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Conserved domains on  [gi|530360250|ref|XP_005244777|]
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tRNA pseudouridine synthase-like 1 isoform X4 [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 ...
18-158 4.58e-41

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 cd02570:

Pssm-ID: 469624 [Multi-domain]  Cd Length: 239  Bit Score: 139.92  E-value: 4.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  18 FQYVGTDFNGVAAVRGtqrAVGVQNYLEEAAERLNSvEPVRFTISSRTDAGVHALSNAAHLDVQRRsgrppFPPEVLAEA 97
Cdd:cd02570    3 IEYDGTNFSGWQRQPN---GRTVQGELEKALSKIAG-EPVRVIGAGRTDAGVHALGQVAHFDTPSE-----IPLEKLIKA 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360250  98 LNTHLRHPaIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLPAE 158
Cdd:cd02570   74 LNSLLPPD-IRVLSAEEVPDDFHARFSAKSRTYRYRILNRPVP----SPFLRRYVWHVPRP 129
 
Name Accession Description Interval E-value
PseudoU_synth_EcTruA cd02570
Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA; This group consists ...
18-158 4.58e-41

Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA; This group consists of eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA, Pseudomonas aeruginosa truA and human pseudouridine synthase-like 1 (PUSL1). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E. coli TruA makes psi38/39 and/or 40 in tRNA. psi38 and psi39 in tRNAs are highly phylogenetically conserved. P. aeruginosa truA is required for induction of type III secretory genes and may act through modifying tRNAs critical for the expression of type III genes or their regulators.


Pssm-ID: 211337 [Multi-domain]  Cd Length: 239  Bit Score: 139.92  E-value: 4.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  18 FQYVGTDFNGVAAVRGtqrAVGVQNYLEEAAERLNSvEPVRFTISSRTDAGVHALSNAAHLDVQRRsgrppFPPEVLAEA 97
Cdd:cd02570    3 IEYDGTNFSGWQRQPN---GRTVQGELEKALSKIAG-EPVRVIGAGRTDAGVHALGQVAHFDTPSE-----IPLEKLIKA 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360250  98 LNTHLRHPaIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLPAE 158
Cdd:cd02570   74 LNSLLPPD-IRVLSAEEVPDDFHARFSAKSRTYRYRILNRPVP----SPFLRRYVWHVPRP 129
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
13-156 2.70e-37

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 130.26  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  13 RYLVYFQYVGTDFngvaavRGTQR---AVGVQNYLEEAAERLnSVEPVRFTISSRTDAGVHALSNAAHLDVQRrsgrpPF 89
Cdd:PRK00021   3 RIALTIEYDGTNF------HGWQRqpnGRTVQGELEKALSKL-AGEPVRVIGAGRTDAGVHALGQVAHFDTPA-----PR 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360250  90 PPEVLAEALNTHLrHPAIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLP 156
Cdd:PRK00021  71 PPEKWRRALNALL-PDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNRPAR----PPFLRGYVWHYP 132
TruA COG0101
tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]; ...
13-156 3.23e-37

tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]; tRNA U38,U39,U40 pseudouridine synthase TruA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439871 [Multi-domain]  Cd Length: 250  Bit Score: 130.22  E-value: 3.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  13 RYLVYFQYVGTDFngvaavRGTQR---AVGVQNYLEEAAERLNSvEPVRFTISSRTDAGVHALSNAAHLDVQRrsgrpPF 89
Cdd:COG0101    3 RIKLTIEYDGTNF------HGWQRqpnGRTVQGELEKALSKLLG-EPVRVIGAGRTDAGVHALGQVAHFDTPS-----PI 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360250  90 PPEVLAEALNTHLrHPAIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLP 156
Cdd:COG0101   71 PPERLVRALNALL-PPDIAVLWAEEVPDDFHARFSAKSRRYRYRIYNRPVR----SPFLRGYVWHVP 132
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
13-132 5.70e-17

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: 76.58  E-value: 5.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250   13 RYLVYFQYVGTDFNGVAaVRGTQRavGVQNYLEEAAERLNsVEPVRFTISSRTDAGVHALSNAAHLDVqrRSGRppfPPE 92
Cdd:TIGR00071   2 KIALKIAYDGSNYHGWQ-RQPNKR--TVQGELEKALEAIG-KKKITIMSAGRTDKGVHAMGQVISFDT--PKEI---PDN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530360250   93 VLAEALNTHLRhPAIRVLRAFRVPSDFHARHAATSRTYLY 132
Cdd:TIGR00071  73 KLNAKLNALLP-PDIRVKALAPVNDNFHARFSASKRHYRY 111
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
19-122 9.74e-09

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: 51.38  E-value: 9.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250   19 QYVGTDFNGVAAVRGTQRAVGVQNYLEEAAERLNSVEP--VRFTI--SSRTDAGVHALSNAAhLDVqrrsGRPPFPPEVL 94
Cdd:pfam01416   4 LYVGTHDFGNFCKQDQPKKNTVRTILEAAVSRVGGEDGdlIVFEVrgSGFLDHMVRAMVGVL-FLV----GQGKEPPEWI 78
                          90       100
                  ....*....|....*....|....*....
gi 530360250   95 AEALNTHLRhPAIRVLRAFRVP-SDFHAR 122
Cdd:pfam01416  79 AELLNAKDP-RKIAGPTAPPVGlYLFHVR 106
 
Name Accession Description Interval E-value
PseudoU_synth_EcTruA cd02570
Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA; This group consists ...
18-158 4.58e-41

Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA; This group consists of eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA, Pseudomonas aeruginosa truA and human pseudouridine synthase-like 1 (PUSL1). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E. coli TruA makes psi38/39 and/or 40 in tRNA. psi38 and psi39 in tRNAs are highly phylogenetically conserved. P. aeruginosa truA is required for induction of type III secretory genes and may act through modifying tRNAs critical for the expression of type III genes or their regulators.


Pssm-ID: 211337 [Multi-domain]  Cd Length: 239  Bit Score: 139.92  E-value: 4.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  18 FQYVGTDFNGVAAVRGtqrAVGVQNYLEEAAERLNSvEPVRFTISSRTDAGVHALSNAAHLDVQRRsgrppFPPEVLAEA 97
Cdd:cd02570    3 IEYDGTNFSGWQRQPN---GRTVQGELEKALSKIAG-EPVRVIGAGRTDAGVHALGQVAHFDTPSE-----IPLEKLIKA 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360250  98 LNTHLRHPaIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLPAE 158
Cdd:cd02570   74 LNSLLPPD-IRVLSAEEVPDDFHARFSAKSRTYRYRILNRPVP----SPFLRRYVWHVPRP 129
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
13-156 2.70e-37

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 130.26  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  13 RYLVYFQYVGTDFngvaavRGTQR---AVGVQNYLEEAAERLnSVEPVRFTISSRTDAGVHALSNAAHLDVQRrsgrpPF 89
Cdd:PRK00021   3 RIALTIEYDGTNF------HGWQRqpnGRTVQGELEKALSKL-AGEPVRVIGAGRTDAGVHALGQVAHFDTPA-----PR 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360250  90 PPEVLAEALNTHLrHPAIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLP 156
Cdd:PRK00021  71 PPEKWRRALNALL-PDDIAVLWAEEVPDDFHARFSAKARRYRYRIYNRPAR----PPFLRGYVWHYP 132
TruA COG0101
tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]; ...
13-156 3.23e-37

tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]; tRNA U38,U39,U40 pseudouridine synthase TruA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439871 [Multi-domain]  Cd Length: 250  Bit Score: 130.22  E-value: 3.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  13 RYLVYFQYVGTDFngvaavRGTQR---AVGVQNYLEEAAERLNSvEPVRFTISSRTDAGVHALSNAAHLDVQRrsgrpPF 89
Cdd:COG0101    3 RIKLTIEYDGTNF------HGWQRqpnGRTVQGELEKALSKLLG-EPVRVIGAGRTDAGVHALGQVAHFDTPS-----PI 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360250  90 PPEVLAEALNTHLrHPAIRVLRAFRVPSDFHARHAATSRTYLYRLATGCHRrdelPVFERNLCWTLP 156
Cdd:COG0101   71 PPERLVRALNALL-PPDIAVLWAEEVPDDFHARFSAKSRRYRYRIYNRPVR----SPFLRGYVWHVP 132
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
13-132 5.70e-17

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: 76.58  E-value: 5.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250   13 RYLVYFQYVGTDFNGVAaVRGTQRavGVQNYLEEAAERLNsVEPVRFTISSRTDAGVHALSNAAHLDVqrRSGRppfPPE 92
Cdd:TIGR00071   2 KIALKIAYDGSNYHGWQ-RQPNKR--TVQGELEKALEAIG-KKKITIMSAGRTDKGVHAMGQVISFDT--PKEI---PDN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530360250   93 VLAEALNTHLRhPAIRVLRAFRVPSDFHARHAATSRTYLY 132
Cdd:TIGR00071  73 KLNAKLNALLP-PDIRVKALAPVNDNFHARFSASKRHYRY 111
PseudoU_synth_TruA_like cd00497
Pseudouridine synthase, TruA family; This group consists of eukaryotic, bacterial and archeal ...
18-132 3.17e-15

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: 71.65  E-value: 3.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  18 FQYVGTDFNGVaavrgtQRAVGVQNYLEE--AAERLNSVEPVRFTISSRTDAGVHALSNAAHLDVQRRsgrppFPPEVLA 95
Cdd:cd00497    1 FGYDGTKYHGF------QRQNDVPTVEGEliIALLKAGNIPYFIKAAARTDRGVSALGQVVAIETERR-----LTPEALN 69
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530360250  96 EALNTHlrhpaIRVLRAFRVPSDFHARHAATSRTYLY 132
Cdd:cd00497   70 GILPGD-----IRVFAVHSVPPDFHAPRYCDHRTYRY 101
PseudoU_synth_PUS1_PUS2 cd02568
Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine ...
18-132 2.49e-14

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: 69.56  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  18 FQYVGTDFngvaavRGTQRAVG----VQNYLEEAAERLNSVEP--------VRFTISSRTDAGVHALSNAAHLDVQRRSG 85
Cdd:cd02568    3 FGYCGTGY------HGMQYNPGayktIEGELERALFKAGAISEsnagdpkkIGFSRAARTDKGVHAARNVVSLKVIIDDP 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530360250  86 RPPFPPEVLAEALNTHLRhPAIRVLRAFRVPSDFHARHAATSRTYLY 132
Cdd:cd02568   77 EGLGILEDLVEKLNSHLP-SDIRVFGITRVTKSFNARKACDSRTYEY 122
PseudoU_synth_TruA_Archea cd02866
Archeal pseudouridine synthases; This group consists of archeal pseudouridine synthases. ...
20-134 1.45e-12

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: 64.32  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  20 YVGTDFNGvaavrgTQRAVG---VQNYLEEAAERLNSVEP-VRFTISSRTDAGVHALSNAahldVQRRSGRPPFPPEVLA 95
Cdd:cd02866    5 YDGTNFHG------FQRQPDvrtVEGELIKALEELGIIESrARLYSAGRTDRGVHALGNV----VVFETEKEPIPPMINA 74
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530360250  96 EALnthlrhPAIRVLRAFRVPSDFHARHAATSRTYLYRL 134
Cdd:cd02866   75 KLP------KDIWVLAGAKVPEDFDPRRWAHRKYYRYNL 107
PseudoU_synth_ScPus3 cd02569
Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like; This group consists of eukaryotic ...
18-132 5.16e-09

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: 54.98  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  18 FQYVGTDFNGVAAVRGTQRAVgvQNYLEEAAERLNSVEPVR---FTISSRTDAGVHALSNAAHLDVqrRSGRPP-----F 89
Cdd:cd02569    3 FAYLGWNYNGFAVQEETTNTV--EETLFEALEKTRLIEDRQtsnYSRCGRTDKGVSAFGQVISLDV--RSNLKPedgldP 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530360250  90 PPEVLAEALNTHLRH---------PAIRVLRAFRVPSDFHARHAATSRTYLY 132
Cdd:cd02569   79 STDVKSTADEEELPYckilnrvlpPDIRILAWAPVPPDFSARFSCVSRTYRY 130
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
19-122 9.74e-09

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: 51.38  E-value: 9.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250   19 QYVGTDFNGVAAVRGTQRAVGVQNYLEEAAERLNSVEP--VRFTI--SSRTDAGVHALSNAAhLDVqrrsGRPPFPPEVL 94
Cdd:pfam01416   4 LYVGTHDFGNFCKQDQPKKNTVRTILEAAVSRVGGEDGdlIVFEVrgSGFLDHMVRAMVGVL-FLV----GQGKEPPEWI 78
                          90       100
                  ....*....|....*....|....*....
gi 530360250   95 AEALNTHLRhPAIRVLRAFRVP-SDFHAR 122
Cdd:pfam01416  79 AELLNAKDP-RKIAGPTAPPVGlYLFHVR 106
PLN03078 PLN03078
Putative tRNA pseudouridine synthase; Provisional
20-134 6.40e-04

Putative tRNA pseudouridine synthase; Provisional


Pssm-ID: 215562 [Multi-domain]  Cd Length: 513  Bit Score: 40.27  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360250  20 YVGTDFNGVAAVRGTQRAVGVQNYLEEAAERLNSV--------EPVRFTISSRTDAGVHALSNAAHL--DVQRRSGRPPF 89
Cdd:PLN03078  79 YVGTDYRGLQKQRDLSSLSTIEGELETAIFKAGGIresnygnlHKIGWARSSRTDKGVHSLATMISLkmEIPENAWKDDP 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530360250  90 PPEVLAEALNTHLRHpAIRVLRAFRVPSDFHARHAATSRTYLYRL 134
Cdd:PLN03078 159 DGIALAKFINSHLPD-NIRVFSILPAQRSFDPRRECDLRKYSYLL 202
 
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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