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 21357113     5 CRICGERifTPHPKNIFEKRNHRIRMA--IEQITGLEIVLENMLPQHICACCLLDLTQAVAFRQRCLETHANLHQR 78
Cdd:pfam07776   2 CRLCLDE--SDELIPIFDPSDSEKTLAeiLEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.

                          10        20
                  ....*....|....*....|....*.
gi 21357113   322 HICLTCNKEFKEAQFLHRHYSTKYHR 347
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27

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 21357113     5 CRICGERifTPHPKNIFEKRNHRIRMA--IEQITGLEIVLENMLPQHICACCLLDLTQAVAFRQRCLETHANLHQR 78
Cdd:pfam07776   2 CRLCLDE--SDELIPIFDPSDSEKTLAeiLEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75

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 21357113 212 CGWSFNDHSNMKDH-KLRHFeekfSCDECGRKFYTMPLLRLHI-RVHH 257
Cdd:cd20908   7 CDREFDDEKILIQHqKAKHF----KCHICHKKLYTAGGLAVHClQVHK 50

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 21357113   249 LRLHIRVHHkGEKPYVCKFCGMGFAN 274
Cdd:pfam13465   2 LKRHMRTHT-GEKPYKCPECGKSFKS 26

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 21357113     5 CRICGERifTPHPKNIFEKRNHRIRMA--IEQITGLEIVLENMLPQHICACCLLDLTQAVAFRQRCLETHANLHQR 78
Cdd:pfam07776   2 CRLCLDE--SDELIPIFDPSDSEKTLAeiLEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75

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 21357113 212 CGWSFNDHSNMKDH-KLRHFeekfSCDECGRKFYTMPLLRLHI-RVHH 257
Cdd:cd20908   7 CDREFDDEKILIQHqKAKHF----KCHICHKKLYTAGGLAVHClQVHK 50

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 21357113   249 LRLHIRVHHkGEKPYVCKFCGMGFAN 274
Cdd:pfam13465   2 LKRHMRTHT-GEKPYKCPECGKSFKS 26