NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|150010617|ref|NP_001092793|]
View 

zinc finger protein 483 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 44-132 3.75e-42

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: 147.63  E-value: 3.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617   44 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLV 123
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 150010617  124 EDLNQTLEE 132
Cdd:pfam02023  81 EDLLLERGE 89
KRAB smart00349
krueppel associated box;
170-223 7.77e-20

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 7.77e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 150010617   170 VTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFLGSPVSKLDLISHLK 223
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
537-725 1.28e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 537 KPYTCKECGKSFTHSSSLSKHQR--IHTGE--KPYKCNE--CGKAFRQNSCLTRHQKIHTGEKPFLCKDCGLSF------ 604
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSkfspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 605 --RLFSSIMYHQRLHAgEKPYKCTH--CEKGFPSHSRLSRHLRCHTGAKPYKCKecgktfrqssslnlhirthtgekpyk 680
Cdd:COG5048  368 nnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCK-------------------------- 420

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 150010617 681 CDYCGAAFTRSTILIEHVKTHTNVQYECkKCGKTFKSRTTSLKHH 725
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHTNHAPLL-CSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
462-608 1.23e-06

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 462 KAPKASASPKPHNKADRK--EKRYKCDECGKRFAELYFLTHHQRT--HTGE--KPYVCKH--CGRPFSDYSSFYQHQRIH 533
Cdd:COG5048  267 TASSQSSSPNESDSSSEKgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 534 TGEKPYTCK--ECGKSFTHSSSLSKHQRIHT-------------------------------------GEKPYKCNECGK 574
Cdd:COG5048  347 TSISPAKEKllNSSSKFSPLLNNEPPQSLQQykdlkndkksetlsnscirnfkrdsnlslhiithlsfRPYNCKNPPCSK 426

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150010617 575 AFRQNSCLTRHQKIHTGEKPFLCKDCGLSFRLFS 608
Cdd:COG5048  427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
PRK07219 super family cl35562
DNA topoisomerase I; Validated
 383-489 5.68e-03

DNA topoisomerase I; Validated


The actual alignment was detected with superfamily member PRK07219:

Pssm-ID: 235971 [Multi-domain]  Cd Length: 822  Bit Score: 39.98  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 383 PKIGSLS-KTETCSKCGVAFTQILENCIE-SSQCEKCRKNlfqdeapnQDKEPDPEEASKCGKC-GKAFEPGTKRSVCLE 459
Cdd:PRK07219 639 PSTGRIKvLDEVCEKCGLPVIKILRGKQTfVVGCPDCEAE--------KEEEDPDEVIGPCPKCgGELAIKQLKYGSFLG 710

                         90       100       110
                 ....*....|....*....|....*....|
gi 150010617 460 CRKAPKASASPKPHNKADRKEKRYKCDECG 489
Cdd:PRK07219 711 CTNYPKCKYTLPLPRRGKITVTDEKCPECG 740
 
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 ...
 44-132 3.75e-42

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: 147.63  E-value: 3.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617   44 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLV 123
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 150010617  124 EDLNQTLEE 132
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
45-132 3.05e-40

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 143.21  E-value: 3.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617    45 ESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLVE 124
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81


                   ....*...
gi 150010617   125 DLNQTLEE 132
Cdd:smart00431  82 DLERELDE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 44-126 9.02e-37

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: 132.38  E-value: 9.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617  44 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLV 123
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ...
gi 150010617 124 EDL 126
Cdd:cd07936   81 EDL 83
KRAB smart00349
krueppel associated box;
170-223 7.77e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 7.77e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 150010617   170 VTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFLGSPVSKLDLISHLK 223
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 169-210 5.10e-18

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: 77.90  E-value: 5.10e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 150010617  169 SVTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFLG 210
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 170-209 3.51e-16

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: 72.58  E-value: 3.51e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 150010617 170 VTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFL 209
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
537-725 1.28e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 537 KPYTCKECGKSFTHSSSLSKHQR--IHTGE--KPYKCNE--CGKAFRQNSCLTRHQKIHTGEKPFLCKDCGLSF------ 604
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSkfspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 605 --RLFSSIMYHQRLHAgEKPYKCTH--CEKGFPSHSRLSRHLRCHTGAKPYKCKecgktfrqssslnlhirthtgekpyk 680
Cdd:COG5048  368 nnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCK-------------------------- 420

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 150010617 681 CDYCGAAFTRSTILIEHVKTHTNVQYECkKCGKTFKSRTTSLKHH 725
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHTNHAPLL-CSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
462-608 1.23e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 462 KAPKASASPKPHNKADRK--EKRYKCDECGKRFAELYFLTHHQRT--HTGE--KPYVCKH--CGRPFSDYSSFYQHQRIH 533
Cdd:COG5048  267 TASSQSSSPNESDSSSEKgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 534 TGEKPYTCK--ECGKSFTHSSSLSKHQRIHT-------------------------------------GEKPYKCNECGK 574
Cdd:COG5048  347 TSISPAKEKllNSSSKFSPLLNNEPPQSLQQykdlkndkksetlsnscirnfkrdsnlslhiithlsfRPYNCKNPPCSK 426

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150010617 575 AFRQNSCLTRHQKIHTGEKPFLCKDCGLSFRLFS 608
Cdd:COG5048  427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
553-578 3.86e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.86e-05
                          10        20
                  ....*....|....*....|....*.
gi 150010617  553 SLSKHQRIHTGEKPYKCNECGKAFRQ 578
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 510-557 3.60e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 41.01  E-value: 3.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 150010617 510 PYVCKHCGRPFSDYSSFYQHQRIHTGEKpyTCKECGKSFTHSSSLSKH 557
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 509-561 3.70e-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: 39.85  E-value: 3.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 150010617 509 KPYvCKHCGRPFSDYSSFYQHQRIHTgekpYTCKECGKSFTHSSSLSKH-QRIH 561
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49
PRK07219 PRK07219
DNA topoisomerase I; Validated
 383-489 5.68e-03

DNA topoisomerase I; Validated


Pssm-ID: 235971 [Multi-domain]  Cd Length: 822  Bit Score: 39.98  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 383 PKIGSLS-KTETCSKCGVAFTQILENCIE-SSQCEKCRKNlfqdeapnQDKEPDPEEASKCGKC-GKAFEPGTKRSVCLE 459
Cdd:PRK07219 639 PSTGRIKvLDEVCEKCGLPVIKILRGKQTfVVGCPDCEAE--------KEEEDPDEVIGPCPKCgGELAIKQLKYGSFLG 710

                         90       100       110
                 ....*....|....*....|....*....|
gi 150010617 460 CRKAPKASASPKPHNKADRKEKRYKCDECG 489
Cdd:PRK07219 711 CTNYPKCKYTLPLPRRGKITVTDEKCPECG 740
PHA00733 PHA00733
hypothetical protein
 678-726 7.49e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 150010617 678 PYKCDYCGAAFTRSTILIEHVK--THTNVqyeCKKCGKTFKSRTTSLKHHC 726
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKV---CPVCGKEFRNTDSTLDHVC 120
 
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 ...
 44-132 3.75e-42

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: 147.63  E-value: 3.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617   44 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLV 123
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ....*....
gi 150010617  124 EDLNQTLEE 132
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
45-132 3.05e-40

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 143.21  E-value: 3.05e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617    45 ESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLVE 124
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81


                   ....*...
gi 150010617   125 DLNQTLEE 132
Cdd:smart00431  82 DLERELDE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 44-126 9.02e-37

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: 132.38  E-value: 9.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617  44 LESFRQKFRWFCYSQEEGPRKTLNQLWELCKQWLRPDIHTKEQILELLVFEQFLRVLPGEMRIWVNSQHPGSSVEVVTLV 123
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ...
gi 150010617 124 EDL 126
Cdd:cd07936   81 EDL 83
KRAB smart00349
krueppel associated box;
170-223 7.77e-20

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 83.41  E-value: 7.77e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 150010617   170 VTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFLGSPVSKLDLISHLK 223
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLE 54
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 169-210 5.10e-18

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: 77.90  E-value: 5.10e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 150010617  169 SVTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFLG 210
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 170-209 3.51e-16

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: 72.58  E-value: 3.51e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 150010617 170 VTFEDVSVDFSRGEWKLLEPSQRELYKEVLLENLGTLEFL 209
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
537-725 1.28e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.78  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 537 KPYTCKECGKSFTHSSSLSKHQR--IHTGE--KPYKCNE--CGKAFRQNSCLTRHQKIHTGEKPFLCKDCGLSF------ 604
Cdd:COG5048  288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSkfspll 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 605 --RLFSSIMYHQRLHAgEKPYKCTH--CEKGFPSHSRLSRHLRCHTGAKPYKCKecgktfrqssslnlhirthtgekpyk 680
Cdd:COG5048  368 nnEPPQSLQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCK-------------------------- 420

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 150010617 681 CDYCGAAFTRSTILIEHVKTHTNVQYECkKCGKTFKSRTTSLKHH 725
Cdd:COG5048  421 NPPCSKSFNRHYNLIPHKKIHTNHAPLL-CSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
309-725 5.01e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 309 TSSGKRVKQTSDtlkhRKASLSKMSQRSKEgKKPFSFHSALVNRRELR---REKSRKCGEPEKDPRRhLSPAERKRHPKI 385
Cdd:COG5048   12 NNSVLSSTPKST----LKSLSNAPRPDSCP-NCTDSFSRLEHLTRHIRshtGEKPSQCSYSGCDKSF-SRPLELSRHLRT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 386 GSLSKTETCSKCGVAFTQILENCIESSQCEKCRKNLFQDEAPNQDKEPDPEEASKCGKC--GKAFEPGTKRSVClecrKA 463
Cdd:COG5048   86 HHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISnlRNNPLPGNNSSSV----NT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 464 PKASASPKPHNKADRKEKRYKCDEcgkrfaelyFLTHHQRTHTGEKPYVCKHCgRPFSDYSSFYQHQRIHTGEKPYTCKE 543
Cdd:COG5048  162 PQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPL-SSSYSIPSSSSDQNLENSSSSLPLTT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 544 CGKSFTHSSSLSKHQRIHTGEKPYKCNECGKAFRQNSCLTRHQKIHTGE-------KPFLCKDCGLSFRLFSSIMYHQR- 615
Cdd:COG5048  232 NSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRs 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 616 -LHAGE--KPYKCTH--CEKGFPSHSRLSRHLRCHTGAKPYKCKECGKTFRQSSSLN----LHIRTHTGEKPYK---CDY 683
Cdd:COG5048  312 vNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppQSLQQYKDLKNDKkseTLS 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 150010617 684 --CGAAFTRSTILIEHVKTHTNVQYECKKCGKTFK--SRTTSLKHH 725
Cdd:COG5048  392 nsCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKsfNRHYNLIPH 437
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
462-608 1.23e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 462 KAPKASASPKPHNKADRK--EKRYKCDECGKRFAELYFLTHHQRT--HTGE--KPYVCKH--CGRPFSDYSSFYQHQRIH 533
Cdd:COG5048  267 TASSQSSSPNESDSSSEKgfSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 534 TGEKPYTCK--ECGKSFTHSSSLSKHQRIHT-------------------------------------GEKPYKCNECGK 574
Cdd:COG5048  347 TSISPAKEKllNSSSKFSPLLNNEPPQSLQQykdlkndkksetlsnscirnfkrdsnlslhiithlsfRPYNCKNPPCSK 426

                        170       180       190
                 ....*....|....*....|....*....|....
gi 150010617 575 AFRQNSCLTRHQKIHTGEKPFLCKDCGLSFRLFS 608
Cdd:COG5048  427 SFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
553-578 3.86e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.82  E-value: 3.86e-05
                          10        20
                  ....*....|....*....|....*.
gi 150010617  553 SLSKHQRIHTGEKPYKCNECGKAFRQ 578
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
665-690 8.37e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 8.37e-05
                          10        20
                  ....*....|....*....|....*.
gi 150010617  665 SLNLHIRTHTGEKPYKCDYCGAAFTR 690
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
649-727 8.84e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 649 KPYKCKECGKTFRQSSSLNLHIRTHTGEKPYKCDY--CGAAFTRSTILIEHVKTHTN--VQYECKKCGKTFKSRTTSLKH 724
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNnpSDLNSKSLPLSNSKASSSSLS 111


                 ...
gi 150010617 725 HCT 727
Cdd:COG5048  112 SSS 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
525-550 9.14e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 9.14e-05
                          10        20
                  ....*....|....*....|....*.
gi 150010617  525 SFYQHQRIHTGEKPYTCKECGKSFTH 550
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 651-673 1.10e-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: 39.59  E-value: 1.10e-04
                          10        20
                  ....*....|....*....|...
gi 150010617  651 YKCKECGKTFRQSSSLNLHIRTH 673
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 539-561 1.83e-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: 1.83e-04
                          10        20
                  ....*....|....*....|...
gi 150010617  539 YTCKECGKSFTHSSSLSKHQRIH 561
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
637-662 3.21e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.21e-04
                          10        20
                  ....*....|....*....|....*.
gi 150010617  637 RLSRHLRCHTGAKPYKCKECGKTFRQ 662
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA00733 PHA00733
hypothetical protein
 510-557 3.60e-04

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 41.01  E-value: 3.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 150010617 510 PYVCKHCGRPFSDYSSFYQHQRIHTGEKpyTCKECGKSFTHSSSLSKH 557
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDH 118
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 509-561 3.70e-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: 39.85  E-value: 3.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 150010617 509 KPYvCKHCGRPFSDYSSFYQHQRIHTgekpYTCKECGKSFTHSSSLSKH-QRIH 561
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 ...
 567-589 4.83e-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: 4.83e-04
                          10        20
                  ....*....|....*....|...
gi 150010617  567 YKCNECGKAFRQNSCLTRHQKIH 589
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
621-727 6.73e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 621 KPYKCTHCEKGFPSHSRLSRHLRCHTGAKPYKCKECGKTFRQSSSLNL--HIRTHTGEKPYKCDYCG--AAFTRSTILIE 696
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDLNSKSLplSNSKASSSSLS 111

                         90       100       110
                 ....*....|....*....|....*....|.
gi 150010617 697 HVKTHTNVQYECKKCGKTFKSRTTSLKHHCT 727
Cdd:COG5048  112 SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLS 142
PRK07219 PRK07219
DNA topoisomerase I; Validated
 383-489 5.68e-03

DNA topoisomerase I; Validated


Pssm-ID: 235971 [Multi-domain]  Cd Length: 822  Bit Score: 39.98  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150010617 383 PKIGSLS-KTETCSKCGVAFTQILENCIE-SSQCEKCRKNlfqdeapnQDKEPDPEEASKCGKC-GKAFEPGTKRSVCLE 459
Cdd:PRK07219 639 PSTGRIKvLDEVCEKCGLPVIKILRGKQTfVVGCPDCEAE--------KEEEDPDEVIGPCPKCgGELAIKQLKYGSFLG 710

                         90       100       110
                 ....*....|....*....|....*....|
gi 150010617 460 CRKAPKASASPKPHNKADRKEKRYKCDECG 489
Cdd:PRK07219 711 CTNYPKCKYTLPLPRRGKITVTDEKCPECG 740
PHA00733 PHA00733
hypothetical protein
 678-726 7.49e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 37.16  E-value: 7.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 150010617 678 PYKCDYCGAAFTRSTILIEHVK--THTNVqyeCKKCGKTFKSRTTSLKHHC 726
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRytEHSKV---CPVCGKEFRNTDSTLDHVC 120
PRK05580 PRK05580
primosome assembly protein PriA; Validated
 594-659 7.61e-03

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 39.75  E-value: 7.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150010617 594 PF-LCKDCGLSFrlfssimyhqrlhagekpyKCTHCEKGFPSHsRLSRHLRCH----TGAKPYKCKECGKT 659
Cdd:PRK05580 380 PFlLCRDCGWVA-------------------ECPHCDASLTLH-RFQRRLRCHhcgyQEPIPKACPECGST 430
PHA00733 PHA00733
hypothetical protein
 650-701 9.90e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 36.78  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 150010617 650 PYKCKECGKTFRQSSSLNLHIRTHTGEKpyKCDYCGAAFTRSTILIEHV-KTH 701
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIRYTEHSK--VCPVCGKEFRNTDSTLDHVcKKH 123
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH