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Conserved domains on  [gi|119622953|gb|EAX02548|]
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zinc finger protein 195, isoform CRA_a [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204268)

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
Gene Ontology:  GO:0003700|GO:0046872
PubMed:  22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-64 5.73e-33

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 5.73e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119622953     4 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWN 64
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
225-629 5.95e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 5.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 225 FDNFSNLHRRNISNTGEKPFKC--QECGKSFQMLSFLTEHQKIHT-GKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYK 301
Cdd:COG5048   43 FSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 302 CQECNNVIKTCSVLTKNriyaggehyrceefgkvFNQCSHLTEhehgteekpCKYEECSSVFISCSSLSNQQMILAGEKL 381
Cdd:COG5048  123 LSSHSLPPSSRDPQLPD-----------------LLSISNLRN---------NPLPGNNSSSVNTPQSNSLHPPLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 382 SKCETWYKGFNHSPNPSkhqrneIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECgkayTQSSHLSEHRRIHT 461
Cdd:COG5048  177 SKDPSSNLSLLISSNVS------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 462 GEKP-YQCEECGKVFRTCSSLSNHKRTHSEE----------KPYTCEECGNIFKQLSDLTKHKKT--HTGE--KPYKCDE 526
Cdd:COG5048  247 SLSSsDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPY 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 527 --CGKNFTQSSNLIVHKRIHTGEKPYKCEECGR-------VFMWFSDITKHKKTHTGEKPYKCD--ECGKNFTQSSNLIV 595
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfsplLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 119622953 596 HKRIHTGEKP--YKCEKCGKAFTQFSHLTVHESIHT 629
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-64 5.73e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 5.73e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119622953     4 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWN 64
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-44 1.93e-22

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: 90.22  E-value: 1.93e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119622953    3 LLTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-42 7.50e-19

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: 79.90  E-value: 7.50e-19
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119622953   4 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFS 42
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
225-629 5.95e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 5.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 225 FDNFSNLHRRNISNTGEKPFKC--QECGKSFQMLSFLTEHQKIHT-GKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYK 301
Cdd:COG5048   43 FSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 302 CQECNNVIKTCSVLTKNriyaggehyrceefgkvFNQCSHLTEhehgteekpCKYEECSSVFISCSSLSNQQMILAGEKL 381
Cdd:COG5048  123 LSSHSLPPSSRDPQLPD-----------------LLSISNLRN---------NPLPGNNSSSVNTPQSNSLHPPLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 382 SKCETWYKGFNHSPNPSkhqrneIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECgkayTQSSHLSEHRRIHT 461
Cdd:COG5048  177 SKDPSSNLSLLISSNVS------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 462 GEKP-YQCEECGKVFRTCSSLSNHKRTHSEE----------KPYTCEECGNIFKQLSDLTKHKKT--HTGE--KPYKCDE 526
Cdd:COG5048  247 SLSSsDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPY 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 527 --CGKNFTQSSNLIVHKRIHTGEKPYKCEECGR-------VFMWFSDITKHKKTHTGEKPYKCD--ECGKNFTQSSNLIV 595
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfsplLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 119622953 596 HKRIHTGEKP--YKCEKCGKAFTQFSHLTVHESIHT 629
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-617 6.51e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.51e-05
                          10        20
                  ....*....|....*....|....*.
gi 119622953  592 NLIVHKRIHTGEKPYKCEKCGKAFTQ 617
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
4-64 5.73e-33

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 120.39  E-value: 5.73e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119622953     4 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVGLTVCKPGLITCLEQRKEPWN 64
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 3-44 1.93e-22

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: 90.22  E-value: 1.93e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 119622953    3 LLTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFSVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 4-42 7.50e-19

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: 79.90  E-value: 7.50e-19
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119622953   4 LTFRDVAIEFSLEEWKCLDLAQQNLYRDVMLENYRNLFS 42
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
225-629 5.95e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.47  E-value: 5.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 225 FDNFSNLHRRNISNTGEKPFKC--QECGKSFQMLSFLTEHQKIHT-GKKFQKCGECGKTFIQCSHFTEPENIDTGEKPYK 301
Cdd:COG5048   43 FSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 302 CQECNNVIKTCSVLTKNriyaggehyrceefgkvFNQCSHLTEhehgteekpCKYEECSSVFISCSSLSNQQMILAGEKL 381
Cdd:COG5048  123 LSSHSLPPSSRDPQLPD-----------------LLSISNLRN---------NPLPGNNSSSVNTPQSNSLHPPLPANSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 382 SKCETWYKGFNHSPNPSkhqrneIGGKPFKCEECDSIFKWFSDLTKHKRIHTGEKPYKCDECgkayTQSSHLSEHRRIHT 461
Cdd:COG5048  177 SKDPSSNLSLLISSNVS------TSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN----SQLSPKSLLSQSPS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 462 GEKP-YQCEECGKVFRTCSSLSNHKRTHSEE----------KPYTCEECGNIFKQLSDLTKHKKT--HTGE--KPYKCDE 526
Cdd:COG5048  247 SLSSsDSSSSASESPRSSLPTASSQSSSPNEsdsssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPY 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 527 --CGKNFTQSSNLIVHKRIHTGEKPYKCEECGR-------VFMWFSDITKHKKTHTGEKPYKCD--ECGKNFTQSSNLIV 595
Cdd:COG5048  327 slCGKLFSRNDALKRHILLHTSISPAKEKLLNSsskfsplLNNEPPQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSL 406

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 119622953 596 HKRIHTGEKP--YKCEKCGKAFTQFSHLTVHESIHT 629
Cdd:COG5048  407 HIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
392-569 1.07e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 392 NHSPNPSKHQRNEIGGKPFKCEECDSIFKWFSDLTKHKR--IHTGE--KPYKCDE--CGKAYTQSSHLSEHRRIHTGEKP 465
Cdd:COG5048  272 SSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISP 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 466 YQC--EECGKVFRTCS-----SLSNHKRTHSEEKPYTCE--ECGNIFKQLSDLTKHKKTHTGEKPY--KCDECGKNFTQS 534
Cdd:COG5048  352 AKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRH 431

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119622953 535 SNLIVHKRIHTGEKPYKCEECGRVFMWFSDITKHK 569
Cdd:COG5048  432 YNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
436-497 2.11e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119622953 436 KPYKCDECGKAYTQSSHLSEHRRIHTGEKPYQC--EECGKVFRTCSSLSNHKRTHSEEKPYTCE 497
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS 95
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 434-517 3.71e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 46.63  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 434 GEKPYKCD--ECGKAYTQSSHLSEHRrIHTgekpyqceECGKVFRTCSSLSNHKRTHSEEKPYTCEECGNIFKQLSDLTK 511
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHM-LHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ....*.
gi 119622953 512 HKKTHT 517
Cdd:COG5189  417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
592-617 6.51e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 6.51e-05
                          10        20
                  ....*....|....*....|....*.
gi 119622953  592 NLIVHKRIHTGEKPYKCEKCGKAFTQ 617
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
424-449 1.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.12e-04
                          10        20
                  ....*....|....*....|....*.
gi 119622953  424 DLTKHKRIHTGEKPYKCDECGKAYTQ 449
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
508-533 1.93e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.93e-04
                          10        20
                  ....*....|....*....|....*.
gi 119622953  508 DLTKHKKTHTGEKPYKCDECGKNFTQ 533
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
452-477 2.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.33e-04
                          10        20
                  ....*....|....*....|....*.
gi 119622953  452 HLSEHRRIHTGEKPYQCEECGKVFRT 477
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
567-589 6.59e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.59e-04
                          10        20
                  ....*....|....*....|...
gi 119622953  567 KHKKTHTGEKPYKCDECGKNFTQ 589
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
536-559 7.79e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.79e-04
                          10        20
                  ....*....|....*....|....
gi 119622953  536 NLIVHKRIHTGEKPYKCEECGRVF 559
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
520-613 2.78e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.45  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119622953 520 KPYKCDECGKNFTQSSNLIVHKRIHTGEKPYKCEECGrvfmwfsditkhkkthtgekpykcdeCGKNFTQSSNLIVHKRI 599
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSG--------------------------CDKSFSRPLELSRHLRT 85

                         90
                 ....*....|....
gi 119622953 600 HTGEKPYKCEKCGK 613
Cdd:COG5048   86 HHNNPSDLNSKSLP 99
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 522-544 2.89e-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: 2.89e-03
                          10        20
                  ....*....|....*....|...
gi 119622953  522 YKCDECGKNFTQSSNLIVHKRIH 544
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 578-600 2.89e-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: 2.89e-03
                          10        20
                  ....*....|....*....|...
gi 119622953  578 YKCDECGKNFTQSSNLIVHKRIH 600
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 466-488 4.45e-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: 34.97  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|...
gi 119622953  466 YQCEECGKVFRTCSSLSNHKRTH 488
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 438-460 8.26e-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: 34.20  E-value: 8.26e-03
                          10        20
                  ....*....|....*....|...
gi 119622953  438 YKCDECGKAYTQSSHLSEHRRIH 460
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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