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Conserved domains on  [gi|157818909|ref|NP_001100943|]
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zinc finger, imprinted 1 [Rattus norvegicus]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12204378)

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 smart00349
krueppel associated box;
51-106 1.66e-27

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 104.98  E-value: 1.66e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157818909    51 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLISVEYYIFKPKLITRLEQG 106
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQG 56
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
178-426 7.68e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 178 TSKSDDRPSQNKEKSDSTSTTEAGKTTNPGNQENESAAPGTSSSQTPSTTAPQSTPPEKSTSGKDGQGKSPNTSSSTNPK 257
Cdd:COG5048  205 LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEK 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 258 RKPARqgknhFKCKECGKTFNQTLHLVEHER--IHTGE--KPHKCD--TCGKSFRHLSYFLTHYRIHTGVRPYKCK--EC 329
Cdd:COG5048  285 GFSLP-----IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKllNS 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 330 GKAFNSSSTLNNHCRIH-----SGEKPFKCD--ECGKTFKQSTKLTRHQRIHTGEKP--YKCGECNKCFGRSSSLREHKR 400
Cdd:COG5048  360 SSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKK 439

                        250       260
                 ....*....|....*....|....*.
gi 157818909 401 IHTGEKPYRCQVCGKtFRVNSHLSEH 426
Cdd:COG5048  440 IHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 9.88e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.88e-03
                          10        20
                  ....*....|....*....|....*.
gi 157818909  422 HLSEHQRLHLKVKPYKCDKCGKHFRN 447
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
51-106 1.66e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 104.98  E-value: 1.66e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157818909    51 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLISVEYYIFKPKLITRLEQG 106
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQG 56
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 50-90 2.69e-23

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: 92.53  E-value: 2.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 157818909   50 PVIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLISV 90
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 51-89 4.08e-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: 86.45  E-value: 4.08e-21
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157818909  51 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLIS 89
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
178-426 7.68e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 178 TSKSDDRPSQNKEKSDSTSTTEAGKTTNPGNQENESAAPGTSSSQTPSTTAPQSTPPEKSTSGKDGQGKSPNTSSSTNPK 257
Cdd:COG5048  205 LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEK 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 258 RKPARqgknhFKCKECGKTFNQTLHLVEHER--IHTGE--KPHKCD--TCGKSFRHLSYFLTHYRIHTGVRPYKCK--EC 329
Cdd:COG5048  285 GFSLP-----IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKllNS 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 330 GKAFNSSSTLNNHCRIH-----SGEKPFKCD--ECGKTFKQSTKLTRHQRIHTGEKP--YKCGECNKCFGRSSSLREHKR 400
Cdd:COG5048  360 SSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKK 439

                        250       260
                 ....*....|....*....|....*.
gi 157818909 401 IHTGEKPYRCQVCGKtFRVNSHLSEH 426
Cdd:COG5048  440 IHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
282-307 4.42e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.42e-05
                          10        20
                  ....*....|....*....|....*.
gi 157818909  282 HLVEHERIHTGEKPHKCDTCGKSFRH 307
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 9.88e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.88e-03
                          10        20
                  ....*....|....*....|....*.
gi 157818909  422 HLSEHQRLHLKVKPYKCDKCGKHFRN 447
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
51-106 1.66e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 104.98  E-value: 1.66e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157818909    51 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLISVEYYIFKPKLITRLEQG 106
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQG 56
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 50-90 2.69e-23

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: 92.53  E-value: 2.69e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 157818909   50 PVIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLISV 90
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 51-89 4.08e-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: 86.45  E-value: 4.08e-21
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157818909  51 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYGNLIS 89
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
178-426 7.68e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.09  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 178 TSKSDDRPSQNKEKSDSTSTTEAGKTTNPGNQENESAAPGTSSSQTPSTTAPQSTPPEKSTSGKDGQGKSPNTSSSTNPK 257
Cdd:COG5048  205 LSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEK 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 258 RKPARqgknhFKCKECGKTFNQTLHLVEHER--IHTGE--KPHKCD--TCGKSFRHLSYFLTHYRIHTGVRPYKCK--EC 329
Cdd:COG5048  285 GFSLP-----IKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKllNS 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 330 GKAFNSSSTLNNHCRIH-----SGEKPFKCD--ECGKTFKQSTKLTRHQRIHTGEKP--YKCGECNKCFGRSSSLREHKR 400
Cdd:COG5048  360 SSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKK 439

                        250       260
                 ....*....|....*....|....*.
gi 157818909 401 IHTGEKPYRCQVCGKtFRVNSHLSEH 426
Cdd:COG5048  440 IHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
238-575 4.88e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 49.31  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 238 TSGKDGQGKSPNTSSSTNPKRKPARQGKNHFKCKECGKTFNQTLHLVEHERIHTGEKPHKC--DTCGKSF-RHLSYFLTH 314
Cdd:COG5048    4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFsRPLELSRHL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 315 YRIHTGVRPYKCKECGKAFNSSSTLNNHCRIHSGEKPFKCDECGKTFKQSTKLTRHQRIHTGEKPYKCGECNKCFGRSS- 393
Cdd:COG5048   84 RTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPq 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 394 ---------------------SLREHKRIHTGEKPYRCQVCGKTFRVNSHLSEHQRLHLKVKPYKCDKCGKHFRNSSYLS 452
Cdd:COG5048  164 snslhpplpanslskdpssnlSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQ 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 453 EHKQIHVPGARVDCPECGKVFACKVAL-LKHQKRHEANS------RYRCKGCGKTFRCKSSIQRHER--LHAGE--KPFV 521
Cdd:COG5048  244 SPSSLSSSDSSSSASESPRSSLPTASSqSSSPNESDSSSekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFS 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157818909 522 CTK--CDKGFTDKTTLNNHLKIHSGDRPDPC--AQCGRTFKKLATLLIHQKKHNKKKP 575
Cdd:COG5048  324 CPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQYKDL 381
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 348-426 1.20e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 47.79  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 348 GEKPFKCD--ECGKTFKQSTKLTRHqRIHtgekpykcGECNKCFGRSSSLREHKRIHTGEKPYRCQVCGKTFRVNSHLSE 425
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 .
gi 157818909 426 H 426
Cdd:COG5189  417 H 417
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
323-475 2.43e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 323 PYKCKECGKAFNSSSTLNNH--CRIHSGE--KPFKCDE--CGKTFKQSTKLTRHQRIHTGEKPYKC--GECNKCFGRSS- 393
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLn 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 394 ----SLREHKRIHTGEKPYRCQV--CGKTFRVNSHLSEHQRLHLKVKP--YKCDKCGKHFRNSSYLSEHKQIHVPGARVD 465
Cdd:COG5048  369 neppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLL 448

                        170
                 ....*....|
gi 157818909 466 CPECGKVFAC 475
Cdd:COG5048  449 CSILKSFRRD 458
zf-H2C2_2 pfam13465
Zinc-finger double domain;
282-307 4.42e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.42e-05
                          10        20
                  ....*....|....*....|....*.
gi 157818909  282 HLVEHERIHTGEKPHKCDTCGKSFRH 307
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
394-417 4.88e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.88e-05
                          10        20
                  ....*....|....*....|....
gi 157818909  394 SLREHKRIHTGEKPYRCQVCGKTF 417
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
339-363 5.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 5.28e-05
                          10        20
                  ....*....|....*....|....*
gi 157818909  339 LNNHCRIHSGEKPFKCDECGKTFKQ 363
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 352-374 4.34e-04

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: 37.66  E-value: 4.34e-04
                          10        20
                  ....*....|....*....|...
gi 157818909  352 FKCDECGKTFKQSTKLTRHQRIH 374
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
286-557 7.16e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 286 HERIHTGEKPHKCDTCGKSFRHLSYFLTHYRIHTGVRPYKCKECGKAFNSSSTLNNHCRIHSGEKPFKCDECGKTFKQST 365
Cdd:COG5048  189 SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 366 KLTRHQRIHTGE-------KPYKCGECNKCFGRSSSLREHKR--IHTGE--KPYRC--QVCGKTFRVNSHLSEHQRLHLK 432
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTS 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 433 VKPYKCdkcgkHFRNSSYLSEhkqihvpgarvdcpecGKVFACKVALLKHQKRHEANSRYRC--KGCGKTFRCKSSIQRH 510
Cdd:COG5048  349 ISPAKE-----KLLNSSSKFS----------------PLLNNEPPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 157818909 511 ERLHAGEKP--FVCTKCDKGFTDKTTLNNHLKIHSGDRPDPCAQCGRTF 557
Cdd:COG5048  408 IITHLSFRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-389 7.60e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.60e-04
                          10        20
                  ....*....|....*....|...
gi 157818909  367 LTRHQRIHTGEKPYKCGECNKCF 389
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
314-335 1.30e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|..
gi 157818909  314 HYRIHTGVRPYKCKECGKAFNS 335
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 376-455 1.41e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818909 376 GEKPYKCG--ECNKCFGRSSSLREHkRIHTGekpyrcqvCGKTFRVNSHLSEHQRLHLKVKPYKCDKCGKHFRNSSYLSE 453
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLHGH--------QNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ..
gi 157818909 454 HK 455
Cdd:COG5189  417 HR 418
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 408-430 4.66e-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: 34.58  E-value: 4.66e-03
                          10        20
                  ....*....|....*....|...
gi 157818909  408 YRCQVCGKTFRVNSHLSEHQRLH 430
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 380-402 7.68e-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: 7.68e-03
                          10        20
                  ....*....|....*....|...
gi 157818909  380 YKCGECNKCFGRSSSLREHKRIH 402
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
422-447 9.88e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.88e-03
                          10        20
                  ....*....|....*....|....*.
gi 157818909  422 HLSEHQRLHLKVKPYKCDKCGKHFRN 447
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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