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Conserved domains on  [gi|32813445|ref|NP_862829|]
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zinc finger and SCAN domain-containing protein 22 isoform 1 [Homo sapiens]

Protein Classification

SCAN and COG5048 domain-containing protein( domain architecture ID 12029559)

SCAN and COG5048 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 45-133 1.77e-47

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.


:

Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.81  E-value: 1.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445    45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 32813445   125 EDLTQVLDK 133
Cdd:pfam02023  81 EDLLLERGE 89
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
174-482 1.57e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 174 FVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGreSGASRNSSSAWPNLTSQEKPPSEDKFDLVDA 253
Cdd:COG5048 146 LRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNV--STSIPSSSENSPLSSSYSIPSSSSDQNLENS 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 254 YGTEPPYTYSGKrsskcreCRKMFQSASALEAHQKTHSRKTP--YACSECGKAFSRSTHLAQHQVVHTGA-KPHECKECG 330
Cdd:COG5048 224 SSSLPLTTNSQL-------SPKSLLSQSPSSLSSSDSSSSASesPRSSLPTASSQSSSPNESDSSSEKGFsLPIKSKQCN 296

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 331 KAFSRVTHLTQHQR--IHTGE--KPYKCGE--CGKTFSRSTHLTQHQRVHTGERPYECDA--CGKAFSQSTH-----LTQ 397
Cdd:COG5048 297 ISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNneppqSLQ 376

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 398 HQRIHTGEKPYKCD--ACGRAFSDCSALIRHLRIHSGEKPYQCK--VCPKAFAQSSSLIEHQRIHTGEKPYKCSDCGkaF 473
Cdd:COG5048 377 QYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILK--S 454


                ....*....
gi 32813445 474 SRSSALMVH 482
Cdd:COG5048 455 FRRDLDLSN 463
 
Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 45-133 1.77e-47

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.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.81  E-value: 1.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445    45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 32813445   125 EDLTQVLDK 133
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
45-135 2.70e-46

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 156.70  E-value: 2.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445     45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90
                   ....*....|.
gi 32813445    125 EDLTQVLDKRG 135
Cdd:smart00431  81 EDLERELDEPG 91
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 45-129 9.50e-40

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.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 138.16  E-value: 9.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445  45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:cd07936   1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                ....*
gi 32813445 125 EDLTQ 129
Cdd:cd07936  81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
174-482 1.57e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 174 FVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGreSGASRNSSSAWPNLTSQEKPPSEDKFDLVDA 253
Cdd:COG5048 146 LRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNV--STSIPSSSENSPLSSSYSIPSSSSDQNLENS 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 254 YGTEPPYTYSGKrsskcreCRKMFQSASALEAHQKTHSRKTP--YACSECGKAFSRSTHLAQHQVVHTGA-KPHECKECG 330
Cdd:COG5048 224 SSSLPLTTNSQL-------SPKSLLSQSPSSLSSSDSSSSASesPRSSLPTASSQSSSPNESDSSSEKGFsLPIKSKQCN 296

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 331 KAFSRVTHLTQHQR--IHTGE--KPYKCGE--CGKTFSRSTHLTQHQRVHTGERPYECDA--CGKAFSQSTH-----LTQ 397
Cdd:COG5048 297 ISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNneppqSLQ 376

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 398 HQRIHTGEKPYKCD--ACGRAFSDCSALIRHLRIHSGEKPYQCK--VCPKAFAQSSSLIEHQRIHTGEKPYKCSDCGkaF 473
Cdd:COG5048 377 QYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILK--S 454


                ....*....
gi 32813445 474 SRSSALMVH 482
Cdd:COG5048 455 FRRDLDLSN 463
zf-H2C2_2 pfam13465
Zinc-finger double domain;
338-363 1.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 32813445   338 HLTQHQRIHTGEKPYKCGECGKTFSR 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 434-486 1.50e-04

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.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 40.23  E-value: 1.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 32813445 434 KPYqCKVCPKAFAQSSSLIEHQRIHTgekpYKCSDCGKAFSRSSALMVH-LRIH 486
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 267-430 1.28e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 41.40  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445  267 SSKCRECRKMFQSASAL--EAHQKTHSRKTPYAcsECGKAFsRSTHLAQHqvVHtgakpheCKECGKAFSRvTHLTQHQR 344
Cdd:PLN03086 407 TVECRNCKHYIPSRSIAlhEAYCSRHNVVCPHD--GCGIVL-RVEEAKNH--VH-------CEKCGQAFQQ-GEMEKHMK 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445  345 IHtgEKPYKCGeCGKTFSRStHLTQHQRVHTGERPYECDACGKAFSQSTH----------LTQHQRIhTGEKPYKCDACG 414
Cdd:PLN03086 474 VF--HEPLQCP-CGVVLEKE-QMVQHQASTCPLRLITCRFCGDMVQAGGSamdvrdrlrgMSEHESI-CGSRTAPCDSCG 548

                        170
                 ....*....|....*.
gi 32813445  415 RafsdcSALIRHLRIH 430
Cdd:PLN03086 549 R-----SVMLKEMDIH 559
 
Name Accession Description Interval E-value
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 45-133 1.77e-47

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.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 158.81  E-value: 1.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445    45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 32813445   125 EDLTQVLDK 133
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
45-135 2.70e-46

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 156.70  E-value: 2.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445     45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90
                   ....*....|.
gi 32813445    125 EDLTQVLDKRG 135
Cdd:smart00431  81 EDLERELDEPG 91
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 45-129 9.50e-40

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.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 138.16  E-value: 9.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445  45 SEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLV 124
Cdd:cd07936   1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                ....*
gi 32813445 125 EDLTQ 129
Cdd:cd07936  81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
174-482 1.57e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 66.26  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 174 FVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGreSGASRNSSSAWPNLTSQEKPPSEDKFDLVDA 253
Cdd:COG5048 146 LRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNV--STSIPSSSENSPLSSSYSIPSSSSDQNLENS 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 254 YGTEPPYTYSGKrsskcreCRKMFQSASALEAHQKTHSRKTP--YACSECGKAFSRSTHLAQHQVVHTGA-KPHECKECG 330
Cdd:COG5048 224 SSSLPLTTNSQL-------SPKSLLSQSPSSLSSSDSSSSASesPRSSLPTASSQSSSPNESDSSSEKGFsLPIKSKQCN 296

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 331 KAFSRVTHLTQHQR--IHTGE--KPYKCGE--CGKTFSRSTHLTQHQRVHTGERPYECDA--CGKAFSQSTH-----LTQ 397
Cdd:COG5048 297 ISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLLNneppqSLQ 376

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 398 HQRIHTGEKPYKCD--ACGRAFSDCSALIRHLRIHSGEKPYQCK--VCPKAFAQSSSLIEHQRIHTGEKPYKCSDCGkaF 473
Cdd:COG5048 377 QYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILK--S 454


                ....*....
gi 32813445 474 SRSSALMVH 482
Cdd:COG5048 455 FRRDLDLSN 463
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
221-488 1.55e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 63.18  E-value: 1.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 221 RESGASRNSSSAWPNLTSQEKPPSEDKFDLVDAYGTEPPYTYSgkrsSKCRECRKMFQSASALEAHQKTHSRKTPYACSE 300
Cdd:COG5048 156 SSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPS----SSENSPLSSSYSIPSSSSDQNLENSSSSLPLTT 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 301 CGKAFSRSTHLAQHQVVHTGAKPHECKECGKAF--SRVTHLTQHQRIHTGE-----KPYKCGECGKTFSRSTHLTQHQR- 372
Cdd:COG5048 232 NSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSlpTASSQSSSPNESDSSSekgfsLPIKSKQCNISFSRSSPLTRHLRs 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 373 -VHTGE--RPYECDA--CGKAFSQSTHLTQHQRIHTGEKPYKCDACGRAFSDCSALIR----HLRIHSGEKPYQCKV--- 440
Cdd:COG5048 312 vNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqSLQQYKDLKNDKKSEtls 391

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 32813445 441 --CPKAFAQSSSLIEHQRIHTGEKP--YKCSDCGKAFSRSSALMVHLRIHIT 488
Cdd:COG5048 392 nsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
378-454 2.19e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.16  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 378 RPYECDACGKAFSQSTHLTQHQRIHTGEKPYKCDACGRA--FSDCSALIRHLRIHSGEKPYQC--KVCPKAFAQSSSLIE 453
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDksFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLS 111


                .
gi 32813445 454 H 454
Cdd:COG5048 112 S 112
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
406-471 1.10e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.10e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32813445 406 KPYKCDACGRAFSDCSALIRHLRIHSGEKPYQCKVCPKAFAQS--SSLIEHQRIHTGEKPYKCSDCGK 471
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSKSLP 99
zf-H2C2_2 pfam13465
Zinc-finger double domain;
338-363 1.40e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.40e-05
                          10        20
                  ....*....|....*....|....*.
gi 32813445   338 HLTQHQRIHTGEKPYKCGECGKTFSR 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 1.71e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 1.71e-05
                          10        20
                  ....*....|....*....|....*.
gi 32813445   422 ALIRHLRIHSGEKPYQCKVCPKAFAQ 447
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
267-428 1.83e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 267 SSKCRECRKMFQSASALEAHQKT--HSRK--TPYACSE--CGKAFSRSTHLAQHQVVHTGAKPHECKEC-------GKAF 333
Cdd:COG5048 289 PIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLN 368

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445 334 SRVTHLTQHQRIHTGEKPYKC--GECGKTFSRSTHLTQHQRVHTGERPYECD--ACGKAFSQSTHLTQHQRIHTGEKPYK 409
Cdd:COG5048 369 NEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLL 448

                       170
                ....*....|....*....
gi 32813445 410 CDACGRaFSDCSALIRHLR 428
Cdd:COG5048 449 CSILKS-FRRDLDLSNHGK 466
zf-H2C2_2 pfam13465
Zinc-finger double domain;
450-475 2.60e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 2.60e-05
                          10        20
                  ....*....|....*....|....*.
gi 32813445   450 SLIEHQRIHTGEKPYKCSDCGKAFSR 475
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-418 3.73e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.73e-05
                          10        20
                  ....*....|....*....|....*
gi 32813445   394 HLTQHQRIHTGEKPYKCDACGRAFS 418
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
366-391 3.96e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 3.96e-05
                          10        20
                  ....*....|....*....|....*.
gi 32813445   366 HLTQHQRVHTGERPYECDACGKAFSQ 391
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
322-393 6.31e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 6.31e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32813445 322 KPHECKECGKAFSRVTHLTQHQRIHTGEKPYKCG--ECGKTFSRSTHLTQHQRVHTGERPYECDACGKAFSQST 393
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKA 105
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 352-374 9.38e-05

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.21  E-value: 9.38e-05
                          10        20
                  ....*....|....*....|...
gi 32813445   352 YKCGECGKTFSRSTHLTQHQRVH 374
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
434-486 9.50e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 9.50e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32813445 434 KPYQCKVCPKAFAQSSSLIEHQRIHTGEKPYKCSD--CGKAFSRSSALMVHLRIH 486
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTH 86
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 464-486 1.49e-04

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 1.49e-04
                          10        20
                  ....*....|....*....|...
gi 32813445   464 YKCSDCGKAFSRSSALMVHLRIH 486
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 434-486 1.50e-04

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.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 40.23  E-value: 1.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 32813445 434 KPYqCKVCPKAFAQSSSLIEHQRIHTgekpYKCSDCGKAFSRSSALMVH-LRIH 486
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
293-351 1.53e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.53e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32813445 293 KTPYACSECGKAFSRSTHLAQHQVVHTGAKPHEC--KECGKAFSRVTHLTQHQRIHTGEKP 351
Cdd:COG5048  31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPS 91
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 326-374 4.14e-04

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.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 4.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 32813445 326 CKECGKAFSRVTHLTQHQRIHTgekpYKCGECGKTFSRSTHLTQH-QRVH 374
Cdd:cd20908   4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
350-415 1.06e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 1.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32813445 350 KPYKCGECGKTFSRSTHLTQHQRVHTGERPYECDA--CGKAFSQSTHLTQHQRIHTGEKPYKCDACGR 415
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 324-346 1.10e-03

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|...
gi 32813445   324 HECKECGKAFSRVTHLTQHQRIH 346
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
310-335 1.18e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 32813445   310 HLAQHQVVHTGAKPHECKECGKAFSR 335
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 267-430 1.28e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 41.40  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445  267 SSKCRECRKMFQSASAL--EAHQKTHSRKTPYAcsECGKAFsRSTHLAQHqvVHtgakpheCKECGKAFSRvTHLTQHQR 344
Cdd:PLN03086 407 TVECRNCKHYIPSRSIAlhEAYCSRHNVVCPHD--GCGIVL-RVEEAKNH--VH-------CEKCGQAFQQ-GEMEKHMK 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32813445  345 IHtgEKPYKCGeCGKTFSRStHLTQHQRVHTGERPYECDACGKAFSQSTH----------LTQHQRIhTGEKPYKCDACG 414
Cdd:PLN03086 474 VF--HEPLQCP-CGVVLEKE-QMVQHQASTCPLRLITCRFCGDMVQAGGSamdvrdrlrgMSEHESI-CGSRTAPCDSCG 548

                        170
                 ....*....|....*.
gi 32813445  415 RafsdcSALIRHLRIH 430
Cdd:PLN03086 549 R-----SVMLKEMDIH 559
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 436-458 1.38e-03

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.38e-03
                          10        20
                  ....*....|....*....|...
gi 32813445   436 YQCKVCPKAFAQSSSLIEHQRIH 458
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 380-402 1.56e-03

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 1.56e-03
                          10        20
                  ....*....|....*....|...
gi 32813445   380 YECDACGKAFSQSTHLTQHQRIH 402
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA00733 PHA00733
hypothetical protein
 435-483 2.84e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.93  E-value: 2.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 32813445  435 PYQCKVCPKAFAQSSSLIEHQRIHTGEKpyKCSDCGKAFSRSSALMVHL 483
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHV 119
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 408-430 2.90e-03

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|...
gi 32813445   408 YKCDACGRAFSDCSALIRHLRIH 430
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
282-307 5.20e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 32813445   282 ALEAHQKTHSRKTPYACSECGKAFSR 307
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 378-430 5.78e-03

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.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.00  E-value: 5.78e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 32813445 378 RPYeCDACGKAFSQSTHLTQHQRIHTgekpYKCDACGRAFSDCSALIRH-LRIH 430
Cdd:cd20908   1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 296-318 8.80e-03

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.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 8.80e-03
                          10        20
                  ....*....|....*....|...
gi 32813445   296 YACSECGKAFSRSTHLAQHQVVH 318
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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