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Conserved domains on  [gi|1622922175|ref|XP_014989879|]
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zinc finger protein with KRAB and SCAN domains 5 isoform X4 [Macaca mulatta]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 18089715)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription; similar to Homo sapiens zinc finger protein 714

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217|GO:0003700
PubMed:  8183940|22803940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB super family cl42959
krueppel associated box;
73-111 3.12e-14

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 67.62  E-value: 3.12e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622922175   73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMGYE 111
Cdd:smart00349   5 DVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
390-688 1.81e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 390 HKKSSTGERPHKCNECGKSFIQSAHLIQHQRIHTGEKPFRC--EECGKSYNQRVHLTQHQRVHTGEKPYTC--PLCGKAF 465
Cdd:COG5048    24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 466 RVRSHLVQHQSVHSgERPFKCNECGKGFGRRSHLAGHLRLHSREKAHQCRECGEIFFQY--VSLIEHQVLHMGQKNEKHG 543
Cdd:COG5048   104 KASSSSLSSSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPANSLSKDPSS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 544 VCEEAYSWNLTVIEDKKIELQEQ--------------------PYQCDICGKAFGYSSDLIQHYRTHTAEKPYQCDTCRE 603
Cdd:COG5048   183 NLSLLISSNVSTSIPSSSENSPLsssysipssssdqnlensssSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 604 NVGQCSHTKQHQKIYSS-------TKSHQCHECGRGFTLKPHLNQHQR--IHTGE--KPFQCKE--CGMNFSWSCSLFKH 670
Cdd:COG5048   263 SSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330
                  ....*....|....*...
gi 1622922175 671 LRSHERTDPINTLSVEGS 688
Cdd:COG5048   343 ILLHTSISPAKEKLLNSS 360
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-262 1.77e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....
gi 1622922175 239 HLTQHQRVHTGEKPYKCQVCGKAF 262
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-236 1.26e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622922175 211 NFIQHRRIHTGEKPFKCGECGKSYNQ 236
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
73-111 3.12e-14

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 67.62  E-value: 3.12e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622922175   73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMGYE 111
Cdd:smart00349   5 DVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 73-108 6.21e-13

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: 63.34  E-value: 6.21e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622922175  73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSM 108
Cdd:cd07765     5 DVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 73-109 3.57e-12

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 60.95  E-value: 3.57e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622922175  73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMG 109
Cdd:pfam01352   6 DVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
390-688 1.81e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 390 HKKSSTGERPHKCNECGKSFIQSAHLIQHQRIHTGEKPFRC--EECGKSYNQRVHLTQHQRVHTGEKPYTC--PLCGKAF 465
Cdd:COG5048    24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 466 RVRSHLVQHQSVHSgERPFKCNECGKGFGRRSHLAGHLRLHSREKAHQCRECGEIFFQY--VSLIEHQVLHMGQKNEKHG 543
Cdd:COG5048   104 KASSSSLSSSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPANSLSKDPSS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 544 VCEEAYSWNLTVIEDKKIELQEQ--------------------PYQCDICGKAFGYSSDLIQHYRTHTAEKPYQCDTCRE 603
Cdd:COG5048   183 NLSLLISSNVSTSIPSSSENSPLsssysipssssdqnlensssSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 604 NVGQCSHTKQHQKIYSS-------TKSHQCHECGRGFTLKPHLNQHQR--IHTGE--KPFQCKE--CGMNFSWSCSLFKH 670
Cdd:COG5048   263 SSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330
                  ....*....|....*...
gi 1622922175 671 LRSHERTDPINTLSVEGS 688
Cdd:COG5048   343 ILLHTSISPAKEKLLNSS 360
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-439 1.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.64e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622922175 414 HLIQHQRIHTGEKPFRCEECGKSYNQ 439
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-262 1.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....
gi 1622922175 239 HLTQHQRVHTGEKPYKCQVCGKAF 262
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-236 1.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622922175 211 NFIQHRRIHTGEKPFKCGECGKSYNQ 236
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 400-450 3.14e-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: 37.15  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622922175 400 HKCNECGKSFIQSAHLIQHQRIHTgekpFRCEECGKSYNQ----RVHLTQhqrVH 450
Cdd:cd20908     2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTagglAVHCLQ---VH 49
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
73-111 3.12e-14

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 67.62  E-value: 3.12e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622922175   73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMGYE 111
Cdd:smart00349   5 DVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 73-108 6.21e-13

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: 63.34  E-value: 6.21e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622922175  73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSM 108
Cdd:cd07765     5 DVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 73-109 3.57e-12

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 60.95  E-value: 3.57e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622922175  73 DVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMG 109
Cdd:pfam01352   6 DVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
390-688 1.81e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.85  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 390 HKKSSTGERPHKCNECGKSFIQSAHLIQHQRIHTGEKPFRC--EECGKSYNQRVHLTQHQRVHTGEKPYTC--PLCGKAF 465
Cdd:COG5048    24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 466 RVRSHLVQHQSVHSgERPFKCNECGKGFGRRSHLAGHLRLHSREKAHQCRECGEIFFQY--VSLIEHQVLHMGQKNEKHG 543
Cdd:COG5048   104 KASSSSLSSSSSNS-NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTpqSNSLHPPLPANSLSKDPSS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 544 VCEEAYSWNLTVIEDKKIELQEQ--------------------PYQCDICGKAFGYSSDLIQHYRTHTAEKPYQCDTCRE 603
Cdd:COG5048   183 NLSLLISSNVSTSIPSSSENSPLsssysipssssdqnlensssSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPR 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 604 NVGQCSHTKQHQKIYSS-------TKSHQCHECGRGFTLKPHLNQHQR--IHTGE--KPFQCKE--CGMNFSWSCSLFKH 670
Cdd:COG5048   263 SSLPTASSQSSSPNESDsssekgfSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRH 342

                         330
                  ....*....|....*...
gi 1622922175 671 LRSHERTDPINTLSVEGS 688
Cdd:COG5048   343 ILLHTSISPAKEKLLNSS 360
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
609-674 1.36e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622922175 609 SHTKQHQKIYSSTKSHQCHECGRGFTLKPHLNQHQRIHTGEKPFQC--KECGMNFSWSCSLFKHLRSH 674
Cdd:COG5048    19 TPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTH 86
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
169-613 1.59e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 169 SRQNPSQKRNPDVITDLSPKQSTHgERGHRCSDCGKFFLQASNFIQHRRIHTGEKPFKCG--ECGKSYNQRVHLTQHQRV 246
Cdd:COG5048     7 QSSSSNNSVLSSTPKSTLKSLSNA-PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 247 HTGEKPYKC--QVCGKAFRVSSHLVQHHSVHSgerPYGCNECGKNFGRHSHLIEHLKRHFREKSQRCSDKRSKNTKLSVK 324
Cdd:COG5048    86 HHNNPSDLNskSLPLSNSKASSSSLSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 325 KKISEYSEADMELSGKTQRNVSQVqdfgegyelQSKLDRKQGIPMKEIVGQPSSKRMNYSEVPYVHKKSSTGERPhkCNE 404
Cdd:COG5048   163 QSNSLHPPLPANSLSKDPSSNLSL---------LISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLP--LTT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 405 CgkSFIQSAHLIQHQRIHTGEK--PFRCEECGKSYNQRVHLTQHQRVHTGE-------KPYTCPLCGKAFRVRSHLVQHQ 475
Cdd:COG5048   232 N--SQLSPKSLLSQSPSSLSSSdsSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 476 --SVHSGE--RPFKCNE--CGKGFGRRSHLAGHLRLHSREKAHQCRECGEIFFQYVSLIE--------HQVLHMGQKNEK 541
Cdd:COG5048   310 rsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNeppqslqqYKDLKNDKKSET 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622922175 542 HGVCEEAYSW-NLTVIEDKKIELQEQPYQCD--ICGKAFGYSSDLIQHYRTHTAEKPYQCDTCRENVGQ---CSHTKQ 613
Cdd:COG5048   390 LSNSCIRNFKrDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDldlSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
414-439 1.64e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.64e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622922175 414 HLIQHQRIHTGEKPFRCEECGKSYNQ 439
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
239-262 1.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....
gi 1622922175 239 HLTQHQRVHTGEKPYKCQVCGKAF 262
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
442-465 2.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.34e-04
                          10        20
                  ....*....|....*....|....
gi 1622922175 442 HLTQHQRVHTGEKPYTCPLCGKAF 465
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
638-662 5.02e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.02e-04
                          10        20
                  ....*....|....*....|....*
gi 1622922175 638 HLNQHQRIHTGEKPFQCKECGMNFS 662
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
251-662 7.09e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 251 KPYKCQVCGKAFRVSSHLVQHHSVHSGERPYGCN--ECGKNFGRHSHLIEHLKRHFREKSQRCSDKRSKNTKLSVKKKIS 328
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 329 EYSEADMELSGktqrnvsqvqdfgegyelqskldrkqgipmkeIVGQPSSKRMNYSEVPYVHKKSSTGERPHK-CNECGK 407
Cdd:COG5048   112 SSSSNSNDNNL--------------------------------LSSHSLPPSSRDPQLPDLLSISNLRNNPLPgNNSSSV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 408 SFIQSAHLIQhqrihtgEKPFRCEECGKSYNQRVHLtqHQRVHTGEKPYTCPLCGKAFRVRSHLVQHQSVHSGERPFKCN 487
Cdd:COG5048   160 NTPQSNSLHP-------PLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 488 ECGKGFGRRSHLAGHLRLHSREKAHQCRECGEIFFQYVSLIEHQVLHMGQKNEKhgvceeayswnltviedkkieLQEQP 567
Cdd:COG5048   231 TNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEK---------------------GFSLP 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922175 568 YQCDICGKAFGYSSDLIQHYRthtaekpyqcdtcrenvgQCSHTKQHQKIYSSTKShqchECGRGFTLKPHLNQHQRIHT 647
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLR------------------SVNHSGESLKPFSCPYS----LCGKLFSRNDALKRHILLHT 347

                         410
                  ....*....|....*
gi 1622922175 648 GEKPFQCKECGMNFS 662
Cdd:COG5048   348 SISPAKEKLLNSSSK 362
zf-H2C2_2 pfam13465
Zinc-finger double domain;
211-236 1.26e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622922175 211 NFIQHRRIHTGEKPFKCGECGKSYNQ 236
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 400-422 2.04e-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: 2.04e-03
                          10        20
                  ....*....|....*....|...
gi 1622922175 400 HKCNECGKSFIQSAHLIQHQRIH 422
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 400-450 3.14e-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: 37.15  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622922175 400 HKCNECGKSFIQSAHLIQHQRIHTgekpFRCEECGKSYNQ----RVHLTQhqrVH 450
Cdd:cd20908     2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTagglAVHCLQ---VH 49
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 428-450 6.05e-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: 34.58  E-value: 6.05e-03
                          10        20
                  ....*....|....*....|...
gi 1622922175 428 FRCEECGKSYNQRVHLTQHQRVH 450
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 568-590 7.66e-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: 34.20  E-value: 7.66e-03
                          10        20
                  ....*....|....*....|...
gi 1622922175 568 YQCDICGKAFGYSSDLIQHYRTH 590
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 225-247 8.45e-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: 34.20  E-value: 8.45e-03
                          10        20
                  ....*....|....*....|...
gi 1622922175 225 FKCGECGKSYNQRVHLTQHQRVH 247
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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