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Conserved domains on  [gi|755519338|ref|XP_011248799|]
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zinc finger, imprinted 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
50-105 1.53e-27

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 104.98  E-value: 1.53e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755519338    50 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLISVEYYIFKPKLITRLEQG 105
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQG 56
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-427 1.63e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.01  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 226 TTTPQSAPSEKPTSGKDVEGKPQTMRSSSTNPKRKPARQGKNHFKCKECGKTFNQTLHLVEHER--IHTGE--KPHKCD- 300
Cdd:COG5048  247 SLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPy 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 301 -TCGKSFRHLSYFLTHYRIHTGVRPYKCK--ECGKAFNSSSTLNNHCRIH-----SGEKPFKCD--ECGKTFKQSTKLTR 370
Cdd:COG5048  327 sLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSL 406

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755519338 371 HQRIHTGEKPY--KCGECNKCFGRSSSLREHKRIHTGEKPYCCQVCGKtFRVNSHLSEH 427
Cdd:COG5048  407 HIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
PRK13335 super family cl31400
superantigen-like protein SSL3; Reviewed;
137-269 8.13e-05

superantigen-like protein SSL3; Reviewed;


The actual alignment was detected with superfamily member PRK13335:

Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 45.12  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 137 TGDNSTKAEIRKPDNSKTTSLEKQKAADQGRGSQSLrAEKTSKsddrPSQNKEKCASTSTTEASKTSIPgNKENESAIPG 216
Cdd:PRK13335  56 AGANSATTQAANTRQERTPKLEKAPNTNEEKTSASK-IEKISQ----PKQEEQKSLNISATPAPKQEQS-QTTTESTTPK 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755519338 217 TS-SGQTSAATTTP-QSAPSEKPTS------GKDVEGKPQTMRSSSTnpkrKPARQGKNHF 269
Cdd:PRK13335 130 TKvTTPPSTNTPQPmQSTKSDTPQSptikqaQTDMTPKYEDLRAYYT----KPSFEFEKQF 186
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 437-459 5.05e-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: 5.05e-03
                          10        20
                  ....*....|....*....|...
gi 755519338  437 YKCDKCGKHFRNSSYLTEHKQIH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 521-543 7.33e-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: 7.33e-03
                          10        20
                  ....*....|....*....|...
gi 755519338  521 FVCHKCDKGFTDKTTLNNHLKIH 543
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
50-105 1.53e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 104.98  E-value: 1.53e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755519338    50 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLISVEYYIFKPKLITRLEQG 105
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQG 56
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 49-89 2.39e-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: 2.39e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755519338   49 PVIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLISV 89
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 50-88 2.41e-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: 86.83  E-value: 2.41e-21
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755519338  50 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLIS 88
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-427 1.63e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.01  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 226 TTTPQSAPSEKPTSGKDVEGKPQTMRSSSTNPKRKPARQGKNHFKCKECGKTFNQTLHLVEHER--IHTGE--KPHKCD- 300
Cdd:COG5048  247 SLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPy 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 301 -TCGKSFRHLSYFLTHYRIHTGVRPYKCK--ECGKAFNSSSTLNNHCRIH-----SGEKPFKCD--ECGKTFKQSTKLTR 370
Cdd:COG5048  327 sLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSL 406

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755519338 371 HQRIHTGEKPY--KCGECNKCFGRSSSLREHKRIHTGEKPYCCQVCGKtFRVNSHLSEH 427
Cdd:COG5048  407 HIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
283-308 4.10e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.10e-05
                          10        20
                  ....*....|....*....|....*.
gi 755519338  283 HLVEHERIHTGEKPHKCDTCGKSFRH 308
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
137-269 8.13e-05

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 45.12  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 137 TGDNSTKAEIRKPDNSKTTSLEKQKAADQGRGSQSLrAEKTSKsddrPSQNKEKCASTSTTEASKTSIPgNKENESAIPG 216
Cdd:PRK13335  56 AGANSATTQAANTRQERTPKLEKAPNTNEEKTSASK-IEKISQ----PKQEEQKSLNISATPAPKQEQS-QTTTESTTPK 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755519338 217 TS-SGQTSAATTTP-QSAPSEKPTS------GKDVEGKPQTMRSSSTnpkrKPARQGKNHF 269
Cdd:PRK13335 130 TKvTTPPSTNTPQPmQSTKSDTPQSptikqaQTDMTPKYEDLRAYYT----KPSFEFEKQF 186
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 437-459 5.05e-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: 5.05e-03
                          10        20
                  ....*....|....*....|...
gi 755519338  437 YKCDKCGKHFRNSSYLTEHKQIH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 521-543 7.33e-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: 7.33e-03
                          10        20
                  ....*....|....*....|...
gi 755519338  521 FVCHKCDKGFTDKTTLNNHLKIH 543
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
flgF PRK12641
flagellar basal-body rod protein FlgF;
26-114 8.29e-03

flagellar basal-body rod protein FlgF;


Pssm-ID: 105809 [Multi-domain]  Cd Length: 252  Bit Score: 38.39  E-value: 8.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338  26 TANQLSEKKRRIP--ITSLPT-WYKEPVIFKdvavyfsqkewqLLEPAQKDLYKDvmlenyENLISVEYYIFKPKLITRL 102
Cdd:PRK12641  11 AANKLLEKQAIIAnnLANISTtGFKEKFILA------------IQNHNVKNLYNS------DKKITKEYYNLSPGTLRYT 72

                         90
                 ....*....|..
gi 755519338 103 EQGVDLFAKEND 114
Cdd:PRK12641  73 GRNLDLFIKDNG 84
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
50-105 1.53e-27

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 104.98  E-value: 1.53e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755519338    50 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLISVEYYIFKPKLITRLEQG 105
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQG 56
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 49-89 2.39e-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: 2.39e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755519338   49 PVIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLISV 89
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 50-88 2.41e-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: 86.83  E-value: 2.41e-21
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755519338  50 VIFKDVAVYFSQKEWQLLEPAQKDLYKDVMLENYENLIS 88
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
226-427 1.63e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 57.01  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 226 TTTPQSAPSEKPTSGKDVEGKPQTMRSSSTNPKRKPARQGKNHFKCKECGKTFNQTLHLVEHER--IHTGE--KPHKCD- 300
Cdd:COG5048  247 SLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPy 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 301 -TCGKSFRHLSYFLTHYRIHTGVRPYKCK--ECGKAFNSSSTLNNHCRIH-----SGEKPFKCD--ECGKTFKQSTKLTR 370
Cdd:COG5048  327 sLCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSCIRNFKRDSNLSL 406

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755519338 371 HQRIHTGEKPY--KCGECNKCFGRSSSLREHKRIHTGEKPYCCQVCGKtFRVNSHLSEH 427
Cdd:COG5048  407 HIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKS-FRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
237-551 2.34e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 237 PTSGKDVEGKPQTMRSSStNPKRKPARQGKNHFKCKECGKTFNQTLHLVEHERIHTGEKPHKC--DTCGKSF-RHLSYFL 313
Cdd:COG5048    3 LTSSQSSSSNNSVLSSTP-KSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFsRPLELSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 314 THYRIHTGVRPYKCKECGKAFNSSSTLNNHCRIHSGEKPFKCDECGKTFKQSTKLTRHQRIHTGEKPYKCGECNKCFGRS 393
Cdd:COG5048   82 HLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 394 S----------------------SLREHKRIHTGEKPYCCQVCGKTFRVNSHLSEHQRLHLKVKPYKCDKCG----KHFR 447
Cdd:COG5048  162 PqsnslhpplpanslskdpssnlSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSqlspKSLL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 448 NSSYLTEHKQIHVPGARVDCPECGKVFACKVALLKH---QKRHEANSRYRCKGCGKTFRCKSSIQRHER--LHAGE--KP 520
Cdd:COG5048  242 SQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNEsdsSSEKGFSLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKP 321

                        330       340       350
                 ....*....|....*....|....*....|...
gi 755519338 521 FVC--HKCDKGFTDKTTLNNHLKIHSGDRPDPC 551
Cdd:COG5048  322 FSCpySLCGKLFSRNDALKRHILLHTSISPAKE 354
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
324-476 2.34e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 324 PYKCKECGKAFNSSSTLNNH--CRIHSGE--KPFKCDE--CGKTFKQSTKLTRHQRIHTGEKPYKC--GECNKCFGRSS- 394
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHlrSVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLn 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 395 ----SLREHKRIHTGEKPYCCQV--CGKTFRVNSHLSEHQRLHLKVKPY--KCDKCGKHFRNSSYLTEHKQIHVPGARVD 466
Cdd:COG5048  369 neppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNRHYNLIPHKKIHTNHAPLL 448

                        170
                 ....*....|
gi 755519338 467 CPECGKVFAC 476
Cdd:COG5048  449 CSILKSFRRD 458
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
183-524 1.17e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 183 RPSQNKEKCASTSTTEASKTSIPGNKENeSAIPGTSSGQTSAATTTPQSAPSEKPTSGKDVEGKPQTMRSSSTNPKRKPA 262
Cdd:COG5048   89 NPSDLNSKSLPLSNSKASSSSLSSSSSN-SNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSL 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 263 RQGKNHFkCKECGKTFNQTLHLveHERIHTGEKPHKCDTCGKSFRHLSYFLTHYRIHTGVRPYKCKECGKAFNSSSTLNN 342
Cdd:COG5048  168 HPPLPAN-SLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 343 HCRIHSGEKPFKCDECGKTFKQSTKLTRHQRIHTGE-------KPYKCGECNKCFGRSSSLREHKR--IHTGE--KPYCC 411
Cdd:COG5048  245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSC 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 412 --QVCGKTFRVNSHLSEHQRLHLKVKPYKC--DKCGKHFRNSSY-----LTEHKQIHVPGARVDCPECGKVFACK----V 478
Cdd:COG5048  325 pySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSNSCIRNFKrdsnL 404

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 755519338 479 ALLKHQKRHEANSRYRCKGCGKTFRCKSSIQRHERLHAGEKPFVCH 524
Cdd:COG5048  405 SLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS 450
zf-H2C2_2 pfam13465
Zinc-finger double domain;
283-308 4.10e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.10e-05
                          10        20
                  ....*....|....*....|....*.
gi 755519338  283 HLVEHERIHTGEKPHKCDTCGKSFRH 308
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-364 4.84e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 4.84e-05
                          10        20
                  ....*....|....*....|....*
gi 755519338  340 LNNHCRIHSGEKPFKCDECGKTFKQ 364
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 349-427 6.99e-05

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 45.48  E-value: 6.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 349 GEKPFKCD--ECGKTFKQSTKLTRHqRIHtgekpykcGECNKCFGRSSSLREHKRIHTGEKPYCCQVCGKTFRVNSHLSE 426
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 .
gi 755519338 427 H 427
Cdd:COG5189  417 H 417
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
137-269 8.13e-05

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 45.12  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 137 TGDNSTKAEIRKPDNSKTTSLEKQKAADQGRGSQSLrAEKTSKsddrPSQNKEKCASTSTTEASKTSIPgNKENESAIPG 216
Cdd:PRK13335  56 AGANSATTQAANTRQERTPKLEKAPNTNEEKTSASK-IEKISQ----PKQEEQKSLNISATPAPKQEQS-QTTTESTTPK 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755519338 217 TS-SGQTSAATTTP-QSAPSEKPTS------GKDVEGKPQTMRSSSTnpkrKPARQGKNHF 269
Cdd:PRK13335 130 TKvTTPPSTNTPQPmQSTKSDTPQSptikqaQTDMTPKYEDLRAYYT----KPSFEFEKQF 186
zf-H2C2_2 pfam13465
Zinc-finger double domain;
395-418 1.29e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.29e-04
                          10        20
                  ....*....|....*....|....
gi 755519338  395 SLREHKRIHTGEKPYCCQVCGKTF 418
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 353-375 3.98e-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: 3.98e-04
                          10        20
                  ....*....|....*....|...
gi 755519338  353 FKCDECGKTFKQSTKLTRHQRIH 375
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
368-390 6.77e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.77e-04
                          10        20
                  ....*....|....*....|...
gi 755519338  368 LTRHQRIHTGEKPYKCGECNKCF 390
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 377-456 9.91e-04

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: 9.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 377 GEKPYKCG--ECNKCFGRSSSLREHKRihtgeKPYCCQVCGKTFRVNSHlsehQRLHLKVKPYKCDKCGKHFRNSSYLTE 454
Cdd:COG5189  346 DGKPYKCPveGCNKKYKNQNGLKYHML-----HGHQNQKLHENPSPEKM----NIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                 ..
gi 755519338 455 HK 456
Cdd:COG5189  417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
315-336 1.16e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|..
gi 755519338  315 HYRIHTGVRPYKCKECGKAFNS 336
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 437-459 5.05e-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: 5.05e-03
                          10        20
                  ....*....|....*....|...
gi 755519338  437 YKCDKCGKHFRNSSYLTEHKQIH 459
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK08581 PRK08581
amidase domain-containing protein;
74-270 6.47e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 39.39  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338  74 LYKDVMLENYENLISVEYYIFKPKLITRLEQgvdLFAKENDVPGDPQQGEagvSRSDTSAGKKTGDNSTKaeirkpDNSK 153
Cdd:PRK08581  95 IYKNLPQTNINQLLTKNKYDDNYSLTTLIQN---LFNLNSDISDYEQPRN---SEKSTNDSNKNSDSSIK------NDTD 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338 154 TTSLEKQKAADQGRGSQSLRAEKTSKSDDRPSQ--NKEKCASTSTTEASKTSIPGNKENE----SAIPGTSSGQTSAATT 227
Cdd:PRK08581 163 TQSSKQDKADNQKAPSSNNTKPSTSNKQPNSPKptQPNQSNSQPASDDTANQKSSSKDNQsmsdSALDSILDQYSEDAKK 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755519338 228 TPQS--APSEKPTSGKDVEGKPQTMRSSSTNPKRKPARQGKNHFK 270
Cdd:PRK08581 243 TQKDyaSQSKKDKTETSNTKNPQLPTQDELKHKSKPAQSFENDVN 287
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 381-403 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 755519338  381 YKCGECNKCFGRSSSLREHKRIH 403
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 521-543 7.33e-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: 7.33e-03
                          10        20
                  ....*....|....*....|...
gi 755519338  521 FVCHKCDKGFTDKTTLNNHLKIH 543
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
flgF PRK12641
flagellar basal-body rod protein FlgF;
26-114 8.29e-03

flagellar basal-body rod protein FlgF;


Pssm-ID: 105809 [Multi-domain]  Cd Length: 252  Bit Score: 38.39  E-value: 8.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519338  26 TANQLSEKKRRIP--ITSLPT-WYKEPVIFKdvavyfsqkewqLLEPAQKDLYKDvmlenyENLISVEYYIFKPKLITRL 102
Cdd:PRK12641  11 AANKLLEKQAIIAnnLANISTtGFKEKFILA------------IQNHNVKNLYNS------DKKITKEYYNLSPGTLRYT 72

                         90
                 ....*....|..
gi 755519338 103 EQGVDLFAKEND 114
Cdd:PRK12641  73 GRNLDLFIKDNG 84
zf-H2C2_2 pfam13465
Zinc-finger double domain;
423-448 9.14e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 9.14e-03
                          10        20
                  ....*....|....*....|....*.
gi 755519338  423 HLSEHQRLHLKVKPYKCDKCGKHFRN 448
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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