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Conserved domains on  [gi|1543862901|gb|RTZ68427|]
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MAG: RluA family pseudouridine synthase [Tenericutes bacterium]

Protein Classification

RluA family pseudouridine synthase( domain architecture ID 11426207)

RluA family pseudouridine synthase catalyzes the isomerization of specific uridines in rRNA or tRNA to pseudouridines

CATH:  3.30.2350.10
EC:  5.4.99.-
Gene Ontology:  GO:0003723|GO:0001522|GO:0009982
PubMed:  17113994
SCOP:  4002679|4002691

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rluA_subfam super family cl31434
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
11-254 7.07e-46

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]


The actual alignment was detected with superfamily member TIGR00005:

Pssm-ID: 161659 [Multi-domain]  Cd Length: 299  Bit Score: 155.94  E-value: 7.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  11 EGRTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGVSSTgySTKNIFTKIKFNIIFEDKNI 90
Cdd:TIGR00005   4 AGQRLDDFLASLLPDLSRSRIQKLIENGQVKVNGKVTANPKLKVKDGDRITVRVPEEE--EHEVPPQDIPLDILFEDEDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  91 LVIDKPHGYPVHDAENSIDNQVLTYLKFMQKD---SFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKyssnfekvyEFKs 167
Cdd:TIGR00005  82 IVINKPSGLVVHPGGGNPFGTVLNALLAHCPPiagVERVGIVHRLDRDTSGLMVVAKTPLALRELQR---------QLK- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 168 dlNRSITTEYK---IGH-----------------NEAKKKEEVMEEGKVTKTEFIIVGKHKFA-----KLYTGRKHQIRV 222
Cdd:TIGR00005 152 --NRTVTKEYValvHGQfdsgggtvdaplgrvpnNRGLMAVHPSSEGKPAVTHFRVLERFGNAslvecELETGRTHQIRV 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1543862901 223 SLSKLGYPIYGDYKYGGK-----------KADRVYLHSAQLKF 254
Cdd:TIGR00005 230 HLQYLGHPLAGDPLYGNKpvpgnnlngllNFDRQALHAYELGF 272
 
Name Accession Description Interval E-value
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
11-254 7.07e-46

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: 155.94  E-value: 7.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  11 EGRTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGVSSTgySTKNIFTKIKFNIIFEDKNI 90
Cdd:TIGR00005   4 AGQRLDDFLASLLPDLSRSRIQKLIENGQVKVNGKVTANPKLKVKDGDRITVRVPEEE--EHEVPPQDIPLDILFEDEDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  91 LVIDKPHGYPVHDAENSIDNQVLTYLKFMQKD---SFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKyssnfekvyEFKs 167
Cdd:TIGR00005  82 IVINKPSGLVVHPGGGNPFGTVLNALLAHCPPiagVERVGIVHRLDRDTSGLMVVAKTPLALRELQR---------QLK- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 168 dlNRSITTEYK---IGH-----------------NEAKKKEEVMEEGKVTKTEFIIVGKHKFA-----KLYTGRKHQIRV 222
Cdd:TIGR00005 152 --NRTVTKEYValvHGQfdsgggtvdaplgrvpnNRGLMAVHPSSEGKPAVTHFRVLERFGNAslvecELETGRTHQIRV 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1543862901 223 SLSKLGYPIYGDYKYGGK-----------KADRVYLHSAQLKF 254
Cdd:TIGR00005 230 HLQYLGHPLAGDPLYGNKpvpgnnlngllNFDRQALHAYELGF 272
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
83-255 3.22e-39

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: 136.03  E-value: 3.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  83 IIFEDKNILVIDKPHGYPVHDAENSIDNQVLTYLKFMQKDSFKPSHIG---RLDKVTSGLMVYGKTYEAVKELNK--YSS 157
Cdd:COG0564     1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRAHLGELSGVPRPGlvhRLDRDTSGLLLVAKTRKAARRLSEqfRER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 158 NFEKVY------EFKSDlnrSITTEYKIGHNEAKKKEEVM--EEGKVTKTEFIIVGKHKFA-----KLYTGRKHQIRVSL 224
Cdd:COG0564    81 EVEKRYlalvegKPKED---EGTIDAPLGRDPKDRKKMAVvdEDGKPAVTHYRVLERFGGYslvevRLETGRTHQIRVHL 157
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1543862901 225 SKLGYPIYGDYKYGGKK------ADRVYLHSAQLKFQ 255
Cdd:COG0564   158 AHIGHPIVGDPLYGGDRsnrllgLDRQALHAYRLGFP 194
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
90-254 4.79e-38

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: 132.08  E-value: 4.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  90 ILVIDKPHGYPVHDAENSIDNQVLTYLKF---MQKDSFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKYSSN--FEKVY- 163
Cdd:cd02869     1 LLVVNKPAGLPVHPGPGHLTGTLVNALLKlllLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKErkVKKTYl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 164 -----EFKSDlNRSITTEYKIGHNEAKKKEEVMEEGKVTKTEFIIVGKHKF-----AKLYTGRKHQIRVSLSKLGYPIYG 233
Cdd:cd02869    81 alvdgKPPED-EGTIDAPLGRKKRKKRARVVVSEDGKPAITHYKVLERFGNvtlveLQLETGRTHQIRVHLASIGHPIVG 159
                         170       180
                  ....*....|....*....|....*.
gi 1543862901 234 DYKYGGKKAD-----RVYLHSAQLKF 254
Cdd:cd02869   160 DPKYGGKASDspglkRLALHAYRLSF 185
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
5-254 8.17e-22

23S rRNA pseudouridine(1911/1915/1917) synthase RluD;


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 92.82  E-value: 8.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901   5 NATLNDE--GRTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGV--SSTGYSTKNIftkiK 80
Cdd:PRK11180    8 TATVSESqlGQRLDQALAELFPDYSRSRIKEWILDQRVLVNGKVINKPKEKVLGGEQVAIDAEieEEARFEPQDI----P 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  81 FNIIFEDKNILVIDKPHGYPVHDAENSIDNQVLTYLKFMQKDSFKPSHIG---RLDKVTSGLMVYGKTYEA----VKELN 153
Cdd:PRK11180   84 LDIVYEDDDILVINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADVPRAGivhRLDKDTTGLMVVAKTVPAqtrlVEALQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 154 KyssnfekvyefksdlnRSITTEYK---IGHNEAKKKEE--------------VMEEGKVTKTEFIIVGKHKF-----AK 211
Cdd:PRK11180  164 K----------------REITREYEavaIGHMTAGGTVDepisrhptkrthmaVHPMGKPAVTHYRIMEHFRVhtrlrLR 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1543862901 212 LYTGRKHQIRVSLSKLGYPIYGDYKYGG-----KKA-----------DRVYLHSAQLKF 254
Cdd:PRK11180  228 LETGRTHQIRVHMAHITHPLVGDQVYGGrprppKGAseefistlrkfDRQALHATMLRL 286
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
90-226 2.58e-17

RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.


Pssm-ID: 459961 [Multi-domain]  Cd Length: 151  Bit Score: 76.68  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  90 ILVIDKPHGYPVHDAENSIDNQVLTYLKFMQKD-SFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKYSSN--FEKVYEFK 166
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDSLTKLLSLLALLLRRELgVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPErkIEKEYLAL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543862901 167 SDLNRS----ITTEYKIGHNEAKKKEEVMEEGKVTKTEFIIVGKHKFAK-------LYTGRKHQIRVSLSK 226
Cdd:pfam00849  81 VDKPEEeegtIKSPIKKEKNKSPFRKEEELGGKKAVTHLKVLKSGSKGDyslleleLVTGRKHQIRAHLAA 151
S4 smart00363
S4 RNA-binding domain;
15-66 1.61e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 36.03  E-value: 1.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1543862901   15 LFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGVS 66
Cdd:smart00363   3 LDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKE 54
 
Name Accession Description Interval E-value
rluA_subfam TIGR00005
pseudouridine synthase, RluA family; In E. coli, RluD (SfhB) modifies uridine to pseudouridine ...
11-254 7.07e-46

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: 155.94  E-value: 7.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  11 EGRTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGVSSTgySTKNIFTKIKFNIIFEDKNI 90
Cdd:TIGR00005   4 AGQRLDDFLASLLPDLSRSRIQKLIENGQVKVNGKVTANPKLKVKDGDRITVRVPEEE--EHEVPPQDIPLDILFEDEDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  91 LVIDKPHGYPVHDAENSIDNQVLTYLKFMQKD---SFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKyssnfekvyEFKs 167
Cdd:TIGR00005  82 IVINKPSGLVVHPGGGNPFGTVLNALLAHCPPiagVERVGIVHRLDRDTSGLMVVAKTPLALRELQR---------QLK- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 168 dlNRSITTEYK---IGH-----------------NEAKKKEEVMEEGKVTKTEFIIVGKHKFA-----KLYTGRKHQIRV 222
Cdd:TIGR00005 152 --NRTVTKEYValvHGQfdsgggtvdaplgrvpnNRGLMAVHPSSEGKPAVTHFRVLERFGNAslvecELETGRTHQIRV 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1543862901 223 SLSKLGYPIYGDYKYGGK-----------KADRVYLHSAQLKF 254
Cdd:TIGR00005 230 HLQYLGHPLAGDPLYGNKpvpgnnlngllNFDRQALHAYELGF 272
RluA COG0564
Pseudouridine synthase RluA, 23S rRNA- or tRNA-specific [Translation, ribosomal structure and ...
83-255 3.22e-39

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: 136.03  E-value: 3.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  83 IIFEDKNILVIDKPHGYPVHDAENSIDNQVLTYLKFMQKDSFKPSHIG---RLDKVTSGLMVYGKTYEAVKELNK--YSS 157
Cdd:COG0564     1 ILYEDEDLLVVNKPAGLVVHPGSGGDDGTLVNALRAHLGELSGVPRPGlvhRLDRDTSGLLLVAKTRKAARRLSEqfRER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 158 NFEKVY------EFKSDlnrSITTEYKIGHNEAKKKEEVM--EEGKVTKTEFIIVGKHKFA-----KLYTGRKHQIRVSL 224
Cdd:COG0564    81 EVEKRYlalvegKPKED---EGTIDAPLGRDPKDRKKMAVvdEDGKPAVTHYRVLERFGGYslvevRLETGRTHQIRVHL 157
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1543862901 225 SKLGYPIYGDYKYGGKK------ADRVYLHSAQLKFQ 255
Cdd:COG0564   158 AHIGHPIVGDPLYGGDRsnrllgLDRQALHAYRLGFP 194
PseudoU_synth_RluA_like cd02869
Pseudouridine synthase, RluA family; This group is comprised of eukaryotic, bacterial and ...
90-254 4.79e-38

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: 132.08  E-value: 4.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  90 ILVIDKPHGYPVHDAENSIDNQVLTYLKF---MQKDSFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKYSSN--FEKVY- 163
Cdd:cd02869     1 LLVVNKPAGLPVHPGPGHLTGTLVNALLKlllLLGEEFRPGLVHRLDKDTSGLLLVAKNKKAAAKLSKQFKErkVKKTYl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 164 -----EFKSDlNRSITTEYKIGHNEAKKKEEVMEEGKVTKTEFIIVGKHKF-----AKLYTGRKHQIRVSLSKLGYPIYG 233
Cdd:cd02869    81 alvdgKPPED-EGTIDAPLGRKKRKKRARVVVSEDGKPAITHYKVLERFGNvtlveLQLETGRTHQIRVHLASIGHPIVG 159
                         170       180
                  ....*....|....*....|....*.
gi 1543862901 234 DYKYGGKKAD-----RVYLHSAQLKF 254
Cdd:cd02869   160 DPKYGGKASDspglkRLALHAYRLSF 185
PseudoU_synth_ScRIB2 cd02557
Pseudouridine synthases similar to Saccharomyces cerevisiae RIB2; Pseudouridine synthase, ...
80-262 1.85e-24

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: 97.32  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  80 KFNIIFEDKNILVIDKPHGYPVHDAENSIDNQVLTYLKfMQKDSFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKY--SS 157
Cdd:cd02557    15 PIKIVHEDDDLLVVDKPSGIPVHPTGRYRYNTVTEILK-SEYGLTELRPCHRLDRLTSGLLLFAKTSQTASRLQQQirSR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 158 NFEKVY------EFKSDlnrSITTEYKIGHNEAKKKEE--VMEEGKVTKTEF--IIVGKHK-----FAKLYTGRKHQIRV 222
Cdd:cd02557    94 EVKKEYlarvkgEFPDG---EVVVDQPIGLVSPKGGLRndVDEKGKDARTIFkrLSYNGDLntsvvLCKPITGRTHQIRV 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1543862901 223 SLSKLGYPIYGDYKYGgkkADRVYLHSaqLKFQGIKGKLE 262
Cdd:cd02557   171 HLQYLGHPIVNDPIYN---NLGIYLHA--LRYEGPDWSYE 205
rluD PRK11180
23S rRNA pseudouridine(1911/1915/1917) synthase RluD;
5-254 8.17e-22

23S rRNA pseudouridine(1911/1915/1917) synthase RluD;


Pssm-ID: 183020 [Multi-domain]  Cd Length: 325  Bit Score: 92.82  E-value: 8.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901   5 NATLNDE--GRTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGV--SSTGYSTKNIftkiK 80
Cdd:PRK11180    8 TATVSESqlGQRLDQALAELFPDYSRSRIKEWILDQRVLVNGKVINKPKEKVLGGEQVAIDAEieEEARFEPQDI----P 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  81 FNIIFEDKNILVIDKPHGYPVHDAENSIDNQVLTYLKFMQKDSFKPSHIG---RLDKVTSGLMVYGKTYEA----VKELN 153
Cdd:PRK11180   84 LDIVYEDDDILVINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADVPRAGivhRLDKDTTGLMVVAKTVPAqtrlVEALQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 154 KyssnfekvyefksdlnRSITTEYK---IGHNEAKKKEE--------------VMEEGKVTKTEFIIVGKHKF-----AK 211
Cdd:PRK11180  164 K----------------REITREYEavaIGHMTAGGTVDepisrhptkrthmaVHPMGKPAVTHYRIMEHFRVhtrlrLR 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1543862901 212 LYTGRKHQIRVSLSKLGYPIYGDYKYGG-----KKA-----------DRVYLHSAQLKF 254
Cdd:PRK11180  228 LETGRTHQIRVHMAHITHPLVGDQVYGGrprppKGAseefistlrkfDRQALHATMLRL 286
PRK11025 PRK11025
23S rRNA pseudouridine(955/2504/2580) synthase RluC;
1-255 4.41e-20

23S rRNA pseudouridine(955/2504/2580) synthase RluC;


Pssm-ID: 182909 [Multi-domain]  Cd Length: 317  Bit Score: 87.86  E-value: 4.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901   1 MKVFNATL------NDE-GRTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKrYIVKHGDEIVVYGVSSTGYSTK 73
Cdd:PRK11025    1 MKTETPSVkivtisADEaGQRIDNFLRTQLKGVPKSMIYRILRKGEVRVNKKRIKPE-YKLEAGDEVRIPPVRVAEREEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  74 NIFTKI------KFNIIFEDKNILVIDKPHGYPVHDAeNSIDNQVLTYLKFMQKDSFKPSHIGRLDKVTSGLMVYGKTYE 147
Cdd:PRK11025   80 AVSPKLqkvaalADVILYEDDHILVLNKPSGTAVHGG-SGLSFGVIEGLRALRPEARFLELVHRLDRDTSGVLLVAKKRS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 148 AVKELNKY--SSNFEKVY------EFKSDLNrsiTTEYKIGHNEAKKKE---EVMEEGKVTKTEFIIVGKHKFAKL---- 212
Cdd:PRK11025  159 ALRSLHEQlrEKGMQKDYlalvrgQWQSHVK---VVQAPLLKNILQSGErivRVSQEGKPSETRFKVEERYAFATLvras 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1543862901 213 -YTGRKHQIRVSLSKLGYPIYGDYKYGGKKAD---------RVYLHSAQLKFQ 255
Cdd:PRK11025  236 pVTGRTHQIRVHTQYAGHPIAFDDRYGDREFDqqltgtglnRLFLHAAALKFT 288
PseudoU_synth_2 pfam00849
RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA ...
90-226 2.58e-17

RNA pseudouridylate synthase; Members of this family are involved in modifying bases in RNA molecules. They carry out the conversion of uracil bases to pseudouridine. This family includes RluD, a pseudouridylate synthase that converts specific uracils to pseudouridine in 23S rRNA. RluA from E. coli converts bases in both rRNA and tRNA.


Pssm-ID: 459961 [Multi-domain]  Cd Length: 151  Bit Score: 76.68  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  90 ILVIDKPHGYPVHDAENSIDNQVLTYLKFMQKD-SFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKYSSN--FEKVYEFK 166
Cdd:pfam00849   1 YIVVNKPAGVPVHPTDSLTKLLSLLALLLRRELgVKRLYPVHRLDKNTSGLLLLAKDGEAANKLNKLFPErkIEKEYLAL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543862901 167 SDLNRS----ITTEYKIGHNEAKKKEEVMEEGKVTKTEFIIVGKHKFAK-------LYTGRKHQIRVSLSK 226
Cdd:pfam00849  81 VDKPEEeegtIKSPIKKEKNKSPFRKEEELGGKKAVTHLKVLKSGSKGDyslleleLVTGRKHQIRAHLAA 151
PseudoU_synth_Rsu_Rlu_like cd02550
Pseudouridine synthase, Rsu/Rlu family; This group is comprised of eukaryotic, bacterial and ...
90-231 1.24e-16

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: 75.10  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  90 ILVIDKPHGYPVHDAENSIDNQVLTYLKfmQKDSFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKYSSNFEKVYEFKSdl 169
Cdd:cd02550     1 ILVLNKPSGLVCHPTDRDRDPTVVVRLD--KLHGPRVHAAGRLDKDTSGLLLLTNDGRLQRRLTEPRREIEKEYLVTV-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543862901 170 nRSITTEYKIG----HNEAKKKEEVMEEGKVTKTEFIIVGKHKFAKLY-----TGRKHQIRVSLSKLGYPI 231
Cdd:cd02550    77 -RGELDEEGIEdlatVRRGRLSGLVDEGVPLAVTKVRVIGEHGGTGRLrltlkTGRTHQIRRHCAAVGFPV 146
PseudoU_synth_TruC cd02563
tRNA pseudouridine isomerase C; Pseudouridine synthases catalyze the isomerization of specific ...
83-254 2.45e-13

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: 67.36  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  83 IIFEDKNILVIDKPHGYPVHDAENSIDNQV--LTYLKFMQKDSFKPSHigRLDKVTSGLMVYGKTYEAVKELNKYSSN-- 158
Cdd:cd02563     3 ILYQDEHLVAINKPSGLLVHRSELDRHETRfaLQTLRDQLGQHVYPVH--RLDRPTSGVLLFALSSEVARKLGEQFTEhr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 159 FEKVY------------EFKSDLNRSITTEYKIGHNEAKKKEEVMEEGKVTKTEF--IIVGKHKFAKlY--------TGR 216
Cdd:cd02563    81 VHKTYlavvrgyvpesgTIDYPLSEELDKLADKFASDDKAPQAATTHYRLLAVEElpVVVGKYPTSR-YslveltphTGR 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1543862901 217 KHQIRVSLSKLGYPIYGDYKYGGKKADRVY----------LHSAQLKF 254
Cdd:cd02563   160 KHQLRRHLAHIRHPIIGDTTHGDGRHNRFFrehfgchrllLAATRLEF 207
PSRA_1 cd02558
Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial ...
83-237 7.80e-13

Pseudouridine synthase, a subgroup of the RluA family; This group is comprised of bacterial proteins assigned to the RluA 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 RluA family is comprised of proteins related to Escherichia coli RluA.


Pssm-ID: 211332 [Multi-domain]  Cd Length: 246  Bit Score: 66.53  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  83 IIFEDKNILVIDKPHGYPVHDAENSIDNQVLTYLKF-MQKDSFKPSHigRLDKVTSGLMVYGKTYEavkELNKYSSNFE- 160
Cdd:cd02558    41 ILHQDEHLLVADKPHFLPVTPRGRYVTETLLVRLRRqTGNPDLTPAH--RLDRLTAGLVLFSKRPE---TRGAYQTLFAr 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 161 ----KVYE----FKSDLNRSITTEYKIGhneakkKEE-----VMEEGKV-TKTEFIIVGKHKFAKLY-----TGRKHQIR 221
Cdd:cd02558   116 revsKTYEavapYVPALTFPLTVRSRIV------KGRgffqaREVEGEPnAETRIELLARRGGWGLYrlsphTGKTHQLR 189
                         170
                  ....*....|....*.
gi 1543862901 222 VSLSKLGYPIYGDYKY 237
Cdd:cd02558   190 VHMAALGVPILNDPFY 205
PRK10158 PRK10158
bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;
83-252 7.30e-12

bifunctional tRNA pseudouridine(32) synthase/23S rRNA pseudouridine(746) synthase RluA;


Pssm-ID: 236659 [Multi-domain]  Cd Length: 219  Bit Score: 63.47  E-value: 7.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  83 IIFEDKNILVIDKPHGY---PVHDAENSidNQVLTYLkfmQKDSFKPSHIGRLDKVTSGLMVYGKTYEAVKELNKyssnf 159
Cdd:PRK10158   16 ILYQDEHIMVVNKPSGLlsvPGRLEEHK--DSVMTRI---QRDYPQAESVHRLDMATSGVIVVALTKAAERELKR----- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 160 ekvyEFKSDLNRSITTEYKIGHNEAKK---------------KEEV-MEEGKVTKTEFIIVgkhKFA---------KLYT 214
Cdd:PRK10158   86 ----QFREREPKKQYVARVWGHPSPAEglvdlplicdwpnrpKQKVcYETGKPAQTEYEVV---EYAadntarvvlKPIT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1543862901 215 GRKHQIRVSLSKLGYPIYGDYKYGGKK----ADRVYLHSAQL 252
Cdd:PRK10158  159 GRSHQLRVHMLALGHPILGDRFYASPEaramAPRLLLHAEML 200
PRK11112 PRK11112
tRNA pseudouridine synthase C; Provisional
83-254 3.01e-07

tRNA pseudouridine synthase C; Provisional


Pssm-ID: 182971 [Multi-domain]  Cd Length: 257  Bit Score: 50.43  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901  83 IIFEDKNILVIDKPHGYPVHDAENSIDNQVLTylkfMQ--KDSFK----PSHigRLDKVTSGLMVYGKTYEAVKELnkyS 156
Cdd:PRK11112    4 ILYQDEWLVAVNKPAGWLVHRSWLDRHETVFV----MQtvRDQIGqhvfTAH--RLDRPTSGVLLMALSSEVARLL---A 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543862901 157 SNFE-----KVY--------EFKSDLNRSITTEY-KIGHNEAKKKEE----VMEEGKVTKTEF-IIVGKHKFAKlY---- 213
Cdd:PRK11112   75 QQFEqhqiqKTYhaivrgwlMEEAVLDYPLKEELdKIADKFAREDKApqpaVTHYRGLATVEMpVATGRYPTTR-Yslve 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1543862901 214 ----TGRKHQIRVSLSKLGYPIYGDYKYGGKK----------ADRVYLHSAQLKF 254
Cdd:PRK11112  154 lepkTGRKHQLRRHMAHLRHPIIGDTKHGDLRqnrslaehfgCSRLMLHASELSL 208
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
15-93 5.34e-06

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 43.39  E-value: 5.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543862901  15 LFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGVSstgystkniftkIKFNIIFEDKNILVI 93
Cdd:cd00165     3 LDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIEVDGKS------------IEEDIVYEDKKLLVV 69
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
13-60 1.96e-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: 38.24  E-value: 1.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1543862901  13 RTLFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEI 60
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKPGDEI 48
S4 smart00363
S4 RNA-binding domain;
15-66 1.61e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 36.03  E-value: 1.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1543862901   15 LFKFLVKSFPDVPKGKLESVFRKKDVKVNGKRLKDKRYIVKHGDEIVVYGVS 66
Cdd:smart00363   3 LDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKE 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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