Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 133922567  169 LSQHRRTHSGEKPYRCPDCGKSFSH 193
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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 133922567  322 YRCPHCGKAFGQSSNLQHHLRIH 344
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 133922567  336 NLQHHLRIHTGERPYACPHCSKAF 359
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 133922567  225 LLKHRSSHSGEKPHHCPVCGKAF 247
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

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 133922567  378 YRCQLCGKAFGQASSLTKHKRVH 400
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 133922567  364 ALLQHLHVHSGERPYRCQLCGKAF 387
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 133922567  169 LSQHRRTHSGEKPYRCPDCGKSFSH 193
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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 133922567  322 YRCPHCGKAFGQSSNLQHHLRIH 344
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 133922567  336 NLQHHLRIHTGERPYACPHCSKAF 359
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567  72 PRSILGKPDLDSQDLDPMSSSFDLDPDPDVIGPVPLVLDPSNDTPSPAAPDVDSLPSGLTATPEILATSPAVLPAPASPP 151
Cdd:COG5048  204 PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSE 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567 152 R----PFSCPDCGRAFRRSSGLSQHRRT--HSGE--KPYRCP--DCGKSFSHGATLAQHRGIHTGARPYQCaacgkafgw 221
Cdd:COG5048  284 KgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKE--------- 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567 222 rstLLKHRSSHSGEKPHHCPvcgkafgHGSLLAQHLRTHGgpRPHKCPV--CAKGFGQGSALLKHLRTHTGERP--YPCP 297
Cdd:COG5048  355 ---KLLNSSSKFSPLLNNEP-------PQSLQQYKDLKND--KKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 133922567 298 QCGKAFGQSSALLQHQRTHTAERPYrCPHCGKAFGQSSNLQHHLR 342
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPL-LCSILKSFRRDLDLSNHGK 466

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 133922567  225 LLKHRSSHSGEKPHHCPVCGKAF 247
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

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 133922567  378 YRCQLCGKAFGQASSLTKHKRVH 400
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 133922567  364 ALLQHLHVHSGERPYRCQLCGKAF 387
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 133922567   322 YRCPHCGKAFGQSSNLQHHLRIH 344
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

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 133922567 111 PSNDTPSPAAPDVDSLPSGLTATPEI-LATSPAVLPAPASPPRPFSCPdcgrAFRRSSGLSQHRRTHSGEKPYRCPDCGK 189
Cdd:cd23959  178 SPGEVASPFASGTVSASPFATATDTApSSGAPDGFPAEASAPSPFAAP----ASAASFPAAPVANGEAATPTHACTICGK 253

                         90
                 ....*....|..
gi 133922567 190 SFSHGATLAQHR 201
Cdd:cd23959  254 AFSTHEGLRMHS 265

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 133922567  197 LAQHRGIHTGARPYQCAACGKAF 219
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 133922567  169 LSQHRRTHSGEKPYRCPDCGKSFSH 193
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 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 133922567  322 YRCPHCGKAFGQSSNLQHHLRIH 344
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 133922567  336 NLQHHLRIHTGERPYACPHCSKAF 359
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567  72 PRSILGKPDLDSQDLDPMSSSFDLDPDPDVIGPVPLVLDPSNDTPSPAAPDVDSLPSGLTATPEILATSPAVLPAPASPP 151
Cdd:COG5048  204 PLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSE 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567 152 R----PFSCPDCGRAFRRSSGLSQHRRT--HSGE--KPYRCP--DCGKSFSHGATLAQHRGIHTGARPYQCaacgkafgw 221
Cdd:COG5048  284 KgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKE--------- 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567 222 rstLLKHRSSHSGEKPHHCPvcgkafgHGSLLAQHLRTHGgpRPHKCPV--CAKGFGQGSALLKHLRTHTGERP--YPCP 297
Cdd:COG5048  355 ---KLLNSSSKFSPLLNNEP-------PQSLQQYKDLKND--KKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNP 422

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 133922567 298 QCGKAFGQSSALLQHQRTHTAERPYrCPHCGKAFGQSSNLQHHLR 342
Cdd:COG5048  423 PCSKSFNRHYNLIPHKKIHTNHAPL-LCSILKSFRRDLDLSNHGK 466

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 133922567  225 LLKHRSSHSGEKPHHCPVCGKAF 247
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

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 133922567  294 YPCPQCGKAFGQSSALLQHQRTH 316
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 133922567  378 YRCQLCGKAFGQASSLTKHKRVH 400
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922567 319 ERPYRCP--HCGKAFGQSSNLQHHlRIHTgerpyacpHCSKAFGQSSALLQHLHVHSGERPYRCQLCGKAFGQASSLTKH 396
Cdd:COG5189  347 GKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417

                 .
gi 133922567 397 K 397
Cdd:COG5189  418 R 418

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 133922567 292 RPYpCPQCGKAFGQSSALLQHQRTHTaerpYRCPHCGKAFGQSSNLQHH-LRIH 344
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49

hypothetical protein

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 133922567 321 PYRCPHCGKAFGQSSNLQHHLRIhtGERPYACPHCSKAFGQSSALLQHL 369
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRY--TEHSKVCPVCGKEFRNTDSTLDHV 119

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 133922567 111 PSNDTPSPAAPDVDSLPSGLTATPEI-LATSPAVLPAPASPPRPFSCPdcgrAFRRSSGLSQHRRTHSGEKPYRCPDCGK 189
Cdd:cd23959  178 SPGEVASPFASGTVSASPFATATDTApSSGAPDGFPAEASAPSPFAAP----ASAASFPAAPVANGEAATPTHACTICGK 253

                         90
                 ....*....|..
gi 133922567 190 SFSHGATLAQHR 201
Cdd:cd23959  254 AFSTHEGLRMHS 265

C2H2-type zinc-finger domain;

                          10        20
                  ....*....|....*....|....*
gi 133922567  322 YRCPHCGKAFGQSSNLQHHLRIHTG 346
Cdd:pfam13909   1 YKCSQCDYSTAWKSNLKRHLRKHTG 25

Transposase InsA [Mobilome: prophages, transposons];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 133922567 151 PRPFSCPDCGrafrrSSGLSQHRRTHSGEKPYRCPDCGKSFS 192
Cdd:COG3677   14 PNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFT 50

AIDA-I family autotransporter YfaL;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 133922567  496 SSDPKPGHVADPDVVPSPDQESDPSPNPDlvpsPDPKPKSQ 536
Cdd:PRK09752  915 SQEVTPPSPPDPDPTPDPDPTPDPDPTPD----PEPTPAYQ 951

AIDA-I family autotransporter YfaL;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 133922567  492 DLVLSSDPKPGHVADPDVVPSPDQESDPSPNPDLVPSPDPKPKSQTDP 539
Cdd:PRK09752  901 DYTLVEDNNDWYLRSQEVTPPSPPDPDPTPDPDPTPDPDPTPDPEPTP 948

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 133922567   378 YRCQLCGKAFGQASSLTKHKRVH 400
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 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 133922567  182 YRCPDCGKSFSHGATLAQHRGIH 204
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 133922567  197 LAQHRGIHTGARPYQCAACGKAF 219
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24