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Conserved domains on  [gi|1907153620|ref|XP_036019420|]
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uncharacterized protein LOC100041677 isoform X2 [Mus musculus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

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:0003700|GO:0005515|GO:0008270|GO:0003677|GO:0006355|GO:0001217
PubMed:  22803940|8183940|2023909|8183939|10748030|27867147|28765213|11361095|30718982|10940247
SCOP:  4003583|4002243

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-52 7.99e-20

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


:

Pssm-ID: 460171  Cd Length: 42  Bit Score: 82.52  E-value: 7.99e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907153620  12 LLTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLFV 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-524 4.65e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 212 KKIYKCSECDKCFTHKSHLNIHQRIHTGENPYKCS--ECDKCFKHKFSFSMHQRIHTGEKPYKCSecDKCFTQKSHLSVH 289
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS--KSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 290 QRIHTGEKPykcSECDKCFTHKSHLNSHQRIHtgEKPYKCSECDKCFTKNGSLRIHQRIHTGENPYKCS--ECDKCFTHK 367
Cdd:COG5048   109 SLSSSSSNS---NDNNLLSSHSLPPSSRDPQL--PDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPanSLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 368 SNLNIHQRIHTGEKPYKCSECDKCFTHKSHLNSHQRIHTGEKPYKCSECDKCFTRKFHLSIHQRIHTGENPYKCSECDKC 447
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 448 FTQKSNLNIHQRIHTGE-------KPYKCSECDKCFTEKGSLRIHQR--IHTGEN--PYKCSE--CDKCFTRKFHLSIHQ 514
Cdd:COG5048   264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESlkPFSCPYslCGKLFSRNDALKRHI 343

                         330
                  ....*....|
gi 1907153620 515 KIHTGEKPYK 524
Cdd:COG5048   344 LLHTSISPAK 353
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-52 7.99e-20

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 82.52  E-value: 7.99e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907153620  12 LLTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLFV 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
13-55 1.54e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.56  E-value: 1.54e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907153620   13 LTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLFVENH 55
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 13-51 3.17e-16

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 72.20  E-value: 3.17e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907153620  13 LTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLF 51
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-524 4.65e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 212 KKIYKCSECDKCFTHKSHLNIHQRIHTGENPYKCS--ECDKCFKHKFSFSMHQRIHTGEKPYKCSecDKCFTQKSHLSVH 289
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS--KSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 290 QRIHTGEKPykcSECDKCFTHKSHLNSHQRIHtgEKPYKCSECDKCFTKNGSLRIHQRIHTGENPYKCS--ECDKCFTHK 367
Cdd:COG5048   109 SLSSSSSNS---NDNNLLSSHSLPPSSRDPQL--PDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPanSLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 368 SNLNIHQRIHTGEKPYKCSECDKCFTHKSHLNSHQRIHTGEKPYKCSECDKCFTRKFHLSIHQRIHTGENPYKCSECDKC 447
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 448 FTQKSNLNIHQRIHTGE-------KPYKCSECDKCFTEKGSLRIHQR--IHTGEN--PYKCSE--CDKCFTRKFHLSIHQ 514
Cdd:COG5048   264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESlkPFSCPYslCGKLFSRNDALKRHI 343

                         330
                  ....*....|
gi 1907153620 515 KIHTGEKPYK 524
Cdd:COG5048   344 LLHTSISPAK 353
zf-H2C2_2 pfam13465
Zinc-finger double domain;
397-422 7.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.33e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 397 HLNSHQRIHTGEKPYKCSECDKCFTR 422
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 12-52 7.99e-20

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 82.52  E-value: 7.99e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907153620  12 LLTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLFV 52
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
13-55 1.54e-18

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 79.56  E-value: 1.54e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907153620   13 LTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLFVENH 55
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQ 43
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 13-51 3.17e-16

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 72.20  E-value: 3.17e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907153620  13 LTFKDVALYFSLEEWECLSFAQRTLYMDVMLENYNNLLF 51
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
212-524 4.65e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 212 KKIYKCSECDKCFTHKSHLNIHQRIHTGENPYKCS--ECDKCFKHKFSFSMHQRIHTGEKPYKCSecDKCFTQKSHLSVH 289
Cdd:COG5048    31 PRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNS--KSLPLSNSKASSS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 290 QRIHTGEKPykcSECDKCFTHKSHLNSHQRIHtgEKPYKCSECDKCFTKNGSLRIHQRIHTGENPYKCS--ECDKCFTHK 367
Cdd:COG5048   109 SLSSSSSNS---NDNNLLSSHSLPPSSRDPQL--PDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPanSLSKDPSSN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 368 SNLNIHQRIHTGEKPYKCSECDKCFTHKSHLNSHQRIHTGEKPYKCSECDKCFTRKFHLSIHQRIHTGENPYKCSECDKC 447
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 448 FTQKSNLNIHQRIHTGE-------KPYKCSECDKCFTEKGSLRIHQR--IHTGEN--PYKCSE--CDKCFTRKFHLSIHQ 514
Cdd:COG5048   264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGESlkPFSCPYslCGKLFSRNDALKRHI 343

                         330
                  ....*....|
gi 1907153620 515 KIHTGEKPYK 524
Cdd:COG5048   344 LLHTSISPAK 353
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
224-442 1.03e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.24  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 224 FTHKSHLNIHQRIHTGENPYKCSECDKCFKHKFSFSMHQRIHTGEKPYKCSECDKCFTQKSHLSVHQRIHTGE------- 296
Cdd:COG5048   208 SYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfs 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 297 KPYKCSECDKCFTHKSHLNSHQR--IHTGE--KPYKCSE--CDKCFTKNGSLRIHQRIHTGENPYKCSECDKCFTHKSNL 370
Cdd:COG5048   288 LPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLL 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 371 NI----HQRIHTGEKPYKCSECDKCFT-------HKSHLNSHQRIHTGEKPYKCSECDKCFTRKFHLSIHQRIHTGENPY 439
Cdd:COG5048   368 NNeppqSLQQYKDLKNDKKSETLSNSCirnfkrdSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPL 447


                  ...
gi 1907153620 440 KCS 442
Cdd:COG5048   448 LCS 450
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
284-518 2.22e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 284 SHLSVHQRIHTGEKPYKCSECDKCFTHKSHLNSHQRIHTGEKPYKCSECDKCFTKNGSLRIHQRIHTGENPYKCSECDKC 363
Cdd:COG5048   184 LSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRS 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 364 FTHKSNLNIHQRIHTGE-------KPYKCSECDKCFTHKSHLNSHQR--IHTGE--KPYKCSE--CDKCFTRKFHLSIHQ 430
Cdd:COG5048   264 SLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHI 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 431 RIHTGENPYKC--SECDKCFTQKSNLNIHQRI--HTGEKPYKCSECDKCFTEKGSLR-------IHQRIHTGENPYKCSE 499
Cdd:COG5048   344 LLHTSISPAKEklLNSSSKFSPLLNNEPPQSLqqYKDLKNDKKSETLSNSCIRNFKRdsnlslhIITHLSFRPYNCKNPP 423

                         250
                  ....*....|....*....
gi 1907153620 500 CDKCFTRKFHLSIHQKIHT 518
Cdd:COG5048   424 CSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
254-498 1.67e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 254 HKFSFSMHQRIHTGEKPYKCSECDKCFTQKSHLSVHQRIHTGEKPYKCSECDKCFTHKSHLNSHQRIHtgeKPYKCSECD 333
Cdd:COG5048   182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLS---SSDSSSSAS 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 334 KCFTKNGSLRIHQRIH----------TGENPYKCSECDKCFTHKSNLNIHQR--IHTGE--KPYKCSE--CDKCFTHKSH 397
Cdd:COG5048   259 ESPRSSLPTASSQSSSpnesdsssekGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDA 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 398 LNSHQRIHTGEKPYKCSEC------DKCFTRKFHLSIHQRIHTGENPYKC---SECDKCFTQKSN--LNIHQRIHTGEKP 466
Cdd:COG5048   339 LKRHILLHTSISPAKEKLLnssskfSPLLNNEPPQSLQQYKDLKNDKKSEtlsNSCIRNFKRDSNlsLHIITHLSFRPYN 418

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907153620 467 YKCSECDKCFTEKGSLRIHQRIHTGENPYKCS 498
Cdd:COG5048   419 CKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS 450
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 380-485 7.27e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.01  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 380 EKPYKCSECDKCFTHKSHLN---SHQRIHT-GEKPYKCS--ECDKCFTRKFHLSIHqRIHtgenpykcSECDKCFTQKSN 453
Cdd:COG5189   315 KLPCTNSSSNGKLAHGGERNidtPSRMLKVkDGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPS 385

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907153620 454 LNIHQRIHTGEKPYKCSECDKCFTEKGSLRIH 485
Cdd:COG5189   386 PEKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
397-422 7.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.33e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 397 HLNSHQRIHTGEKPYKCSECDKCFTR 422
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 267-345 1.01e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.63  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 267 GEKPYKCS--ECDKCFTQKSHLSVHqRIHtgekpykcSECDKCFTHKSHLNSHQRIHTGEKPYKCSECDKCFTKNGSLRI 344
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  .
gi 1907153620 345 H 345
Cdd:COG5189   417 H 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
313-338 1.25e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.25e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 313 HLNSHQRIHTGEKPYKCSECDKCFTK 338
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
369-394 1.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 369 NLNIHQRIHTGEKPYKCSECDKCFTH 394
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
285-310 1.62e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 285 HLSVHQRIHTGEKPYKCSECDKCFTH 310
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
453-477 2.68e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.68e-03
                          10        20
                  ....*....|....*....|....*
gi 1907153620 453 NLNIHQRIHTGEKPYKCSECDKCFT 477
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 296-401 3.19e-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: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907153620 296 EKPYKCSECDKCFTHKSHLN---SHQRIHT-GEKPYKCS--ECDKCFTKNGSLRIHqRIHTGENPYKCSECDKcfthksn 369
Cdd:COG5189   315 KLPCTNSSSNGKLAHGGERNidtPSRMLKVkDGKPYKCPveGCNKKYKNQNGLKYH-MLHGHQNQKLHENPSP------- 386

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907153620 370 lNIHQRIHTGEKPYKCSECDKCFTHKSHLNSH 401
Cdd:COG5189   387 -EKMNIFSAKDKPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
229-254 4.69e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.69e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 229 HLNIHQRIHTGENPYKCSECDKCFKH 254
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
257-282 5.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.28e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 257 SFSMHQRIHTGEKPYKCSECDKCFTQ 282
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
341-366 5.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.33e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 341 SLRIHQRIHTGENPYKCSECDKCFTH 366
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
481-506 5.60e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 5.60e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 481 SLRIHQRIHTGENPYKCSECDKCFTR 506
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 355-377 7.12e-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: 7.12e-03
                          10        20
                  ....*....|....*....|...
gi 1907153620 355 YKCSECDKCFTHKSNLNIHQRIH 377
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 215-237 7.26e-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: 7.26e-03
                          10        20
                  ....*....|....*....|...
gi 1907153620 215 YKCSECDKCFTHKSHLNIHQRIH 237
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 299-321 7.26e-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: 7.26e-03
                          10        20
                  ....*....|....*....|...
gi 1907153620 299 YKCSECDKCFTHKSHLNSHQRIH 321
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 383-405 7.26e-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: 7.26e-03
                          10        20
                  ....*....|....*....|...
gi 1907153620 383 YKCSECDKCFTHKSHLNSHQRIH 405
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 439-461 7.85e-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: 7.85e-03
                          10        20
                  ....*....|....*....|...
gi 1907153620 439 YKCSECDKCFTQKSNLNIHQRIH 461
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
425-450 9.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.33e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907153620 425 HLSIHQRIHTGENPYKCSECDKCFTQ 450
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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