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Conserved domains on  [gi|1635381407|ref|NP_001357375|]
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nucleoporin NUP42 isoform 5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
19-150 9.33e-03

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23959:

Pssm-ID: 483960 [Multi-domain]  Cd Length: 424  Bit Score: 36.77  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381407  19 AFGFGSSQAATFMSPGF---PVNNSSSDNAQNFSFKTNSGFAAASSGSPAG-FGSSPAFGAAASTSSGISTSAPAFGFGK 94
Cdd:cd23959    98 AFAMAPDESLGPFRAARvpnPFSASSSTQRETHKTAQVAPPKAEPQTAPVTpFGQLPMFGQHPPPAKPLPAAAAAQQSSA 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1635381407  95 PEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAP-AFGGGSSVAGFGSP 150
Cdd:cd23959   178 SPGEVASPFASGTVSASPFATATDTAPSSGAPDGFPAEASAPsPFAAPASAASFPAA 234
 
Name Accession Description Interval E-value
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
19-150 9.33e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 36.77  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381407  19 AFGFGSSQAATFMSPGF---PVNNSSSDNAQNFSFKTNSGFAAASSGSPAG-FGSSPAFGAAASTSSGISTSAPAFGFGK 94
Cdd:cd23959    98 AFAMAPDESLGPFRAARvpnPFSASSSTQRETHKTAQVAPPKAEPQTAPVTpFGQLPMFGQHPPPAKPLPAAAAAQQSSA 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1635381407  95 PEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAP-AFGGGSSVAGFGSP 150
Cdd:cd23959   178 SPGEVASPFASGTVSASPFATATDTAPSSGAPDGFPAEASAPsPFAAPASAASFPAA 234
 
Name Accession Description Interval E-value
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
19-150 9.33e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 36.77  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635381407  19 AFGFGSSQAATFMSPGF---PVNNSSSDNAQNFSFKTNSGFAAASSGSPAG-FGSSPAFGAAASTSSGISTSAPAFGFGK 94
Cdd:cd23959    98 AFAMAPDESLGPFRAARvpnPFSASSSTQRETHKTAQVAPPKAEPQTAPVTpFGQLPMFGQHPPPAKPLPAAAAAQQSSA 177
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1635381407  95 PEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAP-AFGGGSSVAGFGSP 150
Cdd:cd23959   178 SPGEVASPFASGTVSASPFATATDTAPSSGAPDGFPAEASAPsPFAAPASAASFPAA 234
 
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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