N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789   1 MDSSDNSERTGeRVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQ 80
Cdd:cd22537 254 VQSSDNSGESG-KVSPDINETNTNADLFVPTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQ 332

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789  81 AQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQ 158
Cdd:cd22537 333 AQNIQVSTAQPSVQQIQLHESQQPTSQAQIVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQ 412

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 159 VTWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGE 238
Cdd:cd22537 413 ITWQTFQVQGVQNLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSE 492

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 239 NADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQ 318
Cdd:cd22537 493 NADSPADIQIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQ 572

                ..
gi 18091789 319 HI 320
Cdd:cd22537 573 HI 574

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 18091789   379 FVCPECSKRFMRSDHLAKHIKTH 401
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789   1 MDSSDNSERTGeRVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQ 80
Cdd:cd22537 254 VQSSDNSGESG-KVSPDINETNTNADLFVPTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQ 332

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789  81 AQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQ 158
Cdd:cd22537 333 AQNIQVSTAQPSVQQIQLHESQQPTSQAQIVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQ 412

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 159 VTWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGE 238
Cdd:cd22537 413 ITWQTFQVQGVQNLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSE 492

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 239 NADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQ 318
Cdd:cd22537 493 NADSPADIQIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQ 572

                ..
gi 18091789 319 HI 320
Cdd:cd22537 573 HI 574

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 18091789   379 FVCPECSKRFMRSDHLAKHIKTH 401
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 334 SHLRAHLRW--HSGE--RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKKFVCP--ECSKRFMRSDHlAKHIKTHQNKKGI 407
Cdd:COG5048 303 SPLTRHLRSvnHSGEslKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLN-NEPPQSLQQYKDL 381

                ....*....
gi 18091789 408 HSSSTVLAS 416
Cdd:COG5048 382 KNDKKSETL 390

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789   321 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 393
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81

                  ....*
gi 18091789   394 LAKHI 398
Cdd:pfam15909  82 LFKHL 86

N-terminal domain of transcription factor Specificity Protein (SP) 3; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP1 and SP3 can interact with and recruit a large number of proteins including the transcription initiation complex, histone modifying enzymes, and chromatin remodeling complexes, which strongly suggest that SP1 and SP3 are important transcription factors in remodeling chromatin and the regulation of gene expression. SP3 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP3.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789   1 MDSSDNSERTGeRVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQ 80
Cdd:cd22537 254 VQSSDNSGESG-KVSPDINETNTNADLFVPTSSSSQLPVTIDSTGILQQNASSLTTVSGQVHTSDLQGNYIQAPVSDETQ 332

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789  81 AQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQA-SGQNISQQALQNLQLQ-LNPGTFLIQAQTVTPSGQ 158
Cdd:cd22537 333 AQNIQVSTAQPSVQQIQLHESQQPTSQAQIVQGITQQAIQGVQAlGAQAIPQQALQNLQLQlLNPGTFLIQAQTVTPSGQ 412

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 159 VTWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGE 238
Cdd:cd22537 413 ITWQTFQVQGVQNLQNLQIQNAPAQQITLTPVQTLTLGQVGAGGAITSTPVSLSTGQLPNLQTVTVNSIDSAGIQLQQSE 492

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 239 NADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQ 318
Cdd:cd22537 493 NADSPADIQIKEEEPDSEEWQLSGDSTLNTNDLTHLRVQLVEEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQ 572

                ..
gi 18091789 319 HI 320
Cdd:cd22537 573 HI 574

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 18091789 277 QVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHI 320
Cdd:cd22545  39 QVIPQFQDQEPQPGKRLRRVACTCPNCKDGEGRGSEDGKKKQHI 82

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789  80 QAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHG--VQASGQNISQQALQNLQLQLNpgtfliqAQTVTPSG 157
Cdd:cd22553 193 QALQAQVIPQLAQAAQLQPQQLAQVSSQGYIQQIPANASQQQpqMVQQGPNQSGQIIGQVASASS-------IQAAAIPL 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 158 QVTWQTFQVQGVQNLQNlqiqntaAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVnsIDSAGIQLHPG 237
Cdd:cd22553 266 TVYTGALAGQNGSNQQQ-------VGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQGNPLPPGTQ--IIAAGQQLQQD 336

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789 238 ENadspadirikeeepDPEEWQLSGDSTLNTndlthlrvqvvdeegdqqhqeGKRLRRVACTCPNCKEGGGRGTNLGKKK 317
Cdd:cd22553 337 PN--------------DPTKWQVVADGTPGS---------------------KKRLRRVACTCPNCRDGDGTRNGENKKK 381

                ...
gi 18091789 318 QHI 320
Cdd:cd22553 382 QHI 384

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 18091789   365 ELQRHRRTHTGEKKFVCPECSKRF 388
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 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 18091789   349 FVCNwmYCGKRFTRSDELQRHRRTH 373
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23

zinc finger;

                           10        20
                   ....*....|....*....|...
gi 18091789    379 FVCPECSKRFMRSDHLAKHIKTH 401
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18091789   321 CHIPGCGKVYGKTSHLRAHLRWHSGE------RPFVCNWMYCGKRFTRSDELQRHRRTHTGEKK-FVCPECSKRFMRSDH 393
Cdd:pfam15909   2 CSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRyFKCENCLLRFRTHRS 81

                  ....*
gi 18091789   394 LAKHI 398
Cdd:pfam15909  82 LFKHL 86

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 18091789 347 RPFvCnWmYCGKRFtrSDE--LQRHRRTHTgekkFVCPECSKRFMRSDHLAKHIKT 400
Cdd:cd20908   1 KPW-C-Y-YCDREF--DDEkiLIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQ 47