|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
4-291 |
0e+00 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 562.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 4 KTEKLQKILARSGHGSRREIEGYIQQGRISIDGKTATLGDRIEVKPSIKIRLDGRILNIKEPQKTVCRVLAYYKPEGELC 83
Cdd:PRK10700 1 MSEKLQKVLARAGHGSRREIESIIEAGRVSVDGKIATLGDRVEVTPGLKIRIDGHLISVKESAEQICRVLAYYKPEGELC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 84 TRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLTQGV 163
Cdd:PRK10700 81 TRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQLSRGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 164 QLEDGPASFKTITFKGGEGINQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLPKGLPRGGWTELGLEQTNYL 243
Cdd:PRK10700 161 QLEDGPAAFKTIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLPKGLPRGGWTELDLAQTNYL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 498910755 244 RQLVGLGDEMVTKVAVERDQRRIKANQIRRAVKRHAKVASRP-AGKRPA 291
Cdd:PRK10700 241 RELVELPPETSSKVAVEKDRRRMKANQIRRAVKRHSQVSGGRrSGGRNN 289
|
|
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
4-235 |
4.43e-106 |
|
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ribosomal structure and biogenesis]; Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440800 [Multi-domain] Cd Length: 226 Bit Score: 308.12 E-value: 4.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 4 KTEKLQKILARSGHGSRREIEGYIQQGRISIDGKTAT-LGDRieVKPSIKIRLDGRILNIKEPqktvCRVLAYYKPEGEL 82
Cdd:COG1187 1 EGMRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTeLGTK--VDPGDEVTVDGKPLKLPEE----PVYLLLNKPAGVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 83 CTRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLTQG 162
Cdd:COG1187 75 STTKDPEGRPTVFDLLPEARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498910755 163 VQLEDGPASFKTITFKGGEGiNQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLpKGLPRGGWTEL 235
Cdd:COG1187 155 VELEDGPTKPAKVEILSGEA-NTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTL-GDLPPGEWREL 225
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
71-236 |
2.86e-98 |
|
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and eukaryotic proteins similar to E. coli RluB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RluB makes psi2605 in 23S RNA. psi2605 has been detected in eubacteria but, not in eukarya and archea despite the presence of a precursor U at that site.
Pssm-ID: 211330 [Multi-domain] Cd Length: 167 Bit Score: 286.13 E-value: 2.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 71 RVLAYYKPEGELCTRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGE 150
Cdd:cd02556 1 RVLIYHKPEGLICTRKDPKGRPTVFDLLPKLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 151 VDTAKLRQLTQGVQLEDGPASFKTITFKGGEGINQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLPKGLPRG 230
Cdd:cd02556 81 VTDEQLKSLKKGVELEDGFAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIFLPGNLKRG 160
|
....*.
gi 498910755 231 GWTELG 236
Cdd:cd02556 161 QWEELP 166
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
109-235 |
4.38e-60 |
|
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that RNA modifications involved in maturing the protein translation apparatus. Counts per genome vary: two in Staphylococcus aureus, three in Pseudomonas putida, four in E. coli, etc. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272902 Cd Length: 128 Bit Score: 187.92 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 109 VGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLTQGVQLEDGPASFKTITFKGGEGINQWYN 188
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITEPGFPTWLR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 498910755 189 VTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLpKGLPRGGWTEL 235
Cdd:TIGR00093 81 VTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSL-NGLPPGEWRPL 126
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
72-201 |
6.76e-17 |
|
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.
Pssm-ID: 459961 [Multi-domain] Cd Length: 151 Bit Score: 76.29 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 72 VLAYYKPEGELCTRHDPEGRPTVFDRLPRMQGA---RWIAVGRLDINTCGLLLFTTDGELANRLMH--PSQEVEREYAVR 146
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSLTKLLSLLALLLRRELgvkRLYPVHRLDKNTSGLLLLAKDGEAANKLNKlfPERKIEKEYLAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498910755 147 VFGEVDTAKLRQL----------TQGVQLEDGPAS---FKTITFKGGEGINqWYNVTLTEGRNREVRR 201
Cdd:pfam00849 81 VDKPEEEEGTIKSpikkeknkspFRKEEELGGKKAvthLKVLKSGSKGDYS-LLELELVTGRKHQIRA 147
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
8-65 |
2.86e-04 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 38.34 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 498910755 8 LQKILARSG-HGSRREIEGYIQQGRISIDGKTATLGDRIeVKPSIKIRLDGRILNIKEP 65
Cdd:smart00363 3 LDKFLARLGlAPSRSQARRLIEQGRVKVNGKKVTKPSYI-VKPGDVISVRGKELKRLKK 60
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
4-291 |
0e+00 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 562.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 4 KTEKLQKILARSGHGSRREIEGYIQQGRISIDGKTATLGDRIEVKPSIKIRLDGRILNIKEPQKTVCRVLAYYKPEGELC 83
Cdd:PRK10700 1 MSEKLQKVLARAGHGSRREIESIIEAGRVSVDGKIATLGDRVEVTPGLKIRIDGHLISVKESAEQICRVLAYYKPEGELC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 84 TRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLTQGV 163
Cdd:PRK10700 81 TRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQLSRGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 164 QLEDGPASFKTITFKGGEGINQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLPKGLPRGGWTELGLEQTNYL 243
Cdd:PRK10700 161 QLEDGPAAFKTIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLPKGLPRGGWTELDLAQTNYL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 498910755 244 RQLVGLGDEMVTKVAVERDQRRIKANQIRRAVKRHAKVASRP-AGKRPA 291
Cdd:PRK10700 241 RELVELPPETSSKVAVEKDRRRMKANQIRRAVKRHSQVSGGRrSGGRNN 289
|
|
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
4-235 |
4.43e-106 |
|
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ribosomal structure and biogenesis]; Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440800 [Multi-domain] Cd Length: 226 Bit Score: 308.12 E-value: 4.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 4 KTEKLQKILARSGHGSRREIEGYIQQGRISIDGKTAT-LGDRieVKPSIKIRLDGRILNIKEPqktvCRVLAYYKPEGEL 82
Cdd:COG1187 1 EGMRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTeLGTK--VDPGDEVTVDGKPLKLPEE----PVYLLLNKPAGVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 83 CTRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLTQG 162
Cdd:COG1187 75 STTKDPEGRPTVFDLLPEARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498910755 163 VQLEDGPASFKTITFKGGEGiNQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLpKGLPRGGWTEL 235
Cdd:COG1187 155 VELEDGPTKPAKVEILSGEA-NTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTL-GDLPPGEWREL 225
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
71-236 |
2.86e-98 |
|
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and eukaryotic proteins similar to E. coli RluB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RluB makes psi2605 in 23S RNA. psi2605 has been detected in eubacteria but, not in eukarya and archea despite the presence of a precursor U at that site.
Pssm-ID: 211330 [Multi-domain] Cd Length: 167 Bit Score: 286.13 E-value: 2.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 71 RVLAYYKPEGELCTRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGE 150
Cdd:cd02556 1 RVLIYHKPEGLICTRKDPKGRPTVFDLLPKLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 151 VDTAKLRQLTQGVQLEDGPASFKTITFKGGEGINQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLPKGLPRG 230
Cdd:cd02556 81 VTDEQLKSLKKGVELEDGFAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIFLPGNLKRG 160
|
....*.
gi 498910755 231 GWTELG 236
Cdd:cd02556 161 QWEELP 166
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
109-235 |
4.38e-60 |
|
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that RNA modifications involved in maturing the protein translation apparatus. Counts per genome vary: two in Staphylococcus aureus, three in Pseudomonas putida, four in E. coli, etc. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 272902 Cd Length: 128 Bit Score: 187.92 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 109 VGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLTQGVQLEDGPASFKTITFKGGEGINQWYN 188
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITEPGFPTWLR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 498910755 189 VTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLpKGLPRGGWTEL 235
Cdd:TIGR00093 81 VTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSL-NGLPPGEWRPL 126
|
|
| PseudoU_synth_RsuA_like |
cd02870 |
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ... |
72-218 |
3.11e-59 |
|
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the synthesis of pseudouridine from uracil in ribosomal RNA. The RsuA subfamily includes Pseudouridine Synthase similar to Ribosomal small subunit pseudouridine 516 synthase. Most of the proteins in this family are bacterial proteins.
Pssm-ID: 211347 [Multi-domain] Cd Length: 146 Bit Score: 186.16 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 72 VLAYYKPEGELCTRHDPEGRPTVFDRLPRmQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEV 151
Cdd:cd02870 1 YLLLNKPRGVVSTVRDPEGRPTVLDLLKD-VGERLFPVGRLDYDTEGLLLLTNDGELANRLTHPRYGVEKTYLVKVRGVP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498910755 152 DTAKLRQLTQGVQLEDGPASFKTITFKGGEGINQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRY 218
Cdd:cd02870 80 SEEELRRLRAGVELDDGKTAPAKVKVLSRDPKNTLLEVTLHEGRNRQVRRMFEAVGHPVLRLKRVRI 146
|
|
| PseudoU_synth_Rsu_Rlu_like |
cd02550 |
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ... |
72-218 |
7.27e-51 |
|
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli.
Pssm-ID: 211325 [Multi-domain] Cd Length: 154 Bit Score: 165.24 E-value: 7.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 72 VLAYYKPEGELCTRHDPEGRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEV 151
Cdd:cd02550 1 ILVLNKPSGLVCHPTDRDRDPTVVVRLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEKEYLVTVRGEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498910755 152 DTAKLRQL-------TQGVQLEDGPASFKTITFKGGEGINQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRY 218
Cdd:cd02550 81 DEEGIEDLatvrrgrLSGLVDEGVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHCAAVGFPVLRLHRVRI 154
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
74-239 |
3.74e-37 |
|
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and bacterial proteins similar to Escherichia coli RsuA. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RsuA makes psi516 in 16S RNA. Psi at this position is not generally conserved in other organisms.
Pssm-ID: 211327 [Multi-domain] Cd Length: 167 Bit Score: 130.33 E-value: 3.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 74 AYY---KPEGELCTRHDPEGrPTVFDRLPRMQGARWI-AVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFG 149
Cdd:cd02553 1 VYLmlnKPAGVVCATKDPHH-PTVIDLLPEPDRRRDLfPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 150 EVDTAKLRQLTQGVQLEDG----PASFKTITfkggegiNQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLPK 225
Cdd:cd02553 80 PLTEDDIEAFAEGVLLHDGyptkPAKLEILS-------PTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELDD 152
|
170
....*....|....
gi 498910755 226 GLPRGGWTELGLEQ 239
Cdd:cd02553 153 DLAPGEWRPLTEEE 166
|
|
| PRK10475 |
PRK10475 |
23S rRNA pseudouridine(2604) synthase RluF; |
1-300 |
1.11e-30 |
|
23S rRNA pseudouridine(2604) synthase RluF;
Pssm-ID: 236698 [Multi-domain] Cd Length: 290 Bit Score: 116.75 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 1 MSDKTEKLQKILARSGHGSRREIEGYIQQGRISIDGKTATLGDRieVKPSIKIRLDGRILNIKEPQKTVcrVLAYYKPEG 80
Cdd:PRK10475 2 LTDSSTRLNKYISESGICSRREADRYIEQGNVFINGKRATIGDQ--VKAGDVVKVNGQLIEPREAEDLV--LIALNKPVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 81 ELCTRHDPEgRPTVFDRLPrmQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVDTAKLRQLT 160
Cdd:PRK10475 78 IVSTTEDGE-RDNIVDFVN--HSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITDEFIRGMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 161 QGVQLedgpasFKTITFK---GGEGINQwYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLpKGLPRGGWTELGL 237
Cdd:PRK10475 155 AGVPI------LGTVTKKckvKKEAPFV-FRITLVQGLNRQIRRMCEHFGYEVTKLERTRIMNVSL-SGIPLGEWRDLTD 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498910755 238 EQTNYLRQLVglgdEMVTKVAVERDQRRIKANQIRRAVKRHAKVASR-----PAGKRPASSSRQNAGR 300
Cdd:PRK10475 227 DELIDLFKLI----ENSSSEAKPKAKAKPKTAGIKRPVVKMEKTAEKggrpaSNGKRFTSPGRKKKGR 290
|
|
| PseudoU_synth_RluE |
cd02566 |
Pseudouridine synthase, Escherichia coli RluE; This group is comprised of bacterial proteins ... |
72-223 |
7.26e-27 |
|
Pseudouridine synthase, Escherichia coli RluE; This group is comprised of bacterial proteins similar to E. coli RluE. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. Escherichia coli RluE makes psi2457 in 23S RNA. psi2457 is not universally conserved.
Pssm-ID: 211334 [Multi-domain] Cd Length: 168 Bit Score: 103.23 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 72 VLAYYKPEGELCT-RHDPEGRPTVFDRLPrMQGARwiAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGE 150
Cdd:cd02566 1 LILFNKPYGVLSQfTDESEKHKTLKDYID-DPGVY--AAGRLDRDSEGLLLLTDDGRLQHRITDPSFKHPKTYYVQVEGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 151 VDTAKLRQLTQGVQLEDGPASFKTItFKGGEGI----------------NQWYNVTLTEGRNREVRRLWESVGVQVSRLI 214
Cdd:cd02566 78 PTEDALEQLRNGVELGDGLTLPAKV-EKVDEPPwlwereppirfrknipTSWIEITICEGKNRQVRRMTAAVGFPTLRLI 156
|
....*....
gi 498910755 215 RVRYGDINL 223
Cdd:cd02566 157 RVSIGDIGL 165
|
|
| PseudoU_synth_RluF |
cd02554 |
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial ... |
73-235 |
4.79e-23 |
|
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial proteins similar to Escherichia coli RluF. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. E.coli RluF makes psi2604 in 23S RNA. psi2604 has only been detected in E. coli. It is absent from other eubacteria despite a precursor U at that site and from eukarya and archea which lack a precursor U at that site.
Pssm-ID: 211328 [Multi-domain] Cd Length: 164 Bit Score: 93.14 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 73 LAYYKPEGELCTRHDPEgRPTVFDRLPrmQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEVD 152
Cdd:cd02554 3 IAYNKPVGIDCTLERAD-EDNIIDFVN--PPPRIFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEYLVTVNKPIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 153 TAKLRQLTQGVQLEDG---PASFKTITFKGgeginqwYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLpKGLPR 229
Cdd:cd02554 80 DEFIEGMSNGVVILGTvtkPCKVERLAKDK-------FRIVLTQGLNRQIRRMCEALGYRVTDLKRVRIMNIEL-GDLAP 151
|
....*.
gi 498910755 230 GGWTEL 235
Cdd:cd02554 152 GEWRPL 157
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
7-241 |
8.48e-22 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 91.71 E-value: 8.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 7 KLQKILARSGHGSRREIEGYIQQGRISIDGKTATLGdRIEVKPSIKIRLDGRILNikepQKTVCRVLAYYKPEGELCTRH 86
Cdd:PRK10839 2 RLDKFISQQLGVSRAIAGRELRANRVTVDGEIVKNG-AFKLLPEHDVAYDGNPLA----QQHGPRYFMLNKPQGYVCSTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 87 DPEgRPTVFDRLPRMQGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVFGEV--DTAKlrQLTQGVQ 164
Cdd:PRK10839 77 DPD-HPTVLYFLDEPVAYKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVadDTAE--QFAKGVQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 165 LED-----GPASFKTITfkggegiNQWYNVTLTEGRNREVRRLWESVGVQVSRLIRVRYGDINLPKGLPRGGWTELGLEQ 239
Cdd:PRK10839 154 LHNekdltKPAVLEVIT-------PTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDADLAPGEYRPLTEEE 226
|
..
gi 498910755 240 TN 241
Cdd:PRK10839 227 IA 228
|
|
| PRK11394 |
PRK11394 |
23S rRNA pseudouridine(2457) synthase RluE; |
63-234 |
1.71e-18 |
|
23S rRNA pseudouridine(2457) synthase RluE;
Pssm-ID: 183115 Cd Length: 217 Bit Score: 82.10 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 63 KEPQKTVCRVLAYYKPEGELCTRHDPEGRPTVFDRLPrMQGArwIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVERE 142
Cdd:PRK11394 32 RKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIP-VQGV--YAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 143 YAVRVFGEVDTAKLRQLTQGVQLEDGPasfktiTFKGGEGI---------------------NQWYNVTLTEGRNREVRR 201
Cdd:PRK11394 109 YYVQVEGIPTQDALEALRNGVTLNDGP------TLPAGAELvdepawlwprnppirerksipTSWLKITLYEGRNRQVRR 182
|
170 180 190
....*....|....*....|....*....|...
gi 498910755 202 LWESVGVQVSRLIRVRYGDINLpKGLPRGGWTE 234
Cdd:PRK11394 183 MTAHVGFPTLRLIRYAMGDYSL-DNLANGEWRE 214
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
72-201 |
6.76e-17 |
|
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.
Pssm-ID: 459961 [Multi-domain] Cd Length: 151 Bit Score: 76.29 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 72 VLAYYKPEGELCTRHDPEGRPTVFDRLPRMQGA---RWIAVGRLDINTCGLLLFTTDGELANRLMH--PSQEVEREYAVR 146
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSLTKLLSLLALLLRRELgvkRLYPVHRLDKNTSGLLLLAKDGEAANKLNKlfPERKIEKEYLAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498910755 147 VFGEVDTAKLRQL----------TQGVQLEDGPAS---FKTITFKGGEGINqWYNVTLTEGRNREVRR 201
Cdd:pfam00849 81 VDKPEEEEGTIKSpikkeknkspFRKEEELGGKKAvthLKVLKSGSKGDYS-LLELELVTGRKHQIRA 147
|
|
| PSSA_1 |
cd02555 |
Pseudouridine synthase, a subgroup of the RsuA family; This group is comprised of bacterial ... |
76-236 |
1.04e-14 |
|
Pseudouridine synthase, a subgroup of the RsuA family; This group is comprised of bacterial proteins assigned to the RsuA family of pseudouridine synthases. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. The TruA family is comprised of proteins related to Escherichia coli RsuA.
Pssm-ID: 211329 [Multi-domain] Cd Length: 177 Bit Score: 70.90 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 76 YKPEGELCTRHDP---EGRPTVFDRLPRM----QGARWIAVGRLDINTCGLLLFTTDGELANRLMHPSQEVEREYAVRVF 148
Cdd:cd02555 10 HKPAGMVSEQALAllgPGQRSAADRSGRRplkgHFARLAPIGPLDKDASGLLVFSQDGRVLRKLIGDASRLEQEYLVEVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498910755 149 GEVDTAKLRQLTQGVQLEDGPASFKTITfkggeginqWYNVT-----LTEGRNREVRRLWESVGVQVSRLIRVRYGDINL 223
Cdd:cd02555 90 GELTAGGLERLNHGLTYDGRELPPAKVS---------WQNEQrlrfaLKEPQPGQIRRMCESVGLEVVALRRIRIGRVSL 160
|
170
....*....|...
gi 498910755 224 PKgLPRGGWTELG 236
Cdd:cd02555 161 GK-LPLGQWRYLT 172
|
|
| S4 |
cd00165 |
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ... |
8-72 |
2.11e-05 |
|
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.
Pssm-ID: 238095 [Multi-domain] Cd Length: 70 Bit Score: 41.85 E-value: 2.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498910755 8 LQKILARSG-HGSRREIEGYIQQGRISIDGKTAT-LGDRIEVKPSIKIRLDGRILNIKEPQKTVCRV 72
Cdd:cd00165 3 LDKILARLGlAPSRSEARQLIKHGHVLVNGKVVTkPSYKVKPGDVIEVDGKSIEEDIVYEDKKLLVV 69
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
8-65 |
2.86e-04 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 38.34 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 498910755 8 LQKILARSG-HGSRREIEGYIQQGRISIDGKTATLGDRIeVKPSIKIRLDGRILNIKEP 65
Cdd:smart00363 3 LDKFLARLGlAPSRSQARRLIEQGRVKVNGKKVTKPSYI-VKPGDVISVRGKELKRLKK 60
|
|
| S4 |
pfam01479 |
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ... |
6-40 |
1.75e-03 |
|
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.
Pssm-ID: 396182 [Multi-domain] Cd Length: 48 Bit Score: 35.55 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|....*.
gi 498910755 6 EKLQKILARSGHG-SRREIEGYIQQGRISIDGKTAT 40
Cdd:pfam01479 1 RRLDKVLARLGLAsSRSQARQLIEHGRVLVNGKVVK 36
|
|
| PseudoU_synth_ScRIB2 |
cd02557 |
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ... |
111-150 |
5.56e-03 |
|
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, Saccharomyces cerevisiae RIB2_like. This group is comprised of eukaryotic and bacterial proteins similar to Saccharomyces cerevisiae RIB2, S. cerevisiae Pus6p and human hRPUDSD2. S. cerevisiae RIB2 displays two distinct catalytic activities. The N-terminal domain of RIB2 is RNA:psi-synthase which makes psi32 on cytoplasmic tRNAs. Psi32 is highly phylogenetically conserved. The C-terminal domain of RIB2 has a DRAP deaminase activity which catalyses the formation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate from 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate during riboflavin biosynthesis. S. cerevisiae Pus6p makes the psi31 of cytoplasmic and mitochondrial tRNAs.
Pssm-ID: 211331 [Multi-domain] Cd Length: 213 Bit Score: 37.22 E-value: 5.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 498910755 111 RLDINTCGLLLFTTDGELANRL--MHPSQEVEREYAVRVFGE 150
Cdd:cd02557 65 RLDRLTSGLLLFAKTSQTASRLqqQIRSREVKKEYLARVKGE 106
|
|
|