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Conserved domains on  [gi|1907165078|ref|XP_036021225|]
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pseudouridylate synthase 1 homolog isoform X1 [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 ...
54-324 4.03e-124

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: 4.03e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  54 LLMAYSGKGYHGMQRNLGSsqFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 133
Cdd:cd02568     1 LLFGYCGTGYHGMQYNPGA--YKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDK------------------GV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 134 SAAGQVVSLKVWLID--------DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdes 205
Cdd:cd02568    61 HAARNVVSLKVIIDDpeglgileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 206 yrlsaETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGL 284
Cdd:cd02568   130 -----ETLQRFNEILKEYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGL 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907165078 285 VVAIVKGYAPESVLERSWGEEKVD-VPKAPGLGLVLERVHF 324
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 ...
54-324 4.03e-124

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: 4.03e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  54 LLMAYSGKGYHGMQRNLGSsqFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 133
Cdd:cd02568     1 LLFGYCGTGYHGMQYNPGA--YKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDK------------------GV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 134 SAAGQVVSLKVWLID--------DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdes 205
Cdd:cd02568    61 HAARNVVSLKVIIDDpeglgileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 206 yrlsaETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGL 284
Cdd:cd02568   130 -----ETLQRFNEILKEYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGL 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907165078 285 VVAIVKGYAPESVLERSWGEEKVD-VPKAPGLGLVLERVHF 324
Cdd:cd02568   205 AIAIVRGGAPESLIELSFNKDKIIiIPLAPGLGLLLERPHF 245
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
50-319 4.14e-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: 145.15  E-value: 4.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  50 RKIVLLMAYSGKGYHGMQRNLGssqFRTIEDDLVSALVQAGcipenhgtdMRKMSFQRCARTDKplrtsacfclytgflf 129
Cdd:TIGR00071   1 RKIALKIAYDGSNYHGWQRQPN---KRTVQGELEKALEAIG---------KKKITIMSAGRTDK---------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 130 hwGVSAAGQVVSLKvwLIDDILD-----KINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafaHKDRDVqde 204
Cdd:TIGR00071  53 --GVHAMGQVISFD--TPKEIPDnklnaKLNALLPPDIRVKALAPVNDNFHARFSASKRHYRYILY-----NHRHYY--- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 205 sYRLSAETLQQVnrlLACYKGTHNFHNFTSQKGPrEPSARRYILEMYceepfVREGLEFAVIKVKGQSFMMHQIRKMVGL 284
Cdd:TIGR00071 121 -SPLDLEKMRAA---AKQLLGKHDFSNFSKAKSK-SRSPIRTISDIK-----VSESGEYIIFDIIGNSFLWHMVRKIVGA 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907165078 285 VVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVL 319
Cdd:TIGR00071 191 LVLVGRGKLPPEWVAKLLDAKKRNlaPTTAPANGLYL 227
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
50-322 1.61e-29

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 114.85  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  50 RKIVLLMAYSGKGYHGMQRnlgssQ--FRTIEDDLVSALvqagcipenhgtdmRKMSFQR----CA-RTDKplrtsacfc 122
Cdd:PRK00021    2 MRIALTIEYDGTNFHGWQR-----QpnGRTVQGELEKAL--------------SKLAGEPvrviGAgRTDA--------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 123 lytgflfhwGVSAAGQVVSL---KVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPT--FAFAHK 197
Cdd:PRK00021   54 ---------GVHALGQVAHFdtpAPRPPEKWRRALNALLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNrpARPPFL 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 198 DRDVQDESYRLSAETLQQVNRLLacyKGTHNFHNFTSQKGPREpSARRYILEMYCEepfvREGlEFAVIKVKGQSFMMHQ 277
Cdd:PRK00021  125 RGYVWHYPYPLDVDAMNEAAQYL---LGEHDFTSFRASGCQSK-SPVRTIYEADVT----REG-DFIVFDISANGFLHNM 195
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907165078 278 IRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVLERV 322
Cdd:PRK00021  196 VRNIVGTLLEVGKGKRPPEDIKELLEAKDRTlaGPTAPAEGLYLVEV 242
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
223-325 5.48e-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: 5.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 223 YKGTHNFHNFTSQKGPREPSaRRYILEMYCEEPFVREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSW 302
Cdd:pfam01416   5 YVGTHDFGNFCKQDQPKKNT-VRTILEAAVSRVGGEDG-DLIVFEVRGSGFLDHMVRAMVGVLFLVGQGKEPPEWIAELL 82
                          90       100
                  ....*....|....*....|....*.
gi 1907165078 303 GEE---KVDVPKAPGLGLVLERVHFE 325
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 ...
54-324 4.03e-124

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: 4.03e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  54 LLMAYSGKGYHGMQRNLGSsqFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 133
Cdd:cd02568     1 LLFGYCGTGYHGMQYNPGA--YKTIEGELERALFKAGAISESNAGDPKKIGFSRAARTDK------------------GV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 134 SAAGQVVSLKVWLID--------DILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFahkdrdvqdes 205
Cdd:cd02568    61 HAARNVVSLKVIIDDpeglgileDLVEKLNSHLPSDIRVFGITRVTKSFNARKACDSRTYEYLLPTFAL----------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 206 yrlsaETLQQVNRLLACYKGTHNFHNFTSQKGPREPSARRYILEMYCEEPFVR-EGLEFAVIKVKGQSFMMHQIRKMVGL 284
Cdd:cd02568   130 -----ETLQRFNEILKEYVGTHNFHNFTVKKKFEDPSANRFIKSFYVSEPFVIeEGLEWISIKIHGQSFMLHQIRKMIGL 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907165078 285 VVAIVKGYAPESVLERSWGEEKVD-VPKAPGLGLVLERVHF 324
Cdd:cd02568   205 AIAIVRGGAPESLIELSFNKDKIIiIPLAPGLGLLLERPHF 245
PseudoU_synth_TruA_like cd00497
Pseudouridine synthase, TruA family; This group consists of eukaryotic, bacterial and archeal ...
57-324 1.22e-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: 1.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  57 AYSGKGYHGMQRnlgSSQFRTIEDDLVSALVQAGCIPENhgtdmrkmsFQRCARTDKplrtsacfclytgflfhwGVSAA 136
Cdd:cd00497     2 GYDGTKYHGFQR---QNDVPTVEGELIIALLKAGNIPYF---------IKAAARTDR------------------GVSAL 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 137 GQVVSLKV--WLIDDIldkINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFafahkdrDVQDESyrlsaetlq 214
Cdd:cd00497    52 GQVVAIETerRLTPEA---LNGILPGDIRVFAVHSVPPDFHAPRYCDHRTYRYYIPSF-------PLDDER--------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 215 qVNRLLACYKGTHNFHNFTSQKGpREPsaRRYILEMYCEEPFvreglEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAP 294
Cdd:cd00497   113 -LKSAASRFLGTHDFTNFSKKDT-RNT--VRTIISIECKDLN-----PFVVVEFKAKSFLWHQVRRMVGFLMLVGEGLHS 183
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907165078 295 ESVLERSWGEEKVDVPK--APGLGLVLERVHF 324
Cdd:cd00497   184 PSSVSRLLAGPAPPIPMvpAPAEGLLLVDVKY 215
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
50-319 4.14e-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: 145.15  E-value: 4.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  50 RKIVLLMAYSGKGYHGMQRNLGssqFRTIEDDLVSALVQAGcipenhgtdMRKMSFQRCARTDKplrtsacfclytgflf 129
Cdd:TIGR00071   1 RKIALKIAYDGSNYHGWQRQPN---KRTVQGELEKALEAIG---------KKKITIMSAGRTDK---------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 130 hwGVSAAGQVVSLKvwLIDDILD-----KINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafaHKDRDVqde 204
Cdd:TIGR00071  53 --GVHAMGQVISFD--TPKEIPDnklnaKLNALLPPDIRVKALAPVNDNFHARFSASKRHYRYILY-----NHRHYY--- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 205 sYRLSAETLQQVnrlLACYKGTHNFHNFTSQKGPrEPSARRYILEMYceepfVREGLEFAVIKVKGQSFMMHQIRKMVGL 284
Cdd:TIGR00071 121 -SPLDLEKMRAA---AKQLLGKHDFSNFSKAKSK-SRSPIRTISDIK-----VSESGEYIIFDIIGNSFLWHMVRKIVGA 190
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907165078 285 VVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVL 319
Cdd:TIGR00071 191 LVLVGRGKLPPEWVAKLLDAKKRNlaPTTAPANGLYL 227
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
50-322 1.61e-29

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 114.85  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  50 RKIVLLMAYSGKGYHGMQRnlgssQ--FRTIEDDLVSALvqagcipenhgtdmRKMSFQR----CA-RTDKplrtsacfc 122
Cdd:PRK00021    2 MRIALTIEYDGTNFHGWQR-----QpnGRTVQGELEKAL--------------SKLAGEPvrviGAgRTDA--------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 123 lytgflfhwGVSAAGQVVSL---KVWLIDDILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPT--FAFAHK 197
Cdd:PRK00021   54 ---------GVHALGQVAHFdtpAPRPPEKWRRALNALLPDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNrpARPPFL 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 198 DRDVQDESYRLSAETLQQVNRLLacyKGTHNFHNFTSQKGPREpSARRYILEMYCEepfvREGlEFAVIKVKGQSFMMHQ 277
Cdd:PRK00021  125 RGYVWHYPYPLDVDAMNEAAQYL---LGEHDFTSFRASGCQSK-SPVRTIYEADVT----REG-DFIVFDISANGFLHNM 195
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1907165078 278 IRKMVGLVVAIVKGYAPESVLERSWGEEKVD--VPKAPGLGLVLERV 322
Cdd:PRK00021  196 VRNIVGTLLEVGKGKRPPEDIKELLEAKDRTlaGPTAPAEGLYLVEV 242
PLN03078 PLN03078
Putative tRNA pseudouridine synthase; Provisional
49-325 5.73e-27

Putative tRNA pseudouridine synthase; Provisional


Pssm-ID: 215562 [Multi-domain]  Cd Length: 513  Bit Score: 112.30  E-value: 5.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  49 KRKIVLLMAYSGKGYHGMQRNLGSSQFRTIEDDLVSALVQAGCIPENHGTDMRKMSFQRCARTDKplrtsacfclytgfl 128
Cdd:PLN03078   70 KKKVVLRVGYVGTDYRGLQKQRDLSSLSTIEGELETAIFKAGGIRESNYGNLHKIGWARSSRTDK--------------- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 129 fhwGVSAAGQVVSLKV------WLIDD---ILDK-INSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPTFAFAHKD 198
Cdd:PLN03078  135 ---GVHSLATMISLKMeipenaWKDDPdgiALAKfINSHLPDNIRVFSILPAQRSFDPRRECDLRKYSYLLPAEVIGIKS 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 199 RDVQDEsyrlSAETLQQVNRLLACYKGTHNFHNFTSQ------------------------------------------- 235
Cdd:PLN03078  212 GFSSEE----IDEHISEFNSILNGFEGEHPFHNYTARskyrkklpgkhkqrngavsrraksskemssseseenhgeisee 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 236 -------------------KGPREPSARRYILEMYCEEPFVRE----------------------GLEFAVIKVKGQSFM 274
Cdd:PLN03078  288 deedlsfssipsgssdeneDILKFQSSQVQIRARWLHEPDETDrisashfrkifrcscgklekslGFDFVELSIWGESFM 367
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907165078 275 MHQIRKMVGLVVAIVKGYAPESVLERSWGE-EKVDVPKAPGLGLVLERVHFE 325
Cdd:PLN03078  368 LHQIRKMVGTAVAVKRELLPRDIIRLSLTKfSRIVLPLAPSEVLILRGNSFS 419
PseudoU_synth_ScPus3 cd02569
Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like; This group consists of eukaryotic ...
54-324 2.09e-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: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  54 LLMAYSGKGYHGMQRNLGSSQfrTIEDDLVSALVQAGCIPenhgtDMRKMSFQRCARTDKplrtsacfclytgflfhwGV 133
Cdd:cd02569     1 LRFAYLGWNYNGFAVQEETTN--TVEETLFEALEKTRLIE-----DRQTSNYSRCGRTDK------------------GV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 134 SAAGQVVSLKV-------WLIDDILDK--------------INSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYmlptf 192
Cdd:cd02569    56 SAFGQVISLDVrsnlkpeDGLDPSTDVkstadeeelpyckiLNRVLPPDIRILAWAPVPPDFSARFSCVSRTYRY----- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 193 AFAHKDRDVqdesyrlsaETLQQVNRLlacYKGTHNFHNFTSQKGPREP-SARRYILEMYCEE-PFVREGLEFAVIKVKG 270
Cdd:cd02569   131 FFPKGDLDI---------ELMRKAAKL---LLGEHDFRNFCKMDVANQVtNYVRRVLSAEVEPvDQHPDGDGLYYFEVRG 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 271 QSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGEEKvdVPK------APGLGLVLERVHF 324
Cdd:cd02569   199 SAFLWHQVRCMMAVLFLIGQGLEPPSVISQLLDVEK--NPRkpqytmASEVPLVLYDCGF 256
PseudoU_synth_TruA_Archea cd02866
Archeal pseudouridine synthases; This group consists of archeal pseudouridine synthases. ...
54-319 4.06e-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: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078  54 LLMAYSGKGYHGMQRNlgsSQFRTIEDDLVSALVQAGCIPEnhgtdmrKMSFQRCARTDKplrtsacfclytgflfhwGV 133
Cdd:cd02866     1 LKIAYDGTNFHGFQRQ---PDVRTVEGELIKALEELGIIES-------RARLYSAGRTDR------------------GV 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 134 SAAGQVVSlkVWLIDD-ILDKINSHLPSHIRILGLKRVTGGFNSKNKCDARTYCYMLPtfafahkdrdvqdESYRLSAet 212
Cdd:cd02866    53 HALGNVVV--FETEKEpIPPMINAKLPKDIWVLAGAKVPEDFDPRRWAHRKYYRYNLG-------------SDYDVEA-- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 213 LQQVNRLLacyKGTHNFHNFTSQKGPREPSARRYILEmyceepfVREGLEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGY 292
Cdd:cd02866   116 MKEAAKKL---IGTHDFSNFSKRDGRKDPVRTIERIE-------ISENGEFITIDVVGESFLWNMVRRIVGALSEVGKGK 185
                         250       260
                  ....*....|....*....|....*....
gi 1907165078 293 APESVLER--SWGEEKVDVPKAPGLGLVL 319
Cdd:cd02866   186 RENEWVEKllDGEFRPEGVPPAPPEGLIL 214
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
223-325 5.48e-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: 5.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 223 YKGTHNFHNFTSQKGPREPSaRRYILEMYCEEPFVREGlEFAVIKVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSW 302
Cdd:pfam01416   5 YVGTHDFGNFCKQDQPKKNT-VRTILEAAVSRVGGEDG-DLIVFEVRGSGFLDHMVRAMVGVLFLVGQGKEPPEWIAELL 82
                          90       100
                  ....*....|....*....|....*.
gi 1907165078 303 GEE---KVDVPKAPGLGLVLERVHFE 325
Cdd:pfam01416  83 NAKdprKIAGPTAPPVGLYLFHVRYP 108
PRK14587 PRK14587
tRNA pseudouridine synthase ACD; Provisional
132-319 3.36e-08

tRNA pseudouridine synthase ACD; Provisional


Pssm-ID: 173051  Cd Length: 256  Bit Score: 54.06  E-value: 3.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 132 GVSAAGQVVSLKVWLIddiLDKINSHLPSHIRILGLKRVTGGFNSKnKCDARTYCYMLPtfafaHKDRDVqdESYRLSAE 211
Cdd:PRK14587   45 GVSAVGNVVMTSQKLP---LGYVNSKLPRGVWAWAVAEVPEGFNPR-RAKRRRYLYVAP-----HWGEDV--EAMREAAE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165078 212 TLqqvnrllacyKGTHNFHNFTSQKGPREPSARRYILEMYCEepfVREGLEFavIKVKGQSFMMHQIRKMVGLVVAIVKG 291
Cdd:PRK14587  114 LL----------AGTHDYSSFIQRRGEKATPTVTTVYEIGVE---LRGDLIY--LYFVGRGFRNKMIRKMAWAILAAGRG 178
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907165078 292 yapesVLERSWGEEKVD------VPKAPGLGLVL 319
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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