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Conserved domains on  [gi|21357595|ref|NP_650429|]
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uncharacterized protein Dmel_CG6654 [Drosophila melanogaster]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 12222075)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  22803940|11361095|11179890|12665246|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-78 3.50e-13

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


:

Pssm-ID: 214871  Cd Length: 73  Bit Score: 64.84  E-value: 3.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357595      6 ICLTCLSSTGPLLSIYDGGSGSCLADMIREFTKTKPRRNDNLPEKVCLSCLSEISNCYTFKIKCENSSRTLRQ 78
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEASLAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
357-570 5.98e-13

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 5.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 357 NYKCNECekVFVSPDHLAEHQASHG-----AHNCPECGIRCDSKEALSKHMVQ-----GHKRN-LRNQCNICQKVFTMLS 425
Cdd:COG5048 226 SLPLTTN--SQLSPKSLLSQSPSSLsssdsSSSASESPRSSLPTASSQSSSPNesdssSEKGFsLPIKSKQCNISFSRSS 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 426 TLRDHMR--IHTGE--KPFVC--NICGKSFTQNANLRQHKLRHSETKSFKCELCPHSFV-------TKAELTSHARTHTG 492
Cdd:COG5048 304 PLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKfspllnnEPPQSLQQYKDLKN 383

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 493 DKPFECEV--CLARFTTSCSLAKHKRKHTGERPYACD--LCPMRFTALNVLKNHRRTHTgERPYVCPFCSKTFTQRGDCQ 568
Cdd:COG5048 384 DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLS 462


                ..
gi 21357595 569 MH 570
Cdd:COG5048 463 NH 464
 
Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-78 3.50e-13

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 64.84  E-value: 3.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357595      6 ICLTCLSSTGPLLSIYDGGSGSCLADMIREFTKTKPRRNDNLPEKVCLSCLSEISNCYTFKIKCENSSRTLRQ 78
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEASLAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
357-570 5.98e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 5.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 357 NYKCNECekVFVSPDHLAEHQASHG-----AHNCPECGIRCDSKEALSKHMVQ-----GHKRN-LRNQCNICQKVFTMLS 425
Cdd:COG5048 226 SLPLTTN--SQLSPKSLLSQSPSSLsssdsSSSASESPRSSLPTASSQSSSPNesdssSEKGFsLPIKSKQCNISFSRSS 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 426 TLRDHMR--IHTGE--KPFVC--NICGKSFTQNANLRQHKLRHSETKSFKCELCPHSFV-------TKAELTSHARTHTG 492
Cdd:COG5048 304 PLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKfspllnnEPPQSLQQYKDLKN 383

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 493 DKPFECEV--CLARFTTSCSLAKHKRKHTGERPYACD--LCPMRFTALNVLKNHRRTHTgERPYVCPFCSKTFTQRGDCQ 568
Cdd:COG5048 384 DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLS 462


                ..
gi 21357595 569 MH 570
Cdd:COG5048 463 NH 464
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-79 3.46e-11

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 59.39  E-value: 3.46e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21357595     6 ICLTCLSSTGPLLSIYDGGSGSC-LADMIREFTKTKPRRNDNLPEKVCLSCLSEISNCYTFKIKCENSSRTLRQL 79
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKtLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-H2C2_2 pfam13465
Zinc-finger double domain;
427-451 3.97e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.97e-06
                          10        20
                  ....*....|....*....|....*
gi 21357595   427 LRDHMRIHTGEKPFVCNICGKSFTQ 451
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 359-410 3.17e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 3.17e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21357595 359 KCNECEKVFVSPDHLAEHQASHgaH-NCPECGIRCDSKEALSKHMVQGHKRNL 410
Cdd:cd20908   3 WCYYCDREFDDEKILIQHQKAK--HfKCHICHKKLYTAGGLAVHCLQVHKETL 53
 
Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-78 3.50e-13

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 64.84  E-value: 3.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357595      6 ICLTCLSSTGPLLSIYDGGSGSCLADMIREFTKTKPRRNDNLPEKVCLSCLSEISNCYTFKIKCENSSRTLRQ 78
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEASLAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
357-570 5.98e-13

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 71.27  E-value: 5.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 357 NYKCNECekVFVSPDHLAEHQASHG-----AHNCPECGIRCDSKEALSKHMVQ-----GHKRN-LRNQCNICQKVFTMLS 425
Cdd:COG5048 226 SLPLTTN--SQLSPKSLLSQSPSSLsssdsSSSASESPRSSLPTASSQSSSPNesdssSEKGFsLPIKSKQCNISFSRSS 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 426 TLRDHMR--IHTGE--KPFVC--NICGKSFTQNANLRQHKLRHSETKSFKCELCPHSFV-------TKAELTSHARTHTG 492
Cdd:COG5048 304 PLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKfspllnnEPPQSLQQYKDLKN 383

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 493 DKPFECEV--CLARFTTSCSLAKHKRKHTGERPYACD--LCPMRFTALNVLKNHRRTHTgERPYVCPFCSKTFTQRGDCQ 568
Cdd:COG5048 384 DKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSFRRDLDLS 462


                ..
gi 21357595 569 MH 570
Cdd:COG5048 463 NH 464
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 6-79 3.46e-11

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 59.39  E-value: 3.46e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21357595     6 ICLTCLSSTGPLLSIYDGGSGSC-LADMIREFTKTKPRRNDNLPEKVCLSCLSEISNCYTFKIKCENSSRTLRQL 79
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKtLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQEL 75
zf-H2C2_2 pfam13465
Zinc-finger double domain;
427-451 3.97e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.51  E-value: 3.97e-06
                          10        20
                  ....*....|....*....|....*
gi 21357595   427 LRDHMRIHTGEKPFVCNICGKSFTQ 451
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
539-563 1.49e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.49e-05
                          10        20
                  ....*....|....*....|....*
gi 21357595   539 LKNHRRTHTGERPYVCPFCSKTFTQ 563
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
343-473 2.95e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 43.86  E-value: 2.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 343 SLMIHRRQKGCINRNYK-CNECEK--VFVSPDHLAEHQASHGAHNCPE--CGIRCDSKEALSKHMVQGHKRNLRNQCNIC 417
Cdd:COG5236 109 AVVFTASSPADITDRRQwKGREEKvgIFYEGEDVRDEMEDLLSFKCPKskCHRRCGSLKELKKHYKAQHGFVLCSECIGN 188

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357595 418 QKVFT------MLSTLRDHMRIHTGEKPF----VCNICGKSFTQNANLRQH-KLRHSetksfKCELC 473
Cdd:COG5236 189 KKDFWneirlfRSSTLRDHKNGGLEEEGFkghpLCIFCKIYFYDDDELRRHcRLRHE-----ACHIC 250
zf-H2C2_2 pfam13465
Zinc-finger double domain;
510-534 3.14e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.14e-04
                          10        20
                  ....*....|....*....|....*
gi 21357595   510 SLAKHKRKHTGERPYACDLCPMRFT 534
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 445-514 7.19e-04

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 39.32  E-value: 7.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357595   445 CGKSFTQNANLRQHKLRHS------ETKSFKCEL--CPHSFVTKAELTSHARTH-TGDKPFECEVCLARFTTSCSLAKH 514
Cdd:pfam15909   7 CCLSFPSVRDLAQHLRTHCpptqslEGKLFRCSAlsCTETFPSMQELVAHSKLHyKPNRYFKCENCLLRFRTHRSLFKH 85
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 440-462 8.87e-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: 8.87e-04
                          10        20
                  ....*....|....*....|...
gi 21357595   440 FVCNICGKSFTQNANLRQHKLRH 462
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
482-507 1.17e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.17e-03
                          10        20
                  ....*....|....*....|....*.
gi 21357595   482 ELTSHARTHTGDKPFECEVCLARFTT 507
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 359-410 3.17e-03

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


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 36.77  E-value: 3.17e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21357595 359 KCNECEKVFVSPDHLAEHQASHgaH-NCPECGIRCDSKEALSKHMVQGHKRNL 410
Cdd:cd20908   3 WCYYCDREFDDEKILIQHQKAK--HfKCHICHKKLYTAGGLAVHCLQVHKETL 53
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
354-606 5.81e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 39.68  E-value: 5.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 354 INRNYKCNECEKVFVSPDHLAEHQASHGA---HNCPECGIRCDSKE--ALSKHMVQGHKRNLRNQCNICQKVFtmlSTLR 428
Cdd:COG5048  30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGekpSQCSYSGCDKSFSRplELSRHLRTHHNNPSDLNSKSLPLSN---SKAS 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 429 DHMRIHTGEKPFVCNIC-GKSFTQNANLRQHKLRHSETKSFKCEL--CPHSFV-TKAELTSHARTHTGDKPFECEVCLAR 504
Cdd:COG5048 107 SSSLSSSSSNSNDNNLLsSHSLPPSSRDPQLPDLLSISNLRNNPLpgNNSSSVnTPQSNSLHPPLPANSLSKDPSSNLSL 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357595 505 FTtscslakHKRKHTGERPYACDLCPMRFTALNVLKNHRRTHTGERPYVCPFCSKTFTQRGDCQmhQRTHQGERIYICPV 584
Cdd:COG5048 187 LI-------SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQ--SPSSLSSSDSSSSA 257

                       250       260
                ....*....|....*....|..
gi 21357595 585 CNEEFKSMPEMRSHLAGHEQHD 606
Cdd:COG5048 258 SESPRSSLPTASSQSSSPNESD 279
 
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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