SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466898  72 GPQGALGRLRELCRRWLRPEVHTKEQM---------LTMLPKEIQAWLQEHRPESSEEAAALVEDLTQTLQD 134
Cdd:pfam02023  18 GPREALSQLRELCHQWLRPEKHTKEQIlellvleqfLTILPEEIQSWVREHHPESGEEAVALAEDLLLERGE 89

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466898  72 GPQGALGRLRELCRRWLRPEVHTKEQM---------LTMLPKEIQAWLQEHRPESSEEAAALVEDLTQTLQD 134
Cdd:pfam02023  18 GPREALSQLRELCHQWLRPEKHTKEQIlellvleqfLTILPEEIQSWVREHHPESGEEAVALAEDLLLERGE 89

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466898  72 GPQGALGRLRELCRRWLRPEVHTKEQM---------LTMLPKEIQAWLQEHRPESSEEAAALVEDLTQ 130
Cdd:cd07936    18 GPREALQRLRELCRQWLRPEIHTKEQIlellvleqfLIILPPEVQAWVRERKPESGEEAATLAEDLLA 85

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1370466898 488 NLLKHQRIHTGEKPYKCSECGKCFSQ 513
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466898  72 GPQGALGRLRELCRRWLRPEVHTKEQM---------LTMLPKEIQAWLQEHRPESSEEAAALVEDLTQTLQD 134
Cdd:pfam02023  18 GPREALSQLRELCHQWLRPEKHTKEQIlellvleqfLTILPEEIQSWVREHHPESGEEAVALAEDLLLERGE 89

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466898  72 GPQGALGRLRELCRRWLRPEVHTKEQM---------LTMLPKEIQAWLQEHRPESSEEAAALVEDLTQ 130
Cdd:cd07936    18 GPREALQRLRELCRQWLRPEIHTKEQIlellvleqfLIILPPEVQAWVRERKPESGEEAATLAEDLLA 85

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466898 257 KSFSDGSNFSRHQTTHTG-EKPYKCRDCGKSFSRSANLITHQR--IHTGE--KPFQCAE--CGKSFSRSPNLIAHQRTHT 329
Cdd:COG5048   268 ASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHT 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466898 330 GEKPYSCP--ECGKSFG------NRSSLNTHQGIHTgEKPYEC--KECGESFSYNSNLIRHQRIHTGEKP--YKCTDCGQ 397
Cdd:COG5048   348 SISPAKEKllNSSSKFSpllnnePPQSLQQYKDLKN-DKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSK 426

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370466898 398 RFSQSSALITHRRTHTGEKPYQCSECGKSFSRSS 431
Cdd:COG5048   427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1370466898 488 NLLKHQRIHTGEKPYKCSECGKCFSQ 513
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1370466898 292 NLITHQRIHTGEKPFQCAECGKSFSR 317
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1370466898 404 ALITHRRTHTGEKPYQCSECGKSFSR 429
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 1370466898 418 YQCSECGKSFSRSSNLATHRRTH 440
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|..
gi 1370466898 576 HQRIHTGEKPYKCPECGKGFSN 597
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 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 1370466898 502 YKCSECGKCFSQRSQLVVHQRTH 524
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 1370466898 586 YKCPECGKGFSNSSNFITHQRTH 608
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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 1370466898 528 KPYkCLMCGKSFSRGSILVMHQRAhlgdKPYRCPECGKGFSWNSVLIIH-QRIH 580
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKA----KHFKCHICHKKLYTAGGLAVHcLQVH 49

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1370466898 517 LVVHQRTHTGEKPYKCLMCGKSFSR 541
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466898 414 GEKPYQCS--ECGKSFSRSSNLATHRrthmvekpyKCGVCGKSFSQSSSLIAHQGMHTGEKPYECLTCGESFSwSSNLLK 491
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHM---------LHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYK-NLNGLK 415

                  ....*.
gi 1370466898 492 HQRIHT 497
Cdd:COG5189   416 YHRKHS 421

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466898 330 GEKPYSCP--ECGKSFGNRSSLNTHQgIHtgekpyecKECGESFSYNSNLIRHQRIHTGEKPYKCTDCGQRFSQSSALIT 407
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHM-LH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  ....*.
gi 1370466898 408 HrRTHT 413
Cdd:COG5189   417 H-RKHS 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 1370466898 276 KPYkCRDCGKSFSRSANLITHQRIHTgekpFQCAECGKSFSRSPNLIAH 324
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44

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 1370466898 390 YKCTDCGQRFSQSSALITHRRTH 412
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 1370466898 250 YKCDECGKSFSDGSNFSRHQTTH 272
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23