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Conserved domains on  [gi|1046854406|ref|XP_017453841|]
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pseudouridylate synthase 1 homolog isoform X2 [Rattus norvegicus]

Protein Classification

pseudouridine synthase family protein( domain architecture ID 10118740)

pseudouridine synthase family protein may catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines; similar to tRNA pseudouridine synthase 1

CATH:  3.30.2350.10
EC:  5.4.99.-
PubMed:  12762017|12756329
SCOP:  3001360

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseudoU_synth_PUS1_PUS2 cd02568
Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine ...
84-290 5.37e-97

Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus1p, S. cerevisiae Pus2p, Caenorhabditis elegans Pus1p and human PUS1. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae Pus1p catalyzes the formation of psi34 and psi36 in the intron-containing tRNAIle, psi35 in the intron-containing tRNATyr, psi27 and/or psi28 in several yeast cytoplasmic tRNAs and, psi44 in U2 small nuclear RNA (U2 snRNA). The presence of the intron is required for the formation of psi 34, 35 and 36. In addition S. cerevisiae PUS1 makes are psi 26, 65 and 67. C. elegans Pus1p does not modify psi44 in U2 snRNA. Mouse Pus1p makes psi27/28 in pre- tRNASer , tRNAVal and tRNAIle, psi 34/36 in tRNAIle and, psi 32 and potentially 67 in tRNAVal. Psi44 in U2 snRNA and psi32 in tRNAs are highly phylogenetically conserved. Psi 26,27,28,34,35,36,65 and 67 in tRNAs are less highly conserved. Mouse Pus1p regulates nuclear receptor activity through pseudouridylation of Steroid Receptor RNA Activator. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


:

Pssm-ID: 211335 [Multi-domain]  Cd Length: 245  Bit Score: 288.74  E-value: 5.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  84 LLMAYSGKGYHGMQ--------------------------------------------GVSAAGQVVSLKVWLID----- 114
Cdd:cd02568     1 LLFGYCGTGYHGMQynpgayktiegeleralfkagaisesnagdpkkigfsraartdkGVHAARNVVSLKVIIDDpeglg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 115 ---DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdesyrlsaETLQQVNRLLGCYKG 191
Cdd:cd02568    81 ileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------------ETLQRFNEILKEYVG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 192 THNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGE 270
Cdd:cd02568   145 THNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGLAIAIVRGGAPESLIELSFNK 224
                         250       260
                  ....*....|....*....|.
gi 1046854406 271 EKVD-VPKAPGLGLVLERVHF 290
Cdd:cd02568   225 DKIIiIPLAPGLGLLLERPHF 245
 
Name Accession Description Interval E-value
PseudoU_synth_PUS1_PUS2 cd02568
Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine ...
84-290 5.37e-97

Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus1p, S. cerevisiae Pus2p, Caenorhabditis elegans Pus1p and human PUS1. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae Pus1p catalyzes the formation of psi34 and psi36 in the intron-containing tRNAIle, psi35 in the intron-containing tRNATyr, psi27 and/or psi28 in several yeast cytoplasmic tRNAs and, psi44 in U2 small nuclear RNA (U2 snRNA). The presence of the intron is required for the formation of psi 34, 35 and 36. In addition S. cerevisiae PUS1 makes are psi 26, 65 and 67. C. elegans Pus1p does not modify psi44 in U2 snRNA. Mouse Pus1p makes psi27/28 in pre- tRNASer , tRNAVal and tRNAIle, psi 34/36 in tRNAIle and, psi 32 and potentially 67 in tRNAVal. Psi44 in U2 snRNA and psi32 in tRNAs are highly phylogenetically conserved. Psi 26,27,28,34,35,36,65 and 67 in tRNAs are less highly conserved. Mouse Pus1p regulates nuclear receptor activity through pseudouridylation of Steroid Receptor RNA Activator. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


Pssm-ID: 211335 [Multi-domain]  Cd Length: 245  Bit Score: 288.74  E-value: 5.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  84 LLMAYSGKGYHGMQ--------------------------------------------GVSAAGQVVSLKVWLID----- 114
Cdd:cd02568     1 LLFGYCGTGYHGMQynpgayktiegeleralfkagaisesnagdpkkigfsraartdkGVHAARNVVSLKVIIDDpeglg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 115 ---DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdesyrlsaETLQQVNRLLGCYKG 191
Cdd:cd02568    81 ileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------------ETLQRFNEILKEYVG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 192 THNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGE 270
Cdd:cd02568   145 THNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGLAIAIVRGGAPESLIELSFNK 224
                         250       260
                  ....*....|....*....|.
gi 1046854406 271 EKVD-VPKAPGLGLVLERVHF 290
Cdd:cd02568   225 DKIIiIPLAPGLGLLLERPHF 245
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
80-285 1.09e-31

tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme TruA, tRNA pseudouridine(38-40) synthase. In a few species (e.g. Bacillus anthracis), TruA is represented by two paralogs. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272889 [Multi-domain]  Cd Length: 227  Bit Score: 119.34  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  80 RKIVLLMAYSGKGYHGMQ----------------------------------GVSAAGQVVSLKvwLIDDILD-----KI 120
Cdd:TIGR00071   1 RKIALKIAYDGSNYHGWQrqpnkrtvqgelekaleaigkkkitimsagrtdkGVHAMGQVISFD--TPKEIPDnklnaKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 121 NSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafaHKDRDVqdesYRLSAETLQQVnrlLGCYKGTHNFHNFTS 200
Cdd:TIGR00071  79 NALLPPDIRVKALAPVNDNFHARFSASKRHYRYILY-----NHRHYY----SPLDLEKMRAA---AKQLLGKHDFSNFSK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 201 QKGPrEPSARRYILEMYceepfVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKA 278
Cdd:TIGR00071 147 AKSK-SRSPIRTISDIK-----VSESGEYIIFDIIGNSFLWHMVRKIVGALVLVGRGKLPPEWVAKLLDAKKRNlaPTTA 220

                  ....*..
gi 1046854406 279 PGLGLVL 285
Cdd:TIGR00071 221 PANGLYL 227
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
80-288 3.51e-26

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 104.84  E-value: 3.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  80 RKIVLLMAYSGKGYHGMQ----------------------------------GVSAAGQVVSL---KVWLIDDILDKINS 122
Cdd:PRK00021    2 MRIALTIEYDGTNFHGWQrqpngrtvqgelekalsklagepvrvigagrtdaGVHALGQVAHFdtpAPRPPEKWRRALNA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 123 HLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPT--FAFAHKDRDVQDESYRLSAETLQQVNRLLgcyKGTHNFHNFTS 200
Cdd:PRK00021   82 LLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNrpARPPFLRGYVWHYPYPLDVDAMNEAAQYL---LGEHDFTSFRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 201 QKGPREpSARRYILEMYCEepfvREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKA 278
Cdd:PRK00021  159 SGCQSK-SPVRTIYEADVT----REG-DFIVFDISANGFLHNMVRNIVGTLLEVGKGKRPPEDIKELLEAKDRTlaGPTA 232
                         250
                  ....*....|
gi 1046854406 279 PGLGLVLERV 288
Cdd:PRK00021  233 PAEGLYLVEV 242
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
189-291 4.24e-15

tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem and loop of transfer-RNAs Pseudouridine is an isomer of uridine (5-(beta-D-ribofuranosyl) uracil, and id the most abundant modified nucleoside found in all cellular RNAs. The TruA-like proteins also exhibit a conserved sequence with a strictly conserved aspartic acid, likely involved in catalysis.


Pssm-ID: 460204 [Multi-domain]  Cd Length: 108  Bit Score: 70.64  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 189 YKGTHNFHNFTSQKGPREPSaRRYILEMYCEEPFVREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLER-- 266
Cdd:pfam01416   5 YVGTHDFGNFCKQDQPKKNT-VRTILEAAVSRVGGEDG-DLIVFEVRGSGFLDHMVRAMVGVLFLVGQGKEPPEWIAEll 82
                          90       100
                  ....*....|....*....|....*.
gi 1046854406 267 -SWGEEKVDVPKAPGLGLVLERVHFE 291
Cdd:pfam01416  83 nAKDPRKIAGPTAPPVGLYLFHVRYP 108
 
Name Accession Description Interval E-value
PseudoU_synth_PUS1_PUS2 cd02568
Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine ...
84-290 5.37e-97

Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine synthases similar to Saccharomyces cerevisiae Pus1p, S. cerevisiae Pus2p, Caenorhabditis elegans Pus1p and human PUS1. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae Pus1p catalyzes the formation of psi34 and psi36 in the intron-containing tRNAIle, psi35 in the intron-containing tRNATyr, psi27 and/or psi28 in several yeast cytoplasmic tRNAs and, psi44 in U2 small nuclear RNA (U2 snRNA). The presence of the intron is required for the formation of psi 34, 35 and 36. In addition S. cerevisiae PUS1 makes are psi 26, 65 and 67. C. elegans Pus1p does not modify psi44 in U2 snRNA. Mouse Pus1p makes psi27/28 in pre- tRNASer , tRNAVal and tRNAIle, psi 34/36 in tRNAIle and, psi 32 and potentially 67 in tRNAVal. Psi44 in U2 snRNA and psi32 in tRNAs are highly phylogenetically conserved. Psi 26,27,28,34,35,36,65 and 67 in tRNAs are less highly conserved. Mouse Pus1p regulates nuclear receptor activity through pseudouridylation of Steroid Receptor RNA Activator. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


Pssm-ID: 211335 [Multi-domain]  Cd Length: 245  Bit Score: 288.74  E-value: 5.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  84 LLMAYSGKGYHGMQ--------------------------------------------GVSAAGQVVSLKVWLID----- 114
Cdd:cd02568     1 LLFGYCGTGYHGMQynpgayktiegeleralfkagaisesnagdpkkigfsraartdkGVHAARNVVSLKVIIDDpeglg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 115 ---DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdesyrlsaETLQQVNRLLGCYKG 191
Cdd:cd02568    81 ileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------------ETLQRFNEILKEYVG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 192 THNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGE 270
Cdd:cd02568   145 THNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGLAIAIVRGGAPESLIELSFNK 224
                         250       260
                  ....*....|....*....|.
gi 1046854406 271 EKVD-VPKAPGLGLVLERVHF 290
Cdd:cd02568   225 DKIIiIPLAPGLGLLLERPHF 245
PseudoU_synth_TruA_like cd00497
Pseudouridine synthase, TruA family; This group consists of eukaryotic, bacterial and archeal ...
87-290 1.20e-33

Pseudouridine synthase, TruA family; This group consists of eukaryotic, bacterial and archeal pseudouridine synthases similar to Escherichia coli TruA, Saccharomyces cerevisiae Pus1p, S. cerevisiae Pus3p Caenorhabditis elegans Pus1p and human PUS1. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae PUS1 catalyzes the formation of psi34 and psi36 in the intron containing tRNAIle, psi35 in the intron containing tRNATyr, psi27 and/or psi28 in several yeast cytoplasmic tRNAs and, psi44 in U2 small nuclear RNA (U2 snRNA). The presence of the intron is required for the formation of psi 34, 35 and 36. In addition S. cerevisiae PUS1 makes psi 26, 65 and 67. C. elegans Pus1p does not modify psi44 in U2 snRNA. S. cerevisiae Pus3p makes psi38 and psi39 in tRNAs. Psi44 in U2 snRNA and, psi38 and psi39 in tRNAs are highly phylogenetically conserved. Psi 26,27,28,34,35,36,65 and 67 in tRNAs are less highly conserved. Mouse Pus1p regulates nuclear receptor activity through pseudouridylation of Steroid Receptor RNA Activator. Missense mutation in human PUS1 causes mitochondrial myopathy and sideroblastic anemia (MLASA).


Pssm-ID: 211322 [Multi-domain]  Cd Length: 215  Bit Score: 124.42  E-value: 1.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  87 AYSGKGYHGMQ----------------------------------GVSAAGQVVSLKV--WLIDDIldkINSHLPSHIRI 130
Cdd:cd00497     2 GYDGTKYHGFQrqndvptvegeliiallkagnipyfikaaartdrGVSALGQVVAIETerRLTPEA---LNGILPGDIRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 131 LGLKRVTGGFNSKNKCDARTYCYMLPTFafahkdrDVQDESyrlsaetlqqVNRLLGCYKGTHNFHNFTSQKGpREPsaR 210
Cdd:cd00497    79 FAVHSVPPDFHAPRYCDHRTYRYYIPSF-------PLDDER----------LKSAASRFLGTHDFTNFSKKDT-RNT--V 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 211 RYILEMYCEEPFvreglEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVDVPK--APGLGLVLERV 288
Cdd:cd00497   139 RTIISIECKDLN-----PFVVVEFKAKSFLWHQVRRMVGFLMLVGEGLHSPSSVSRLLAGPAPPIPMvpAPAEGLLLVDV 213

                  ..
gi 1046854406 289 HF 290
Cdd:cd00497   214 KY 215
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
80-285 1.09e-31

tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme TruA, tRNA pseudouridine(38-40) synthase. In a few species (e.g. Bacillus anthracis), TruA is represented by two paralogs. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272889 [Multi-domain]  Cd Length: 227  Bit Score: 119.34  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  80 RKIVLLMAYSGKGYHGMQ----------------------------------GVSAAGQVVSLKvwLIDDILD-----KI 120
Cdd:TIGR00071   1 RKIALKIAYDGSNYHGWQrqpnkrtvqgelekaleaigkkkitimsagrtdkGVHAMGQVISFD--TPKEIPDnklnaKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 121 NSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafaHKDRDVqdesYRLSAETLQQVnrlLGCYKGTHNFHNFTS 200
Cdd:TIGR00071  79 NALLPPDIRVKALAPVNDNFHARFSASKRHYRYILY-----NHRHYY----SPLDLEKMRAA---AKQLLGKHDFSNFSK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 201 QKGPrEPSARRYILEMYceepfVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKA 278
Cdd:TIGR00071 147 AKSK-SRSPIRTISDIK-----VSESGEYIIFDIIGNSFLWHMVRKIVGALVLVGRGKLPPEWVAKLLDAKKRNlaPTTA 220

                  ....*..
gi 1046854406 279 PGLGLVL 285
Cdd:TIGR00071 221 PANGLYL 227
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
80-288 3.51e-26

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 104.84  E-value: 3.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  80 RKIVLLMAYSGKGYHGMQ----------------------------------GVSAAGQVVSL---KVWLIDDILDKINS 122
Cdd:PRK00021    2 MRIALTIEYDGTNFHGWQrqpngrtvqgelekalsklagepvrvigagrtdaGVHALGQVAHFdtpAPRPPEKWRRALNA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 123 HLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPT--FAFAHKDRDVQDESYRLSAETLQQVNRLLgcyKGTHNFHNFTS 200
Cdd:PRK00021   82 LLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNrpARPPFLRGYVWHYPYPLDVDAMNEAAQYL---LGEHDFTSFRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 201 QKGPREpSARRYILEMYCEepfvREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKA 278
Cdd:PRK00021  159 SGCQSK-SPVRTIYEADVT----REG-DFIVFDISANGFLHNMVRNIVGTLLEVGKGKRPPEDIKELLEAKDRTlaGPTA 232
                         250
                  ....*....|
gi 1046854406 279 PGLGLVLERV 288
Cdd:PRK00021  233 PAEGLYLVEV 242
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
189-291 4.24e-15

tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem and loop of transfer-RNAs Pseudouridine is an isomer of uridine (5-(beta-D-ribofuranosyl) uracil, and id the most abundant modified nucleoside found in all cellular RNAs. The TruA-like proteins also exhibit a conserved sequence with a strictly conserved aspartic acid, likely involved in catalysis.


Pssm-ID: 460204 [Multi-domain]  Cd Length: 108  Bit Score: 70.64  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 189 YKGTHNFHNFTSQKGPREPSaRRYILEMYCEEPFVREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLER-- 266
Cdd:pfam01416   5 YVGTHDFGNFCKQDQPKKNT-VRTILEAAVSRVGGEDG-DLIVFEVRGSGFLDHMVRAMVGVLFLVGQGKEPPEWIAEll 82
                          90       100
                  ....*....|....*....|....*.
gi 1046854406 267 -SWGEEKVDVPKAPGLGLVLERVHFE 291
Cdd:pfam01416  83 nAKDPRKIAGPTAPPVGLYLFHVRYP 108
PseudoU_synth_ScPus3 cd02569
Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like; This group consists of eukaryotic ...
98-290 1.49e-14

Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like; This group consists of eukaryotic pseudouridine synthases similar to S. cerevisiae Pus3p, mouse Pus3p and, human PUS2. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. S. cerevisiae Pus3p makes psi38 and psi39 in tRNAs. Mouse Pus3p has been shown to makes psi38 and, possibly also psi 39, in tRNAs. Psi38 and psi39 are highly conserved in tRNAs from eubacteria, archea and eukarya.


Pssm-ID: 211336 [Multi-domain]  Cd Length: 256  Bit Score: 72.70  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  98 GVSAAGQVVSLKV-------WLIDDILDK--------------INSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYmlp 156
Cdd:cd02569    54 GVSAFGQVISLDVrsnlkpeDGLDPSTDVkstadeeelpyckiLNRVLPPDIRILAWAPVPPDFSARFSCVSRTYRY--- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 157 tfAFAHKDRDVqdesyrlsaETLQQVNRLlgcYKGTHNFHNFTSQKGPREP-SARRYILEMYCEE-PFVREGLEFAVIKV 234
Cdd:cd02569   131 --FFPKGDLDI---------ELMRKAAKL---LLGEHDFRNFCKMDVANQVtNYVRRVLSAEVEPvDQHPDGDGLYYFEV 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046854406 235 KGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKvdVPK------APGLGLVLERVHF 290
Cdd:cd02569   197 RGSAFLWHQVRCMMAVLFLIGQGLEPPSVISQLLDVEK--NPRkpqytmASEVPLVLYDCGF 256
PseudoU_synth_TruA_Archea cd02866
Archeal pseudouridine synthases; This group consists of archeal pseudouridine synthases. ...
98-285 1.86e-14

Archeal pseudouridine synthases; This group consists of archeal pseudouridine synthases.Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. This group of proteins make Psedouridine in tRNAs.


Pssm-ID: 211343 [Multi-domain]  Cd Length: 219  Bit Score: 71.64  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  98 GVSAAGQVVSlkVWLIDD-ILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafahkdrdvqdESYRLSA 176
Cdd:cd02866    51 GVHALGNVVV--FETEKEpIPPMINAKLPKDIWVLAGAKVPEDFDPRRWAHRKYYRYNLG-------------SDYDVEA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 177 etLQQVNRLLgcyKGTHNFHNFTSQKGPREPSARRYILEmyceepfVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVK 256
Cdd:cd02866   116 --MKEAAKKL---IGTHDFSNFSKRDGRKDPVRTIERIE-------ISENGEFITIDVVGESFLWNMVRRIVGALSEVGK 183
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1046854406 257 GYAPESVLER--SWGEEKVDVPKAPGLGLVL 285
Cdd:cd02866   184 GKRENEWVEKllDGEFRPEGVPPAPPEGLIL 214
PLN03078 PLN03078
Putative tRNA pseudouridine synthase; Provisional
120-291 4.34e-14

Putative tRNA pseudouridine synthase; Provisional


Pssm-ID: 215562 [Multi-domain]  Cd Length: 513  Bit Score: 73.40  E-value: 4.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 120 INSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKDRDVQDESyrlsAETLQQVNRLLGCYKGTHNFHNFT 199
Cdd:PLN03078  167 INSHLPDNIRVFSILPAQRSFDPRRECDLRKYSYLLPAEVIGIKSGFSSEEI----DEHISEFNSILNGFEGEHPFHNYT 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 200 SQ--------------------------------------------------------------KGPREPSARRYILEMY 217
Cdd:PLN03078  243 ARskyrkklpgkhkqrngavsrraksskemssseseenhgeiseedeedlsfssipsgssdeneDILKFQSSQVQIRARW 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 218 CEEPFVRE----------------------GLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGE-EKVD 274
Cdd:PLN03078  323 LHEPDETDrisashfrkifrcscgklekslGFDFVELSIWGESFMLHQIRKMVGTAVAVKRELLPRDIIRLSLTKfSRIV 402
                         250
                  ....*....|....*..
gi 1046854406 275 VPKAPGLGLVLERVHFE 291
Cdd:PLN03078  403 LPLAPSEVLILRGNSFS 419
PRK14587 PRK14587
tRNA pseudouridine synthase ACD; Provisional
90-285 5.60e-08

tRNA pseudouridine synthase ACD; Provisional


Pssm-ID: 173051  Cd Length: 256  Bit Score: 53.29  E-value: 5.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406  90 GKGYHGMQGVSAAGQVVSLKVWLIddiLDKINSHLPSHIRILGLKRVTGGFNSKnKCDARTYCYMLPtfafaHKDRDVqd 169
Cdd:PRK14587   37 GRGSRTDPGVSAVGNVVMTSQKLP---LGYVNSKLPRGVWAWAVAEVPEGFNPR-RAKRRRYLYVAP-----HWGEDV-- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854406 170 ESYRLSAETLqqvnrllgcyKGTHNFHNFTSQKGPREPSARRYILEMYCEepfVREGLEFavIKVKGQSFMMHQIRKMVG 249
Cdd:PRK14587  106 EAMREAAELL----------AGTHDYSSFIQRRGEKATPTVTTVYEIGVE---LRGDLIY--LYFVGRGFRNKMIRKMAW 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1046854406 250 LVVAIVKGyapesVLERSWGEEKVD------VPKAPGLGLVL 285
Cdd:PRK14587  171 AILAAGRG-----VLSRRDIAELLErprpgaVPSAPAEGLVL 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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