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Conserved domains on  [gi|1207181033|ref|XP_021333427|]
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sal-like protein 2 [Danio rerio]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 15770114)

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
SUF4-like super family cl41227
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
364-420 1.58e-06

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.


The actual alignment was detected with superfamily member cd20908:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 47.17  E-value: 1.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207181033  364 HICRFCGKVLSSDSSLQIHLRSHTgerpYQCPVCLSRFTTRGNLKAHFLR-HREQNPE 420
Cdd:cd20908      2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQvHKETLTK 55
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
729-751 2.02e-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: 2.02e-04
                           10        20
                   ....*....|....*....|...
gi 1207181033  729 FPCKLCGRSFSTKGSLRAHLATH 751
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
1052-1074 2.30e-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: 2.30e-03
                           10        20
                   ....*....|....*....|...
gi 1207181033 1052 YSCTECGKEYASRSGLKGHMKIH 1074
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03378 super family cl33729
EBNA-3B; Provisional
58-268 4.11e-03

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.21  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207181033   58 QPPLAP-RPSPGGlHAPSL-----PNESSSPPHWPNHIASYSTSLPNAHSSLSPDFPHPSLSSQTHSPPPGQQKSTRISS 131
Cdd:PHA03378   668 QIGHIPyQPSPTG-ANTMLpiqwaPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207181033  132 HQPHSTVTSPPMGISATTTTSSLSSSSSLGAPPHQGSPSPIHQTPSSPS--EQLQVPPTlavlleELRVLQQRQIHQMQI 209
Cdd:PHA03378   747 PAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTpqPPPQAGPT------SMQLMPRAAPGQQGP 820
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207181033  210 TEEICRQVLRLGGMVSAPDAPQGSVEGQQRDAGSSSPPNGVSGASLInQAPVSKPNLSQ 268
Cdd:PHA03378   821 TKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIV-QAPVFYPPVLQ 878
 
Name Accession Description Interval E-value
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
364-420 1.58e-06

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: 47.17  E-value: 1.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207181033  364 HICRFCGKVLSSDSSLQIHLRSHTgerpYQCPVCLSRFTTRGNLKAHFLR-HREQNPE 420
Cdd:cd20908      2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQvHKETLTK 55
zf-H2C2_2 pfam13465
Zinc-finger double domain;
378-403 1.51e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.51e-05
                           10        20
                   ....*....|....*....|....*.
gi 1207181033  378 SLQIHLRSHTGERPYQCPVCLSRFTT 403
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
729-751 2.02e-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: 2.02e-04
                           10        20
                   ....*....|....*....|...
gi 1207181033  729 FPCKLCGRSFSTKGSLRAHLATH 751
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
1052-1074 2.30e-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: 2.30e-03
                           10        20
                   ....*....|....*....|...
gi 1207181033 1052 YSCTECGKEYASRSGLKGHMKIH 1074
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03378 PHA03378
EBNA-3B; Provisional
58-268 4.11e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.21  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207181033   58 QPPLAP-RPSPGGlHAPSL-----PNESSSPPHWPNHIASYSTSLPNAHSSLSPDFPHPSLSSQTHSPPPGQQKSTRISS 131
Cdd:PHA03378   668 QIGHIPyQPSPTG-ANTMLpiqwaPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207181033  132 HQPHSTVTSPPMGISATTTTSSLSSSSSLGAPPHQGSPSPIHQTPSSPS--EQLQVPPTlavlleELRVLQQRQIHQMQI 209
Cdd:PHA03378   747 PAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTpqPPPQAGPT------SMQLMPRAAPGQQGP 820
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207181033  210 TEEICRQVLRLGGMVSAPDAPQGSVEGQQRDAGSSSPPNGVSGASLInQAPVSKPNLSQ 268
Cdd:PHA03378   821 TKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIV-QAPVFYPPVLQ 878
ZnF_C2H2 smart00355
zinc finger;
1052-1074 7.55e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 7.55e-03
                            10        20
                    ....*....|....*....|...
gi 1207181033  1052 YSCTECGKEYASRSGLKGHMKIH 1074
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
364-420 1.58e-06

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: 47.17  E-value: 1.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207181033  364 HICRFCGKVLSSDSSLQIHLRSHTgerpYQCPVCLSRFTTRGNLKAHFLR-HREQNPE 420
Cdd:cd20908      2 PWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHCLQvHKETLTK 55
zf-H2C2_2 pfam13465
Zinc-finger double domain;
378-403 1.51e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.74  E-value: 1.51e-05
                           10        20
                   ....*....|....*....|....*.
gi 1207181033  378 SLQIHLRSHTGERPYQCPVCLSRFTT 403
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
729-751 2.02e-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: 2.02e-04
                           10        20
                   ....*....|....*....|...
gi 1207181033  729 FPCKLCGRSFSTKGSLRAHLATH 751
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
729-751 1.30e-03

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


Pssm-ID: 464025  Cd Length: 24  Bit Score: 37.24  E-value: 1.30e-03
                           10        20
                   ....*....|....*....|...
gi 1207181033  729 FPCKLCGRSFSTKGSLRAHLATH 751
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
1052-1074 2.30e-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: 2.30e-03
                           10        20
                   ....*....|....*....|...
gi 1207181033 1052 YSCTECGKEYASRSGLKGHMKIH 1074
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
729-754 2.99e-03

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 36.07  E-value: 2.99e-03
                           10        20
                   ....*....|....*....|....*.
gi 1207181033  729 FPCKLCGRSFSTKGSLRAHLATHRAR 754
Cdd:pfam13912    2 HECSECGKSFPSYQALGGHKKSHRKE 27
PHA03378 PHA03378
EBNA-3B; Provisional
58-268 4.11e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.21  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207181033   58 QPPLAP-RPSPGGlHAPSL-----PNESSSPPHWPNHIASYSTSLPNAHSSLSPDFPHPSLSSQTHSPPPGQQKSTRISS 131
Cdd:PHA03378   668 QIGHIPyQPSPTG-ANTMLpiqwaPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARP 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207181033  132 HQPHSTVTSPPMGISATTTTSSLSSSSSLGAPPHQGSPSPIHQTPSSPS--EQLQVPPTlavlleELRVLQQRQIHQMQI 209
Cdd:PHA03378   747 PAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTpqPPPQAGPT------SMQLMPRAAPGQQGP 820
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207181033  210 TEEICRQVLRLGGMVSAPDAPQGSVEGQQRDAGSSSPPNGVSGASLInQAPVSKPNLSQ 268
Cdd:PHA03378   821 TKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIV-QAPVFYPPVLQ 878
ZnF_C2H2 smart00355
zinc finger;
1052-1074 7.55e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 7.55e-03
                            10        20
                    ....*....|....*....|...
gi 1207181033  1052 YSCTECGKEYASRSGLKGHMKIH 1074
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 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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