Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*
gi 564391062  1503 DLTRHMRSHTGERPYKCQTCERTFT 1527
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 564391062    29 SLDRHMLVHSGERPYKCTVCGQSFTT 54
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391062 1320 SSGDADAPEEDTASNQSLDLDFATKMMDFKLAESEA--GAVDSQGPAQQEPKHACNTCGKNFKFLSTLSRHRKA-HGCQE 1396
Cdd:cd23959   194 SPFATATDTAPSSGAPDGFPAEASAPSPFAAPASAAsfPAAPVANGEAATPTHACTICGKAFSTHEGLRMHSKAkHGVEL 273

                  ....
gi 564391062 1397 PKEE 1400
Cdd:cd23959   274 EKAK 277

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 564391062  1517 YKCQTCERTFTLKHSLVRHQRIH 1539
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 564391062    15 HSCSICGKSLSSASSLDRHMLVH 37
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*
gi 564391062  1503 DLTRHMRSHTGERPYKCQTCERTFT 1527
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 564391062    29 SLDRHMLVHSGERPYKCTVCGQSFTT 54
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391062 1320 SSGDADAPEEDTASNQSLDLDFATKMMDFKLAESEA--GAVDSQGPAQQEPKHACNTCGKNFKFLSTLSRHRKA-HGCQE 1396
Cdd:cd23959   194 SPFATATDTAPSSGAPDGFPAEASAPSPFAAPASAAsfPAAPVANGEAATPTHACTICGKAFSTHEGLRMHSKAkHGVEL 273

                  ....
gi 564391062 1397 PKEE 1400
Cdd:cd23959   274 EKAK 277

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 564391062  1517 YKCQTCERTFTLKHSLVRHQRIH 1539
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

zinc finger;

                            10        20
                    ....*....|....*....|...
gi 564391062     43 YKCTVCGQSFTTNGNMHRHMKIH 65
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23

transcriptional regulator ICP4; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391062 1008 KAADPGPSSTSSNAVATDSPGGSIPKASPSPTDIPSSREPTDPApTASSPEEASPPEQGPAASSRKRGRKRGMRNRPLPN 1087
Cdd:PHA03307  317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA-DPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVA 395

                          90
                  ....*....|..
gi 564391062 1088 SSAVDLDSSGEF 1099
Cdd:PHA03307  396 GRARRRDATGRF 407

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*
gi 564391062  1503 DLTRHMRSHTGERPYKCQTCERTFT 1527
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 564391062    29 SLDRHMLVHSGERPYKCTVCGQSFTT 54
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 564391062    43 YKCTVCGQSFTTNGNMHRHMKIH 65
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

C2H2-type zinc finger;

                           10        20
                   ....*....|....*....|..
gi 564391062  1490 VCSVCNKRFWSLQDLTRHMRSH 1511
Cdd:pfam13912    3 ECSECGKSFPSYQALGGHKKSH 24

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                           10        20
                   ....*....|....*....|...
gi 564391062   126 FHCPVCFKEFVCKYGLETHMETH 148
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 564391062    15 HSCSICGKSLSSASSLDRHMLVH 37
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                           10        20
                   ....*....|....*....|...
gi 564391062    43 YKCTVCGQSFTTNGNMHRHMKIH 65
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23