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Conserved domains on  [gi|2174213912|ref|NP_001386347|]
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zinc finger protein 263 [Rattus norvegicus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 12210849)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
41-151 8.73e-55

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 182.50  E-value: 8.73e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912   41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:smart00431   3 IFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLED 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2174213912  121 MQKELGKLRQQVTNQGRGAEVLLEEPLPLET 151
Cdd:smart00431  83 LERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
460-646 2.83e-12

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 460 KPFQCNVCGKSFSCNSNLNRHQRT--HTGE--KPYKCPE--CGEIFAHSSNLLRHQRIHTGERPYRC--SECGKSFSRSS 531
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 532 HLVIHERTHEKERLDP-LPECGQGINDSAPFLTNHRVEKklfecstcgksfrqgmHLTRH--QRTHtgekPYKCILCGEN 608
Cdd:COG5048   368 NNEPPQSLQQYKDLKNdKKSETLSNSCIRNFKRDSNLSL----------------HIITHlsFRPY----NCKNPPCSKS 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2174213912 609 FSHRSNLIRHQRIHTGEKPYTCHECGDSFS--HSSNRIRH 646
Cdd:COG5048   428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRdlDLSNHGKD 467
KRAB_A-box super family cl02581
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 219-257 1.54e-05

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


The actual alignment was detected with superfamily member cd07765:

Pssm-ID: 470626  Cd Length: 40  Bit Score: 42.15  E-value: 1.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2174213912 219 ESLEDMAMYISQ-EWDHQDHSKRAPSRDMVQDSYENVGTL 257
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-531 1.76e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 367 LVQAKEQPKKLHLCALCGKNFSNNSNLIRHQRI------HAAEKLCMDVECGEVFGGHPHFLSLHRTHVGEEAHKC--LE 438
Cdd:COG5048   279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgeSLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLN 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 439 CGKCFSQNTH-----LTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKP--YKCPECGEIFAHSSNLLRHQ 509
Cdd:COG5048   359 SSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHK 438

                         170       180
                  ....*....|....*....|..
gi 2174213912 510 RIHTGERPYRCSECGKSFSRSS 531
Cdd:COG5048   439 KIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
645-667 4.14e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.14e-05
                          10        20
                  ....*....|....*....|...
gi 2174213912 645 RHLRTHTGERPYKCSECGESFSR 667
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
41-151 8.73e-55

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 182.50  E-value: 8.73e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912   41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:smart00431   3 IFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLED 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2174213912  121 MQKELGKLRQQVTNQGRGAEVLLEEPLPLET 151
Cdd:smart00431  83 LERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 41-127 1.06e-43

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: 151.49  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912  41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:pfam02023   3 ASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAED 82


                  ....*..
gi 2174213912 121 MQKELGK 127
Cdd:pfam02023  83 LLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 41-122 7.35e-36

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: 129.69  E-value: 7.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912  41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:cd07936     3 TYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAED 82


                  ..
gi 2174213912 121 MQ 122
Cdd:cd07936    83 LL 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
460-646 2.83e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 460 KPFQCNVCGKSFSCNSNLNRHQRT--HTGE--KPYKCPE--CGEIFAHSSNLLRHQRIHTGERPYRC--SECGKSFSRSS 531
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 532 HLVIHERTHEKERLDP-LPECGQGINDSAPFLTNHRVEKklfecstcgksfrqgmHLTRH--QRTHtgekPYKCILCGEN 608
Cdd:COG5048   368 NNEPPQSLQQYKDLKNdKKSETLSNSCIRNFKRDSNLSL----------------HIITHlsFRPY----NCKNPPCSKS 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2174213912 609 FSHRSNLIRHQRIHTGEKPYTCHECGDSFS--HSSNRIRH 646
Cdd:COG5048   428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRdlDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
476-501 2.23e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 2.23e-06
                          10        20
                  ....*....|....*....|....*.
gi 2174213912 476 NLNRHQRTHTGEKPYKCPECGEIFAH 501
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 219-257 1.54e-05

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 42.15  E-value: 1.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2174213912 219 ESLEDMAMYISQ-EWDHQDHSKRAPSRDMVQDSYENVGTL 257
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-531 1.76e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 367 LVQAKEQPKKLHLCALCGKNFSNNSNLIRHQRI------HAAEKLCMDVECGEVFGGHPHFLSLHRTHVGEEAHKC--LE 438
Cdd:COG5048   279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgeSLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLN 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 439 CGKCFSQNTH-----LTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKP--YKCPECGEIFAHSSNLLRHQ 509
Cdd:COG5048   359 SSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHK 438

                         170       180
                  ....*....|....*....|..
gi 2174213912 510 RIHTGERPYRCSECGKSFSRSS 531
Cdd:COG5048   439 KIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
645-667 4.14e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.14e-05
                          10        20
                  ....*....|....*....|...
gi 2174213912 645 RHLRTHTGERPYKCSECGESFSR 667
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
626-679 9.13e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 9.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2174213912 626 KPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCS--ECGESFSRSSRLTSHQRTHT 679
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 434-456 9.14e-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: 39.59  E-value: 9.14e-05
                          10        20
                  ....*....|....*....|...
gi 2174213912 434 HKCLECGKCFSQNTHLTRHQRTH 456
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 488-560 5.68e-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: 36.38  E-value: 5.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2174213912 488 KPYkCPECGEIFAHSSNLLRHQRIHTgerpYRCSECGKSFSRSSHLVIHERTHEKERLDPLPECGQGINDSAP 560
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEI 68
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
41-151 8.73e-55

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 182.50  E-value: 8.73e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912   41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:smart00431   3 IFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLED 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2174213912  121 MQKELGKLRQQVTNQGRGAEVLLEEPLPLET 151
Cdd:smart00431  83 LERELDEPGQQVSAHVHGQEVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 41-127 1.06e-43

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: 151.49  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912  41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:pfam02023   3 ASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAED 82


                  ....*..
gi 2174213912 121 MQKELGK 127
Cdd:pfam02023  83 LLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 41-122 7.35e-36

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: 129.69  E-value: 7.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912  41 ASHLRFRRFRFQDASGPREALNQLQELCRGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELRPESGEEAVTLVER 120
Cdd:cd07936     3 TYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAED 82


                  ..
gi 2174213912 121 MQ 122
Cdd:cd07936    83 LL 84
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
460-646 2.83e-12

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 69.34  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 460 KPFQCNVCGKSFSCNSNLNRHQRT--HTGE--KPYKCPE--CGEIFAHSSNLLRHQRIHTGERPYRC--SECGKSFSRSS 531
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 532 HLVIHERTHEKERLDP-LPECGQGINDSAPFLTNHRVEKklfecstcgksfrqgmHLTRH--QRTHtgekPYKCILCGEN 608
Cdd:COG5048   368 NNEPPQSLQQYKDLKNdKKSETLSNSCIRNFKRDSNLSL----------------HIITHlsFRPY----NCKNPPCSKS 427

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2174213912 609 FSHRSNLIRHQRIHTGEKPYTCHECGDSFS--HSSNRIRH 646
Cdd:COG5048   428 FNRHYNLIPHKKIHTNHAPLLCSILKSFRRdlDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
434-675 1.06e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 434 HKCLECGKCFSQNTHLTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKPYKC--PECGEIFAHSSNLLRHQ 509
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSSLSSS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 510 rIHTGERPYRCSECGKSFSRSSHLVIHERTHEKERLDPLPEC-GQGINDSAPFLTNHRVEKKLFecstcGKSFRQGMHLT 588
Cdd:COG5048   114 -SSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNnSSSVNTPQSNSLHPPLPANSL-----SKDPSSNLSLL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 589 RHQRTHTGEKPYKCILCGENFSHRSNLIRHQRIHTGEKPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCSECGESFSRS 668
Cdd:COG5048   188 ISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPT 267


                  ....*..
gi 2174213912 669 SRLTSHQ 675
Cdd:COG5048   268 ASSQSSS 274
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
444-679 9.76e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 9.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 444 SQNTHLTRHQRTHTGEKPFQCNVCGKSFSCNSNLNRHQRTHTGEKPYKCPECGEIFAHSSNLLRHQRIHTGERPYRCSEC 523
Cdd:COG5048   181 SSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASES 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 524 G------KSFSRSSHLVIHERTHEKERLDPL-PECGQGINDSAPFLT-----NHRVEKKL-FEC--STCGKSFRQGMHLT 588
Cdd:COG5048   261 PrsslptASSQSSSPNESDSSSEKGFSLPIKsKQCNISFSRSSPLTRhlrsvNHSGESLKpFSCpySLCGKLFSRNDALK 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 589 RHQRTHTGEKPYKCILCGENFSHRSNL-------IRHQRIHTGEKPYTC--HECGDSFSHSSNRIRHLRTHTGERP--YK 657
Cdd:COG5048   341 RHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCK 420

                         250       260
                  ....*....|....*....|..
gi 2174213912 658 CSECGESFSRSSRLTSHQRTHT 679
Cdd:COG5048   421 NPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
369-673 2.21e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.01  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 369 QAKEQPKKLHLCALCGKNFSNNSNLIRHQRIHAAEKL--CMDVECGEVFG----GHPHFLSLHRTHVGEEAHKCL----- 437
Cdd:COG5048    25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPsqCSYSGCDKSFSrpleLSRHLRTHHNNPSDLNSKSLPlsnsk 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 438 -------ECGKCFSQNTHLTRHQRTHTGEKPFQCNVcgkSFSCNSNLNRHQRTHTGEKPYKCP-----------ECGEIF 499
Cdd:COG5048   105 asssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDL---LSISNLRNNPLPGNNSSSVNTPQSnslhpplpansLSKDPS 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 500 AHSSNLLRHQRIHTGERPYRCSECGKSFSRSSHLVIHERTHEKERLdPLPECGQGINDSAPFL--------TNHRVEKKL 571
Cdd:COG5048   182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSL-PLTTNSQLSPKSLLSQspsslsssDSSSSASES 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 572 FECSTCGKSFRQGMHLTRHQRTHTG-EKPYKCILCGENFSHRSNLIRHQR--IHTGE--KPYTCHE--CGDSFSHSSNRI 644
Cdd:COG5048   261 PRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALK 340

                         330       340
                  ....*....|....*....|....*....
gi 2174213912 645 RHLRTHTGERPYKCSECGESFSRSSRLTS 673
Cdd:COG5048   341 RHILLHTSISPAKEKLLNSSSKFSPLLNN 369
zf-H2C2_2 pfam13465
Zinc-finger double domain;
476-501 2.23e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.28  E-value: 2.23e-06
                          10        20
                  ....*....|....*....|....*.
gi 2174213912 476 NLNRHQRTHTGEKPYKCPECGEIFAH 501
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
448-473 2.88e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 2.88e-06
                          10        20
                  ....*....|....*....|....*.
gi 2174213912 448 HLTRHQRTHTGEKPFQCNVCGKSFSC 473
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
504-529 3.47e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 3.47e-06
                          10        20
                  ....*....|....*....|....*.
gi 2174213912 504 NLLRHQRIHTGERPYRCSECGKSFSR 529
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
614-639 1.26e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.26e-05
                          10        20
                  ....*....|....*....|....*.
gi 2174213912 614 NLIRHQRIHTGEKPYTCHECGDSFSH 639
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 219-257 1.54e-05

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 42.15  E-value: 1.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2174213912 219 ESLEDMAMYISQ-EWDHQDHSKRAPSRDMVQDSYENVGTL 257
Cdd:cd07765     1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
367-531 1.76e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.77  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 367 LVQAKEQPKKLHLCALCGKNFSNNSNLIRHQRI------HAAEKLCMDVECGEVFGGHPHFLSLHRTHVGEEAHKC--LE 438
Cdd:COG5048   279 DSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnhsgeSLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLN 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 439 CGKCFSQNTH-----LTRHQRTHTGEKPFQCNV--CGKSFSCNSNLNRHQRTHTGEKP--YKCPECGEIFAHSSNLLRHQ 509
Cdd:COG5048   359 SSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHK 438

                         170       180
                  ....*....|....*....|..
gi 2174213912 510 RIHTGERPYRCSECGKSFSRSS 531
Cdd:COG5048   439 KIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
586-611 3.68e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 2174213912 586 HLTRHQRTHTGEKPYKCILCGENFSH 611
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
645-667 4.14e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 4.14e-05
                          10        20
                  ....*....|....*....|...
gi 2174213912 645 RHLRTHTGERPYKCSECGESFSR 667
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
470-540 8.82e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 8.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2174213912 470 SFSCNSNLN-RHQRTHTGE----KPYKCPECGEIFAHSSNLLRHQRIHTGERPYRCS--ECGKSFSRSSHLVIHERTH 540
Cdd:COG5048     9 SSSNNSVLSsTPKSTLKSLsnapRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTH 86
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
626-679 9.13e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 9.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2174213912 626 KPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCS--ECGESFSRSSRLTSHQRTHT 679
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 434-456 9.14e-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: 39.59  E-value: 9.14e-05
                          10        20
                  ....*....|....*....|...
gi 2174213912 434 HKCLECGKCFSQNTHLTRHQRTH 456
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 518-540 1.33e-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: 39.21  E-value: 1.33e-04
                          10        20
                  ....*....|....*....|...
gi 2174213912 518 YRCSECGKSFSRSSHLVIHERTH 540
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 490-512 2.00e-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: 2.00e-04
                          10        20
                  ....*....|....*....|...
gi 2174213912 490 YKCPECGEIFAHSSNLLRHQRIH 512
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 656-678 4.43e-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: 37.66  E-value: 4.43e-04
                          10        20
                  ....*....|....*....|...
gi 2174213912 656 YKCSECGESFSRSSRLTSHQRTH 678
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 462-484 5.44e-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: 37.66  E-value: 5.44e-04
                          10        20
                  ....*....|....*....|...
gi 2174213912 462 FQCNVCGKSFSCNSNLNRHQRTH 484
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 572-594 1.19e-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: 1.19e-03
                          10        20
                  ....*....|....*....|...
gi 2174213912 572 FECSTCGKSFRQGMHLTRHQRTH 594
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 380-400 2.80e-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: 35.74  E-value: 2.80e-03
                          10        20
                  ....*....|....*....|.
gi 2174213912 380 CALCGKNFSNNSNLIRHQRIH 400
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 458-540 3.17e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174213912 458 GEKPFQCNV--CGKSFScNSNLNRHQRTHTGEKPYKCPECGEIfahssnllRHQRIHTGERPYRCSECGKSFSRSSHLVI 535
Cdd:COG5189   346 DGKPYKCPVegCNKKYK-NQNGLKYHMLHGHQNQKLHENPSPE--------KMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*
gi 2174213912 536 HeRTH 540
Cdd:COG5189   417 H-RKH 420
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 488-560 5.68e-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: 36.38  E-value: 5.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2174213912 488 KPYkCPECGEIFAHSSNLLRHQRIHTgerpYRCSECGKSFSRSSHLVIHERTHEKERLDPLPECGQGINDSAP 560
Cdd:cd20908     1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEI 68
 
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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