIEVVGRANRK 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217291292 394 LRLGQLKGNHFDIVIRNLkkqinDSANLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVhTDQIGLALLKNE 465
Cdd:pfam01142 120 LRLGDLAGNRFRIRVRDA-----DEDEAASRAEAILEELKEFGVPNYFGYQRFGSIRPV-THLVGKAILRGD 185
truD PRK00984
tRNA pseudouridine synthase D; Reviewed
 309-469 1.54e-27

tRNA pseudouridine synthase D; Reviewed


Pssm-ID: 234884 [Multi-domain]  Cd Length: 341  Bit Score: 112.61  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 309 EGKviYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQ---AMVVRKVTPE----RLKNIekEIEKKr 381
Cdd:PRK00984   40 EGE--HLLVRIRKRGWNTLFVARALAKFLGISLRDVGYAGLKDRHAVTTQwfsIHLPGKEEPDlsafQLEGL--EILEL- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 382 mnvfnIRSvDDSLRLGQLKGNHFDIVIRNLKKQindsanlRERIMEAIENVKKKGFVNYYGPQRFGKGRKVHTDqiGLAL 461
Cdd:PRK00984  115 -----GRH-NRKLRLGDLKGNRFTIRLREVSKD-------RDKVEQRLEEIAAGGVPNYFGEQRFGSGGKNLQE--ALRW 179


                  ....*...
gi 2217291292 462 LKNEMRML 469
Cdd:PRK00984  180 ANGEKKVL 187
tRNA_TruD_broad TIGR00094
tRNA pseudouridine synthase, TruD family; an EGAD loading error caused one member to be called ...
 314-464 1.28e-22

tRNA pseudouridine synthase, TruD family; an EGAD loading error caused one member to be called surE, but that's an adjacent gene. MJ11364 is a strong partial match from 50 to 230 aa. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272903 [Multi-domain]  Cd Length: 387  Bit Score: 99.47  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 314 YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKEIekKRMNVFNIRSVDDS 393
Cdd:TIGR00094  44 FIHITVEKENWDTLEVLRVIAKFLGVSRREIGFAGTKDKRAVTTQWVCLPVKLEEEPDASNFQL--KGVKILSYNYHNRK 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217291292 394 LRLGQLKGNHFDIVIRnlkkqinDSANLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVhTDQIGLALLKN 464
Cdd:TIGR00094 122 IRLGDLKGNRFRIRIR-------DVELNSDELEETLNELCKKGFPNYFGSQRFGTFRII-THTVGRELLLS 184
PseudoU_synth_ScPUS7 cd02576
Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases ...
 34-61 1.78e-04

Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). Saccharomyces cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA), psi13 in cytoplasmic tRNAs and psi35 in pre-tRNATyr. Psi35 in yeast U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35.


Pssm-ID: 211341 [Multi-domain]  Cd Length: 371  Bit Score: 43.75  E-value: 1.78e-04
                          10        20
                  ....*....|....*....|....*...
gi 2217291292  34 GFHGTIKSSPSDFIVIEIDEQGQLVNKT 61
Cdd:cd02576     1 GFRGIIKQRYSDFVVNEIDLDGSVVHLT 28
 
Name Accession Description Interval E-value
PseudoU_synth_ScPUS7 cd02576
Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases ...
 310-466 2.70e-62

Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). Saccharomyces cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA), psi13 in cytoplasmic tRNAs and psi35 in pre-tRNATyr. Psi35 in yeast U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35.


Pssm-ID: 211341 [Multi-domain]  Cd Length: 371  Bit Score: 207.08  E-value: 2.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 310 GKVI----YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKeiEKKRMNVF 385
Cdd:cd02576    22 GSVVhltdYLHFTLYKENKDTMEAINKIAKLLRVKPSDFSYAGTKDKRAVTVQRVSVKKVTASRLKALNS--KLRGIRVG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 386 NIRSVDDSLRLGQLKGNHFDIVIRNLKkqindsANLRERIMEAIENVKKKGFVNYYGPQRFGKgRKVHTDQIGLALLKNE 465
Cdd:cd02576   100 NFEYKDEPLKLGDLKGNEFTIVIRNVK------ADSEELIKQALESLKEKGFINYYGLQRFGT-FSIPTHEIGIAILKEN 172


                  .
gi 2217291292 466 M 466
Cdd:cd02576   173 W 173
PseudoU_synth_TruD_like cd02552
Pseudouridine synthase, TruD family; This group consists of eukaryotic, bacterial and archeal ...
 307-447 2.63e-47

Pseudouridine synthase, TruD family; This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruD and Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruD and S. cerevisiae Pus7 make psi13 in cytoplasmic tRNAs. In addition S. cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA) and psi35 in pre-tRNATyr. Psi35 in U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35.


Pssm-ID: 211326 [Multi-domain]  Cd Length: 232  Bit Score: 163.14  E-value: 2.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 307 CQEGKVIYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIekEIEKKRMNVFN 386
Cdd:cd02552    25 WPKGEGEYLHFTLYKENKDTMEALREIAKALGVPPRDIGYAGTKDKRAVTTQRVSVHKPGKERLALL--NLELKGIRILE 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217291292 387 IRSVDDSLRLGQLKGNHFDIVIRNLKkqindsANLRERIMEAIENVKKKGFVNYYGPQRFG 447
Cdd:cd02552   103 FGRHDKKLRLGDLKGNRFTITLRGVS------PEEDELIERRLESLKEKGFPNYFGLQRFG 157
TruD COG0585
tRNA(Glu) U13 pseudouridine synthase TruD [Translation, ribosomal structure and biogenesis]; ...
 303-465 6.29e-33

tRNA(Glu) U13 pseudouridine synthase TruD [Translation, ribosomal structure and biogenesis]; tRNA(Glu) U13 pseudouridine synthase TruD is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440350 [Multi-domain]  Cd Length: 349  Bit Score: 127.62  E-value: 6.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 303 PLSECQEGKviYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVR-KVTPERLKNIE-KEIEkk 380
Cdd:COG0585    34 GFEPSGEGE--HLLLRIEKRGWNTLDVARRLARALGISRRRVGYAGLKDRHAVTTQWFSVHlGKDEPDLSALElEGVE-- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 381 rmnVFNIRSVDDSLRLGQLKGNHFDIVIRNLKKQindsanlRERIMEAIENVKKKGFVNYYGPQRFGKGRkvHTDQIGLA 460
Cdd:COG0585   110 ---VLEVGRHRRKLRRGDLKGNRFTIVLRDVDGD-------RERLEARLEEIAAQGVPNYFGEQRFGSDG--PNLFVAKA 177


                  ....*
gi 2217291292 461 LLKNE 465
Cdd:COG0585   178 LLRGD 182
TruD pfam01142
tRNA pseudouridine synthase D (TruD); TruD is responsible for synthesis of pseudouridine from ...
 314-465 3.45e-30

tRNA pseudouridine synthase D (TruD); TruD is responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. The structure of TruD reveals an overall V-shaped molecule which contains an RNA-binding cleft.


Pssm-ID: 426077 [Multi-domain]  Cd Length: 414  Bit Score: 121.53  E-value: 3.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 314 YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNiekeIEKKRMNVFNIRSVDDS 393
Cdd:pfam01142  44 YLILRLEKRNWDTNDAVRELARALGISRKRIGFAGTKDKRAVTTQYISIYGVDPEELEA----LNLKDIEIEVVGRANRK 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217291292 394 LRLGQLKGNHFDIVIRNLkkqinDSANLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVhTDQIGLALLKNE 465
Cdd:pfam01142 120 LRLGDLAGNRFRIRVRDA-----DEDEAASRAEAILEELKEFGVPNYFGYQRFGSIRPV-THLVGKAILRGD 185
truD PRK00984
tRNA pseudouridine synthase D; Reviewed
 309-469 1.54e-27

tRNA pseudouridine synthase D; Reviewed


Pssm-ID: 234884 [Multi-domain]  Cd Length: 341  Bit Score: 112.61  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 309 EGKviYTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQ---AMVVRKVTPE----RLKNIekEIEKKr 381
Cdd:PRK00984   40 EGE--HLLVRIRKRGWNTLFVARALAKFLGISLRDVGYAGLKDRHAVTTQwfsIHLPGKEEPDlsafQLEGL--EILEL- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 382 mnvfnIRSvDDSLRLGQLKGNHFDIVIRNLKKQindsanlRERIMEAIENVKKKGFVNYYGPQRFGKGRKVHTDqiGLAL 461
Cdd:PRK00984  115 -----GRH-NRKLRLGDLKGNRFTIRLREVSKD-------RDKVEQRLEEIAAGGVPNYFGEQRFGSGGKNLQE--ALRW 179


                  ....*...
gi 2217291292 462 LKNEMRML 469
Cdd:PRK00984  180 ANGEKKVL 187
PSTD1 cd02577
Pseudouridine synthase, a subgroup of the TruD family; This group consists of several ...
 314-465 5.45e-25

Pseudouridine synthase, a subgroup of the TruD family; This group consists of several hypothetical archeal pseudouridine synthases assigned to the TruD family of psuedouridine synthases. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). The TruD family is comprised of proteins related to Escherichia coli TruD.


Pssm-ID: 211342 [Multi-domain]  Cd Length: 319  Bit Score: 105.10  E-value: 5.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 314 YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIeKEIEKKRMnvfnIRSvDDS 393
Cdd:cd02577    26 YLIYLLEKKNWDTLDAVRRIAKALGISRKRIGYAGTKDKHAVTTQYISIFDPKDEEKLSI-KDIELKVL----GRS-RKP 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217291292 394 LRLGQLKGNHFDIVIRNLKKqindsaNLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVhTDQIGLALLKNE 465
Cdd:cd02577   100 LRLGDLWGNRFEITVRDLGD------EEIERIETLVEEVEKGGFPNYFGSQRFGSVRPV-THFVGKLILEGD 164
PseudoU_synth_EcTruD cd02575
Pseudouridine synthase, similar to Escherichia coli TruD; This group consists of bacterial ...
 319-468 3.97e-23

Pseudouridine synthase, similar to Escherichia coli TruD; This group consists of bacterial pseudouridine synthases similar to Escherichia coli TruD. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruD makes the highly phylogenetically conserved psi13 in tRNAs.


Pssm-ID: 211340 [Multi-domain]  Cd Length: 253  Bit Score: 98.05  E-value: 3.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 319 LRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKvtPERLKNIEKEIEKKRMNVFNIRSVDDSLRLGQ 398
Cdd:cd02575    31 IRKTGLNTREVAKELAKALGVKERDVGYAGLKDRHAVTTQWFSVHL--PGKEAPDLSALQLEGVKILEVTRHNRKLRRGH 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217291292 399 LKGNHFDIVIRNLKKQindsanlRERIMEAIENVKKKGFVNYYGPQRFGK-GRKVhtdQIGLALLKNEMRM 468
Cdd:cd02575   109 LKGNRFVIRLRGVSGN-------ADKLEQRLETIAQKGVPNYFGPQRFGRdGGNL---LQGLRLLAGERKV 169
tRNA_TruD_broad TIGR00094
tRNA pseudouridine synthase, TruD family; an EGAD loading error caused one member to be called ...
 314-464 1.28e-22

tRNA pseudouridine synthase, TruD family; an EGAD loading error caused one member to be called surE, but that's an adjacent gene. MJ11364 is a strong partial match from 50 to 230 aa. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272903 [Multi-domain]  Cd Length: 387  Bit Score: 99.47  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291292 314 YTAFTLRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQAMVVRKVTPERLKNIEKEIekKRMNVFNIRSVDDS 393
Cdd:TIGR00094  44 FIHITVEKENWDTLEVLRVIAKFLGVSRREIGFAGTKDKRAVTTQWVCLPVKLEEEPDASNFQL--KGVKILSYNYHNRK 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217291292 394 LRLGQLKGNHFDIVIRnlkkqinDSANLRERIMEAIENVKKKGFVNYYGPQRFGKGRKVhTDQIGLALLKN 464
Cdd:TIGR00094 122 IRLGDLKGNRFRIRIR-------DVELNSDELEETLNELCKKGFPNYFGSQRFGTFRII-THTVGRELLLS 184
PseudoU_synth cd01291
Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to ...
 319-389 6.65e-10

Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi); Pseudouridine synthases contains the RsuA/RluD, TruA, TruB and TruD families. This group consists of eukaryotic, bacterial and archeal pseudouridine synthases. Some psi sites such as psi55,13,38 and 39 in tRNA are highly conserved, being in the same position in eubacteria, archeabacteria and eukaryotes. Other psi sites occur in a more restricted fashion, for example psi2604in 23S RNA made by E.coli RluF has only been detected in E.coli. Human dyskerin with the help of guide RNAs makes the hundreds of psueudouridnes present in rRNA and small nuclear RNAs (snRNAs). Mutations in human dyskerin cause X-linked dyskeratosis congenitas. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


Pssm-ID: 211324 [Multi-domain]  Cd Length: 87  Bit Score: 55.65  E-value: 6.65e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217291292 319 LRKENLEMFEAIGFLAIKLGVIPSDFSYAGLKDKKAITYQ------AMVVRkVTPERLKNIEKEIEKKRMNVFNIRS 389
Cdd:cd01291     1 LYKPGGDTMEAARQLAKLLGIPPKRVGYAGRKDKRAVTTQlvsnrfTITLR-VKPLNLKWPEERKRALVLEFTLPRG 76
PseudoU_synth_ScPUS7 cd02576
Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases ...
 34-61 1.78e-04

Pseudouridine synthase, TruD family; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus7. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). Saccharomyces cerevisiae Pus7 makes psi35 in U2 small nuclear RNA (U2 snRNA), psi13 in cytoplasmic tRNAs and psi35 in pre-tRNATyr. Psi35 in yeast U2 snRNA and psi13 in tRNAs are highly phylogenetically conserved. Psi34 is the mammalian U2 snRNA counterpart of yeast U2 snRNA psi35.


Pssm-ID: 211341 [Multi-domain]  Cd Length: 371  Bit Score: 43.75  E-value: 1.78e-04
                          10        20
                  ....*....|....*....|....*...
gi 2217291292  34 GFHGTIKSSPSDFIVIEIDEQGQLVNKT 61
Cdd:cd02576     1 GFRGIIKQRYSDFVVNEIDLDGSVVHLT 28
 
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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