Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 157822859   111 SLDRHMLVHSGERPYKCTVCGQSFTT 136
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 157822859 1348 SSGDADAPEEDTASNQSLDLDFATKMMDFKLAESEA--GAVDSQGPAQQEPKHACNTCGKNFKFLSTLSRHRKA-HGCQE 1424
Cdd:cd23959   194 SPFATATDTAPSSGAPDGFPAEASAPSPFAAPASAAsfPAAPVANGEAATPTHACTICGKAFSTHEGLRMHSKAkHGVEL 273

                  ....
gi 157822859 1425 PKEE 1428
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 157822859  1545 YKCQTCERTFTLKHSLVRHQRIH 1567
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 157822859    97 HSCSICGKSLSSASSLDRHMLVH 119
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

transcriptional regulator ICP4; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822859 1090 KAADPGPSSTSSNAVATDSPGGSIPKASPSPTDIPSSREPTDPApTASSPEEASPPEQGPAASSRKRGRKRGMRNRPLPN 1169
Cdd:PHA03307  317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA-DPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVA 395

                          90
                  ....*....|..
gi 157822859 1170 SSAVDLDSSGEF 1181
Cdd:PHA03307  396 GRARRRDATGRF 407

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 157822859   111 SLDRHMLVHSGERPYKCTVCGQSFTT 136
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 157822859 1348 SSGDADAPEEDTASNQSLDLDFATKMMDFKLAESEA--GAVDSQGPAQQEPKHACNTCGKNFKFLSTLSRHRKA-HGCQE 1424
Cdd:cd23959   194 SPFATATDTAPSSGAPDGFPAEASAPSPFAAPASAAsfPAAPVANGEAATPTHACTICGKAFSTHEGLRMHSKAkHGVEL 273

                  ....
gi 157822859 1425 PKEE 1428
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 157822859  1545 YKCQTCERTFTLKHSLVRHQRIH 1567
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

zinc finger;

                            10        20
                    ....*....|....*....|...
gi 157822859    125 YKCTVCGQSFTTNGNMHRHMKIH 147
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23

FOG: Zn-finger [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822859   64 SSYNCPLCEKVCTTQHQLTMHIRQHNTDTGGAD-HSC--SICGKSLSSASSLDRHMLVHSGERPYKC--TVCGQSFTTN- 137
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSVNHSGESLKpFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLl 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822859  138 -----GNMHRHMKIHEKDTNSTTAAAPPSPLKRRRLSSKRKLSHDAESEREdpgpakktvedgqssgldkmadetFHCPV 212
Cdd:COG5048   368 nneppQSLQQYKDLKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYN------------------------CKNPP 423

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 157822859  213 CFKEFVCKYGLETHMETHSD-NPLRCDICCVTFRT 246
Cdd:COG5048   424 CSKSFNRHYNLIPHKKIHTNhAPLLCSILKSFRRD 458

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 157822859    66 YNCPLCEKVCTTQHQLTMHIRQH 88
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                           10        20
                   ....*....|....*....|....*.
gi 157822859   111 SLDRHMLVHSGERPYKCTVCGQSFTT 136
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 157822859   125 YKCTVCGQSFTTNGNMHRHMKIH 147
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

C2H2-type zinc finger;

                           10        20
                   ....*....|....*....|..
gi 157822859  1518 VCSVCNKRFWSLQDLTRHMRSH 1539
Cdd:pfam13912    3 ECSECGKSFPSYQALGGHKKSH 24

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

                           10        20
                   ....*....|....*....|...
gi 157822859   208 FHCPVCFKEFVCKYGLETHMETH 230
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 157822859    97 HSCSICGKSLSSASSLDRHMLVH 119
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                           10        20
                   ....*....|....*....|...
gi 157822859   125 YKCTVCGQSFTTNGNMHRHMKIH 147
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 157822859    66 YNCPLCEKVCTTQHQLTMHIRQH 88
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

zinc finger;

                            10        20
                    ....*....|....*....|.
gi 157822859   1250 CPHCPRVFPWASSLQRHMLTH 1270
Cdd:smart00355    3 CPECGKVFKSKSALREHMRTH 23