|
Name |
Accession |
Description |
Interval |
E-value |
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-228 |
7.49e-87 |
|
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: 256.88 E-value: 7.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 1 MRLDKFLVATGVGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEyKDLVTYQGTPL-VYESFVYYLLNKPSGYVSATQDRQ 79
Cdd:COG1187 3 MRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTELGTKVDP-GDEVTVDGKPLkLPEEPVYLLLNKPAGVVSTTKDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 80 Q-ATVMELLDDtARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDYFARGISLKDH 158
Cdd:COG1187 82 GrPTVFDLLPE-ARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREGVELEDG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 159 QCLPAHLEVLAsdlQQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDpSLAEGEFRRLT 228
Cdd:COG1187 161 PTKPAKVEILS---GEANTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTLG-DLPPGEWRELT 226
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
61-232 |
3.57e-82 |
|
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: 242.81 E-value: 3.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 61 VYYLLNKPSGYVSATQDRQQATVMELLDDTARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGI 140
Cdd:cd02553 1 VYLMLNKPAGVVCATKDPHHPTVIDLLPEPDRRRDLFPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 141 MTEADKDYFARGISLKD-HQCLPAHLEVLasdlqqQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDPSL 219
Cdd:cd02553 81 LTEDDIEAFAEGVLLHDgYPTKPAKLEIL------SPTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELDDDL 154
|
170
....*....|...
gi 504220544 220 AEGEFRRLTPEEL 232
Cdd:cd02553 155 APGEWRPLTEEEL 167
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
1-235 |
3.09e-48 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 158.73 E-value: 3.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 1 MRLDKFLVATGVGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEYKDlVTYQGTPLVYESFV-YYLLNKPSGYVSATQDRQ 79
Cdd:PRK10839 1 MRLDKFISQQLGVSRAIAGRELRANRVTVDGEIVKNGAFKLLPEHD-VAYDGNPLAQQHGPrYFMLNKPQGYVCSTDDPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 80 QATVMELLDDTARQKaVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDYFARGISLKDHQ 159
Cdd:PRK10839 80 HPTVLYFLDEPVAYK-LHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNEK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504220544 160 CL--PAHLEVLASdlqqqtSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDPSLAEGEFRRLTPEELQSL 235
Cdd:PRK10839 159 DLtkPAVLEVITP------TQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDADLAPGEYRPLTEEEIASV 230
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
99-229 |
8.89e-43 |
|
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: 141.31 E-value: 8.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 99 VGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDYFARGISLKDHQCLPAHLEVLASDLQQQTsl 178
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITEPGFPTW-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504220544 179 VKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDpSLAEGEFRRLTP 229
Cdd:TIGR00093 79 LRVTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSLN-GLPPGEWRPLTL 128
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
62-197 |
7.04e-26 |
|
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: 98.63 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 62 YYLLNKPSGYVSATQD---RQQATVMELLDDTARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDL--LSPKKHVTKEYLAK 136
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDsltKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLnkLFPERKIEKEYLAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504220544 137 VAGIMTEADK----------DYFARGISLKDHQCLPAHLEVLASDLQQQTSLVKITIQEGKFHQVKRMVAA 197
Cdd:pfam00849 81 VDKPEEEEGTikspikkeknKSPFRKEEELGGKKAVTHLKVLKSGSKGDYSLLELELVTGRKHQIRAHLAA 151
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
1-55 |
7.83e-06 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 42.19 E-value: 7.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504220544 1 MRLDKFLV-ATGVGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEyKDLVTYQGTPL 55
Cdd:smart00363 1 RRLDKFLArLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKP-GDVISVRGKEL 55
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-228 |
7.49e-87 |
|
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: 256.88 E-value: 7.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 1 MRLDKFLVATGVGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEyKDLVTYQGTPL-VYESFVYYLLNKPSGYVSATQDRQ 79
Cdd:COG1187 3 MRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTELGTKVDP-GDEVTVDGKPLkLPEEPVYLLLNKPAGVVSTTKDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 80 Q-ATVMELLDDtARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDYFARGISLKDH 158
Cdd:COG1187 82 GrPTVFDLLPE-ARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREGVELEDG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 159 QCLPAHLEVLAsdlQQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDpSLAEGEFRRLT 228
Cdd:COG1187 161 PTKPAKVEILS---GEANTWLRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTLG-DLPPGEWRELT 226
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
61-232 |
3.57e-82 |
|
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: 242.81 E-value: 3.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 61 VYYLLNKPSGYVSATQDRQQATVMELLDDTARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGI 140
Cdd:cd02553 1 VYLMLNKPAGVVCATKDPHHPTVIDLLPEPDRRRDLFPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 141 MTEADKDYFARGISLKD-HQCLPAHLEVLasdlqqQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDPSL 219
Cdd:cd02553 81 LTEDDIEAFAEGVLLHDgYPTKPAKLEIL------SPTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELDDDL 154
|
170
....*....|...
gi 504220544 220 AEGEFRRLTPEEL 232
Cdd:cd02553 155 APGEWRPLTEEEL 167
|
|
| PseudoU_synth_RsuA_like |
cd02870 |
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ... |
62-209 |
4.41e-49 |
|
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: 158.04 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 62 YYLLNKPSGYVSATQD-RQQATVMELLDDtaRQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGI 140
Cdd:cd02870 1 YLLLNKPRGVVSTVRDpEGRPTVLDLLKD--VGERLFPVGRLDYDTEGLLLLTNDGELANRLTHPRYGVEKTYLVKVRGV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504220544 141 MTEADKDYFARGISLKDHQCLPAHLEVLASDlqQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLS 209
Cdd:cd02870 79 PSEEELRRLRAGVELDDGKTAPAKVKVLSRD--PKNTLLEVTLHEGRNRQVRRMFEAVGHPVLRLKRVR 145
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
1-235 |
3.09e-48 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 158.73 E-value: 3.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 1 MRLDKFLVATGVGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEYKDlVTYQGTPLVYESFV-YYLLNKPSGYVSATQDRQ 79
Cdd:PRK10839 1 MRLDKFISQQLGVSRAIAGRELRANRVTVDGEIVKNGAFKLLPEHD-VAYDGNPLAQQHGPrYFMLNKPQGYVCSTDDPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 80 QATVMELLDDTARQKaVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDYFARGISLKDHQ 159
Cdd:PRK10839 80 HPTVLYFLDEPVAYK-LHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNEK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504220544 160 CL--PAHLEVLASdlqqqtSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDPSLAEGEFRRLTPEELQSL 235
Cdd:PRK10839 159 DLtkPAVLEVITP------TQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDADLAPGEYRPLTEEEIASV 230
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
99-229 |
8.89e-43 |
|
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: 141.31 E-value: 8.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 99 VGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDYFARGISLKDHQCLPAHLEVLASDLQQQTsl 178
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLEDGKTKPAKLKVITEPGFPTW-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504220544 179 VKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDpSLAEGEFRRLTP 229
Cdd:TIGR00093 79 LRVTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSLN-GLPPGEWRPLTL 128
|
|
| PseudoU_synth_RluF |
cd02554 |
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial ... |
61-234 |
7.48e-36 |
|
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: 124.73 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 61 VYYLLNKPSGYVSATQDRQQATVMELLDDTARqkaVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGI 140
Cdd:cd02554 1 VYIAYNKPVGIDCTLERADEDNIIDFVNPPPR---IFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEYLVTVNKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 141 MTEADKDYFARGISLKDHQCLPAHLEVLASDlqqqtsLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDpSLA 220
Cdd:cd02554 78 ITDEFIEGMSNGVVILGTVTKPCKVERLAKD------KFRIVLTQGLNRQIRRMCEALGYRVTDLKRVRIMNIELG-DLA 150
|
170
....*....|....
gi 504220544 221 EGEFRRLTPEELQS 234
Cdd:cd02554 151 PGEWRPLTDAELFE 164
|
|
| PseudoU_synth_Rsu_Rlu_like |
cd02550 |
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ... |
62-210 |
4.44e-32 |
|
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: 114.78 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 62 YYLLNKPSGYVSATQDRQQATVMELLDDTARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIM 141
Cdd:cd02550 1 ILVLNKPSGLVCHPTDRDRDPTVVVRLDKLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEKEYLVTVRGEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504220544 142 TEADKDYFA-------RGISLKDHQCLPAHLEVLASdlQQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSM 210
Cdd:cd02550 81 DEEGIEDLAtvrrgrlSGLVDEGVPLAVTKVRVIGE--HGGTGRLRLTLKTGRTHQIRRHCAAVGFPVLRLHRVRI 154
|
|
| PseudoU_synth_RluE |
cd02566 |
Pseudouridine synthase, Escherichia coli RluE; This group is comprised of bacterial proteins ... |
62-216 |
1.62e-30 |
|
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: 111.32 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 62 YYLLNKPSGYVSATQD--RQQATVMELLDDtarqKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAG 139
Cdd:cd02566 1 LILFNKPYGVLSQFTDesEKHKTLKDYIDD----PGVYAAGRLDRDSEGLLLLTDDGRLQHRITDPSFKHPKTYYVQVEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 140 IMTEADKDYFARGISLKDHQCLPAHLEVLASDLQ-------------QQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQ 206
Cdd:cd02566 77 VPTEDALEQLRNGVELGDGLTLPAKVEKVDEPPWlwereppirfrknIPTSWIEITICEGKNRQVRRMTAAVGFPTLRLI 156
|
170
....*....|
gi 504220544 207 RLSMGPLKLD 216
Cdd:cd02566 157 RVSIGDIGLD 166
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
64-229 |
1.83e-27 |
|
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: 103.16 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 64 LLNKPSGYVSATQD-RQQATVMELLDDtARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMT 142
Cdd:cd02556 4 IYHKPEGLICTRKDpKGRPTVFDLLPK-LGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 143 EADKDYFARGISLKDHqcLPAHLEVLASDLQQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDPSLAEG 222
Cdd:cd02556 83 DEQLKSLKKGVELEDG--FAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIFLPGNLKRG 160
|
....*..
gi 504220544 223 EFRRLTP 229
Cdd:cd02556 161 QWEELPP 167
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
62-197 |
7.04e-26 |
|
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: 98.63 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 62 YYLLNKPSGYVSATQD---RQQATVMELLDDTARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDL--LSPKKHVTKEYLAK 136
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDsltKLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLnkLFPERKIEKEYLAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504220544 137 VAGIMTEADK----------DYFARGISLKDHQCLPAHLEVLASDLQQQTSLVKITIQEGKFHQVKRMVAA 197
Cdd:pfam00849 81 VDKPEEEEGTikspikkeknKSPFRKEEELGGKKAVTHLKVLKSGSKGDYSLLELELVTGRKHQIRAHLAA 151
|
|
| PRK10475 |
PRK10475 |
23S rRNA pseudouridine(2604) synthase RluF; |
1-235 |
4.86e-24 |
|
23S rRNA pseudouridine(2604) synthase RluF;
Pssm-ID: 236698 [Multi-domain] Cd Length: 290 Bit Score: 97.11 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 1 MRLDKFLVATGVGTRSQVKLLLKKKAIFVNQKvetsaKAHI-DEYK--DLVTYQGT---PLVYESFVYYLLNKPSGYVSA 74
Cdd:PRK10475 7 TRLNKYISESGICSRREADRYIEQGNVFINGK-----RATIgDQVKagDVVKVNGQliePREAEDLVLIALNKPVGIVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 75 TQDRQQATVMELLDDTARqkaVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTeadkDYFARGIS 154
Cdd:PRK10475 82 TEDGERDNIVDFVNHSKR---VFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPIT----DEFIRGMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 155 lkdhqclpAHLEVLAS-----DLQQQTSLV-KITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDpSLAEGEFRRLT 228
Cdd:PRK10475 155 --------AGVPILGTvtkkcKVKKEAPFVfRITLVQGLNRQIRRMCEHFGYEVTKLERTRIMNVSLS-GIPLGEWRDLT 225
|
....*..
gi 504220544 229 PEELQSL 235
Cdd:PRK10475 226 DDELIDL 232
|
|
| PRK11394 |
PRK11394 |
23S rRNA pseudouridine(2457) synthase RluE; |
64-228 |
8.90e-23 |
|
23S rRNA pseudouridine(2457) synthase RluE;
Pssm-ID: 183115 Cd Length: 217 Bit Score: 92.50 E-value: 8.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 64 LLNKPSGYVSA-TQDRQQATVMELLDdtarQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMT 142
Cdd:PRK11394 43 LFNKPYDVLPQfTDEAGRKTLKEFIP----VQGVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 143 EADKDYFARGISLKDHQCLPAHLEVLAS---------DLQQQ----TSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLS 209
Cdd:PRK11394 119 QDALEALRNGVTLNDGPTLPAGAELVDEpawlwprnpPIRERksipTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYA 198
|
170
....*....|....*....
gi 504220544 210 MGPLKLDpSLAEGEFRRLT 228
Cdd:PRK11394 199 MGDYSLD-NLANGEWREAT 216
|
|
| PSSA_1 |
cd02555 |
Pseudouridine synthase, a subgroup of the RsuA family; This group is comprised of bacterial ... |
61-231 |
9.74e-19 |
|
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: 80.53 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 61 VYYLLNKPSGYVS--ATQDRQQATVMELLDDTARQ-----KAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEY 133
Cdd:cd02555 5 VTLLLHKPAGMVSeqALALLGPGQRSAADRSGRRPlkghfARLAPIGPLDKDASGLLVFSQDGRVLRKLIGDASRLEQEY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 134 LAKVAGIMTEADKDYFARGISLKDHQCLPAHLEVlasdlqQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPL 213
Cdd:cd02555 85 LVEVRGELTAGGLERLNHGLTYDGRELPPAKVSW------QNEQRLRFALKEPQPGQIRRMCESVGLEVVALRRIRIGRV 158
|
170
....*....|....*...
gi 504220544 214 KLDpSLAEGEFRRLTPEE 231
Cdd:cd02555 159 SLG-KLPLGQWRYLTTGE 175
|
|
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
2-235 |
1.30e-13 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 68.64 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 2 RLDKFLVATGVGTRSQVKLLLKKKAIFVNQKVET---------SAKAHIDEYkdLVTYQGT-PLVYESFVYYllnKPSGY 71
Cdd:PRK10700 4 KLQKVLARAGHGSRREIESIIEAGRVSVDGKIATlgdrvevtpGLKIRIDGH--LISVKESaEQICRVLAYY---KPEGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 72 VSATQDRQ-QATVMELLD--DTARQKAVfpvGRLDKDTRGLLLLTNNGQLAHDLLSPKKHVTKEYLAKVAGIMTEADKDY 148
Cdd:PRK10700 79 LCTRNDPEgRPTVFDRLPklRGARWIAV---GRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 149 FARGISLKDHqclPAHLEVLA-SDLQQQTSLVKITIQEGKFHQVKRMVAACGKGVLDLQRLSMGPLKLDPSLAEGEFRRL 227
Cdd:PRK10700 156 LSRGVQLEDG---PAAFKTIKfSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLPKGLPRGGWTEL 232
|
....*...
gi 504220544 228 TPEELQSL 235
Cdd:PRK10700 233 DLAQTNYL 240
|
|
| PseudoU_synth_RluA_like |
cd02869 |
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ... |
62-190 |
7.94e-13 |
|
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: 64.67 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 62 YYLLNKPSGYVS-ATQDRQQATVMELLDDTARQKA----VFPVGRLDKDTRGLLLLTNNgQLAHDLLS---PKKHVTKEY 133
Cdd:cd02869 1 LLVVNKPAGLPVhPGPGHLTGTLVNALLKLLLLLGeefrPGLVHRLDKDTSGLLLVAKN-KKAAAKLSkqfKERKVKKTY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504220544 134 LAKVAGIMTEA---DKDYFARGISLK------DHQCLPA--HLEVLASDlqQQTSLVKITIQEGKFHQ 190
Cdd:cd02869 80 LALVDGKPPEDegtIDAPLGRKKRKKrarvvvSEDGKPAitHYKVLERF--GNVTLVELQLETGRTHQ 145
|
|
| rluA_subfam |
TIGR00005 |
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ... |
1-192 |
1.37e-11 |
|
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 161659 [Multi-domain] Cd Length: 299 Bit Score: 62.73 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 1 MRLDKFLVAT-GVGTRSQVKLLLKKKAIFVNQKVeTSAKAHIDEYKDLVTY------------QGTPL--VYESFVYYLL 65
Cdd:TIGR00005 6 QRLDDFLASLlPDLSRSRIQKLIENGQVKVNGKV-TANPKLKVKDGDRITVrvpeeeehevppQDIPLdiLFEDEDIIVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 66 NKPSGYVS-ATQDRQQATVMELL----DDTARQKAVFPVGRLDKDTRGLLLLTNNgQLAHDLLS---PKKHVTKEYLAKV 137
Cdd:TIGR00005 85 NKPSGLVVhPGGGNPFGTVLNALlahcPPIAGVERVGIVHRLDRDTSGLMVVAKT-PLALRELQrqlKNRTVTKEYVALV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504220544 138 AGIMTEADKDYFA-----------RGISlKDHQCLPA--HLEVLASDlqQQTSLVKITIQEGKFHQVK 192
Cdd:TIGR00005 164 HGQFDSGGGTVDAplgrvpnnrglMAVH-PSSEGKPAvtHFRVLERF--GNASLVECELETGRTHQIR 228
|
|
| PseudoU_synth_ScRIB2 |
cd02557 |
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ... |
48-191 |
2.05e-11 |
|
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: 61.49 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 48 VTYQGTPLVYESFVYYLLNKPSGY-VSATQDRQQATVMELLDDTARQKAVFPVGRLDKDTRGLLLLTNNGQLAHDLLSP- 125
Cdd:cd02557 11 VTNDPIKIVHEDDDLLVVDKPSGIpVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTSQTASRLQQQi 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504220544 126 -KKHVTKEYLAKVAG------------IMTEADKDYFARGISLKDHQCLpAHLEVLASDLQQQTSLVKITIQEGKFHQV 191
Cdd:cd02557 91 rSREVKKEYLARVKGefpdgevvvdqpIGLVSPKGGLRNDVDEKGKDAR-TIFKRLSYNGDLNTSVVLCKPITGRTHQI 168
|
|
| RluA |
COG0564 |
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ... |
65-190 |
4.05e-08 |
|
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and biogenesis]; Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440330 [Multi-domain] Cd Length: 218 Bit Score: 52.06 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 65 LNKPSGYVS-ATQDRQQATVMELL----DDTARQKAVFPVGRLDKDTRGLLLLTNNgQLAHDLLSP---KKHVTKEYLAK 136
Cdd:COG0564 11 VNKPAGLVVhPGSGGDDGTLVNALrahlGELSGVPRPGLVHRLDRDTSGLLLVAKT-RKAARRLSEqfrEREVEKRYLAL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504220544 137 VAGIMTEA--------DKDYFARGI-SLKDHQCLPA--HLEVLASdlQQQTSLVKITIQEGKFHQ 190
Cdd:COG0564 90 VEGKPKEDegtidaplGRDPKDRKKmAVVDEDGKPAvtHYRVLER--FGGYSLVEVRLETGRTHQ 152
|
|
| S4 |
cd00165 |
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ... |
1-66 |
5.36e-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: 48.78 E-value: 5.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504220544 1 MRLDKFLVATG-VGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEyKDLVTYQGTP----LVYESFVYYLLN 66
Cdd:cd00165 1 MRLDKILARLGlAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKP-GDVIEVDGKSieedIVYEDKKLLVVN 70
|
|
| PRK11112 |
PRK11112 |
tRNA pseudouridine synthase C; Provisional |
66-196 |
1.23e-06 |
|
tRNA pseudouridine synthase C; Provisional
Pssm-ID: 182971 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 66 NKPSGYV--SATQDRQQAT-VMELLDDTARQKaVFPVGRLDKDTRGLLLLTNNGQLAHdLLSPK---KHVTKEYLAKVAG 139
Cdd:PRK11112 15 NKPAGWLvhRSWLDRHETVfVMQTVRDQIGQH-VFTAHRLDRPTSGVLLMALSSEVAR-LLAQQfeqHQIQKTYHAIVRG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 140 IMTEA-----------DK--DYFARgislKDHQCLPA--HLEVLA------SDLQQQT---SLVKITIQEGKFHQVKRMV 195
Cdd:PRK11112 93 WLMEEavldyplkeelDKiaDKFAR----EDKAPQPAvtHYRGLAtvempvATGRYPTtrySLVELEPKTGRKHQLRRHM 168
|
.
gi 504220544 196 A 196
Cdd:PRK11112 169 A 169
|
|
| PseudoU_synth_TruC |
cd02563 |
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ... |
54-193 |
1.48e-06 |
|
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved.
Pssm-ID: 211333 [Multi-domain] Cd Length: 223 Bit Score: 47.72 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 54 PLVYESFVYYLLNKPSGY-VSATQDRQQATV--MELLDDTARQKaVFPVGRLDKDTRGLLLLTNNGQLAHDL--LSPKKH 128
Cdd:cd02563 2 EILYQDEHLVAINKPSGLlVHRSELDRHETRfaLQTLRDQLGQH-VYPVHRLDRPTSGVLLFALSSEVARKLgeQFTEHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 129 VTKEYLAKVAGIMTEAD-------------KDYFARGISLKD----HQCLPAHLEVLASDLQQQT---SLVKITIQEGKF 188
Cdd:cd02563 81 VHKTYLAVVRGYVPESGtidyplseeldklADKFASDDKAPQaattHYRLLAVEELPVVVGKYPTsrySLVELTPHTGRK 160
|
....*
gi 504220544 189 HQVKR 193
Cdd:cd02563 161 HQLRR 165
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
1-55 |
7.83e-06 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 42.19 E-value: 7.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504220544 1 MRLDKFLV-ATGVGTRSQVKLLLKKKAIFVNQKVETSAKAHIDEyKDLVTYQGTPL 55
Cdd:smart00363 1 RRLDKFLArLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKP-GDVISVRGKEL 55
|
|
| rluD |
PRK11180 |
23S rRNA pseudouridine(1911/1915/1917) synthase RluD; |
14-142 |
3.14e-05 |
|
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
Pssm-ID: 183020 [Multi-domain] Cd Length: 325 Bit Score: 44.28 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504220544 14 TRSQVKLLLKKKAIFVNQKVETSAK------------AHIDEYKDLVTyQGTPL--VYESFVYYLLNKPSGYV----SAT 75
Cdd:PRK11180 32 SRSRIKEWILDQRVLVNGKVINKPKekvlggeqvaidAEIEEEARFEP-QDIPLdiVYEDDDILVINKPRDLVvhpgAGN 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504220544 76 QDRqqaTVMELLDDTARQKAVFP----VGRLDKDTRGLLLLTNN----GQLAHDLlsPKKHVTKEYLAKVAGIMT 142
Cdd:PRK11180 111 PDG---TVLNALLHYYPPIADVPragiVHRLDKDTTGLMVVAKTvpaqTRLVEAL--QKREITREYEAVAIGHMT 180
|
|
| S4 |
pfam01479 |
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ... |
1-43 |
2.89e-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: 37.47 E-value: 2.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 504220544 1 MRLDKFLVATGVG-TRSQVKLLLKKKAIFVNQKVETSAKAHIDE 43
Cdd:pfam01479 1 RRLDKVLARLGLAsSRSQARQLIEHGRVLVNGKVVKDPSYRVKP 44
|
|
|