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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  426 KHKCRFCAKVFGSDSALQIHLRSHTgerpFKCNICGNRFSTKGNLKVHF-QRHKEKYPHIqMNPYPVPEYLD-NVPTCSG 503
Cdd:cd20908    1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHClQVHKETLTKV-PNALPGRDDPEiEIFGMEG 75

                 ....*
gi 54144640  504 IPYGM 508
Cdd:cd20908   76 IPEGD 80

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 54144640 1063 CQSCGKTFSSASALQIHERTHTgekpFGCTICGRAFTTKGNLKVHM 1108
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHC 45

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 54144640    752 HSCPICQKKFTNAVVLQQHIRMH 774
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   242 PGPPLKPSASAPGTASVQLQGLTPHAALQLSAGPATASAGSGstlPAAfdGPQHLSQPASGTSTPCSTSAAP--PDSGAH 319
Cdd:PHA03247 2733 PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA---PAA--GPPRRLTRPAVASLSESRESLPspWDPADP 2807

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   320 PACSTGPAPGAVAAASSTVGNAVQPQNASTPPALGPGPLLSS---------------------------------ASNLP 366
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlplggsvapggdvrrrppsrspaakpaaparppVRRLA 2887

                         170
                  ....*....|....*...
gi 54144640   367 NPLLPQTSSSSVIFPNPL 384
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQP 2905

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  426 KHKCRFCAKVFGSDSALQIHLRSHTgerpFKCNICGNRFSTKGNLKVHF-QRHKEKYPHIqMNPYPVPEYLD-NVPTCSG 503
Cdd:cd20908    1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHClQVHKETLTKV-PNALPGRDDPEiEIFGMEG 75

                 ....*
gi 54144640  504 IPYGM 508
Cdd:cd20908   76 IPEGD 80

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 54144640 1063 CQSCGKTFSSASALQIHERTHTgekpFGCTICGRAFTTKGNLKVHM 1108
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHC 45

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 54144640   1091 CTICGRAFTTKGNLKVHMGTH 1111
Cdd:pfam00096    3 CPDCGKSFSRKSNLKRHLRTH 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 54144640    752 HSCPICQKKFTNAVVLQQHIRMH 774
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

zinc finger;

                            10        20
                    ....*....|....*....|...
gi 54144640     752 HSCPICQKKFTNAVVLQQHIRMH 774
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23

zinc finger;

                            10        20
                    ....*....|....*....|...
gi 54144640     427 HKCRFCAKVFGSDSALQIHLRSH 449
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23

zinc finger;

                            10        20
                    ....*....|....*....|...
gi 54144640    1061 HNCQSCGKTFSSASALQIHERTH 1083
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  426 KHKCRFCAKVFGSDSALQIHLRSHTgerpFKCNICGNRFSTKGNLKVHF-QRHKEKYPHIqMNPYPVPEYLD-NVPTCSG 503
Cdd:cd20908    1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHClQVHKETLTKV-PNALPGRDDPEiEIFGMEG 75

                 ....*
gi 54144640  504 IPYGM 508
Cdd:cd20908   76 IPEGD 80

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 54144640 1063 CQSCGKTFSSASALQIHERTHTgekpFGCTICGRAFTTKGNLKVHM 1108
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHC 45

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 54144640   1091 CTICGRAFTTKGNLKVHMGTH 1111
Cdd:pfam00096    3 CPDCGKSFSRKSNLKRHLRTH 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        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 54144640  694 CVICHRVLSCQSALKMHYRTHTgerpFKCKICGRAFTTKGNLKTHF-GVHRAKPPlRVQHSCPI 756
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHClQVHKETLT-KVPNALPG 62

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 54144640   1061 HNCQSCGKTFSSASALQIHERTH 1083
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  419 SAEDPFFKHKCRFCAKVFGSDSALQIHLRSHTGERPFKCN--ICGNRFSTKGNLKVHFQRHKEKYPH-----IQMNPYPV 491
Cdd:COG5048   26 SLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDlnsksLPLSNSKA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  492 PEYLDNVPTCSG----IPYGMSLPPEKPVttWLDSKPVLPTV------------------PTSVGLQLPPTVPGTHNYTD 549
Cdd:COG5048  106 SSSSLSSSSSNSndnnLLSSHSLPPSSRD--PQLPDLLSISNlrnnplpgnnsssvntpqSNSLHPPLPANSLSKDPSSN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  550 SPSITPVSRSPQRPSPASSECTSLSPGLNNTESGITVRPESP-----QPLLGGPSLTKAEPVSLPCTSTRTGDAPVVGGQ 624
Cdd:COG5048  184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSslpltTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640  625 VSGLPTSAATAVTDSACTSLGSPGLPAVSDQFKAQFpfgglldSMQTSETSKLQQLVENIDKKMTDPNQCVICHRVLSCQ 704
Cdd:COG5048  264 SLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISF-------SRSSPLTRHLRSVNHSGESLKPFSCPYSLCGKLFSRN 336

                        330       340
                 ....*....|....*....|...
gi 54144640  705 SALKMHYRTHTGERPFKCKICGR 727
Cdd:COG5048  337 DALKRHILLHTSISPAKEKLLNS 359

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                           10        20
                   ....*....|....*....|...
gi 54144640    455 FKCNICGNRFSTKGNLKVHFQRH 477
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                           10        20
                   ....*....|....*....|...
gi 54144640    720 FKCKICGRAFTTKGNLKTHFGVH 742
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   242 PGPPLKPSASAPGTAsvqlQGLTPHAALQLSAGPATASAGSGSTLPAAFDGPQHLSQPASGTSTPCSTSAAPPDSGA--- 318
Cdd:PHA03247 2551 PPPPLPPAAPPAAPD----RSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHApdp 2626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   319 HPACSTGPAPGAVAAASSTVGNAVQPQNASTPPALGPGPLLSSASNLPNPLLPQTSSSSVIFPNPLVSIAATANALDPls 398
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP-- 2704

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   399 almkhrkGKPPnvsvfEPKASAEDPffkhkcrfcakvfgsdsALQIHLRSHTGERPFkcnicgnrfstkgnlkvhfqrhk 478
Cdd:PHA03247 2705 -------PPTP-----EPAPHALVS-----------------ATPLPPGPAAARQAS----------------------- 2732

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   479 ekyPHIQMNPYPVPeyldnVPTCSGIPYGMSLPPEKPVTtwldSKPVLPTVPTSVGLQLPPTVPGTHNYTDSPSiTPVSR 558
Cdd:PHA03247 2733 ---PALPAAPAPPA-----VPAGPATPGGPARPARPPTT----AGPPAPAPPAAPAAGPPRRLTRPAVASLSES-RESLP 2799

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54144640   559 SPQRPSPASSECTSLSPGLNNTESGITVRPESPQPLLGGPSLTKAEPVslpcTSTRTGDAPVVGGQVSGLPTSAATAVTD 638
Cdd:PHA03247 2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP----PSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875

                         410       420
                  ....*....|....*....|...
gi 54144640   639 SACT-----SLGSPGLPAVSDQF 656
Cdd:PHA03247 2876 AAPArppvrRLARPAVSRSTESF 2898

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                           10        20
                   ....*....|....*....|...
gi 54144640   1089 FGCTICGRAFTTKGNLKVHMGTH 1111
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23

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 54144640   1060 QHNCQSCGKTFSSASALQIHERTH 1083
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLKSK 24

zinc finger;

                            10        20
                    ....*....|....*....|.
gi 54144640    1091 CTICGRAFTTKGNLKVHMGTH 1111
Cdd:smart00355    3 CPECGKVFKSKSALREHMRTH 23

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                           10        20
                   ....*....|....*....|...
gi 54144640    427 HKCRFCAKVFGSDSALQIHLRSH 449
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23