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Conserved domains on  [gi|109126289|ref|XP_001097216|]
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zinc finger protein 584 isoform X1 [Macaca mulatta]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204351)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development, and in regulating viral replication and transcription

CATH:  3.30.160.60|1.10.287.1360
Gene Ontology:  GO:0003677|GO:0008270|GO:0005515|GO:0006355|GO:0001217|GO:0003700
PubMed:  22803940|14519192|8183940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
17-77 9.30e-24

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 93.43  E-value: 9.30e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109126289    17 VMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSLGLAPSRSPVFSQLEKDEQLWV 77
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
201-375 1.22e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 201 THINPRKIRPGETAHVCNECGKAFCYPSKLRKHQ--KVHTG--IKPFKC--SDCGKTFNRKDALVLHQRIHTGERPYEC- 273
Cdd:COG5048  276 NESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEk 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 274 -SKCGKTFSVLST-----LIRHRKVHIGERPYECT--ECGKFFKYSNSFILHQRVHTGERP--FECKQCGKAYVTRSGLY 343
Cdd:COG5048  356 lLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLI 435

                        170       180       190
                 ....*....|....*....|....*....|..
gi 109126289 344 QHWKVHTGERPYECSLCGKTFTTRSYRNRHQQ 375
Cdd:COG5048  436 PHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 383-405 5.77e-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: 5.77e-03
                          10        20
                  ....*....|....*....|...
gi 109126289  383 YECTECGKAFKHSSTLLQHKKVH 405
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
17-77 9.30e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 93.43  E-value: 9.30e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109126289    17 VMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSLGLAPSRSPVFSQLEKDEQLWV 77
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 16-57 1.86e-20

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: 83.67  E-value: 1.86e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 109126289   16 LVMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSLG 57
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 17-56 1.68e-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: 1.68e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 109126289  17 VMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSL 56
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
201-375 1.22e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 201 THINPRKIRPGETAHVCNECGKAFCYPSKLRKHQ--KVHTG--IKPFKC--SDCGKTFNRKDALVLHQRIHTGERPYEC- 273
Cdd:COG5048  276 NESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEk 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 274 -SKCGKTFSVLST-----LIRHRKVHIGERPYECT--ECGKFFKYSNSFILHQRVHTGERP--FECKQCGKAYVTRSGLY 343
Cdd:COG5048  356 lLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLI 435

                        170       180       190
                 ....*....|....*....|....*....|..
gi 109126289 344 QHWKVHTGERPYECSLCGKTFTTRSYRNRHQQ 375
Cdd:COG5048  436 PHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
zf-H2C2_2 pfam13465
Zinc-finger double domain;
230-254 3.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.01e-04
                          10        20
                  ....*....|....*....|....*
gi 109126289  230 LRKHQKVHTGIKPFKCSDCGKTFNR 254
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 383-405 5.77e-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: 5.77e-03
                          10        20
                  ....*....|....*....|...
gi 109126289  383 YECTECGKAFKHSSTLLQHKKVH 405
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
17-77 9.30e-24

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 93.43  E-value: 9.30e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109126289    17 VMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSLGLAPSRSPVFSQLEKDEQLWV 77
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 16-57 1.86e-20

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: 83.67  E-value: 1.86e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 109126289   16 LVMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSLG 57
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 17-56 1.68e-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: 1.68e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 109126289  17 VMFEDVAVYFSREEWGLLNVTQKGLYRDVMLENFALVSSL 56
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
201-375 1.22e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.63  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 201 THINPRKIRPGETAHVCNECGKAFCYPSKLRKHQ--KVHTG--IKPFKC--SDCGKTFNRKDALVLHQRIHTGERPYEC- 273
Cdd:COG5048  276 NESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEk 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 274 -SKCGKTFSVLST-----LIRHRKVHIGERPYECT--ECGKFFKYSNSFILHQRVHTGERP--FECKQCGKAYVTRSGLY 343
Cdd:COG5048  356 lLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLI 435

                        170       180       190
                 ....*....|....*....|....*....|..
gi 109126289 344 QHWKVHTGERPYECSLCGKTFTTRSYRNRHQQ 375
Cdd:COG5048  436 PHKKIHTNHAPLLCSILKSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
222-410 2.26e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 222 KAFCYPSKLRKHQKVHTGI-KPFKCSDCGKTFNRKDALVLHQR--IHTGE--RPYEC--SKCGKTFSVLSTLIRHRKVHI 294
Cdd:COG5048  268 ASSQSSSPNESDSSSEKGFsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHT 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 295 GERPYECTECGKFFKYSNSFIlhqrvhtgERPFECkqcgkayvtrsgLYQHWKVHTgERPYECSL--CGKTFTTRSYRNR 372
Cdd:COG5048  348 SISPAKEKLLNSSSKFSPLLN--------NEPPQS------------LQQYKDLKN-DKKSETLSnsCIRNFKRDSNLSL 406

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 109126289 373 HQQFHTEERSYECT--ECGKAFKHSSTLLQHKKVHTSERP 410
Cdd:COG5048  407 HIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAP 446
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
162-289 4.45e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 162 SDCGKVFSKAFALLDHLITHAEDRPFRCPAGRSASKEKS-----------THINPRKIRPGETAHvcNECGKAFCYPSKL 230
Cdd:COG5048  327 SLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPllnneppqslqQYKDLKNDKKSETLS--NSCIRNFKRDSNL 404

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109126289 231 RKHQKVHT--GIKPFKCSDCGKTFNRKDALVLHQRIHTGERPYECSKCGKtFSVLSTLIRH 289
Cdd:COG5048  405 SLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
230-254 3.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.01e-04
                          10        20
                  ....*....|....*....|....*
gi 109126289  230 LRKHQKVHTGIKPFKCSDCGKTFNR 254
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 323-403 3.70e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.40  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 323 GERPFECK--QCGKAYVTRSGLYQHwKVHtgerpyecSLCGKTFTTRSYRNRHQQFHTEERSYECTECGKAFKHSSTLLQ 400
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ...
gi 109126289 401 HKK 403
Cdd:COG5189  417 HRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
257-281 7.58e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 7.58e-04
                          10        20
                  ....*....|....*....|....*
gi 109126289  257 ALVLHQRIHTGERPYECSKCGKTFS 281
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
193-279 1.05e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109126289 193 RSASKEKSTHINPRKIRPGetaHVCNECGKAFCYPSKLRKHQKVHTGIKPFKCSD--CGKTFNRKDALVLHQRIHTGERP 270
Cdd:COG5048   15 VLSSTPKSTLKSLSNAPRP---DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPS 91


                 ....*....
gi 109126289 271 YECSKCGKT 279
Cdd:COG5048   92 DLNSKSLPL 100
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 243-265 1.18e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|...
gi 109126289  243 FKCSDCGKTFNRKDALVLHQRIH 265
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
286-310 1.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*
gi 109126289  286 LIRHRKVHIGERPYECTECGKFFKY 310
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 215-237 3.46e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.58  E-value: 3.46e-03
                          10        20
                  ....*....|....*....|...
gi 109126289  215 HVCNECGKAFCYPSKLRKHQKVH 237
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
317-338 3.65e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.65e-03
                          10        20
                  ....*....|....*....|..
gi 109126289  317 HQRVHTGERPFECKQCGKAYVT 338
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 271-293 5.08e-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: 5.08e-03
                          10        20
                  ....*....|....*....|...
gi 109126289  271 YECSKCGKTFSVLSTLIRHRKVH 293
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 383-405 5.77e-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: 5.77e-03
                          10        20
                  ....*....|....*....|...
gi 109126289  383 YECTECGKAFKHSSTLLQHKKVH 405
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
371-394 6.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.02e-03
                          10        20
                  ....*....|....*....|....
gi 109126289  371 NRHQQFHTEERSYECTECGKAFKH 394
Cdd:pfam13465   3 KRHMRTHTGEKPYKCPECGKSFKS 26
Mcm2 COG1241
DNA replicative helicase MCM subunit Mcm2, Cdc46/Mcm family [Replication, recombination and ...
 238-298 6.50e-03

DNA replicative helicase MCM subunit Mcm2, Cdc46/Mcm family [Replication, recombination and repair];


Pssm-ID: 440854 [Multi-domain]  Cd Length: 682  Bit Score: 38.63  E-value: 6.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109126289 238 TGIKP------FKCSDCGKTFnrkdalVLHQRIHTGERPYECSKCGKT--FSVL---STLIRHRKVHIGERP 298
Cdd:COG1241  118 TEVKPkiteaaFECPRCGTET------YVPQTGEKLQEPHECPGCGRQgpFKLLpekSEFIDAQKIRIQEPP 183
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
241-290 8.37e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.14  E-value: 8.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109126289 241 KPFKCSDCGKTFNRKDALVLHQRIHTGERPYECSK--CGKTFSVLSTLIRHR 290
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHL 83
zf-H2C2_2 pfam13465
Zinc-finger double domain;
342-366 8.84e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.50  E-value: 8.84e-03
                          10        20
                  ....*....|....*....|....*
gi 109126289  342 LYQHWKVHTGERPYECSLCGKTFTT 366
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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