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Conserved domains on  [gi|16418391|ref|NP_443114|]
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zinc finger imprinted 3 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 16584006)

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:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217|GO:0003700
PubMed:  8183940|22803940|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;
8-68 8.84e-32

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.77  E-value: 8.84e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16418391      8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVSVGQgETTKPDVILRLEQGKEPW 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF-QVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
304-465 4.39e-09

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 4.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 304 QKPFQCTDCGKAFIYKSDLVKHQR--IHTGE--KPYKC--SICEKAFSQKSNVIDHEKIHTGKRAYECDLCGNTFIQKKN 377
Cdd:COG5048 287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPL 366

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 378 L-------IQHKKIHTGEKPYEC--NRCGKAFFQKSNLHSHQKTHSGERT--YRCSECGKTFIRKLNLSLHKKTHTgQKP 446
Cdd:COG5048 367 LnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT-NHA 445

                       170
                ....*....|....*....
gi 16418391 447 YGCSECGKAFADRSYLVRH 465
Cdd:COG5048 446 PLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
237-261 3.53e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.53e-04
                          10        20
                  ....*....|....*....|....*
gi 16418391   237 NLFQHQKMHTKEKPYQCKTCGKAFS 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
157-348 1.33e-03

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


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 157 NNPSKFVGQQLKCNACRKLFSSKSRLQSHLRRHAcqkpfecHScgrafgekwklDKHQKTHaeERPYkcENCGNAYKQKS 236
Cdd:COG5048 280 SSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSVN-------HS-----------GESLKPF--SCPY--SLCGKLFSRND 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 237 NLFQHQKMHTKEKPYQCKTC-------GKAFSWKSSCINHEKIHNAKKSYQC--NECEKSFRQNSTLIQHKKVHTGQKP- 306
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPy 417

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16418391 307 -FQCTDCGKAFIYKSDLVKHQRIHTGEKPYKCSICEKAFSQKS 348
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 8.84e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.77  E-value: 8.84e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16418391      8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVSVGQgETTKPDVILRLEQGKEPW 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF-QVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 8-48 6.42e-24

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: 93.69  E-value: 6.42e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16418391     8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVSVG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 4.85e-20

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: 82.98  E-value: 4.85e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16418391   8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVS 46
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
304-465 4.39e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 4.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 304 QKPFQCTDCGKAFIYKSDLVKHQR--IHTGE--KPYKC--SICEKAFSQKSNVIDHEKIHTGKRAYECDLCGNTFIQKKN 377
Cdd:COG5048 287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPL 366

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 378 L-------IQHKKIHTGEKPYEC--NRCGKAFFQKSNLHSHQKTHSGERT--YRCSECGKTFIRKLNLSLHKKTHTgQKP 446
Cdd:COG5048 367 LnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT-NHA 445

                       170
                ....*....|....*....
gi 16418391 447 YGCSECGKAFADRSYLVRH 465
Cdd:COG5048 446 PLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
321-346 1.66e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.66e-04
                          10        20
                  ....*....|....*....|....*.
gi 16418391   321 DLVKHQRIHTGEKPYKCSICEKAFSQ 346
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
237-261 3.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.53e-04
                          10        20
                  ....*....|....*....|....*
gi 16418391   237 NLFQHQKMHTKEKPYQCKTCGKAFS 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
157-348 1.33e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 157 NNPSKFVGQQLKCNACRKLFSSKSRLQSHLRRHAcqkpfecHScgrafgekwklDKHQKTHaeERPYkcENCGNAYKQKS 236
Cdd:COG5048 280 SSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSVN-------HS-----------GESLKPF--SCPY--SLCGKLFSRND 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 237 NLFQHQKMHTKEKPYQCKTC-------GKAFSWKSSCINHEKIHNAKKSYQC--NECEKSFRQNSTLIQHKKVHTGQKP- 306
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPy 417

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16418391 307 -FQCTDCGKAFIYKSDLVKHQRIHTGEKPYKCSICEKAFSQKS 348
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 271-385 3.35e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.86  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391  271 KIHNAKKSYQCNECEKSFRQNStLIQHKKVHtgQKPFQCTdCGkAFIYKSDLVKHQRIHTGEKPYKCSICEKAFSQKSNV 350
Cdd:PLN03086 446 RVEEAKNHVHCEKCGQAFQQGE-MEKHMKVF--HEPLQCP-CG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVQAGGSA 520

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16418391  351 ID----------HEKIhTGKRAYECDLCGNTFIQKKNLIQHKKIH 385
Cdd:PLN03086 521 MDvrdrlrgmseHESI-CGSRTAPCDSCGRSVMLKEMDIHQIAVH 564
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
8-68 8.84e-32

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 115.77  E-value: 8.84e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16418391      8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVSVGQgETTKPDVILRLEQGKEPW 68
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGF-QVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 8-48 6.42e-24

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: 93.69  E-value: 6.42e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16418391     8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVSVG 48
Cdd:pfam01352   2 VTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-46 4.85e-20

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: 82.98  E-value: 4.85e-20
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16418391   8 VTFEDVTVNFTQGEWQRLNPEQRNLYRDVMLENYSNLVS 46
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
304-465 4.39e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 4.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 304 QKPFQCTDCGKAFIYKSDLVKHQR--IHTGE--KPYKC--SICEKAFSQKSNVIDHEKIHTGKRAYECDLCGNTFIQKKN 377
Cdd:COG5048 287 SLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPL 366

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 378 L-------IQHKKIHTGEKPYEC--NRCGKAFFQKSNLHSHQKTHSGERT--YRCSECGKTFIRKLNLSLHKKTHTgQKP 446
Cdd:COG5048 367 LnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT-NHA 445

                       170
                ....*....|....*....
gi 16418391 447 YGCSECGKAFADRSYLVRH 465
Cdd:COG5048 446 PLLCSILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
321-346 1.66e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.66e-04
                          10        20
                  ....*....|....*....|....*.
gi 16418391   321 DLVKHQRIHTGEKPYKCSICEKAFSQ 346
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
237-261 3.53e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.53e-04
                          10        20
                  ....*....|....*....|....*
gi 16418391   237 NLFQHQKMHTKEKPYQCKTCGKAFS 261
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
377-402 6.43e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 6.43e-04
                          10        20
                  ....*....|....*....|....*.
gi 16418391   377 NLIQHKKIHTGEKPYECNRCGKAFFQ 402
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
157-348 1.33e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 157 NNPSKFVGQQLKCNACRKLFSSKSRLQSHLRRHAcqkpfecHScgrafgekwklDKHQKTHaeERPYkcENCGNAYKQKS 236
Cdd:COG5048 280 SSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSVN-------HS-----------GESLKPF--SCPY--SLCGKLFSRND 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 237 NLFQHQKMHTKEKPYQCKTC-------GKAFSWKSSCINHEKIHNAKKSYQC--NECEKSFRQNSTLIQHKKVHTGQKP- 306
Cdd:COG5048 338 ALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPy 417

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16418391 307 -FQCTDCGKAFIYKSDLVKHQRIHTGEKPYKCSICEKAFSQKS 348
Cdd:COG5048 418 nCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
294-318 1.35e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.35e-03
                          10        20
                  ....*....|....*....|....*
gi 16418391   294 LIQHKKVHTGQKPFQCTDCGKAFIY 318
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
274-408 2.26e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 274 NAKKSYQCNECEKSFRQNSTLIQHKKVHTGQKPFQCTDCGKAFIYK--SDLVKHQRIHTGEKPYKCSICEKAFSQKSNVI 351
Cdd:COG5048  29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS 108

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16418391 352 DHEkIHTGKRAYECDLCGNTFIQKKNLIQHKKIHT-----GEKPYECNRCGKAFFQKSNLHS 408
Cdd:COG5048 109 SLS-SSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSisnlrNNPLPGNNSSSVNTPQSNSLHP 169
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 307-329 2.27e-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: 2.27e-03
                          10        20
                  ....*....|....*....|...
gi 16418391   307 FQCTDCGKAFIYKSDLVKHQRIH 329
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 271-385 3.35e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.86  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391  271 KIHNAKKSYQCNECEKSFRQNStLIQHKKVHtgQKPFQCTdCGkAFIYKSDLVKHQRIHTGEKPYKCSICEKAFSQKSNV 350
Cdd:PLN03086 446 RVEEAKNHVHCEKCGQAFQQGE-MEKHMKVF--HEPLQCP-CG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVQAGGSA 520

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16418391  351 ID----------HEKIhTGKRAYECDLCGNTFIQKKNLIQHKKIH 385
Cdd:PLN03086 521 MDvrdrlrgmseHESI-CGSRTAPCDSCGRSVMLKEMDIHQIAVH 564
zf-H2C2_2 pfam13465
Zinc-finger double domain;
433-457 5.47e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 5.47e-03
                          10        20
                  ....*....|....*....|....*
gi 16418391   433 NLSLHKKTHTGQKPYGCSECGKAFA 457
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 219-299 5.64e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 38.93  E-value: 5.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16418391 219 EERPYKCE--NCGNAYKQKSNLfqhqKMHTKEKpyqckTCGKAFSWKSSCINHEKIHNAKKSYQCNECEKSFRQNSTLIQ 296
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGL----KYHMLHG-----HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ...
gi 16418391 297 HKK 299
Cdd:COG5189 417 HRK 419
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 391-413 7.45e-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: 7.45e-03
                          10        20
                  ....*....|....*....|...
gi 16418391   391 YECNRCGKAFFQKSNLHSHQKTH 413
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 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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