NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1020158986|ref|NP_001310235|]
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 1020158986   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 1020158986 186 VFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYEC--KECGKAFSVSSSLTYHQ 263
Cdd:COG5048     4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 264 KIHTGEKPFECNlcGKAFIRNIHLAHHHRIHTGEKPFKCNICEKafvcraHLTKHQNIHS------------GEKPYKCN 331
Cdd:COG5048    84 RTHHNNPSDLNS--KSLPLSNSKASSSSLSSSSSNSNDNNLLSS------HSLPPSSRDPqlpdllsisnlrNNPLPGNN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 332 ECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKA 392
Cdd:COG5048   156 SSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 393 FRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGE-------KPYTCNICEKAFSDHSALTQHKR--IHT 463
Cdd:COG5048   236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHS 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1020158986 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 1020158986   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 1020158986  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 1020158986  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 1020158986 186 VFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYEC--KECGKAFSVSSSLTYHQ 263
Cdd:COG5048     4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 264 KIHTGEKPFECNlcGKAFIRNIHLAHHHRIHTGEKPFKCNICEKafvcraHLTKHQNIHS------------GEKPYKCN 331
Cdd:COG5048    84 RTHHNNPSDLNS--KSLPLSNSKASSSSLSSSSSNSNDNNLLSS------HSLPPSSRDPqlpdllsisnlrNNPLPGNN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 332 ECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKA 392
Cdd:COG5048   156 SSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 393 FRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGE-------KPYTCNICEKAFSDHSALTQHKR--IHT 463
Cdd:COG5048   236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHS 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1020158986 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 1020158986 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 1020158986   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 1020158986  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 1020158986  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 1020158986 186 VFSKSSTLNKHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQRIHTGEKPYEC--KECGKAFSVSSSLTYHQ 263
Cdd:COG5048     4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 264 KIHTGEKPFECNlcGKAFIRNIHLAHHHRIHTGEKPFKCNICEKafvcraHLTKHQNIHS------------GEKPYKCN 331
Cdd:COG5048    84 RTHHNNPSDLNS--KSLPLSNSKASSSSLSSSSSNSNDNNLLSS------HSLPPSSRDPqlpdllsisnlrNNPLPGNN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 332 ECGKAFNQSTSFLQ-------------------HQRIHTGEKPFECNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKA 392
Cdd:COG5048   156 SSSVNTPQSNSLHPplpanslskdpssnlslliSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 393 FRDNSSFARHRKIHTGEKPYRCGLCEKAFRDQSALAQHQRIHTGE-------KPYTCNICEKAFSDHSALTQHKR--IHT 463
Cdd:COG5048   236 SPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHS 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1020158986 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 1020158986 115 SSSSHWKCASLLEWQCGGQEISLQRVVLTHPNTPSQECDESGSTMSSSLHSDQSQGFQPSKNAFECSECGKVFSKSSTLN 194
Cdd:COG5048   189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 195 KHQKIHNEKNANQKIHIKEKRYECRECGKAFHQSTHLIHHQR--IHTGE--KPYECKE--CGKAFSVSSSLTYHQKIHTG 268
Cdd:COG5048   269 SSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTS 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 269 EKPFECNLC-------GKAFIRNIHLAHHHRIHTGEKPFKC--NICEKAFVCRAHLTKH--QNIHSGEKPYKCNECGKAF 337
Cdd:COG5048   349 ISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSF 428

                         250       260
                  ....*....|....*....|....*....
gi 1020158986 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 1020158986 134 EISLQRVVLTHPNTPSQECDESGSTMSSSLHSDQSQGFQPSKNaFECSECGKVFSKSST--------LNKHQKIHNEKNA 205
Cdd:COG5048   170 PLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIP-SSSSDQNLENSSSSLplttnsqlSPKSLLSQSPSSL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 206 NQKIHIKEKRYECREC-GKAFHQSTHLIHH-QRIHTG-EKPYECKECGKAFSVSSSLTYHQ--KIHTGE--KPFEC--NL 276
Cdd:COG5048   249 SSSDSSSSASESPRSSlPTASSQSSSPNESdSSSEKGfSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCpySL 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 277 CGKAFIRNIHLAHHHRIHTGEKPFKC--NICEKAFV-----CRAHLTKHQNIHSGEKPYKCNECGKAFNQST-SFLQHQR 348
Cdd:COG5048   329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKKSETLSNSCIRNFKRdSNLSLHI 408

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1020158986 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 1020158986 198 KIHNEKNANQKIHIKEKRyecRECGKAFHQSTHLIHHQRIHTGEKPYECKECGKAFSVSSSLTYHQKIH-TGEKPFECNL 276
Cdd:COG5048   157 SSVNTPQSNSLHPPLPAN---SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENsSSSLPLTTNS 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 277 CGKAF----IRNIHLAHHHRIHTGEKPFKCNICEKAFVCRAHLTKHQNIHSG-EKPYKCNECGKAFNQSTSFLQHQR--I 349
Cdd:COG5048   234 QLSPKsllsQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGfSLPIKSKQCNISFSRSSPLTRHLRsvN 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158986 350 HTGE--KPFECNE--CGKAFRVNSSLTEHQRIHTGEKPYKCNEC-------GKAFRDNSSFARHRKIHTGEKPYRC--GL 416
Cdd:COG5048   314 HSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLnssskfsPLLNNEPPQSLQQYKDLKNDKKSETlsNS 393

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1020158986 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 1020158986 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 1020158986 324 GEKPYKCN--ECGKAFNQSTSfLQHQRIHtgekpfecNECGKAFRVNSSLTEHQRIHTGEKPYKCNECGKAFRDNSSFAR 401
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNG-LKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ...
gi 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 436 GEKPYTCNI--CEKAFSDHSALTQHKRI-HTREKPYKCKICEKafirsthltqHQRIHTGEKPYKCNKCGKAFNQTANLI 512
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYHMLHgHQNQKLHENPSPEK----------MNIFSAKDKPYRCEVCDKRYKNLNGLK 415


                  ....*
gi 1020158986 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 1020158986 380 GEKPYKCN--ECGKAFRDNSSFARHRKiHtgekpyrcGLCEKAFRDQSALAQHQRIHTGEKPYTCNICEKAFSDHSALTQ 457
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYHML-H--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ..
gi 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 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 1020158986 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