krueppel associated box;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382651    81 LKVEDVALTLTP-EWTQQDSSQGNLCRDEKQENHGSLVSLGDEKqTKSRDLPPAEELPEKEH 141
Cdd:smart00349   1 VTFEDVAVYFTQeEWEQLDPAQKNLYRDVMLENYSNLVSLGFQV-PKPDLISQLEQGEEPWI 61

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 530382651  196 LSKHRRIHTGEKPYECEECGKAF 218
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

krueppel associated box;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382651    81 LKVEDVALTLTP-EWTQQDSSQGNLCRDEKQENHGSLVSLGDEKqTKSRDLPPAEELPEKEH 141
Cdd:smart00349   1 VTFEDVAVYFTQeEWEQLDPAQKNLYRDVMLENYSNLVSLGFQV-PKPDLISQLEQGEEPWI 61

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530382651  81 LKVEDVALTLTP-EWTQQDSSQGNLCRDEKQENHGSLVSL 119
Cdd:cd07765    1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 530382651  251 DLIKHQRTHTGEKPYECDDCGKTFSQ 276
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 530382651  181 HICHECGKSFAQSSGLSKHRRIH 203
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

hypothetical protein

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530382651 264 PYECDDCGKTFSQSCSLLEHHRIHTGEKpyQCSMCGKAFRRSSHLLRH 311
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118

krueppel associated box;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382651    81 LKVEDVALTLTP-EWTQQDSSQGNLCRDEKQENHGSLVSLGDEKqTKSRDLPPAEELPEKEH 141
Cdd:smart00349   1 VTFEDVAVYFTQeEWEQLDPAQKNLYRDVMLENYSNLVSLGFQV-PKPDLISQLEQGEEPWI 61

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530382651  81 LKVEDVALTLTP-EWTQQDSSQGNLCRDEKQENHGSLVSL 119
Cdd:cd07765    1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382651 263 KPYECDDCGKTFSQSCSLLEH--HRIHTGE--KPYQC--SMCGKAFRRSSHLLRHQRIHTGDKNVQEP-EQGEAWKSRME 335
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKlLNSSSKFSPLL 367

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382651 336 -------SQLENVETPMSYKC---NECERSFTQNTGLIEHQKIHTGEKPYQCN--ACGKGFTRISYLVQHQRSHV 398
Cdd:COG5048  368 nneppqsLQQYKDLKNDKKSEtlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT 442

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530382651 249 SSDLIKHQRTHTGE----KPYECDDCGKTFSQSCSLLEHHRIHTGEKPYQCS--MCGKAFRRSSHLLRHQRIHTGDKN 320
Cdd:COG5048   14 SVLSSTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPS 91

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 530382651  251 DLIKHQRTHTGEKPYECDDCGKTFSQ 276
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 530382651  293 YQCSMCGKAFRRSSHLLRHQRIH 315
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 530382651  223 ALVIHQRVHTGEKPYECEECGKAFSH 248
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 530382651  279 SLLEHHRIHTGEKPYQCSMCGKAFRR 304
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382651 200 RRIHT-GEKPYECE--ECGKAFIGSSALVIHqRVHTgekpyeceECGKAFSHSSDLIKHQRTHTGEKPYECDDCGKTFsQ 276
Cdd:COG5189  340 RMLKVkDGKPYKCPveGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-K 409

                         90
                 ....*....|..
gi 530382651 277 SCSLLEHHRIHT 288
Cdd:COG5189  410 NLNGLKYHRKHS 421

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
                 ....*....|....*....|....*....|....*....|....*.
gi 530382651 348 KCNECERSFTQNTGLIEHQKIHTgekpYQCNACGKGFTRISYLVQH 393
Cdd:cd20908    3 WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382651 180 RHICHECGKSFAQSSGLSKHRR--IHTGE--KPYECEE--CGKAFIGSSALVIHQRVHTGEKPYEC--EECGKAFSHSSD 251
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLN 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382651 252 -----------------------------------LIKHQRTHTGEKPYECDD--CGKTFSQSCSLLEHHRIHTGEKPYQ 294
Cdd:COG5048  369 neppqslqqykdlkndkksetlsnscirnfkrdsnLSLHIITHLSFRPYNCKNppCSKSFNRHYNLIPHKKIHTNHAPLL 448

                        170
                 ....*....|....*..
gi 530382651 295 CSMCGKaFRRSSHLLRH 311
Cdd:COG5048  449 CSILKS-FRRDLDLSNH 464

Transposase InsA [Mobilome: prophages, transposons];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530382651 239 CEECGkafshSSDLIKHQRTHTGEKPYECDDCGKTFS-QSCSLLEHHRIHTGEKPYQCSMCGKAFRRSSHLL 309
Cdd:COG3677   19 CPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTvTTGTIFEGSKLPLWLQAIRLLLNGISLRQIARVL 85