|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
1-289 |
0e+00 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 581.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 1 MSEKLQKVLARAGHGSRREIEAKIEAGRVSVDGKIATLGDRVEIVPGLKIRIDGHLISVKESAEQICRVLAYYKPEGELC 80
Cdd:PRK10700 1 MSEKLQKVLARAGHGSRREIESIIEAGRVSVDGKIATLGDRVEVTPGLKIRIDGHLISVKESAEQICRVLAYYKPEGELC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 81 TRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRGV 160
Cdd:PRK10700 81 TRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQLSRGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 161 QLEDGPAAFKTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLPKGLPRGGYTELDLAQTNYL 240
Cdd:PRK10700 161 QLEDGPAAFKTIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLPKGLPRGGWTELDLAQTNYL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1738471075 241 RELVELTPETSSKVAVEKDRRRLKANQIRRAVKRHSQSSANPRQGNNSN 289
Cdd:PRK10700 241 RELVELPPETSSKVAVEKDRRRMKANQIRRAVKRHSQVSGGRRSGGRNN 289
|
|
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-233 |
8.88e-109 |
|
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: 314.66 E-value: 8.88e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 1 MSEKLQKVLARAGHGSRREIEAKIEAGRVSVDGKIAT-LGDRVEivPGLKIRIDGHLISVKESaeqiCRVLAYYKPEGEL 79
Cdd:COG1187 1 EGMRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTeLGTKVD--PGDEVTVDGKPLKLPEE----PVYLLLNKPAGVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 80 CTRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRG 159
Cdd:COG1187 75 STTKDPEGRPTVFDLLPEARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738471075 160 VQLEDGPAAFKTIKFTGGEGiNQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLpKGLPRGGYTELD 233
Cdd:COG1187 155 VELEDGPTKPAKVEILSGEA-NTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTL-GDLPPGEWRELT 226
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
68-233 |
2.98e-101 |
|
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: 293.45 E-value: 2.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 68 RVLAYYKPEGELCTRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQ 147
Cdd:cd02556 1 RVLIYHKPEGLICTRKDPKGRPTVFDLLPKLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 148 VDEDKLRQLSRGVQLEDGPAAFKTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLPKGLPRG 227
Cdd:cd02556 81 VTDEQLKSLKKGVELEDGFAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIFLPGNLKRG 160
|
....*.
gi 1738471075 228 GYTELD 233
Cdd:cd02556 161 QWEELP 166
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
106-234 |
5.34e-64 |
|
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: 197.55 E-value: 5.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 106 VGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRGVQLEDGPAAFKTIKFTGGEGINQWYN 185
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITEPGFPTWLR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1738471075 186 VTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLpKGLPRGGYTELDL 234
Cdd:TIGR00093 81 VTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSL-NGLPPGEWRPLTL 128
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
69-198 |
8.91e-19 |
|
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: 81.30 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 69 VLAYYKPEGELCTRNDPEG---RPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMH--PSREVEREYAVR 143
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSLTkllSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKlfPERKIEKEYLAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738471075 144 VFG----------QVDEDKLRQLSRGVQLEDGPAA---FKTIKFtGGEGINQWYNVTLTEGRNREVRR 198
Cdd:pfam00849 81 VDKpeeeegtiksPIKKEKNKSPFRKEEELGGKKAvthLKVLKS-GSKGDYSLLELELVTGRKHQIRA 147
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
5-52 |
1.16e-04 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 39.50 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1738471075 5 LQKVLARAG-HGSRREIEAKIEAGRVSVDGKIAT-------LGDRVEIVPGLKIRI 52
Cdd:smart00363 3 LDKFLARLGlAPSRSQARRLIEQGRVKVNGKKVTkpsyivkPGDVISVRGKELKRL 58
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
1-289 |
0e+00 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 581.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 1 MSEKLQKVLARAGHGSRREIEAKIEAGRVSVDGKIATLGDRVEIVPGLKIRIDGHLISVKESAEQICRVLAYYKPEGELC 80
Cdd:PRK10700 1 MSEKLQKVLARAGHGSRREIESIIEAGRVSVDGKIATLGDRVEVTPGLKIRIDGHLISVKESAEQICRVLAYYKPEGELC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 81 TRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRGV 160
Cdd:PRK10700 81 TRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQLSRGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 161 QLEDGPAAFKTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLPKGLPRGGYTELDLAQTNYL 240
Cdd:PRK10700 161 QLEDGPAAFKTIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLPKGLPRGGWTELDLAQTNYL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1738471075 241 RELVELTPETSSKVAVEKDRRRLKANQIRRAVKRHSQSSANPRQGNNSN 289
Cdd:PRK10700 241 RELVELPPETSSKVAVEKDRRRMKANQIRRAVKRHSQVSGGRRSGGRNN 289
|
|
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-233 |
8.88e-109 |
|
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: 314.66 E-value: 8.88e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 1 MSEKLQKVLARAGHGSRREIEAKIEAGRVSVDGKIAT-LGDRVEivPGLKIRIDGHLISVKESaeqiCRVLAYYKPEGEL 79
Cdd:COG1187 1 EGMRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTeLGTKVD--PGDEVTVDGKPLKLPEE----PVYLLLNKPAGVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 80 CTRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRG 159
Cdd:COG1187 75 STTKDPEGRPTVFDLLPEARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738471075 160 VQLEDGPAAFKTIKFTGGEGiNQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLpKGLPRGGYTELD 233
Cdd:COG1187 155 VELEDGPTKPAKVEILSGEA-NTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTL-GDLPPGEWRELT 226
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
68-233 |
2.98e-101 |
|
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: 293.45 E-value: 2.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 68 RVLAYYKPEGELCTRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQ 147
Cdd:cd02556 1 RVLIYHKPEGLICTRKDPKGRPTVFDLLPKLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 148 VDEDKLRQLSRGVQLEDGPAAFKTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLPKGLPRG 227
Cdd:cd02556 81 VTDEQLKSLKKGVELEDGFAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIFLPGNLKRG 160
|
....*.
gi 1738471075 228 GYTELD 233
Cdd:cd02556 161 QWEELP 166
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
106-234 |
5.34e-64 |
|
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: 197.55 E-value: 5.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 106 VGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRGVQLEDGPAAFKTIKFTGGEGINQWYN 185
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITEPGFPTWLR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1738471075 186 VTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLpKGLPRGGYTELDL 234
Cdd:TIGR00093 81 VTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSL-NGLPPGEWRPLTL 128
|
|
| PseudoU_synth_RsuA_like |
cd02870 |
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ... |
69-215 |
6.29e-62 |
|
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: 192.71 E-value: 6.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 69 VLAYYKPEGELCTRNDPEGRPTVFDrLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQV 148
Cdd:cd02870 1 YLLLNKPRGVVSTVRDPEGRPTVLD-LLKDVGERLFPVGRLDYDTEGLLLLTNDGELANRLTHPRYGVEKTYLVKVRGVP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1738471075 149 DEDKLRQLSRGVQLEDGPAAFKTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRY 215
Cdd:cd02870 80 SEEELRRLRAGVELDDGKTAPAKVKVLSRDPKNTLLEVTLHEGRNRQVRRMFEAVGHPVLRLKRVRI 146
|
|
| PseudoU_synth_Rsu_Rlu_like |
cd02550 |
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ... |
69-215 |
1.30e-56 |
|
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: 179.49 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 69 VLAYYKPEGELCTRNDPEGRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQV 148
Cdd:cd02550 1 ILVLNKPSGLVCHPTDRDRDPTVVVRLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEKEYLVTVRGEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738471075 149 DEDKLRQLS-------RGVQLEDGPAAFKTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRY 215
Cdd:cd02550 81 DEEGIEDLAtvrrgrlSGLVDEGVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHCAAVGFPVLRLHRVRI 154
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
71-236 |
1.82e-38 |
|
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: 133.41 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 71 AYY---KPEGELCTRNDPEGrPTVFDRLPKLRGARWI-AVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFG 146
Cdd:cd02553 1 VYLmlnKPAGVVCATKDPHH-PTVIDLLPEPDRRRDLfPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 147 QVDEDKLRQLSRGVQLEDG----PAAFKTIKftggegiNQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLPK 222
Cdd:cd02553 80 PLTEDDIEAFAEGVLLHDGyptkPAKLEILS-------PTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELDD 152
|
170
....*....|....
gi 1738471075 223 GLPRGGYTELDLAQ 236
Cdd:cd02553 153 DLAPGEWRPLTEEE 166
|
|
| PRK10475 |
PRK10475 |
23S rRNA pseudouridine(2604) synthase RluF; |
2-291 |
3.78e-29 |
|
23S rRNA pseudouridine(2604) synthase RluF;
Pssm-ID: 236698 [Multi-domain] Cd Length: 290 Bit Score: 112.52 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 2 SEKLQKVLARAGHGSRREIEAKIEAGRVSVDGKIATLGDRVeiVPGLKIRIDGHLISVKESAEQIcrVLAYYKPEGELCT 81
Cdd:PRK10475 6 STRLNKYISESGICSRREADRYIEQGNVFINGKRATIGDQV--KAGDVVKVNGQLIEPREAEDLV--LIALNKPVGIVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 82 RNDPEgRPTVFDRLPklRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRGVQ 161
Cdd:PRK10475 82 TEDGE-RDNIVDFVN--HSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITDEFIRGMGAGVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 162 L-----------EDGPAAFKtikftggeginqwynVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLpKGLPRGGYT 230
Cdd:PRK10475 159 IlgtvtkkckvkKEAPFVFR---------------ITLVQGLNRQIRRMCEHFGYEVTKLERTRIMNVSL-SGIPLGEWR 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1738471075 231 ELDlaqtnyLRELVELTP--ETSSKVAVEKDRRRLKANQIRRAVKRHSQSSANPRQGNNSNRR 291
Cdd:PRK10475 223 DLT------DDELIDLFKliENSSSEAKPKAKAKPKTAGIKRPVVKMEKTAEKGGRPASNGKR 279
|
|
| PseudoU_synth_RluE |
cd02566 |
Pseudouridine synthase, Escherichia coli RluE; This group is comprised of bacterial proteins ... |
69-220 |
3.56e-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: 104.00 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 69 VLAYYKPEGELCT-RNDPEGRPTVFDRL--PKLRgarwiAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVF 145
Cdd:cd02566 1 LILFNKPYGVLSQfTDESEKHKTLKDYIddPGVY-----AAGRLDRDSEGLLLLTDDGRLQHRITDPSFKHPKTYYVQVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 146 GQVDEDKLRQLSRGVQLEDGPA----AFKT------------IKFTGgEGINQWYNVTLTEGRNREVRRLWEAVGVQVSR 209
Cdd:cd02566 76 GVPTEDALEQLRNGVELGDGLTlpakVEKVdeppwlwereppIRFRK-NIPTSWIEITICEGKNRQVRRMTAAVGFPTLR 154
|
170
....*....|.
gi 1738471075 210 LIRVRYGDILL 220
Cdd:cd02566 155 LIRVSIGDIGL 165
|
|
| PseudoU_synth_RluF |
cd02554 |
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial ... |
70-232 |
6.28e-25 |
|
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: 97.77 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 70 LAYYKPEGELCTRNDPEgRPTVFDRLPKlrGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVD 149
Cdd:cd02554 3 IAYNKPVGIDCTLERAD-EDNIIDFVNP--PPRIFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEYLVTVNKPIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 150 EDKLRQLSRGVQLEDGPaafkTIKFTGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLpKGLPRGGY 229
Cdd:cd02554 80 DEFIEGMSNGVVILGTV----TKPCKVERLAKDKFRIVLTQGLNRQIRRMCEALGYRVTDLKRVRIMNIEL-GDLAPGEW 154
|
...
gi 1738471075 230 TEL 232
Cdd:cd02554 155 RPL 157
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
4-232 |
1.19e-24 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 99.03 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 4 KLQKVLARAGHGSRREIEAKIEAGRVSVDGKIATLGdRVEIVPGLKIRIDGHLISVKESAeqicRVLAYYKPEGELCTRN 83
Cdd:PRK10839 2 RLDKFISQQLGVSRAIAGRELRANRVTVDGEIVKNG-AFKLLPEHDVAYDGNPLAQQHGP----RYFMLNKPQGYVCSTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 84 DPEgRPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDEDKLRQLSRGVQLE 163
Cdd:PRK10839 77 DPD-HPTVLYFLDEPVAYKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738471075 164 D-----GPAAFKTIKftggegiNQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDILLPKGLPRGGYTEL 232
Cdd:PRK10839 156 NekdltKPAVLEVIT-------PTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDADLAPGEYRPL 222
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
69-198 |
8.91e-19 |
|
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: 81.30 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 69 VLAYYKPEGELCTRNDPEG---RPTVFDRLPKLRGARWIAVGRLDVNTCGLLLFTTDGELANRLMH--PSREVEREYAVR 143
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSLTkllSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKlfPERKIEKEYLAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738471075 144 VFG----------QVDEDKLRQLSRGVQLEDGPAA---FKTIKFtGGEGINQWYNVTLTEGRNREVRR 198
Cdd:pfam00849 81 VDKpeeeegtiksPIKKEKNKSPFRKEEELGGKKAvthLKVLKS-GSKGDYSLLELELVTGRKHQIRA 147
|
|
| PRK11394 |
PRK11394 |
23S rRNA pseudouridine(2457) synthase RluE; |
51-220 |
1.22e-17 |
|
23S rRNA pseudouridine(2457) synthase RluE;
Pssm-ID: 183115 Cd Length: 217 Bit Score: 79.79 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 51 RIDGHLISVKESAEQICRVLAYYKPEGELCTRNDPEGRPTVFDRLPkLRGArwIAVGRLDVNTCGLLLFTTDGELANRLM 130
Cdd:PRK11394 23 RFSSQRSTRRKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIP-VQGV--YAAGRLDRDSEGLLVLTNNGALQARLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 131 HPSREVEREYAVRVFGQVDEDKLRQLSRGVQLEDGPAAFKTIKFTGGEGI---------------NQWYNVTLTEGRNRE 195
Cdd:PRK11394 100 QPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAGAELVDEPAWlwprnppirerksipTSWLKITLYEGRNRQ 179
|
170 180
....*....|....*....|....*
gi 1738471075 196 VRRLWEAVGVQVSRLIRVRYGDILL 220
Cdd:PRK11394 180 VRRMTAHVGFPTLRLIRYAMGDYSL 204
|
|
| PSSA_1 |
cd02555 |
Pseudouridine synthase, a subgroup of the RsuA family; This group is comprised of bacterial ... |
73-227 |
1.61e-13 |
|
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: 67.43 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 73 YKPEGELCTRNDP---EGRPTVFDRLPK--LRG--ARWIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVF 145
Cdd:cd02555 10 HKPAGMVSEQALAllgPGQRSAADRSGRrpLKGhfARLAPIGPLDKDASGLLVFSQDGRVLRKLIGDASRLEQEYLVEVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738471075 146 GQVDEDKLRQLSRGVQLEDG--PAAFKTikftggeginqWYNVT-----LTEGRNREVRRLWEAVGVQVSRLIRVRYGDI 218
Cdd:cd02555 90 GELTAGGLERLNHGLTYDGRelPPAKVS-----------WQNEQrlrfaLKEPQPGQIRRMCESVGLEVVALRRIRIGRV 158
|
....*....
gi 1738471075 219 LLPKgLPRG 227
Cdd:cd02555 159 SLGK-LPLG 166
|
|
| S4 |
cd00165 |
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ... |
5-64 |
2.08e-06 |
|
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: 44.55 E-value: 2.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738471075 5 LQKVLARAG-HGSRREIEAKIEAGRVSVDGKIAT-LGDRVEivPGLKIRIDGHLISVKESAE 64
Cdd:cd00165 3 LDKILARLGlAPSRSEARQLIKHGHVLVNGKVVTkPSYKVK--PGDVIEVDGKSIEEDIVYE 62
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
5-52 |
1.16e-04 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 39.50 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1738471075 5 LQKVLARAG-HGSRREIEAKIEAGRVSVDGKIAT-------LGDRVEIVPGLKIRI 52
Cdd:smart00363 3 LDKFLARLGlAPSRSQARRLIEQGRVKVNGKKVTkpsyivkPGDVISVRGKELKRL 58
|
|
| S4 |
pfam01479 |
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ... |
3-43 |
5.71e-04 |
|
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: 37.09 E-value: 5.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1738471075 3 EKLQKVLARAGHG-SRREIEAKIEAGRVSVDGKIAT-LGDRVE 43
Cdd:pfam01479 1 RRLDKVLARLGLAsSRSQARQLIEHGRVLVNGKVVKdPSYRVK 43
|
|
| PseudoU_synth_ScRIB2 |
cd02557 |
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ... |
108-154 |
2.72e-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: 38.38 E-value: 2.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1738471075 108 RLDVNTCGLLLFTTDGELANRL--MHPSREVEREYAVRVFGQVDEDKLR 154
Cdd:cd02557 65 RLDRLTSGLLLFAKTSQTASRLqqQIRSREVKKEYLARVKGEFPDGEVV 113
|
|
| |
