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Conserved domains on  [gi|254281232|ref|NP_001156863|]
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zinc finger and SCAN domain-containing protein 12 [Homo sapiens]

Protein Classification

SCAN and COG5048 domain-containing protein( domain architecture ID 12210946)

protein containing domains SCAN, COG5048, and zf-C2H2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-152 4.85e-69

leucine rich region;


:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 219.10  E-value: 4.85e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232    42 REVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVL 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 254281232   122 EDLERELDEPGEQVSVHTGEQEMFLQETVRL 152
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPL 111
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
299-579 8.67e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.88  E-value: 8.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 299 DRPYKCEECGKAFRGRTVLIRHKIIHTGEKPYKCN--ECGKAFGRWSALNQHQRLHTGEK-HYHCNDCGKAFSQKAGLFH 375
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPsDLNSKSLPLSNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 376 HIKIHTRDKPYQCTQCNKSFSRRSILTQ--------------------------------------------------HQ 405
Cdd:COG5048  111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPdllsisnlrnnplpgnnsssvntpqsnslhpplpanslskdpssnlslliSS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 406 GVHTGAKPYECNECGKAFVYNSSLVSHQEIHHKEKCYQCKECGKSFSQSgLIQHQRIHTGEK---PYKCDVCEKAFI-QR 481
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS-LLSQSPSSLSSSdssSSASESPRSSLPtAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 482 TSLTEHQRIHTGER-----PYKCDKCGKAFTQRSVLTEHQR--IHTGE--RPYKCDE--CGNAFRGITSLIQHQRIHTGE 550
Cdd:COG5048  270 SQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350
                 ....*....|....*....|....*....|.
gi 254281232 551 KPYQC--DECGKAFRQRSDLSKHQRIHNRRG 579
Cdd:COG5048  350 SPAKEklLNSSSKFSPLLNNEPPQSLQQYKD 380
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 581-603 4.12e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.12e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  581 YVCKECGKSFRQNSALTQHQTIH 603
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 276-296 9.87e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 9.87e-03
                          10        20
                  ....*....|....*....|.
gi 254281232  276 CDDCGKAFSQHSHLIEHQRIH 296
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-152 4.85e-69

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 219.10  E-value: 4.85e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232    42 REVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVL 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 254281232   122 EDLERELDEPGEQVSVHTGEQEMFLQETVRL 152
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPL 111
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 43-130 8.16e-53

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: 175.37  E-value: 8.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232   43 EVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVLE 122
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 254281232  123 DLERELDE 130
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 43-126 1.18e-42

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: 147.79  E-value: 1.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232  43 EVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVLE 122
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 254281232 123 DLER 126
Cdd:cd07936   82 DLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
299-579 8.67e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.88  E-value: 8.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 299 DRPYKCEECGKAFRGRTVLIRHKIIHTGEKPYKCN--ECGKAFGRWSALNQHQRLHTGEK-HYHCNDCGKAFSQKAGLFH 375
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPsDLNSKSLPLSNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 376 HIKIHTRDKPYQCTQCNKSFSRRSILTQ--------------------------------------------------HQ 405
Cdd:COG5048  111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPdllsisnlrnnplpgnnsssvntpqsnslhpplpanslskdpssnlslliSS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 406 GVHTGAKPYECNECGKAFVYNSSLVSHQEIHHKEKCYQCKECGKSFSQSgLIQHQRIHTGEK---PYKCDVCEKAFI-QR 481
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS-LLSQSPSSLSSSdssSSASESPRSSLPtAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 482 TSLTEHQRIHTGER-----PYKCDKCGKAFTQRSVLTEHQR--IHTGE--RPYKCDE--CGNAFRGITSLIQHQRIHTGE 550
Cdd:COG5048  270 SQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350
                 ....*....|....*....|....*....|.
gi 254281232 551 KPYQC--DECGKAFRQRSDLSKHQRIHNRRG 579
Cdd:COG5048  350 SPAKEklLNSSSKFSPLLNNEPPQSLQQYKD 380
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-564 7.33e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.33e-05
                          10        20
                  ....*....|....*....|....*.
gi 254281232  539 SLIQHQRIHTGEKPYQCDECGKAFRQ 564
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 384-440 5.88e-04

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 5.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254281232 384 KPYqCTQCNKSFSRRSILTQHQGvhtgAKPYECNECGKAFVYNSSLVSHQEIHHKEK 440
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQVHKET 52
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 581-603 4.12e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.12e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  581 YVCKECGKSFRQNSALTQHQTIH 603
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 396-519 6.21e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.47  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 396 SRRSILTQHQG------VHTGAKPYECNECGKAFvYNSSLVSHQEIHHKEkcYQCKeCGKSFSQSGLIQHQRIHTGEKPY 469
Cdd:PLN03086 430 SRHNVVCPHDGcgivlrVEEAKNHVHCEKCGQAF-QQGEMEKHMKVFHEP--LQCP-CGVVLEKEQMVQHQASTCPLRLI 505

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 470 KCDVCEKAFIQRTS----------LTEHQRIhTGERPYKCDKCGkaftqRSVLTEHQRIH 519
Cdd:PLN03086 506 TCRFCGDMVQAGGSamdvrdrlrgMSEHESI-CGSRTAPCDSCG-----RSVMLKEMDIH 559
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 276-296 9.87e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 9.87e-03
                          10        20
                  ....*....|....*....|.
gi 254281232  276 CDDCGKAFSQHSHLIEHQRIH 296
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-152 4.85e-69

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 219.10  E-value: 4.85e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232    42 REVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVL 121
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 254281232   122 EDLERELDEPGEQVSVHTGEQEMFLQETVRL 152
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPL 111
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 43-130 8.16e-53

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: 175.37  E-value: 8.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232   43 EVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVLE 122
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 254281232  123 DLERELDE 130
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 43-126 1.18e-42

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: 147.79  E-value: 1.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232  43 EVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVLE 122
Cdd:cd07936    2 ETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLAE 81


                 ....
gi 254281232 123 DLER 126
Cdd:cd07936   82 DLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
299-579 8.67e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 70.88  E-value: 8.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 299 DRPYKCEECGKAFRGRTVLIRHKIIHTGEKPYKCN--ECGKAFGRWSALNQHQRLHTGEK-HYHCNDCGKAFSQKAGLFH 375
Cdd:COG5048   31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPsDLNSKSLPLSNSKASSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 376 HIKIHTRDKPYQCTQCNKSFSRRSILTQ--------------------------------------------------HQ 405
Cdd:COG5048  111 SSSSSNSNDNNLLSSHSLPPSSRDPQLPdllsisnlrnnplpgnnsssvntpqsnslhpplpanslskdpssnlslliSS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 406 GVHTGAKPYECNECGKAFVYNSSLVSHQEIHHKEKCYQCKECGKSFSQSgLIQHQRIHTGEK---PYKCDVCEKAFI-QR 481
Cdd:COG5048  191 NVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKS-LLSQSPSSLSSSdssSSASESPRSSLPtAS 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 482 TSLTEHQRIHTGER-----PYKCDKCGKAFTQRSVLTEHQR--IHTGE--RPYKCDE--CGNAFRGITSLIQHQRIHTGE 550
Cdd:COG5048  270 SQSSSPNESDSSSEkgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSI 349

                        330       340       350
                 ....*....|....*....|....*....|.
gi 254281232 551 KPYQC--DECGKAFRQRSDLSKHQRIHNRRG 579
Cdd:COG5048  350 SPAKEklLNSSSKFSPLLNNEPPQSLQQYKD 380
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
285-459 9.60e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.33  E-value: 9.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 285 QHSHLIEHQRIHTgdrPYKCEECGKAFRGRTVLIRHK--IIHTGE--KPYKCNE--CGKAFGRWSALNQHQRLHTGEKHY 358
Cdd:COG5048  276 NESDSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 359 HC--NDCGKAFSQK-----AGLFHHIKIHTRDKPYQCT--QCNKSFSRRSILTQHQGVHTGAKPYECN--ECGKAFVYNS 427
Cdd:COG5048  353 KEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHY 432

                        170       180       190
                 ....*....|....*....|....*....|..
gi 254281232 428 SLVSHQEIHHKEKCYQCKECGKSFSQSGLIQH 459
Cdd:COG5048  433 NLIPHKKIHTNHAPLLCSILKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
382-571 8.65e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 382 RDKPYQCTQCNKSFSRRSILTQHQ--GVHTG--AKPYECNE--CGKAFVYNSSLVSHQEIHHKEKCYQCKECGKSFSQSG 455
Cdd:COG5048  286 FSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSP 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 456 LIqhqrihTGEKPykcdvcekafiqrtSLTEHQRIHTGERPYKCD--KCGKAFTQRSVLTEHQRIHTGERPY--KCDECG 531
Cdd:COG5048  366 LL------NNEPP--------------QSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCS 425

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 254281232 532 NAFRGITSLIQHQRIHTGEKPYQCDECGKaFRQRSDLSKH 571
Cdd:COG5048  426 KSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-564 7.33e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 7.33e-05
                          10        20
                  ....*....|....*....|....*.
gi 254281232  539 SLIQHQRIHTGEKPYQCDECGKAFRQ 564
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
483-508 1.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.11e-04
                          10        20
                  ....*....|....*....|....*.
gi 254281232  483 SLTEHQRIHTGERPYKCDKCGKAFTQ 508
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
456-480 1.54e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.54e-04
                          10        20
                  ....*....|....*....|....*
gi 254281232  456 LIQHQRIHTGEKPYKCDVCEKAFIQ 480
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
317-339 3.13e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|...
gi 254281232  317 LIRHKIIHTGEKPYKCNECGKAF 339
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
288-311 3.81e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.81e-04
                          10        20
                  ....*....|....*....|....
gi 254281232  288 HLIEHQRIHTGDRPYKCEECGKAF 311
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 384-440 5.88e-04

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 39.08  E-value: 5.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254281232 384 KPYqCTQCNKSFSRRSILTQHQGvhtgAKPYECNECGKAFVYNSSLVSHQEIHHKEK 440
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVHCLQVHKET 52
zf-H2C2_2 pfam13465
Zinc-finger double domain;
344-369 6.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.80e-04
                          10        20
                  ....*....|....*....|....*.
gi 254281232  344 ALNQHQRLHTGEKHYHCNDCGKAFSQ 369
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-575 7.93e-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: 36.89  E-value: 7.93e-04
                          10        20
                  ....*....|....*....|...
gi 254281232  553 YQCDECGKAFRQRSDLSKHQRIH 575
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
512-534 1.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  512 LTEHQRIHTGERPYKCDECGNAF 534
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 480-575 3.02e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 480 QRTSLTEHQRIHT-GERPYKCD--KCGKAFTQRSVLTEHqRIHtgerpykcDECGNAFRGITSLIQHQRIHTGEKPYQCD 556
Cdd:COG5189  332 ERNIDTPSRMLKVkDGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCE 402

                         90
                 ....*....|....*....
gi 254281232 557 ECGKAFRQRSDLsKHQRIH 575
Cdd:COG5189  403 VCDKRYKNLNGL-KYHRKH 420
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 330-352 3.26e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.35  E-value: 3.26e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  330 YKCNECGKAFGRWSALNQHQRLH 352
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 581-603 4.12e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 4.12e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  581 YVCKECGKSFRQNSALTQHQTIH 603
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 396-519 6.21e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.47  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 396 SRRSILTQHQG------VHTGAKPYECNECGKAFvYNSSLVSHQEIHHKEkcYQCKeCGKSFSQSGLIQHQRIHTGEKPY 469
Cdd:PLN03086 430 SRHNVVCPHDGcgivlrVEEAKNHVHCEKCGQAF-QQGEMEKHMKVFHEP--LQCP-CGVVLEKEQMVQHQASTCPLRLI 505

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254281232 470 KCDVCEKAFIQRTS----------LTEHQRIhTGERPYKCDKCGkaftqRSVLTEHQRIH 519
Cdd:PLN03086 506 TCRFCGDMVQAGGSamdvrdrlrgMSEHESI-CGSRTAPCDSCG-----RSVMLKEMDIH 559
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 497-519 7.00e-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: 7.00e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  497 YKCDKCGKAFTQRSVLTEHQRIH 519
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 358-380 7.07e-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: 7.07e-03
                          10        20
                  ....*....|....*....|...
gi 254281232  358 YHCNDCGKAFSQKAGLFHHIKIH 380
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 328-376 7.89e-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: 35.61  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254281232 328 KPYkCNECGKAFGRWSALNQHQRlhtgEKHYHCNDCGKAFSQKAGLFHH 376
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQK----AKHFKCHICHKKLYTAGGLAVH 44
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 276-296 9.87e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.81  E-value: 9.87e-03
                          10        20
                  ....*....|....*....|.
gi 254281232  276 CDDCGKAFSQHSHLIEHQRIH 296
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 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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