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Conserved domains on  [gi|70906468|ref|NP_001020732|]
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pseudouridylate synthase 1 homolog isoform 1 [Mus musculus]

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 ...
84-354 1.14e-123

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: 358.85  E-value: 1.14e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  84 LLMAYSGKGYHGMQRNLGSsqFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 163
Cdd:cd02568   1 LLFGYCGTGYHGMQYNPGA--YKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDK------------------GV 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 164 SAAGQVVSLKVWLID--------DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdes 235
Cdd:cd02568  61 HAARNVVSLKVIIDDpeglgileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 236 yrlsaETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGL 314
Cdd:cd02568 130 -----ETLQRFNEILKEYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGL 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 70906468 315 VVAIVKGYAPESVLERSWGEEKVD-VPKAPGLGLVLERVHF 354
Cdd:cd02568 205 AIAIVRGGAPESLIELSFNKDKIIiIPLAPGLGLLLERPHF 245
 
Name Accession Description Interval E-value
PseudoU_synth_PUS1_PUS2 cd02568
Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine ...
84-354 1.14e-123

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: 358.85  E-value: 1.14e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  84 LLMAYSGKGYHGMQRNLGSsqFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 163
Cdd:cd02568   1 LLFGYCGTGYHGMQYNPGA--YKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDK------------------GV 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 164 SAAGQVVSLKVWLID--------DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdes 235
Cdd:cd02568  61 HAARNVVSLKVIIDDpeglgileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 236 yrlsaETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGL 314
Cdd:cd02568 130 -----ETLQRFNEILKEYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGL 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 70906468 315 VVAIVKGYAPESVLERSWGEEKVD-VPKAPGLGLVLERVHF 354
Cdd:cd02568 205 AIAIVRGGAPESLIELSFNKDKIIiIPLAPGLGLLLERPHF 245
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
80-349 5.21e-41

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: 145.54  E-value: 5.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468    80 RKIVLLMAYSGKGYHGMQRNLGssqFRTIEDDLVSALVQAGcipenhgtdMRKMSFQRCARTDKplrtsacfclytgflf 159
Cdd:TIGR00071   1 RKIALKIAYDGSNYHGWQRQPN---KRTVQGELEKALEAIG---------KKKITIMSAGRTDK---------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   160 hwGVSAAGQVVSLKvwLIDDILD-----KINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafaHKDRDVqde 234
Cdd:TIGR00071  53 --GVHAMGQVISFD--TPKEIPDnklnaKLNALLPPDIRVKALAPVNDNFHARFSASKRHYRYILY-----NHRHYY--- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   235 sYRLSAETLQQVnrlLACYKGTHNFHNFTSQKGPrEPSARRYILEMYceepfVREGLEFAVIKVKGQSFMMHQIRKMVGL 314
Cdd:TIGR00071 121 -SPLDLEKMRAA---AKQLLGKHDFSNFSKAKSK-SRSPIRTISDIK-----VSESGEYIIFDIIGNSFLWHMVRKIVGA 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 70906468   315 VVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVL 349
Cdd:TIGR00071 191 LVLVGRGKLPPEWVAKLLDAKKRNlaPTTAPANGLYL 227
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
80-352 2.86e-29

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 114.47  E-value: 2.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   80 RKIVLLMAYSGKGYHGMQRnlgssQ--FRTIEDDLVSALvqagcipenhgtdmRKMSFQR----CA-RTDKplrtsacfc 152
Cdd:PRK00021   2 MRIALTIEYDGTNFHGWQR-----QpnGRTVQGELEKAL--------------SKLAGEPvrviGAgRTDA--------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  153 lytgflfhwGVSAAGQVVSL---KVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPT--FAFAHK 227
Cdd:PRK00021  54 ---------GVHALGQVAHFdtpAPRPPEKWRRALNALLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNrpARPPFL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  228 DRDVQDESYRLSAETLQQVNRLLacyKGTHNFHNFTSQKGPREpSARRYILEMYCEepfvREGlEFAVIKVKGQSFMMHQ 307
Cdd:PRK00021 125 RGYVWHYPYPLDVDAMNEAAQYL---LGEHDFTSFRASGCQSK-SPVRTIYEADVT----REG-DFIVFDISANGFLHNM 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 70906468  308 IRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVLERV 352
Cdd:PRK00021 196 VRNIVGTLLEVGKGKRPPEDIKELLEAKDRTlaGPTAPAEGLYLVEV 242
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
253-355 6.00e-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: 6.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   253 YKGTHNFHNFTSQKGPREPSaRRYILEMYCEEPFVREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLER-- 330
Cdd:pfam01416   5 YVGTHDFGNFCKQDQPKKNT-VRTILEAAVSRVGGEDG-DLIVFEVRGSGFLDHMVRAMVGVLFLVGQGKEPPEWIAEll 82
                          90       100
                  ....*....|....*....|....*.
gi 70906468   331 -SWGEEKVDVPKAPGLGLVLERVHFE 355
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 ...
84-354 1.14e-123

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: 358.85  E-value: 1.14e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  84 LLMAYSGKGYHGMQRNLGSsqFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 163
Cdd:cd02568   1 LLFGYCGTGYHGMQYNPGA--YKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDK------------------GV 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 164 SAAGQVVSLKVWLID--------DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdes 235
Cdd:cd02568  61 HAARNVVSLKVIIDDpeglgileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 236 yrlsaETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGL 314
Cdd:cd02568 130 -----ETLQRFNEILKEYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGL 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 70906468 315 VVAIVKGYAPESVLERSWGEEKVD-VPKAPGLGLVLERVHF 354
Cdd:cd02568 205 AIAIVRGGAPESLIELSFNKDKIIiIPLAPGLGLLLERPHF 245
PseudoU_synth_TruA_like cd00497
Pseudouridine synthase, TruA family; This group consists of eukaryotic, bacterial and archeal ...
87-354 2.30e-44

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: 154.08  E-value: 2.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  87 AYSGKGYHGMQRnlgSSQFRTIEDDLVSALVQAGCIPENhgtdmrkmsFQRCARTDKplrtsacfclytgflfhwGVSAA 166
Cdd:cd00497   2 GYDGTKYHGFQR---QNDVPTVEGELIIALLKAGNIPYF---------IKAAARTDR------------------GVSAL 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 167 GQVVSLKV--WLIDDIldkINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFafahkdrDVQDESyrlsaetlq 244
Cdd:cd00497  52 GQVVAIETerRLTPEA---LNGILPGDIRVFAVHSVPPDFHAPRYCDHRTYRYYIPSF-------PLDDER--------- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 245 qVNRLLACYKGTHNFHNFTSQKGpREPsaRRYILEMYCEEPFvreglEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAP 324
Cdd:cd00497 113 -LKSAASRFLGTHDFTNFSKKDT-RNT--VRTIISIECKDLN-----PFVVVEFKAKSFLWHQVRRMVGFLMLVGEGLHS 183
                       250       260       270
                ....*....|....*....|....*....|..
gi 70906468 325 ESVLERSWGEEKVDVPK--APGLGLVLERVHF 354
Cdd:cd00497 184 PSSVSRLLAGPAPPIPMvpAPAEGLLLVDVKY 215
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
80-349 5.21e-41

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: 145.54  E-value: 5.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468    80 RKIVLLMAYSGKGYHGMQRNLGssqFRTIEDDLVSALVQAGcipenhgtdMRKMSFQRCARTDKplrtsacfclytgflf 159
Cdd:TIGR00071   1 RKIALKIAYDGSNYHGWQRQPN---KRTVQGELEKALEAIG---------KKKITIMSAGRTDK---------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   160 hwGVSAAGQVVSLKvwLIDDILD-----KINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafaHKDRDVqde 234
Cdd:TIGR00071  53 --GVHAMGQVISFD--TPKEIPDnklnaKLNALLPPDIRVKALAPVNDNFHARFSASKRHYRYILY-----NHRHYY--- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   235 sYRLSAETLQQVnrlLACYKGTHNFHNFTSQKGPrEPSARRYILEMYceepfVREGLEFAVIKVKGQSFMMHQIRKMVGL 314
Cdd:TIGR00071 121 -SPLDLEKMRAA---AKQLLGKHDFSNFSKAKSK-SRSPIRTISDIK-----VSESGEYIIFDIIGNSFLWHMVRKIVGA 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 70906468   315 VVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVL 349
Cdd:TIGR00071 191 LVLVGRGKLPPEWVAKLLDAKKRNlaPTTAPANGLYL 227
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
80-352 2.86e-29

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 114.47  E-value: 2.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   80 RKIVLLMAYSGKGYHGMQRnlgssQ--FRTIEDDLVSALvqagcipenhgtdmRKMSFQR----CA-RTDKplrtsacfc 152
Cdd:PRK00021   2 MRIALTIEYDGTNFHGWQR-----QpnGRTVQGELEKAL--------------SKLAGEPvrviGAgRTDA--------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  153 lytgflfhwGVSAAGQVVSL---KVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPT--FAFAHK 227
Cdd:PRK00021  54 ---------GVHALGQVAHFdtpAPRPPEKWRRALNALLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNrpARPPFL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  228 DRDVQDESYRLSAETLQQVNRLLacyKGTHNFHNFTSQKGPREpSARRYILEMYCEepfvREGlEFAVIKVKGQSFMMHQ 307
Cdd:PRK00021 125 RGYVWHYPYPLDVDAMNEAAQYL---LGEHDFTSFRASGCQSK-SPVRTIYEADVT----REG-DFIVFDISANGFLHNM 195
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 70906468  308 IRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVLERV 352
Cdd:PRK00021 196 VRNIVGTLLEVGKGKRPPEDIKELLEAKDRTlaGPTAPAEGLYLVEV 242
PLN03078 PLN03078
Putative tRNA pseudouridine synthase; Provisional
79-355 9.68e-27

Putative tRNA pseudouridine synthase; Provisional


Pssm-ID: 215562 [Multi-domain]  Cd Length: 513  Bit Score: 112.30  E-value: 9.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   79 KRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgfl 158
Cdd:PLN03078  70 KKKVVLRVGYVGTDYRGLQKQRDLSSLSTIEGELETAIFKAGGIRESNYGNLHKIGWARSSRTDK--------------- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  159 fhwGVSAAGQVVSLKV------WLIDD---ILDK-INSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKD 228
Cdd:PLN03078 135 ---GVHSLATMISLKMeipenaWKDDPdgiALAKfINSHLPDNIRVFSILPAQRSFDPRRECDLRKYSYLLPAEVIGIKS 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  229 RDVQDEsyrlSAETLQQVNRLLACYKGTHNFHNFTSQ------------------------------------------- 265
Cdd:PLN03078 212 GFSSEE----IDEHISEFNSILNGFEGEHPFHNYTARskyrkklpgkhkqrngavsrraksskemssseseenhgeisee 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  266 -------------------KGPREPSARRYILEMYCEEPFVRE----------------------GLEFAVIKVKGQSFM 304
Cdd:PLN03078 288 deedlsfssipsgssdeneDILKFQSSQVQIRARWLHEPDETDrisashfrkifrcscgklekslGFDFVELSIWGESFM 367
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 70906468  305 MHQIRKMVGLVVAIVKGYAPESVLERSWGE-EKVDVPKAPGLGLVLERVHFE 355
Cdd:PLN03078 368 LHQIRKMVGTAVAVKRELLPRDIIRLSLTKfSRIVLPLAPSEVLILRGNSFS 419
PseudoU_synth_ScPus3 cd02569
Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like; This group consists of eukaryotic ...
84-354 3.38e-23

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: 98.13  E-value: 3.38e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  84 LLMAYSGKGYHGMQRNLGSSQfrTIEDDLVSALVQAGCIPenhgtDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 163
Cdd:cd02569   1 LRFAYLGWNYNGFAVQEETTN--TVEETLFEALEKTRLIE-----DRQTSNYSRCGRTDK------------------GV 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 164 SAAGQVVSLKV-------WLIDDILDK--------------INSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYmlptf 222
Cdd:cd02569  56 SAFGQVISLDVrsnlkpeDGLDPSTDVkstadeeelpyckiLNRVLPPDIRILAWAPVPPDFSARFSCVSRTYRY----- 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 223 AFAHKDRDVqdesyrlsaETLQQVNRLlacYKGTHNFHNFTSQKGPREP-SARRYILEMYCEE-PFVREGLEFAVIKVKG 300
Cdd:cd02569 131 FFPKGDLDI---------ELMRKAAKL---LLGEHDFRNFCKMDVANQVtNYVRRVLSAEVEPvDQHPDGDGLYYFEVRG 198
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 301 QSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKvdVPK------APGLGLVLERVHF 354
Cdd:cd02569 199 SAFLWHQVRCMMAVLFLIGQGLEPPSVISQLLDVEK--NPRkpqytmASEVPLVLYDCGF 256
PseudoU_synth_TruA_Archea cd02866
Archeal pseudouridine synthases; This group consists of archeal pseudouridine synthases. ...
84-349 7.05e-22

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: 93.60  E-value: 7.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  84 LLMAYSGKGYHGMQRNlgsSQFRTIEDDLVSALVQAGCIPEnhgtdmrKMSFQRCARTDKplrtsacfclytgflfhwGV 163
Cdd:cd02866   1 LKIAYDGTNFHGFQRQ---PDVRTVEGELIKALEELGIIES-------RARLYSAGRTDR------------------GV 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 164 SAAGQVVSlkVWLIDD-ILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafahkdrdvqdESYRLSAet 242
Cdd:cd02866  53 HALGNVVV--FETEKEpIPPMINAKLPKDIWVLAGAKVPEDFDPRRWAHRKYYRYNLG-------------SDYDVEA-- 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468 243 LQQVNRLLacyKGTHNFHNFTSQKGPREPSARRYILEmyceepfVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGY 322
Cdd:cd02866 116 MKEAAKKL---IGTHDFSNFSKRDGRKDPVRTIERIE-------ISENGEFITIDVVGESFLWNMVRRIVGALSEVGKGK 185
                       250       260
                ....*....|....*....|....*....
gi 70906468 323 APESVLER--SWGEEKVDVPKAPGLGLVL 349
Cdd:cd02866 186 RENEWVEKllDGEFRPEGVPPAPPEGLIL 214
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
253-355 6.00e-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: 6.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468   253 YKGTHNFHNFTSQKGPREPSaRRYILEMYCEEPFVREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLER-- 330
Cdd:pfam01416   5 YVGTHDFGNFCKQDQPKKNT-VRTILEAAVSRVGGEDG-DLIVFEVRGSGFLDHMVRAMVGVLFLVGQGKEPPEWIAEll 82
                          90       100
                  ....*....|....*....|....*.
gi 70906468   331 -SWGEEKVDVPKAPGLGLVLERVHFE 355
Cdd:pfam01416  83 nAKDPRKIAGPTAPPVGLYLFHVRYP 108
PRK14587 PRK14587
tRNA pseudouridine synthase ACD; Provisional
162-349 9.05e-08

tRNA pseudouridine synthase ACD; Provisional


Pssm-ID: 173051  Cd Length: 256  Bit Score: 52.91  E-value: 9.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  162 GVSAAGQVVSLKVWLIddiLDKINSHLPSHIRILGLKRVTGGFNSKnKCDARTYCYMLPtfafaHKDRDVqdESYRLSAE 241
Cdd:PRK14587  45 GVSAVGNVVMTSQKLP---LGYVNSKLPRGVWAWAVAEVPEGFNPR-RAKRRRYLYVAP-----HWGEDV--EAMREAAE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70906468  242 TLqqvnrllacyKGTHNFHNFTSQKGPREPSARRYILEMYCEepfVREGLEFavIKVKGQSFMMHQIRKMVGLVVAIVKG 321
Cdd:PRK14587 114 LL----------AGTHDYSSFIQRRGEKATPTVTTVYEIGVE---LRGDLIY--LYFVGRGFRNKMIRKMAWAILAAGRG 178
                        170       180       190
                 ....*....|....*....|....*....|....
gi 70906468  322 yapesVLERSWGEEKVD------VPKAPGLGLVL 349
Cdd:PRK14587 179 -----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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