|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10475 |
PRK10475 |
23S rRNA pseudouridine(2604) synthase RluF; |
1-225 |
2.01e-115 |
|
23S rRNA pseudouridine(2604) synthase RluF;
Pssm-ID: 236698 [Multi-domain] Cd Length: 290 Bit Score: 331.31 E-value: 2.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKASRRGADKLINERRVIINGKVAKIGDQVNPGDDVRVNGEQL--RIARDHVYIALNKPVGITCTSEKAV 78
Cdd:PRK10475 7 TRLNKYISESGICSRREADRYIEQGNVFINGKRATIGDQVKAGDVVKVNGQLIepREAEDLVLIALNKPVGIVSTTEDGE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 79 KGNIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKTLP 158
Cdd:PRK10475 87 RDNIVDFVNHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITDEFIRGMGAGVPILGTVTKK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447144905 159 CEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLSKKEKRRLF 225
Cdd:PRK10475 167 CKVKKEAPFVFRITLVQGLNRQIRRMCEHFGYEVTKLERTRIMNVSLSGIPLGEWRDLTDDELIDLF 233
|
|
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-217 |
2.01e-103 |
|
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: 298.49 E-value: 2.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKASRRGADKLINERRVIINGKVAK-IGDQVNPGDDVRVNGEQLRIARDHVYIALNKPVGITCT-SEKAV 78
Cdd:COG1187 3 MRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTeLGTKVDPGDEVTVDGKPLKLPEEPVYLLLNKPAGVVSTtKDPEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 79 KGNIIDLV--NHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKT 156
Cdd:COG1187 83 RPTVFDLLpeARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREGVELEDGPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447144905 157 LPCEVTQLS---KYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLS 217
Cdd:COG1187 163 KPAKVEILSgeaNTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTLGDLPPGEWRELT 226
|
|
| PseudoU_synth_RluF |
cd02554 |
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial ... |
60-220 |
4.41e-96 |
|
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: 277.65 E-value: 4.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 60 VYIALNKPVGITCTSEKAVKGNIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITP 139
Cdd:cd02554 1 VYIAYNKPVGIDCTLERADEDNIIDFVNPPPRIFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEYLVTVNKPITD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 140 DFLEKMAAGVKILGTKTLPCEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLSKK 219
Cdd:cd02554 81 EFIEGMSNGVVILGTVTKPCKVERLAKDKFRIVLTQGLNRQIRRMCEALGYRVTDLKRVRIMNIELGDLAPGEWRPLTDA 160
|
.
gi 447144905 220 E 220
Cdd:cd02554 161 E 161
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
95-217 |
1.55e-52 |
|
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: 165.96 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 95 IGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKTLPCEVTQLS----KYEFQ 170
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITepgfPTWLR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 447144905 171 IILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLS 217
Cdd:TIGR00093 81 VTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSLNGLPPGEWRPLT 127
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
61-187 |
4.20e-21 |
|
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: 85.92 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 61 YIALNKPVGITCTSEKAVKG------NIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEI--LRAENKHEKEYIVS 132
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSLTKllsllaLLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLnkLFPERKIEKEYLAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447144905 133 VDKPI-------TPDFLEKMAAGVKILGTKTLPCEVTQLSKYEF---------QIILTQGLNRQIRRMCEA 187
Cdd:pfam00849 81 VDKPEeeegtikSPIKKEKNKSPFRKEEELGGKKAVTHLKVLKSgskgdysllELELVTGRKHQIRAHLAA 151
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
1-58 |
5.90e-08 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 47.97 E-value: 5.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKA-SRRGADKLINERRVIINGKVAKI-GDQVNPGDDVRVNGEQLRIARD 58
Cdd:smart00363 1 RRLDKFLARLGLApSRSQARRLIEQGRVKVNGKKVTKpSYIVKPGDVISVRGKELKRLKK 60
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10475 |
PRK10475 |
23S rRNA pseudouridine(2604) synthase RluF; |
1-225 |
2.01e-115 |
|
23S rRNA pseudouridine(2604) synthase RluF;
Pssm-ID: 236698 [Multi-domain] Cd Length: 290 Bit Score: 331.31 E-value: 2.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKASRRGADKLINERRVIINGKVAKIGDQVNPGDDVRVNGEQL--RIARDHVYIALNKPVGITCTSEKAV 78
Cdd:PRK10475 7 TRLNKYISESGICSRREADRYIEQGNVFINGKRATIGDQVKAGDVVKVNGQLIepREAEDLVLIALNKPVGIVSTTEDGE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 79 KGNIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKTLP 158
Cdd:PRK10475 87 RDNIVDFVNHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITDEFIRGMGAGVPILGTVTKK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447144905 159 CEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLSKKEKRRLF 225
Cdd:PRK10475 167 CKVKKEAPFVFRITLVQGLNRQIRRMCEHFGYEVTKLERTRIMNVSLSGIPLGEWRDLTDDELIDLF 233
|
|
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-217 |
2.01e-103 |
|
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: 298.49 E-value: 2.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKASRRGADKLINERRVIINGKVAK-IGDQVNPGDDVRVNGEQLRIARDHVYIALNKPVGITCT-SEKAV 78
Cdd:COG1187 3 MRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTeLGTKVDPGDEVTVDGKPLKLPEEPVYLLLNKPAGVVSTtKDPEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 79 KGNIIDLV--NHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKT 156
Cdd:COG1187 83 RPTVFDLLpeARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREGVELEDGPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447144905 157 LPCEVTQLS---KYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLS 217
Cdd:COG1187 163 KPAKVEILSgeaNTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTLGDLPPGEWRELT 226
|
|
| PseudoU_synth_RluF |
cd02554 |
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial ... |
60-220 |
4.41e-96 |
|
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: 277.65 E-value: 4.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 60 VYIALNKPVGITCTSEKAVKGNIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITP 139
Cdd:cd02554 1 VYIAYNKPVGIDCTLERADEDNIIDFVNPPPRIFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEYLVTVNKPITD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 140 DFLEKMAAGVKILGTKTLPCEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLSKK 219
Cdd:cd02554 81 EFIEGMSNGVVILGTVTKPCKVERLAKDKFRIVLTQGLNRQIRRMCEALGYRVTDLKRVRIMNIELGDLAPGEWRPLTDA 160
|
.
gi 447144905 220 E 220
Cdd:cd02554 161 E 161
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
95-217 |
1.55e-52 |
|
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: 165.96 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 95 IGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKTLPCEVTQLS----KYEFQ 170
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITepgfPTWLR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 447144905 171 IILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLS 217
Cdd:TIGR00093 81 VTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSLNGLPPGEWRPLT 127
|
|
| PseudoU_synth_RsuA_like |
cd02870 |
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ... |
61-200 |
5.46e-51 |
|
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: 162.66 E-value: 5.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 61 YIALNKPVGITCTS--EKAVKGNIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPIT 138
Cdd:cd02870 1 YLLLNKPRGVVSTVrdPEGRPTVLDLLKDVGERLFPVGRLDYDTEGLLLLTNDGELANRLTHPRYGVEKTYLVKVRGVPS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447144905 139 PDFLEKMAAGVKILGTKTLPCEVTQLS----KYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRI 200
Cdd:cd02870 81 EEELRRLRAGVELDDGKTAPAKVKVLSrdpkNTLLEVTLHEGRNRQVRRMFEAVGHPVLRLKRVRI 146
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
60-221 |
2.26e-43 |
|
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: 143.81 E-value: 2.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 60 VYIALNKPVGITCTSEKAVKGNIIDLVNHPLR---ISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKP 136
Cdd:cd02553 1 VYLMLNKPAGVVCATKDPHHPTVIDLLPEPDRrrdLFPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 137 ITPDFLEKMAAGVKIL-GTKTLPCEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIEL-NNLPVGQWR 214
Cdd:cd02553 81 LTEDDIEAFAEGVLLHdGYPTKPAKLEILSPTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELdDDLAPGEWR 160
|
....*..
gi 447144905 215 DLSKKEK 221
Cdd:cd02553 161 PLTEEEL 167
|
|
| PseudoU_synth_Rsu_Rlu_like |
cd02550 |
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ... |
61-200 |
2.80e-35 |
|
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: 122.87 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 61 YIALNKPVGITCTSEKAVKGNII---DLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPI 137
Cdd:cd02550 1 ILVLNKPSGLVCHPTDRDRDPTVvvrLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEKEYLVTVRGEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447144905 138 TPDFLEKMA-------AGVKILGTKTLPCEVTQLSKYE----FQIILTQGLNRQIRRMCEALGYQVYTLKRTRI 200
Cdd:cd02550 81 DEEGIEDLAtvrrgrlSGLVDEGVPLAVTKVRVIGEHGgtgrLRLTLKTGRTHQIRRHCAAVGFPVLRLHRVRI 154
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
1-220 |
1.24e-34 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 123.29 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKASRRGADKLINERRVIINGKVAKIGD-QVNPGDDVRVNGEQLRIARDHVYIALNKPVGITCTSEKAVK 79
Cdd:PRK10839 1 MRLDKFISQQLGVSRAIAGRELRANRVTVDGEIVKNGAfKLLPEHDVAYDGNPLAQQHGPRYFMLNKPQGYVCSTDDPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 80 GNIIDLVNHPL--RISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKTL 157
Cdd:PRK10839 81 PTVLYFLDEPVayKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNEKDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447144905 158 --PCEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELN-NLPVGQWRDLSKKE 220
Cdd:PRK10839 161 tkPAVLEVITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDaDLAPGEYRPLTEEE 226
|
|
| PSSA_1 |
cd02555 |
Pseudouridine synthase, a subgroup of the RsuA family; This group is comprised of bacterial ... |
60-221 |
6.52e-32 |
|
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: 114.81 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 60 VYIALNKPVGITCTSEKAVKG----------NIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEY 129
Cdd:cd02555 5 VTLLLHKPAGMVSEQALALLGpgqrsaadrsGRRPLKGHFARLAPIGPLDKDASGLLVFSQDGRVLRKLIGDASRLEQEY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 130 IVSVDKPITPDFLEKMAAGVKILGTKTLPCEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLP 209
Cdd:cd02555 85 LVEVRGELTAGGLERLNHGLTYDGRELPPAKVSWQNEQRLRFALKEPQPGQIRRMCESVGLEVVALRRIRIGRVSLGKLP 164
|
170
....*....|..
gi 447144905 210 VGQWRDLSKKEK 221
Cdd:cd02555 165 LGQWRYLTTGER 176
|
|
| PseudoU_synth_RluE |
cd02566 |
Pseudouridine synthase, Escherichia coli RluE; This group is comprised of bacterial proteins ... |
61-208 |
1.16e-29 |
|
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: 108.62 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 61 YIALNKPVGITC--TSEKAVKGNIIDLVNHPlRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPIT 138
Cdd:cd02566 1 LILFNKPYGVLSqfTDESEKHKTLKDYIDDP-GVYAAGRLDRDSEGLLLLTDDGRLQHRITDPSFKHPKTYYVQVEGVPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 139 PDFLEKMAAGVKILGTKTLPCEVTQLSKYE-------------------FQIILTQGLNRQIRRMCEALGYQVYTLKRTR 199
Cdd:cd02566 80 EDALEQLRNGVELGDGLTLPAKVEKVDEPPwlwereppirfrkniptswIEITICEGKNRQVRRMTAAVGFPTLRLIRVS 159
|
....*....
gi 447144905 200 IMNIELNNL 208
Cdd:cd02566 160 IGDIGLDNL 168
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
62-218 |
1.12e-26 |
|
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: 100.85 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 62 IALNKPVGITCT-----SEKAVKGNIIDLVNHplRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKP 136
Cdd:cd02556 3 LIYHKPEGLICTrkdpkGRPTVFDLLPKLGIP--RWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 137 ITPDFLEKMAAGVKILGTKTLPCEVTQLSKYE----FQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNI-ELNNLPVG 211
Cdd:cd02556 81 VTDEQLKSLKKGVELEDGFAGFKSIQLEGGEGknswYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIfLPGNLKRG 160
|
....*..
gi 447144905 212 QWRDLSK 218
Cdd:cd02556 161 QWEELPP 167
|
|
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
2-216 |
6.68e-24 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 96.76 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 2 RINKFISEAGKASRRGADKLINERRVIINGKVAKIGD--QVNPGDDVRVNGEQLRIARDHVYI----ALNKPVGITCT-S 74
Cdd:PRK10700 4 KLQKVLARAGHGSRREIESIIEAGRVSVDGKIATLGDrvEVTPGLKIRIDGHLISVKESAEQIcrvlAYYKPEGELCTrN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 75 EKAVKGNIIDLVNHpLRISH---IGRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKI 151
Cdd:PRK10700 84 DPEGRPTVFDRLPK-LRGARwiaVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQLSRGVQL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 152 ----LGTKTLPCEVTQLSKYEFQIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIEL-NNLPVGQWRDL 216
Cdd:PRK10700 163 edgpAAFKTIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLpKGLPRGGWTEL 232
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
61-187 |
4.20e-21 |
|
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: 85.92 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 61 YIALNKPVGITCTSEKAVKG------NIIDLVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEI--LRAENKHEKEYIVS 132
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSLTKllsllaLLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLnkLFPERKIEKEYLAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447144905 133 VDKPI-------TPDFLEKMAAGVKILGTKTLPCEVTQLSKYEF---------QIILTQGLNRQIRRMCEA 187
Cdd:pfam00849 81 VDKPEeeegtikSPIKKEKNKSPFRKEEELGGKKAVTHLKVLKSgskgdysllELELVTGRKHQIRAHLAA 151
|
|
| PRK11394 |
PRK11394 |
23S rRNA pseudouridine(2457) synthase RluE; |
96-217 |
3.87e-15 |
|
23S rRNA pseudouridine(2457) synthase RluE;
Pssm-ID: 183115 Cd Length: 217 Bit Score: 71.70 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 96 GRLDKDSDGLILLTNDGDIVNEILRAENKHEKEYIVSVDKPITPDFLEKMAAGVKILGTKTLPCEVTQLSKYEF------ 169
Cdd:PRK11394 76 GRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAGAELVDEPAWlwprnp 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447144905 170 -------------QIILTQGLNRQIRRMCEALGYQVYTLKRTRIMNIELNNLPVGQWRDLS 217
Cdd:PRK11394 156 pirerksiptswlKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSLDNLANGEWREAT 216
|
|
| S4 |
cd00165 |
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ... |
1-65 |
1.15e-08 |
|
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: 50.33 E-value: 1.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKA-SRRGADKLINERRVIINGKVAKI-GDQVNPGDDVRVNGEQLR---IARDHVYIALN 65
Cdd:cd00165 1 MRLDKILARLGLApSRSEARQLIKHGHVLVNGKVVTKpSYKVKPGDVIEVDGKSIEediVYEDKKLLVVN 70
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
1-58 |
5.90e-08 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 47.97 E-value: 5.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 1 MRINKFISEAGKA-SRRGADKLINERRVIINGKVAKI-GDQVNPGDDVRVNGEQLRIARD 58
Cdd:smart00363 1 RRLDKFLARLGLApSRSQARRLIEQGRVKVNGKKVTKpSYIVKPGDVISVRGKELKRLKK 60
|
|
| S4 |
pfam01479 |
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ... |
1-46 |
8.47e-08 |
|
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: 47.49 E-value: 8.47e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 447144905 1 MRINKFISEAGKA-SRRGADKLINERRVIINGKVAKI-GDQVNPGDDV 46
Cdd:pfam01479 1 RRLDKVLARLGLAsSRSQARQLIEHGRVLVNGKVVKDpSYRVKPGDEI 48
|
|
| PseudoU_synth_RluA_like |
cd02869 |
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ... |
61-190 |
2.05e-04 |
|
Pseudouridine synthase, RluA 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: 211346 [Multi-domain] Cd Length: 185 Bit Score: 40.78 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447144905 61 YIALNKPVGITCTSEKAVKGNIID--------LVNHPLRISHIGRLDKDSDGLILLTNDGDIVNEILRAENKH--EKEYI 130
Cdd:cd02869 1 LLVVNKPAGLPVHPGPGHLTGTLVnallklllLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKERkvKKTYL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447144905 131 VSVDKPITPDFLE---KMAAGVKILGTKTLPCEVTQLSKYEFQIILTQG---LNR---------QIRRMCEALGY 190
Cdd:cd02869 81 ALVDGKPPEDEGTidaPLGRKKRKKRARVVVSEDGKPAITHYKVLERFGnvtLVElqletgrthQIRVHLASIGH 155
|
|
| HslR |
COG1188 |
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ... |
1-48 |
8.41e-03 |
|
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440801 Cd Length: 120 Bit Score: 35.19 E-value: 8.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447144905 1 MRINKFIseagKASR----RG-ADKLINERRVIINGKVAKIGDQVNPGDDVRV 48
Cdd:COG1188 5 MRLDKWL----WAARffktRSlAAEACDGGRVRVNGQRAKPSREVKVGDVLTI 53
|
|
| |
