NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|296010895|ref|NP_001171560|]
View 

zinc finger protein 454 isoform 1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 2.70e-30

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.30  E-value: 2.70e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296010895    14 VTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSLGLLGPKPDTFSQLEKR-EVWM 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
186-522 5.70e-11

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 5.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 186 VFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYEC--KECGKAFSVSSSLTYHQ 263
Cdd:COG5048    4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 264 KIHTGEKPFECNlcGKAFIRNIHLAHHHRIHTGEKPFKCNICEKafvcraHLTKHQNIHS------------GEKPYKCN 331
Cdd:COG5048   84 RTHHNNPSDLNS--KSLPLSNSKASSSSLSSSSSNSNDNNLLSS------HSLPPSSRDPqlpdllsisnlrNNPLPGNN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 332 ECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKA 392
Cdd:COG5048  156 SSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 393 FRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGE-------KPYTCNICEKAFSDHSALTQHKR--IHT 463
Cdd:COG5048  236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHS 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010895 464 RE--KPYKC--KICEKAFIRSTHLTQHQRIHTGEKPYKC--NKCGKAFNQ--TANLIQHQRHHIGEK 522
Cdd:COG5048  316 GEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllNNEPPQSLQQYKDLK 382
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 2.70e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.30  E-value: 2.70e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296010895    14 VTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSLGLLGPKPDTFSQLEKR-EVWM 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 5.56e-25

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: 97.16  E-value: 5.56e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 296010895   13 SVTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
14-53 1.30e-21

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: 87.60  E-value: 1.30e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 296010895  14 VTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSL 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
186-522 5.70e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 5.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 186 VFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYEC--KECGKAFSVSSSLTYHQ 263
Cdd:COG5048    4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 264 KIHTGEKPFECNlcGKAFIRNIHLAHHHRIHTGEKPFKCNICEKafvcraHLTKHQNIHS------------GEKPYKCN 331
Cdd:COG5048   84 RTHHNNPSDLNS--KSLPLSNSKASSSSLSSSSSNSNDNNLLSS------HSLPPSSRDPqlpdllsisnlrNNPLPGNN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 332 ECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKA 392
Cdd:COG5048  156 SSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 393 FRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGE-------KPYTCNICEKAFSDHSALTQHKR--IHT 463
Cdd:COG5048  236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHS 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010895 464 RE--KPYKC--KICEKAFIRSTHLTQHQRIHTGEKPYKC--NKCGKAFNQ--TANLIQHQRHHIGEK 522
Cdd:COG5048  316 GEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllNNEPPQSLQQYKDLK 382
zf-H2C2_2 pfam13465
Zinc-finger double domain;
482-507 8.11e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.11e-05
                          10        20
                  ....*....|....*....|....*.
gi 296010895  482 HLTQHQRIHTGEKPYKCNKCGKAFNQ 507
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
14-73 2.70e-30

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 112.30  E-value: 2.70e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296010895    14 VTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSLGLLGPKPDTFSQLEKR-EVWM 73
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGeEPWI 61
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
13-54 5.56e-25

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: 97.16  E-value: 5.56e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 296010895   13 SVTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSLG 54
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
14-53 1.30e-21

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: 87.60  E-value: 1.30e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 296010895  14 VTFKDVAILFTQEEWGQLSPAQRALYRDVMLENYSNLVSL 53
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVSL 40
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
186-522 5.70e-11

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 64.72  E-value: 5.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 186 VFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYEC--KECGKAFSVSSSLTYHQ 263
Cdd:COG5048    4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 264 KIHTGEKPFECNlcGKAFIRNIHLAHHHRIHTGEKPFKCNICEKafvcraHLTKHQNIHS------------GEKPYKCN 331
Cdd:COG5048   84 RTHHNNPSDLNS--KSLPLSNSKASSSSLSSSSSNSNDNNLLSS------HSLPPSSRDPqlpdllsisnlrNNPLPGNN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 332 ECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKA 392
Cdd:COG5048  156 SSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 393 FRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGE-------KPYTCNICEKAFSDHSALTQHKR--IHT 463
Cdd:COG5048  236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHS 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010895 464 RE--KPYKC--KICEKAFIRSTHLTQHQRIHTGEKPYKC--NKCGKAFNQ--TANLIQHQRHHIGEK 522
Cdd:COG5048  316 GEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPllNNEPPQSLQQYKDLK 382
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
115-366 5.20e-09

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.55  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 115 SSSSHWKCASLLEWQCGGQEISLQRVVLTHPNTPSQECDESGSTMSSSLHSDQSQGFQPSKNAFECSECGKVFSKSSTLN 194
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 195 KHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQR--IHTGE--KPYECKE--CGKAFSVSSSLTYHQKIHTG 268
Cdd:COG5048  269 SSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 269 EKPFECNLC-------GKAFIRNIHLAHHHRIHTGEKPFKC--NICEKAFVCRAHLTKH--QNIHSGEKPYKCNECGKAF 337
Cdd:COG5048  349 ISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSF 428
                        250       260
                 ....*....|....*....|....*....
gi 296010895 338 NQSTSFLQHQRIHTGEKPFECNECGKAFR 366
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRR 457
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
134-403 1.26e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.40  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 134 EISLQRVVLTHPNTPSQECDESGSTMSSSLHSDQSQGFQPSKNaFECSECGKVFSKSST--------LNKHQKIHNEKNA 205
Cdd:COG5048  170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIP-SSSSDQNLENSSSSLplttnsqlSPKSLLSQSPSSL 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 206 NQKIHIKEKRYECREC-GKAFHQSTHLIHH-QRIHTG-EKPYECKECGKAFSVSSSLTYHQ--KIHTGE--KPFEC--NL 276
Cdd:COG5048  249 SSSDSSSSASESPRSSlPTASSQSSSPNESdSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySL 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 277 CGKAFIRNIHLAHHHRIHTGEKPFKC--NICEKAFV-----CRAHLTKHQNIHSGEKPYKCNECGKAFNQST-SFLQHQR 348
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRdSNLSLHI 408
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296010895 349 IHT---GEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKAFRDNSSFARHR 403
Cdd:COG5048  409 ITHlsfRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLDLSNHGK 466
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
198-481 8.96e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 8.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 198 KIHNEKNANQKIHIKEKRyecRECGKAFHQSTHLIHHQRIHTGEKPYECKECGKAFSVSSSLTYHQKIH-TGEKPFECNL 276
Cdd:COG5048  157 SSVNTPQSNSLHPPLPAN---SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENsSSSLPLTTNS 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 277 CGKAF----IRNIHLAHHHRIHTGEKPFKCNICEKAFVCRAHLTKHQNIHSG-EKPYKCNECGKAFNQSTSFLQHQR--I 349
Cdd:COG5048  234 QLSPKsllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvN 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 350 HTGE--KPFECNE--CGKAFRVNSSLTEHQRIHTGEKPYKCNEC-------GKAFRDNSSFARHRKIHTGEKPYRC--GL 416
Cdd:COG5048  314 HSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNS 393
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296010895 417 CEKAFRDQSALAQHQRIHTGEKPYTCN--ICEKAFSDHSALTQHKRIHTREKPYKCKICEKAFIRST 481
Cdd:COG5048  394 CIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
482-507 8.11e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 8.11e-05
                          10        20
                  ....*....|....*....|....*.
gi 296010895  482 HLTQHQRIHTGEKPYKCNKCGKAFNQ 507
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
324-404 3.36e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 324 GEKPYKCN--ECGKAFNQSTSfLQHQRIHtgekpfecNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKAFRDNSSFAR 401
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNG-LKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ...
gi 296010895 402 HRK 404
Cdd:COG5189  417 HRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
370-393 3.46e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.46e-04
                          10        20
                  ....*....|....*....|....
gi 296010895  370 SLTEHQRIHTGEKPYKCNECGKAF 393
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
314-339 9.52e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 9.52e-04
                          10        20
                  ....*....|....*....|....*.
gi 296010895  314 HLTKHQNIHSGEKPYKCNECGKAFNQ 339
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 1.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 296010895  454 ALTQHKRIHTREKPYKCKICEKAFIR 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
426-450 1.06e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.06e-03
                          10        20
                  ....*....|....*....|....*
gi 296010895  426 ALAQHQRIHTGEKPYTCNICEKAFS 450
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
234-254 1.17e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.17e-03
                          10        20
                  ....*....|....*....|.
gi 296010895  234 HQRIHTGEKPYECKECGKAFS 254
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFK 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
345-365 1.44e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.44e-03
                          10        20
                  ....*....|....*....|.
gi 296010895  345 QHQRIHTGEKPFECNECGKAF 365
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
258-283 1.45e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 296010895  258 SLTYHQKIHTGEKPFECNLCGKAFIR 283
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
436-517 3.29e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.09  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 436 GEKPYTCNI--CEKAFSDHSALTQHKRI-HTREKPYKCKICEKafirsthltqHQRIHTGEKPYKCNKCGKAFNQTANLI 512
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGLKYHMLHgHQNQKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGLK 415

                 ....*
gi 296010895 513 QHQRH 517
Cdd:COG5189  416 YHRKH 420
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
380-459 3.98e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010895 380 GEKPYKCN--ECGKAFRDNSSFARHRKiHtgekpyrcGLCEKAFRDQSALAQHQRIHTGEKPYTCNICEKAFSDHSALTQ 457
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ..
gi 296010895 458 HK 459
Cdd:COG5189  417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-311 5.36e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.36e-03
                          10        20
                  ....*....|....*....|..
gi 296010895  290 HHRIHTGEKPFKCNICEKAFVC 311
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
178-200 5.89e-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: 34.20  E-value: 5.89e-03
                          10        20
                  ....*....|....*....|...
gi 296010895  178 FECSECGKVFSKSSTLNKHQKIH 200
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
468-490 7.52e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 7.52e-03
                          10        20
                  ....*....|....*....|...
gi 296010895  468 YKCKICEKAFIRSTHLTQHQRIH 490
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
384-406 8.22e-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: 8.22e-03
                          10        20
                  ....*....|....*....|...
gi 296010895  384 YKCNECGKAFRDNSSFARHRKIH 406
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-421 9.39e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.39e-03
                          10        20
                  ....*....|....*....|....
gi 296010895  398 SFARHRKIHTGEKPYRCGLCEKAF 421
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH