hypothetical protein

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583142  175 LSDSQLEQLESPAYEMRTVDYAAVELKHYNLDEYNEANRLLDVEPSGSQAIYKCQYCPLAYASPQYLKTHVR---NSHVC 251
Cdd:PHA00733  23 VTLEELKRYHSLTPEQKRLIRAVVKTLIYNPQLLDESSYLYKLLTSKAVSPYVCPLCLMPFSSSVSLKQHIRyteHSKVC 102

                         90       100
                 ....*....|....*....|.
gi 24583142  252 KYCTTAFAKVRDLNEHIRQKH 272
Cdd:PHA00733 103 PVCGKEFRNTDSTLDHVCKKH 123

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.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 24583142 269 RQKHPHHQCVVCSNNFSTSSNLRAHLKKIHGVQLP 303
Cdd:cd23959 240 EAATPTHACTICGKAFSTHEGLRMHSKAKHGVELE 274

hypothetical protein

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583142  175 LSDSQLEQLESPAYEMRTVDYAAVELKHYNLDEYNEANRLLDVEPSGSQAIYKCQYCPLAYASPQYLKTHVR---NSHVC 251
Cdd:PHA00733  23 VTLEELKRYHSLTPEQKRLIRAVVKTLIYNPQLLDESSYLYKLLTSKAVSPYVCPLCLMPFSSSVSLKQHIRyteHSKVC 102

                         90       100
                 ....*....|....*....|.
gi 24583142  252 KYCTTAFAKVRDLNEHIRQKH 272
Cdd:PHA00733 103 PVCGKEFRNTDSTLDHVCKKH 123

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.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 24583142 269 RQKHPHHQCVVCSNNFSTSSNLRAHLKKIHGVQLP 303
Cdd:cd23959 240 EAATPTHACTICGKAFSTHEGLRMHSKAKHGVELE 274

hypothetical protein

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24583142  175 LSDSQLEQLESPAYEMRTVDYAAVELKHYNLDEYNEANRLLDVEPSGSQAIYKCQYCPLAYASPQYLKTHVR---NSHVC 251
Cdd:PHA00733  23 VTLEELKRYHSLTPEQKRLIRAVVKTLIYNPQLLDESSYLYKLLTSKAVSPYVCPLCLMPFSSSVSLKQHIRyteHSKVC 102

                         90       100
                 ....*....|....*....|.
gi 24583142  252 KYCTTAFAKVRDLNEHIRQKH 272
Cdd:PHA00733 103 PVCGKEFRNTDSTLDHVCKKH 123

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.

                        10        20        30
                ....*....|....*....|....*....|....*
gi 24583142 269 RQKHPHHQCVVCSNNFSTSSNLRAHLKKIHGVQLP 303
Cdd:cd23959 240 EAATPTHACTICGKAFSTHEGLRMHSKAKHGVELE 274

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24583142      6 LCRICFVDSASVDireHRSGGSSDQTVLQLIEAMFGwnIALNLTEELP-MICNDCLEDcLQQYAFFRKLTFANQQLLQ 82
Cdd:smart00868   1 VCRLCLSESENLV---SIFDESSEASLAEKIEECTG--IEIEPDDGLPkVICGDCLEK-LESFHKFRERCRESDELLR 72