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Conserved domains on  [gi|24585948|ref|NP_610201|]
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uncharacterized protein Dmel_CG7849 [Drosophila melanogaster]

Protein Classification

pseudouridine synthase family protein; rRNA pseudouridine synthase( domain architecture ID 10120731)

pseudouridine synthase family protein may catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines| rRNA pseudouridine synthase catalyzes the formation of pseudouridine at position 516 in 16S or position 2605 in 23S rRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
18-292 4.19e-114

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


:

Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 328.96  E-value: 4.19e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  18 GILNVYKPSGMKVKHVRNAILSNICKglnemeqrkprklqenisllgtgtaadhvlhnigeqtdlsdhllstgprYLPRD 97
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK-------------------------------------------------YFPED 31
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  98 LICTTVSSLGDHTSGVLLFGINRGAGQSSSIRKNRPVRVYHLIGHLGIATENNLPDSRVIMRSNHRHVSADRISSLAASM 177
Cdd:cd02868  32 KVLVGVHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVI 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948 178 QASHQRKMFELCGVDLQTQEAYELACRGLLRPADDSQPVVYGIKLIHFDRPHFTLELHAINETQEYLATLVHDMALDLRT 257
Cdd:cd02868 112 QSGHQQKAFELCSVDDQSQQAAELAARGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24585948 258 VAHCSQLRCVRHAHFDVTDSLLRHAWHLPGIIKNL 292
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
 
Name Accession Description Interval E-value
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
18-292 4.19e-114

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 328.96  E-value: 4.19e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  18 GILNVYKPSGMKVKHVRNAILSNICKglnemeqrkprklqenisllgtgtaadhvlhnigeqtdlsdhllstgprYLPRD 97
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK-------------------------------------------------YFPED 31
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  98 LICTTVSSLGDHTSGVLLFGINRGAGQSSSIRKNRPVRVYHLIGHLGIATENNLPDSRVIMRSNHRHVSADRISSLAASM 177
Cdd:cd02868  32 KVLVGVHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVI 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948 178 QASHQRKMFELCGVDLQTQEAYELACRGLLRPADDSQPVVYGIKLIHFDRPHFTLELHAINETQEYLATLVHDMALDLRT 257
Cdd:cd02868 112 QSGHQQKAFELCSVDDQSQQAAELAARGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24585948 258 VAHCSQLRCVRHAHFDVTDSLLRHAWHLPGIIKNL 292
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
truB PRK02193
tRNA pseudouridine synthase B; Provisional
196-276 9.30e-03

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 37.04  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  196 QEAYELACRGLLRPADDSQPVVYGIKLIHFDRPHFTLELHAINETQEYLATLVHDMALDLRTVAHCSQLRCVRHAHFDVT 275
Cdd:PRK02193 123 KRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTGAYMSDLERTKIGNLDKN 202

                 .
gi 24585948  276 D 276
Cdd:PRK02193 203 F 203
 
Name Accession Description Interval E-value
PseudoU_synth_hTruB2_like cd02868
Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine ...
18-292 4.19e-114

Pseudouridine synthase, humanTRUB2_like; This group consists of eukaryotic pseudouridine synthases similar to human TruB pseudouridine synthase homolog 2 (TRUB2). Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi).


Pssm-ID: 211345 [Multi-domain]  Cd Length: 226  Bit Score: 328.96  E-value: 4.19e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  18 GILNVYKPSGMKVKHVRNAILSNICKglnemeqrkprklqenisllgtgtaadhvlhnigeqtdlsdhllstgprYLPRD 97
Cdd:cd02868   1 GLFAVYKPPGVHWKHVRDTIESNLLK-------------------------------------------------YFPED 31
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  98 LICTTVSSLGDHTSGVLLFGINRGAGQSSSIRKNRPVRVYHLIGHLGIATENNLPDSRVIMRSNHRHVSADRISSLAASM 177
Cdd:cd02868  32 KVLVGVHRLDAFSSGVLVLGVNHGNKLLSHLYSNHPTRVYTIRGLLGKATENFFHTGRVIEKTTYDHITREKIERLLAVI 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948 178 QASHQRKMFELCGVDLQTQEAYELACRGLLRPADDSQPVVYGIKLIHFDRPHFTLELHAINETQEYLATLVHDMALDLRT 257
Cdd:cd02868 112 QSGHQQKAFELCSVDDQSQQAAELAARGLIRPADKSPPIIYGIRLLEFRPPEFTLEVQCINETQEYLRKLIHEIGLELRS 191
                       250       260       270
                ....*....|....*....|....*....|....*
gi 24585948 258 VAHCSQLRCVRHAHFDVTDSLLRHAWHLPGIIKNL 292
Cdd:cd02868 192 SAVCTQVRRTRDGPFTVDDALLRKQWNLQNIISNI 226
truB PRK02193
tRNA pseudouridine synthase B; Provisional
196-276 9.30e-03

tRNA pseudouridine synthase B; Provisional


Pssm-ID: 179381 [Multi-domain]  Cd Length: 279  Bit Score: 37.04  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585948  196 QEAYELACRGLLRPADDSQPVVYGIKLIHFDRPHFTLELHAINETQEYLATLVHDMALDLRTVAHCSQLRCVRHAHFDVT 275
Cdd:PRK02193 123 KRAYDLARQGKQIELKPIEIKISKIELLNFDEKLQNCVFMWVVSRGTYIRSLIHDLGKMLKTGAYMSDLERTKIGNLDKN 202

                 .
gi 24585948  276 D 276
Cdd:PRK02193 203 F 203
 
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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