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Conserved domains on  [gi|2071063207|ref|NP_001382538|]
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tRNA pseudouridine synthase-like 1 isoform 2 [Rattus norvegicus]

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 ...
18-234 1.28e-61

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: 193.07  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  18 FQYLGTDFNGVAAVRGnhrAVGVQNFLEEAAKRLNSvEPVRFTISSRTDAGVHALSNAAHLDIQRRpgrppFSPEIVTKA 97
Cdd:cd02570     3 IEYDGTNFSGWQRQPN---GRTVQGELEKALSKIAG-EPVRVIGAGRTDAGVHALGQVAHFDTPSE-----IPLEKLIKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  98 LNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDFSAFQS 133
Cdd:cd02570    74 LNSLLPPDirvlsaeevpddfharfsAKsrtyRYrilnrpvpspflrryvwhvprpLDIEAMQEAAKLLLGTHDFSSFRA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 134 AGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILESQDP 213
Cdd:cd02570   154 AGCQSKSTVRTIYRADV-------------YREGDLIVFEIRANGFLYHMVRNIVGTLLEVGRGKLSPEDIKEILEAKDR 220
                         250       260
                  ....*....|....*....|.
gi 2071063207 214 lgKYQARVAPAHGLFLKSVLY 234
Cdd:cd02570   221 --TAAGPTAPAHGLYLVKVEY 239
 
Name Accession Description Interval E-value
PseudoU_synth_EcTruA cd02570
Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA; This group consists ...
18-234 1.28e-61

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: 193.07  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  18 FQYLGTDFNGVAAVRGnhrAVGVQNFLEEAAKRLNSvEPVRFTISSRTDAGVHALSNAAHLDIQRRpgrppFSPEIVTKA 97
Cdd:cd02570     3 IEYDGTNFSGWQRQPN---GRTVQGELEKALSKIAG-EPVRVIGAGRTDAGVHALGQVAHFDTPSE-----IPLEKLIKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  98 LNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDFSAFQS 133
Cdd:cd02570    74 LNSLLPPDirvlsaeevpddfharfsAKsrtyRYrilnrpvpspflrryvwhvprpLDIEAMQEAAKLLLGTHDFSSFRA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 134 AGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILESQDP 213
Cdd:cd02570   154 AGCQSKSTVRTIYRADV-------------YREGDLIVFEIRANGFLYHMVRNIVGTLLEVGRGKLSPEDIKEILEAKDR 220
                         250       260
                  ....*....|....*....|.
gi 2071063207 214 lgKYQARVAPAHGLFLKSVLY 234
Cdd:cd02570   221 --TAAGPTAPAHGLYLVKVEY 239
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
13-234 2.34e-53

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 172.25  E-value: 2.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  13 RYLVFFQYLGTDFNGVAavRGNHrAVGVQNFLEEAAKRLnSVEPVRFTISSRTDAGVHALSNAAHLDIQRrpgrpPFSPE 92
Cdd:PRK00021    3 RIALTIEYDGTNFHGWQ--RQPN-GRTVQGELEKALSKL-AGEPVRVIGAGRTDAGVHALGQVAHFDTPA-----PRPPE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  93 IVTKALNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDF 128
Cdd:PRK00021   74 KWRRALNALLPDDiavlwaeevpddfharfsAKarryRYriynrparppflrgyvwhypypLDVDAMNEAAQYLLGEHDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 129 SAFQSAGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVIL 208
Cdd:PRK00021  154 TSFRASGCQSKSPVRTIYEADV-------------TREGDFIVFDISANGFLHNMVRNIVGTLLEVGKGKRPPEDIKELL 220
                         250       260
                  ....*....|....*....|....*.
gi 2071063207 209 ESQDPlgKYQARVAPAHGLFLKSVLY 234
Cdd:PRK00021  221 EAKDR--TLAGPTAPAEGLYLVEVDY 244
TruA COG0101
tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]; ...
13-236 6.23e-53

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: 171.44  E-value: 6.23e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  13 RYLVFFQYLGTDFNGvAAVRGNHRavGVQNFLEEAAKRLNSvEPVRFTISSRTDAGVHALSNAAHLDIQRrpgrpPFSPE 92
Cdd:COG0101     3 RIKLTIEYDGTNFHG-WQRQPNGR--TVQGELEKALSKLLG-EPVRVIGAGRTDAGVHALGQVAHFDTPS-----PIPPE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  93 IVTKALNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDF 128
Cdd:COG0101    74 RLVRALNALLPPDiavlwaeevpddfharfsAKsrryRYriynrpvrspflrgyvwhvprpLDVEAMNEAAQLLLGEHDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 129 SAFQSAGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVIL 208
Cdd:COG0101   154 SSFRAAGCQAKSTVRTIYRAEV-------------EREGDLIVFEIEANGFLHNMVRNIVGTLVEVGRGKLSPEWIKEIL 220
                         250       260
                  ....*....|....*....|....*...
gi 2071063207 209 ESQDPlgKYQARVAPAHGLFLKSVLYDN 236
Cdd:COG0101   221 EAKDR--TRAGPTAPAHGLYLVEVDYPE 246
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
13-229 2.50e-34

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: 122.81  E-value: 2.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  13 RYLVFFQYLGTDFNGVAaVRGNHRavGVQNFLEEAAKRLNsVEPVRFTISSRTDAGVHALSNAAHLDIqrrPGRPPfsPE 92
Cdd:TIGR00071   2 KIALKIAYDGSNYHGWQ-RQPNKR--TVQGELEKALEAIG-KKKITIMSAGRTDKGVHAMGQVISFDT---PKEIP--DN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  93 IVTKALNTHLK---------------HP-------AIRY-----------LDIAAMQEAAQHLLGTHDFSAFQSAGSPVP 139
Cdd:TIGR00071  73 KLNAKLNALLPpdirvkalapvndnfHArfsaskrHYRYilynhrhyyspLDLEKMRAAAKQLLGKHDFSNFSKAKSKSR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 140 HAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILESQDPlgKYQA 219
Cdd:TIGR00071 153 SPIRTISDIKV-------------SESGEYIIFDIIGNSFLWHMVRKIVGALVLVGRGKLPPEWVAKLLDAKKR--NLAP 217
                         250
                  ....*....|
gi 2071063207 220 RVAPAHGLFL 229
Cdd:TIGR00071 218 TTAPANGLYL 227
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
118-235 8.43e-30

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: 107.23  E-value: 8.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 118 AAQHLLGTHDFSAFQSAGSPVPHAVRTLRRVSVSPGPaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLG 197
Cdd:pfam01416   1 AAKLYVGTHDFGNFCKQDQPKKNTVRTILEAAVSRVG---------GEDGDLIVFEVRGSGFLDHMVRAMVGVLFLVGQG 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2071063207 198 ILAPTQVKVILESQDPlGKYQARVAPAHGLFLKSVLYD 235
Cdd:pfam01416  72 KEPPEWIAELLNAKDP-RKIAGPTAPPVGLYLFHVRYP 108
 
Name Accession Description Interval E-value
PseudoU_synth_EcTruA cd02570
Eukaryotic and bacterial pseudouridine synthases similar to E. coli TruA; This group consists ...
18-234 1.28e-61

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: 193.07  E-value: 1.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  18 FQYLGTDFNGVAAVRGnhrAVGVQNFLEEAAKRLNSvEPVRFTISSRTDAGVHALSNAAHLDIQRRpgrppFSPEIVTKA 97
Cdd:cd02570     3 IEYDGTNFSGWQRQPN---GRTVQGELEKALSKIAG-EPVRVIGAGRTDAGVHALGQVAHFDTPSE-----IPLEKLIKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  98 LNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDFSAFQS 133
Cdd:cd02570    74 LNSLLPPDirvlsaeevpddfharfsAKsrtyRYrilnrpvpspflrryvwhvprpLDIEAMQEAAKLLLGTHDFSSFRA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 134 AGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILESQDP 213
Cdd:cd02570   154 AGCQSKSTVRTIYRADV-------------YREGDLIVFEIRANGFLYHMVRNIVGTLLEVGRGKLSPEDIKEILEAKDR 220
                         250       260
                  ....*....|....*....|.
gi 2071063207 214 lgKYQARVAPAHGLFLKSVLY 234
Cdd:cd02570   221 --TAAGPTAPAHGLYLVKVEY 239
truA PRK00021
tRNA pseudouridine(38-40) synthase TruA;
13-234 2.34e-53

tRNA pseudouridine(38-40) synthase TruA;


Pssm-ID: 234577 [Multi-domain]  Cd Length: 244  Bit Score: 172.25  E-value: 2.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  13 RYLVFFQYLGTDFNGVAavRGNHrAVGVQNFLEEAAKRLnSVEPVRFTISSRTDAGVHALSNAAHLDIQRrpgrpPFSPE 92
Cdd:PRK00021    3 RIALTIEYDGTNFHGWQ--RQPN-GRTVQGELEKALSKL-AGEPVRVIGAGRTDAGVHALGQVAHFDTPA-----PRPPE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  93 IVTKALNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDF 128
Cdd:PRK00021   74 KWRRALNALLPDDiavlwaeevpddfharfsAKarryRYriynrparppflrgyvwhypypLDVDAMNEAAQYLLGEHDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 129 SAFQSAGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVIL 208
Cdd:PRK00021  154 TSFRASGCQSKSPVRTIYEADV-------------TREGDFIVFDISANGFLHNMVRNIVGTLLEVGKGKRPPEDIKELL 220
                         250       260
                  ....*....|....*....|....*.
gi 2071063207 209 ESQDPlgKYQARVAPAHGLFLKSVLY 234
Cdd:PRK00021  221 EAKDR--TLAGPTAPAEGLYLVEVDY 244
TruA COG0101
tRNA U38,U39,U40 pseudouridine synthase TruA [Translation, ribosomal structure and biogenesis]; ...
13-236 6.23e-53

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: 171.44  E-value: 6.23e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  13 RYLVFFQYLGTDFNGvAAVRGNHRavGVQNFLEEAAKRLNSvEPVRFTISSRTDAGVHALSNAAHLDIQRrpgrpPFSPE 92
Cdd:COG0101     3 RIKLTIEYDGTNFHG-WQRQPNGR--TVQGELEKALSKLLG-EPVRVIGAGRTDAGVHALGQVAHFDTPS-----PIPPE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  93 IVTKALNTHLKHP------------------AI----RY----------------------LDIAAMQEAAQHLLGTHDF 128
Cdd:COG0101    74 RLVRALNALLPPDiavlwaeevpddfharfsAKsrryRYriynrpvrspflrgyvwhvprpLDVEAMNEAAQLLLGEHDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 129 SAFQSAGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVIL 208
Cdd:COG0101   154 SSFRAAGCQAKSTVRTIYRAEV-------------EREGDLIVFEIEANGFLHNMVRNIVGTLVEVGRGKLSPEWIKEIL 220
                         250       260
                  ....*....|....*....|....*...
gi 2071063207 209 ESQDPlgKYQARVAPAHGLFLKSVLYDN 236
Cdd:COG0101   221 EAKDR--TRAGPTAPAHGLYLVEVDYPE 246
hisT_truA TIGR00071
tRNA pseudouridine(38-40) synthase; Members of this family are the tRNA modification enzyme ...
13-229 2.50e-34

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: 122.81  E-value: 2.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  13 RYLVFFQYLGTDFNGVAaVRGNHRavGVQNFLEEAAKRLNsVEPVRFTISSRTDAGVHALSNAAHLDIqrrPGRPPfsPE 92
Cdd:TIGR00071   2 KIALKIAYDGSNYHGWQ-RQPNKR--TVQGELEKALEAIG-KKKITIMSAGRTDKGVHAMGQVISFDT---PKEIP--DN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  93 IVTKALNTHLK---------------HP-------AIRY-----------LDIAAMQEAAQHLLGTHDFSAFQSAGSPVP 139
Cdd:TIGR00071  73 KLNAKLNALLPpdirvkalapvndnfHArfsaskrHYRYilynhrhyyspLDLEKMRAAAKQLLGKHDFSNFSKAKSKSR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 140 HAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILESQDPlgKYQA 219
Cdd:TIGR00071 153 SPIRTISDIKV-------------SESGEYIIFDIIGNSFLWHMVRKIVGALVLVGRGKLPPEWVAKLLDAKKR--NLAP 217
                         250
                  ....*....|
gi 2071063207 220 RVAPAHGLFL 229
Cdd:TIGR00071 218 TTAPANGLYL 227
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
118-235 8.43e-30

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: 107.23  E-value: 8.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 118 AAQHLLGTHDFSAFQSAGSPVPHAVRTLRRVSVSPGPaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLG 197
Cdd:pfam01416   1 AAKLYVGTHDFGNFCKQDQPKKNTVRTILEAAVSRVG---------GEDGDLIVFEVRGSGFLDHMVRAMVGVLFLVGQG 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2071063207 198 ILAPTQVKVILESQDPlGKYQARVAPAHGLFLKSVLYD 235
Cdd:pfam01416  72 KEPPEWIAELLNAKDP-RKIAGPTAPPVGLYLFHVRYP 108
PseudoU_synth_TruA_like cd00497
Pseudouridine synthase, TruA family; This group consists of eukaryotic, bacterial and archeal ...
18-234 5.15e-26

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: 100.54  E-value: 5.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  18 FQYLGTDFNGVAavRGNHRAVGVQNFLEeaAKRLNSVEPVRFTISSRTDAGVHALSNAAHLDIQRRPGrppfsPEIVTKA 97
Cdd:cd00497     1 FGYDGTKYHGFQ--RQNDVPTVEGELII--ALLKAGNIPYFIKAAARTDRGVSALGQVVAIETERRLT-----PEALNGI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  98 LNTHLKHPAI------------------RY------LDIAAMQEAAQHLLGTHDFSAFQSAGSPVPhaVRTLRRVSVSPG 153
Cdd:cd00497    72 LPGDIRVFAVhsvppdfhaprycdhrtyRYyipsfpLDDERLKSAASRFLGTHDFTNFSKKDTRNT--VRTIISIECKDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 154 paSLFVLpqesrrlqfwtLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILESQDPLGKYQArvAPAHGLFLKSVL 233
Cdd:cd00497   150 --NPFVV-----------VEFKAKSFLWHQVRRMVGFLMLVGEGLHSPSSVSRLLAGPAPPIPMVP--APAEGLLLVDVK 214

                  .
gi 2071063207 234 Y 234
Cdd:cd00497   215 Y 215
PseudoU_synth_TruA_Archea cd02866
Archeal pseudouridine synthases; This group consists of archeal pseudouridine synthases. ...
57-234 7.33e-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: 89.74  E-value: 7.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  57 VRFTISSRTDAGVHALSNAAHLDIQRRPGRPPFS---------------PEIVTKALNTHLKHpaIRYL-----DIAAMQ 116
Cdd:cd02866    40 ARLYSAGRTDRGVHALGNVVVFETEKEPIPPMINaklpkdiwvlagakvPEDFDPRRWAHRKY--YRYNlgsdyDVEAMK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 117 EAAQHLLGTHDFSAFqSAGSPVPHAVRTLRRVSVspgpaslfvlpqeSRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGL 196
Cdd:cd02866   118 EAAKKLIGTHDFSNF-SKRDGRKDPVRTIERIEI-------------SENGEFITIDVVGESFLWNMVRRIVGALSEVGK 183
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2071063207 197 GILAPTQVKVIL-ESQDPLGKyqaRVAPAHGLFLKSVLY 234
Cdd:cd02866   184 GKRENEWVEKLLdGEFRPEGV---PPAPPEGLILVDVKY 219
PseudoU_synth_ScPus3 cd02569
Pseudouridine synthase, Saccharomyces cerevisiae Pus3 like; This group consists of eukaryotic ...
18-235 4.03e-17

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: 77.71  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  18 FQYLGTDFNGVAAvrGNHRAVGVQNFLEEAAKRLNSVEPVR---FTISSRTDAGVHALSNAAHLDI------------QR 82
Cdd:cd02569     3 FAYLGWNYNGFAV--QEETTNTVEETLFEALEKTRLIEDRQtsnYSRCGRTDKGVSAFGQVISLDVrsnlkpedgldpST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  83 RPGRPPFSPEI-VTKALNTHLKhPAIR-----------------------Y------LDIAAMQEAAQHLLGTHDFSAF- 131
Cdd:cd02569    81 DVKSTADEEELpYCKILNRVLP-PDIRilawapvppdfsarfscvsrtyrYffpkgdLDIELMRKAAKLLLGEHDFRNFc 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 132 -QSAGSPVPHAVRTLRRVSVSPgpaslfvLPQESRRLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQVKVILES 210
Cdd:cd02569   160 kMDVANQVTNYVRRVLSAEVEP-------VDQHPDGDGLYYFEVRGSAFLWHQVRCMMAVLFLIGQGLEPPSVISQLLDV 232
                         250       260
                  ....*....|....*....|....*
gi 2071063207 211 QDPLGKYQARVAPAHGLflksVLYD 235
Cdd:cd02569   233 EKNPRKPQYTMASEVPL----VLYD 253
PseudoU_synth_PUS1_PUS2 cd02568
Pseudouridine synthase, PUS1/ PUS2 like; This group consists of eukaryotic pseudouridine ...
18-234 4.26e-16

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: 74.96  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  18 FQYLGTDFNGVAAVRGNHRAVgvQNFLEEAAKRLNSVEP--------VRFTISSRTDAGVHALSNAAHLDIQRRPGRPPF 89
Cdd:cd02568     3 FGYCGTGYHGMQYNPGAYKTI--EGELERALFKAGAISEsnagdpkkIGFSRAARTDKGVHAARNVVSLKVIIDDPEGLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  90 SPEIVTKALNTHLKhPAIRYLDI------------------------------AAMQEAAQHLLGTHDFSAF---QSAGS 136
Cdd:cd02568    81 ILEDLVEKLNSHLP-SDIRVFGItrvtksfnarkacdsrtyeyllptfaletlQRFNEILKEYVGTHNFHNFtvkKKFED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 137 PVphAVRTLRRVSVSPGpaslFVLPQEsrrLQFWTLEFESQSFLYRQVRRMTAVLVAVGLGiLAPTqvkvilESQDP-LG 215
Cdd:cd02568   160 PS--ANRFIKSFYVSEP----FVIEEG---LEWISIKIHGQSFMLHQIRKMIGLAIAIVRG-GAPE------SLIELsFN 223
                         250       260
                  ....*....|....*....|..
gi 2071063207 216 KYQARV---APAHGLFLKSVLY 234
Cdd:cd02568   224 KDKIIIiplAPGLGLLLERPHF 245
PRK14587 PRK14587
tRNA pseudouridine synthase ACD; Provisional
63-235 4.43e-08

tRNA pseudouridine synthase ACD; Provisional


Pssm-ID: 173051  Cd Length: 256  Bit Score: 52.52  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  63 SRTDAGVHALSNAAHLDIQRRPG----RPP-----FSPEIVTKALNTHlKHPAIRYL--------DIAAMQEAAQHLLGT 125
Cdd:PRK14587   40 SRTDPGVSAVGNVVMTSQKLPLGyvnsKLPrgvwaWAVAEVPEGFNPR-RAKRRRYLyvaphwgeDVEAMREAAELLAGT 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207 126 HDFSAF-QSAGSPVPHAVRTLRRVSVspgpaslfvlpqESR-RLQFwtLEFESQSFLYRQVRRMTAVLVAVGLGILAPTQ 203
Cdd:PRK14587  119 HDYSSFiQRRGEKATPTVTTVYEIGV------------ELRgDLIY--LYFVGRGFRNKMIRKMAWAILAAGRGVLSRRD 184
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2071063207 204 VKVILESQDPlGKYQArvAPAHGLFLKSVLYD 235
Cdd:PRK14587  185 IAELLERPRP-GAVPS--APAEGLVLLDIEYD 213
PseudoU_synth_1 pfam01416
tRNA pseudouridine synthase; Involved in the formation of pseudouridine at the anticodon stem ...
19-108 5.25e-04

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: 38.28  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2071063207  19 QYLGT-DFNGVAAVRGNHRaVGVQNFLE----EAAKRLNSVEPVRFTISSRTDAGVHALSNAAhLDIqrrpGRPPFSPEI 93
Cdd:pfam01416   4 LYVGThDFGNFCKQDQPKK-NTVRTILEaavsRVGGEDGDLIVFEVRGSGFLDHMVRAMVGVL-FLV----GQGKEPPEW 77
                          90
                  ....*....|....*.
gi 2071063207  94 VTKALNTHL-KHPAIR 108
Cdd:pfam01416  78 IAELLNAKDpRKIAGP 93
 
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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