|
Name |
Accession |
Description |
Interval |
E-value |
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-229 |
3.00e-98 |
|
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: 285.77 E-value: 3.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADMGLGSRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEIIT-YQKDFYYILHKPAGVISATQDNH 79
Cdd:COG1187 3 MRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTELGTKVDP-GDEVTVDGKPLKlPEEPVYLLLNKPAGVVSTTKDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 80 D-QTVIDLLEDqDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDgD 158
Cdd:COG1187 82 GrPTVFDLLPE-ARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREGVELE-D 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214761 159 EQTLPAKLQIDQVDQETEtsiIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLNKGQYRPMT 229
Cdd:COG1187 160 GPTKPAKVEILSGEANTW---LRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTL-GDLPPGEWRELT 226
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
61-233 |
9.62e-90 |
|
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: 262.07 E-value: 9.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 61 FYYILHKPAGVISATQDNHDQTVIDLLEDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGI 140
Cdd:cd02553 1 VYLMLNKPAGVVCATKDPHHPTVIDLLPEPDRRRDLFPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 141 MTEEDIRLFAEGLIIDGDEQTLPAKLQIdqvdqeTETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLPKDL 220
Cdd:cd02553 81 LTEDDIEAFAEGVLLHDGYPTKPAKLEI------LSPTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELDDDL 154
|
170
....*....|...
gi 488214761 221 NKGQYRPMTKEEL 233
Cdd:cd02553 155 APGEWRPLTEEEL 167
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
1-236 |
5.16e-46 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 152.95 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADMgLG-SRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEIITYQKD-FYYILHKPAGVISATQDN 78
Cdd:PRK10839 1 MRLDKFISQQ-LGvSRAIAGRELRANRVTVDGEIVKNGAFKLLP-EHDVAYDGNPLAQQHGpRYFMLNKPQGYVCSTDDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 79 HDQTVIDLLeDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDGD 158
Cdd:PRK10839 79 DHPTVLYFL-DEPVAYKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488214761 159 EQ-TLPAKLQIdqvdqeTETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLPKDLNKGQYRPMTKEELEQV 236
Cdd:PRK10839 158 KDlTKPAVLEV------ITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDADLAPGEYRPLTEEEIASV 230
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
99-229 |
1.18e-38 |
|
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: 130.53 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 99 VGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDgDEQTLPAKLQIdqVDQETETS 178
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLE-DGKTKPAKLKV--ITEPGFPT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488214761 179 IIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLNKGQYRPMT 229
Cdd:TIGR00093 78 WLRVTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSL-NGLPPGEWRPLT 127
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
62-195 |
1.42e-20 |
|
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: 84.76 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVISATQDN---HDQTVIDLLEDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQL--LSPKKHVEKEYLAE 136
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSltkLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLnkLFPERKIEKEYLAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488214761 137 VSGIMTEEDIR----LFAEGLIIDGDEQTLPAKLQIDQVDQ-----ETETSIIRLILHEGKFHQVKRM 195
Cdd:pfam00849 81 VDKPEEEEGTIkspiKKEKNKSPFRKEEELGGKKAVTHLKVlksgsKGDYSLLELELVTGRKHQIRAH 148
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
1-54 |
2.76e-05 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 40.65 E-value: 2.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488214761 1 MRLDKFLADMGLG-SRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEI 54
Cdd:smart00363 1 RRLDKFLARLGLApSRSQARRLIEQGRVKVNGKKVTKPSYIVKP-GDVISVRGKE 54
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsuA |
COG1187 |
Pseudouridylate synthase RsuA, specific for 16S rRNA U516 and 23S rRNA U2605 [Translation, ... |
1-229 |
3.00e-98 |
|
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: 285.77 E-value: 3.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADMGLGSRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEIIT-YQKDFYYILHKPAGVISATQDNH 79
Cdd:COG1187 3 MRLQKFLANAGVGSRREAEELIEAGRVTVNGKVVTELGTKVDP-GDEVTVDGKPLKlPEEPVYLLLNKPAGVVSTTKDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 80 D-QTVIDLLEDqDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDgD 158
Cdd:COG1187 82 GrPTVFDLLPE-ARKERLFPVGRLDKDTEGLLLLTNDGELAHRLTHPKYGVEKEYLVRVDGPVTEEDLERLREGVELE-D 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214761 159 EQTLPAKLQIDQVDQETEtsiIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLNKGQYRPMT 229
Cdd:COG1187 160 GPTKPAKVEILSGEANTW---LRITLTEGRNRQVRRMFEAVGLPVVRLKRVRIGPLTL-GDLPPGEWRELT 226
|
|
| PseudoU_synth_RsuA |
cd02553 |
Pseudouridine synthase, Escherichia coli RsuA like; This group is comprised of eukaryotic and ... |
61-233 |
9.62e-90 |
|
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: 262.07 E-value: 9.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 61 FYYILHKPAGVISATQDNHDQTVIDLLEDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGI 140
Cdd:cd02553 1 VYLMLNKPAGVVCATKDPHHPTVIDLLPEPDRRRDLFPVGRLDKDTTGLLLLTNDGQLAHRLTSPKKHVPKTYEVTLAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 141 MTEEDIRLFAEGLIIDGDEQTLPAKLQIdqvdqeTETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLPKDL 220
Cdd:cd02553 81 LTEDDIEAFAEGVLLHDGYPTKPAKLEI------LSPTTVRLTITEGKYHQVKRMFAAVGNKVVALHRIRIGGLELDDDL 154
|
170
....*....|...
gi 488214761 221 NKGQYRPMTKEEL 233
Cdd:cd02553 155 APGEWRPLTEEEL 167
|
|
| PseudoU_synth_RsuA_like |
cd02870 |
Pseudouridine synthases, RsuA subfamily; Pseudouridine synthases are responsible for the ... |
62-210 |
9.99e-57 |
|
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: 177.30 E-value: 9.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVISATQDNHD-QTVIDLLEDQDYRedLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGI 140
Cdd:cd02870 1 YLLLNKPRGVVSTVRDPEGrPTVLDLLKDVGER--LFPVGRLDYDTEGLLLLTNDGELANRLTHPRYGVEKTYLVKVRGV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 141 MTEEDIRLFAEGLIIDgDEQTLPAKlqIDQVDQETETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIR 210
Cdd:cd02870 79 PSEEELRRLRAGVELD-DGKTAPAK--VKVLSRDPKNTLLEVTLHEGRNRQVRRMFEAVGHPVLRLKRVR 145
|
|
| PRK10839 |
PRK10839 |
16S rRNA pseudouridine(516) synthase RsuA; |
1-236 |
5.16e-46 |
|
16S rRNA pseudouridine(516) synthase RsuA;
Pssm-ID: 236774 [Multi-domain] Cd Length: 232 Bit Score: 152.95 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADMgLG-SRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEIITYQKD-FYYILHKPAGVISATQDN 78
Cdd:PRK10839 1 MRLDKFISQQ-LGvSRAIAGRELRANRVTVDGEIVKNGAFKLLP-EHDVAYDGNPLAQQHGpRYFMLNKPQGYVCSTDDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 79 HDQTVIDLLeDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDGD 158
Cdd:PRK10839 79 DHPTVLYFL-DEPVAYKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488214761 159 EQ-TLPAKLQIdqvdqeTETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLPKDLNKGQYRPMTKEELEQV 236
Cdd:PRK10839 158 KDlTKPAVLEV------ITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGAITLDADLAPGEYRPLTEEEIASV 230
|
|
| PseudoU_synth_RluF |
cd02554 |
Pseudouridine synthase, Escherichia coli RluF like; This group is comprised of bacterial ... |
62-235 |
6.77e-39 |
|
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: 132.43 E-value: 6.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVISATQDNHDQTVIDLLedqDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIM 141
Cdd:cd02554 2 YIAYNKPVGIDCTLERADEDNIIDFV---NPPPRIFPIGRLDKDSEGLILLTNDGDLVNKILHADNNHEKEYLVTVNKPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 142 TEEDIRLFAEGLIIdGDEQTLPAKlqidqVDQETETSiIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLN 221
Cdd:cd02554 79 TDEFIEGMSNGVVI-LGTVTKPCK-----VERLAKDK-FRIVLTQGLNRQIRRMCEALGYRVTDLKRVRIMNIEL-GDLA 150
|
170
....*....|....
gi 488214761 222 KGQYRPMTKEELEQ 235
Cdd:cd02554 151 PGEWRPLTDAELFE 164
|
|
| TIGR00093 |
TIGR00093 |
pseudouridine synthase; This model identifies panels of pseudouridine synthase enzymes that ... |
99-229 |
1.18e-38 |
|
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: 130.53 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 99 VGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDgDEQTLPAKLQIdqVDQETETS 178
Cdd:TIGR00093 1 VGRLDRDSEGLLLLTNDGELVHRLTHPGHHHEKEYLVTVEGPVTDEDLEALRKGVQLE-DGKTKPAKLKV--ITEPGFPT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488214761 179 IIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLNKGQYRPMT 229
Cdd:TIGR00093 78 WLRVTLSEGRNRQVRRMFAAVGFPVLRLHRVRIGDVSL-NGLPPGEWRPLT 127
|
|
| PseudoU_synth_Rsu_Rlu_like |
cd02550 |
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ... |
62-211 |
3.10e-36 |
|
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: 125.18 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVISATQD-NHDQTVIDLLEDQDYrEDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGI 140
Cdd:cd02550 1 ILVLNKPSGLVCHPTDrDRDPTVVVRLDKLHG-PRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEKEYLVTVRGE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488214761 141 MTEEDIRLFAEGLIIDG----DEQTLPAKLQIDQVDQETETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRM 211
Cdd:cd02550 80 LDEEGIEDLATVRRGRLsglvDEGVPLAVTKVRVIGEHGGTGRLRLTLKTGRTHQIRRHCAAVGFPVLRLHRVRI 154
|
|
| PRK10475 |
PRK10475 |
23S rRNA pseudouridine(2604) synthase RluF; |
1-233 |
2.54e-32 |
|
23S rRNA pseudouridine(2604) synthase RluF;
Pssm-ID: 236698 [Multi-domain] Cd Length: 290 Bit Score: 119.07 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADMGLGSRKEVKGLIKKGTIEVNG-------QVVKSDKAQVNefedavtylGEIIT--YQKDFYYI-LHKPAG 70
Cdd:PRK10475 7 TRLNKYISESGICSRREADRYIEQGNVFINGkratigdQVKAGDVVKVN---------GQLIEprEAEDLVLIaLNKPVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 71 VISATQDNHDQTVIDLLedqDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFA 150
Cdd:PRK10475 78 IVSTTEDGERDNIVDFV---NHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITDEFIRGMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 151 EGLIIDGdeqTLPAKLQIDQVdqetETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLNKGQYRPMTK 230
Cdd:PRK10475 155 AGVPILG---TVTKKCKVKKE----APFVFRITLVQGLNRQIRRMCEHFGYEVTKLERTRIMNVSL-SGIPLGEWRDLTD 226
|
...
gi 488214761 231 EEL 233
Cdd:PRK10475 227 DEL 229
|
|
| PseudoU_synth_RluB |
cd02556 |
Pseudouridine synthase, Escherichia coli RluB like; This group is comprised of bacterial and ... |
64-230 |
1.23e-30 |
|
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: 111.25 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 64 ILHKPAGVISATQDNHDQ-TVIDLLEdQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMT 142
Cdd:cd02556 4 IYHKPEGLICTRKDPKGRpTVFDLLP-KLGIPRWISVGRLDLNTEGLLLFTNDGELANRLMHPSNEIEREYAVRVFGQVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 143 EEDIRLFAEGLIIDGdeqTLPAKLQIDQVDQETETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLPKDLNK 222
Cdd:cd02556 83 DEQLKSLKKGVELED---GFAGFKSIQLEGGEGKNSWYRVTLREGRNREVRRLWEAFGLQVSRLIRIRYGPIFLPGNLKR 159
|
....*...
gi 488214761 223 GQYRPMTK 230
Cdd:cd02556 160 GQWEELPP 167
|
|
| PseudoU_synth_RluE |
cd02566 |
Pseudouridine synthase, Escherichia coli RluE; This group is comprised of bacterial proteins ... |
62-216 |
1.16e-28 |
|
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: 106.31 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVISA-TQDNHDQ-TVIDLLEDQDyredLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSG 139
Cdd:cd02566 1 LILFNKPYGVLSQfTDESEKHkTLKDYIDDPG----VYAAGRLDRDSEGLLLLTDDGRLQHRITDPSFKHPKTYYVQVEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 140 IMTEEDIRLFAEGLIIdGDEQTLPAK-LQIDQVDQETE------------TSIIRLILHEGKFHQVKRMVKAVGKEVLYL 206
Cdd:cd02566 77 VPTEDALEQLRNGVEL-GDGLTLPAKvEKVDEPPWLWEreppirfrknipTSWIEITICEGKNRQVRRMTAAVGFPTLRL 155
|
170
....*....|
gi 488214761 207 KRIRMGKFWL 216
Cdd:cd02566 156 IRVSIGDIGL 165
|
|
| PSSA_1 |
cd02555 |
Pseudouridine synthase, a subgroup of the RsuA family; This group is comprised of bacterial ... |
63-232 |
2.34e-24 |
|
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: 95.17 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 63 YILHKPAGVIS---------ATQDNHDQTVIDLLEDQDYRedLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEY 133
Cdd:cd02555 7 LLLHKPAGMVSeqalallgpGQRSAADRSGRRPLKGHFAR--LAPIGPLDKDASGLLVFSQDGRVLRKLIGDASRLEQEY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 134 LAEVSGIMTEEDIRLFAEGLIIDGDEQTlPAKlqidqVDQETETSiIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGK 213
Cdd:cd02555 85 LVEVRGELTAGGLERLNHGLTYDGRELP-PAK-----VSWQNEQR-LRFALKEPQPGQIRRMCESVGLEVVALRRIRIGR 157
|
170
....*....|....*....
gi 488214761 214 FWLpKDLNKGQYRPMTKEE 232
Cdd:cd02555 158 VSL-GKLPLGQWRYLTTGE 175
|
|
| PRK10700 |
PRK10700 |
23S rRNA pseudouridine(2605) synthase RluB; |
2-238 |
3.47e-24 |
|
23S rRNA pseudouridine(2605) synthase RluB;
Pssm-ID: 182659 [Multi-domain] Cd Length: 289 Bit Score: 97.53 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 2 RLDKFLADMGLGSRKEVKGLIKKGTIEVNGQVVK-SDKAQVNEfEDAVTYLGEIITY---QKDFYYIL--HKPAGVISAT 75
Cdd:PRK10700 4 KLQKVLARAGHGSRREIESIIEAGRVSVDGKIATlGDRVEVTP-GLKIRIDGHLISVkesAEQICRVLayYKPEGELCTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 76 QDNHDQ-TVIDLLED-QDYRedLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGL 153
Cdd:PRK10700 83 NDPEGRpTVFDRLPKlRGAR--WIAVGRLDVNTCGLLLFTTDGELANRLMHPSREVEREYAVRVFGQVDDAKLRQLSRGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 154 II-DGdeqtlPAKLQ-IDQVDQETETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLPKDLNKGQYRPMTKE 231
Cdd:PRK10700 161 QLeDG-----PAAFKtIKFSGGEGINQWYNVTLTEGRNREVRRLWEAVGVQVSRLIRVRYGDIPLPKGLPRGGWTELDLA 235
|
....*..
gi 488214761 232 ELEQVRE 238
Cdd:PRK10700 236 QTNYLRE 242
|
|
| PseudoU_synth_2 |
pfam00849 |
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ... |
62-195 |
1.42e-20 |
|
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: 84.76 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVISATQDN---HDQTVIDLLEDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQL--LSPKKHVEKEYLAE 136
Cdd:pfam00849 1 YIVVNKPAGVPVHPTDSltkLLSLLALLLRRELGVKRLYPVHRLDKNTSGLLLLAKDGEAANKLnkLFPERKIEKEYLAL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488214761 137 VSGIMTEEDIR----LFAEGLIIDGDEQTLPAKLQIDQVDQ-----ETETSIIRLILHEGKFHQVKRM 195
Cdd:pfam00849 81 VDKPEEEEGTIkspiKKEKNKSPFRKEEELGGKKAVTHLKVlksgsKGDYSLLELELVTGRKHQIRAH 148
|
|
| PRK11394 |
PRK11394 |
23S rRNA pseudouridine(2457) synthase RluE; |
94-229 |
7.12e-19 |
|
23S rRNA pseudouridine(2457) synthase RluE;
Pssm-ID: 183115 Cd Length: 217 Bit Score: 81.71 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 94 EDLFPVGRLDKDTEGLLILTNDGVFAHQLLSPKKHVEKEYLAEVSGIMTEEDIRLFAEGLIIDgDEQTLPAKlqIDQVDQ 173
Cdd:PRK11394 70 QGVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLN-DGPTLPAG--AELVDE 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214761 174 ---------------ETETSIIRLILHEGKFHQVKRMVKAVGKEVLYLKRIRMGKFWLpKDLNKGQYRPMT 229
Cdd:PRK11394 147 pawlwprnppirerkSIPTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSL-DNLANGEWREAT 216
|
|
| PseudoU_synth_RluA_like |
cd02869 |
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ... |
62-191 |
3.45e-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: 65.82 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 62 YYILHKPAGVIS-ATQDNHDQTVIDLLEDQDYRED----LFPVGRLDKDTEGLLILTNDGvFAHQLLS---PKKHVEKEY 133
Cdd:cd02869 1 LLVVNKPAGLPVhPGPGHLTGTLVNALLKLLLLLGeefrPGLVHRLDKDTSGLLLVAKNK-KAAAKLSkqfKERKVKKTY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488214761 134 LAEVSGIMTEEDIRLFAE--------GLIIDGDEQTLPAKLQIDQVDQETETSIIRLILHEGKFHQ 191
Cdd:cd02869 80 LALVDGKPPEDEGTIDAPlgrkkrkkRARVVVSEDGKPAITHYKVLERFGNVTLVELQLETGRTHQ 145
|
|
| RluA |
COG0564 |
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ... |
57-191 |
1.65e-12 |
|
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: 64.39 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 57 YQKDFYYILHKPAGVIS-ATQDNHDQTVIDLLEDQDYR----EDLFPVGRLDKDTEGLLILT-NDgvFAHQLLSP---KK 127
Cdd:COG0564 3 YEDEDLLVVNKPAGLVVhPGSGGDDGTLVNALRAHLGElsgvPRPGLVHRLDRDTSGLLLVAkTR--KAARRLSEqfrER 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488214761 128 HVEKEYLAEVSGIMTEEDIRLFA----------EGLIIDGDEQtlPAKLQIDQVDQETETSIIRLILHEGKFHQ 191
Cdd:COG0564 81 EVEKRYLALVEGKPKEDEGTIDAplgrdpkdrkKMAVVDEDGK--PAVTHYRVLERFGGYSLVEVRLETGRTHQ 152
|
|
| rluA_subfam |
TIGR00005 |
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ... |
1-193 |
2.67e-12 |
|
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: 65.04 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADM-GLGSRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEI--------------ITYQKDFYYIL 65
Cdd:TIGR00005 6 QRLDDFLASLlPDLSRSRIQKLIENGQVKVNGKVTANPKLKVKD-GDRITVRVPEeeehevppqdipldILFEDEDIIVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 66 HKPAGVIS-ATQDNHDQTVIDLLEDQDYR----EDLFPVGRLDKDTEGLLIL--TNDG--VFAHQLlsPKKHVEKEYLAE 136
Cdd:TIGR00005 85 NKPSGLVVhPGGGNPFGTVLNALLAHCPPiagvERVGIVHRLDRDTSGLMVVakTPLAlrELQRQL--KNRTVTKEYVAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488214761 137 VSGIMTEED---------IRLFAEGLIIDGDEQTLPAKLQIDQVDQETETSIIRLILHEGKFHQVK 193
Cdd:TIGR00005 163 VHGQFDSGGgtvdaplgrVPNNRGLMAVHPSSEGKPAVTHFRVLERFGNASLVECELETGRTHQIR 228
|
|
| PseudoU_synth_ScRIB2 |
cd02557 |
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ... |
55-192 |
1.34e-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: 61.88 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 55 ITYQKDFYYILHKPAGV-ISATQDNHDQTVIDLLEDQDYREDLFPVGRLDKDTEGLLILTNDGVFAHQLLSP--KKHVEK 131
Cdd:cd02557 18 IVHEDDDLLVVDKPSGIpVHPTGRYRYNTVTEILKSEYGLTELRPCHRLDRLTSGLLLFAKTSQTASRLQQQirSREVKK 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214761 132 EYLAEVSGIMTEEDIRLFAE--------GLIIDGDEQTLPAKLQIDQV--DQETETSIIRLILHEGKFHQV 192
Cdd:cd02557 98 EYLARVKGEFPDGEVVVDQPiglvspkgGLRNDVDEKGKDARTIFKRLsyNGDLNTSVVLCKPITGRTHQI 168
|
|
| S4 |
cd00165 |
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ... |
1-66 |
2.32e-09 |
|
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: 52.25 E-value: 2.32e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488214761 1 MRLDKFLADMGL-GSRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEI----ITYQKDFYYILH 66
Cdd:cd00165 1 MRLDKILARLGLaPSRSEARQLIKHGHVLVNGKVVTKPSYKVKP-GDVIEVDGKSieedIVYEDKKLLVVN 70
|
|
| rluD |
PRK11180 |
23S rRNA pseudouridine(1911/1915/1917) synthase RluD; |
1-142 |
2.02e-07 |
|
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
Pssm-ID: 183020 [Multi-domain] Cd Length: 325 Bit Score: 50.83 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 1 MRLDKFLADMGLG-SRKEVKGLIKKGTIEVNGQVVKSDKAQV---------NEFEDAVTYLGEI----ITYQKDFYYILH 66
Cdd:PRK11180 18 QRLDQALAELFPDySRSRIKEWILDQRVLVNGKVINKPKEKVlggeqvaidAEIEEEARFEPQDipldIVYEDDDILVIN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 67 KPAG-VISATQDNHDQTVIDLLEDQDYREDLFP----VGRLDKDTEGLLILTNDGVFAHQLLSP--KKHVEKEYLAEVSG 139
Cdd:PRK11180 98 KPRDlVVHPGAGNPDGTVLNALLHYYPPIADVPragiVHRLDKDTTGLMVVAKTVPAQTRLVEAlqKREITREYEAVAIG 177
|
...
gi 488214761 140 IMT 142
Cdd:PRK11180 178 HMT 180
|
|
| S4 |
pfam01479 |
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ... |
1-36 |
6.46e-07 |
|
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: 44.79 E-value: 6.46e-07
10 20 30
....*....|....*....|....*....|....*..
gi 488214761 1 MRLDKFLADMGLG-SRKEVKGLIKKGTIEVNGQVVKS 36
Cdd:pfam01479 1 RRLDKVLARLGLAsSRSQARQLIEHGRVLVNGKVVKD 37
|
|
| PseudoU_synth_TruC |
cd02563 |
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ... |
55-146 |
1.59e-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: 47.33 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 55 ITYQKDFYYILHKPAG--VISATQDNH-DQTVIDLLEDQdYREDLFPVGRLDKDTEGLLILTNDGVFAHQL--LSPKKHV 129
Cdd:cd02563 3 ILYQDEHLVAINKPSGllVHRSELDRHeTRFALQTLRDQ-LGQHVYPVHRLDRPTSGVLLFALSSEVARKLgeQFTEHRV 81
|
90
....*....|....*..
gi 488214761 130 EKEYLAEVSGIMTEEDI 146
Cdd:cd02563 82 HKTYLAVVRGYVPESGT 98
|
|
| PRK11112 |
PRK11112 |
tRNA pseudouridine synthase C; Provisional |
53-146 |
5.70e-06 |
|
tRNA pseudouridine synthase C; Provisional
Pssm-ID: 182971 [Multi-domain] Cd Length: 257 Bit Score: 46.19 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214761 53 EIItYQKDFYYILHKPAG--VISATQDNHD-QTVIDLLEDQdYREDLFPVGRLDKDTEGLLILTNDGVFAHqLLSPK--- 126
Cdd:PRK11112 3 EIL-YQDEWLVAVNKPAGwlVHRSWLDRHEtVFVMQTVRDQ-IGQHVFTAHRLDRPTSGVLLMALSSEVAR-LLAQQfeq 79
|
90 100
....*....|....*....|
gi 488214761 127 KHVEKEYLAEVSGIMTEEDI 146
Cdd:PRK11112 80 HQIQKTYHAIVRGWLMEEAV 99
|
|
| S4 |
smart00363 |
S4 RNA-binding domain; |
1-54 |
2.76e-05 |
|
S4 RNA-binding domain;
Pssm-ID: 214638 [Multi-domain] Cd Length: 60 Bit Score: 40.65 E-value: 2.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488214761 1 MRLDKFLADMGLG-SRKEVKGLIKKGTIEVNGQVVKSDKAQVNEfEDAVTYLGEI 54
Cdd:smart00363 1 RRLDKFLARLGLApSRSQARRLIEQGRVKVNGKKVTKPSYIVKP-GDVISVRGKE 54
|
|
|