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Conserved domains on  [gi|219521356|gb|AAI71888|]
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ZFP57 protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
44-104 1.40e-28

krueppel associated box;


:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 107.68  E-value: 1.40e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521356    44 VTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTSVArIFLHKPELITKLEQEEEQW 104
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGEEPW 60
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
185-430 1.06e-05

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 185 SRRSYLYSHQFVHNPKLTNSCSQCGKLFRSPKSLSYHRRMHLGER-PFCCTLCDKTYCDASGLSRHRRVHL----GYRPH 259
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 260 SC--SVCGKSFRDQSELKRHQKIHQNQEPvdgnqectlripgtqaeFQTPIARSQGSIQGLLDvnhapvARSQEPIFRTE 337
Cdd:COG5048  323 SCpySLCGKLFSRNDALKRHILLHTSISP-----------------AKEKLLNSSSKFSPLLN------NEPPQSLQQYK 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 338 GPMAQNQASVLKNQAPVTRTQAPItgtlcqdARSNSHPVKPSRLNVFCCPHCSLTFSKKSYLSRHQKAHLTEPPnYCFHC 417
Cdd:COG5048  380 DLKNDKKSETLSNSCIRNFKRDSN-------LSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAP-LLCSI 451

                        250
                 ....*....|...
gi 219521356 418 SKSFSSFSRLVRH 430
Cdd:COG5048  452 LKSFRRDLDLSNH 464
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 102-250 8.55e-04

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.01  E-value: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 102 EQWREFVHLPNTEGLSEGK-KKELREqhPSLRDEGTSDDKvfLACRGAGQCPLSAPAG--TMDRTRVLQASQAGPPFFCY 178
Cdd:COG5189  278 ELFEESSLGFDYEFIHKSVgNKEIRG--GISTGEMIDVRK--LPCTNSSSNGKLAHGGerNIDTPSRMLKVKDGKPYKCP 353

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521356 179 T--CDKCFSRRSYLYSHqfvhnpKLTNSCSQCGKLFRSPKSlsyHRRMHLGERPFCCTLCDKTYCDASGLSRHR 250
Cdd:COG5189  354 VegCNKKYKNQNGLKYH------MLHGHQNQKLHENPSPEK---MNIFSAKDKPYRCEVCDKRYKNLNGLKYHR 418
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
44-104 1.40e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 107.68  E-value: 1.40e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521356    44 VTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTSVArIFLHKPELITKLEQEEEQW 104
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 43-83 6.34e-21

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: 85.60  E-value: 6.34e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 219521356   43 PVTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTSV 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 44-82 1.26e-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: 73.35  E-value: 1.26e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 219521356  44 VTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTS 82
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
185-430 1.06e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 185 SRRSYLYSHQFVHNPKLTNSCSQCGKLFRSPKSLSYHRRMHLGER-PFCCTLCDKTYCDASGLSRHRRVHL----GYRPH 259
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 260 SC--SVCGKSFRDQSELKRHQKIHQNQEPvdgnqectlripgtqaeFQTPIARSQGSIQGLLDvnhapvARSQEPIFRTE 337
Cdd:COG5048  323 SCpySLCGKLFSRNDALKRHILLHTSISP-----------------AKEKLLNSSSKFSPLLN------NEPPQSLQQYK 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 338 GPMAQNQASVLKNQAPVTRTQAPItgtlcqdARSNSHPVKPSRLNVFCCPHCSLTFSKKSYLSRHQKAHLTEPPnYCFHC 417
Cdd:COG5048  380 DLKNDKKSETLSNSCIRNFKRDSN-------LSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAP-LLCSI 451

                        250
                 ....*....|...
gi 219521356 418 SKSFSSFSRLVRH 430
Cdd:COG5048  452 LKSFRRDLDLSNH 464
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 259-281 2.80e-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: 38.05  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|...
gi 219521356  259 HSCSVCGKSFRDQSELKRHQKIH 281
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 102-250 8.55e-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: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 102 EQWREFVHLPNTEGLSEGK-KKELREqhPSLRDEGTSDDKvfLACRGAGQCPLSAPAG--TMDRTRVLQASQAGPPFFCY 178
Cdd:COG5189  278 ELFEESSLGFDYEFIHKSVgNKEIRG--GISTGEMIDVRK--LPCTNSSSNGKLAHGGerNIDTPSRMLKVKDGKPYKCP 353

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521356 179 T--CDKCFSRRSYLYSHqfvhnpKLTNSCSQCGKLFRSPKSlsyHRRMHLGERPFCCTLCDKTYCDASGLSRHR 250
Cdd:COG5189  354 VegCNKKYKNQNGLKYH------MLHGHQNQKLHENPSPEK---MNIFSAKDKPYRCEVCDKRYKNLNGLKYHR 418
PHA00733 PHA00733
hypothetical protein
 196-277 2.50e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 196 VHNPKLTNSCSQCGKLFRSpKSLSyhrrmhlgerPFCCTLCDKTYCDASGLSRHRRvhlgYRPHS--CSVCGKSFRDQSE 273
Cdd:PHA00733  50 IYNPQLLDESSYLYKLLTS-KAVS----------PYVCPLCLMPFSSSVSLKQHIR----YTEHSkvCPVCGKEFRNTDS 114


                 ....
gi 219521356 274 LKRH 277
Cdd:PHA00733 115 TLDH 118
 
Name Accession Description Interval E-value
KRAB smart00349
krueppel associated box;
44-104 1.40e-28

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 107.68  E-value: 1.40e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521356    44 VTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTSVArIFLHKPELITKLEQEEEQW 104
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLG-FQVPKPDLISQLEQGEEPW 60
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 43-83 6.34e-21

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: 85.60  E-value: 6.34e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 219521356   43 PVTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTSV 83
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 44-82 1.26e-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: 73.35  E-value: 1.26e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 219521356  44 VTFEDVAVNFTQEEWDCLDASQRVLYQDVMSETFKNLTS 82
Cdd:cd07765    1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
185-430 1.06e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.15  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 185 SRRSYLYSHQFVHNPKLTNSCSQCGKLFRSPKSLSYHRRMHLGER-PFCCTLCDKTYCDASGLSRHRRVHL----GYRPH 259
Cdd:COG5048  243 QSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRSVNhsgeSLKPF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 260 SC--SVCGKSFRDQSELKRHQKIHQNQEPvdgnqectlripgtqaeFQTPIARSQGSIQGLLDvnhapvARSQEPIFRTE 337
Cdd:COG5048  323 SCpySLCGKLFSRNDALKRHILLHTSISP-----------------AKEKLLNSSSKFSPLLN------NEPPQSLQQYK 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 338 GPMAQNQASVLKNQAPVTRTQAPItgtlcqdARSNSHPVKPSRLNVFCCPHCSLTFSKKSYLSRHQKAHLTEPPnYCFHC 417
Cdd:COG5048  380 DLKNDKKSETLSNSCIRNFKRDSN-------LSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAP-LLCSI 451

                        250
                 ....*....|...
gi 219521356 418 SKSFSSFSRLVRH 430
Cdd:COG5048  452 LKSFRRDLDLSNH 464
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
180-296 2.16e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.92  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 180 CDKCFSRRSYLYSHQFVHNPKLTNSC--SQCGKLFRSPK-----SLSYHRRMHLGERPFCCTL--CDKTYCDASGLSRHR 250
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHI 408

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 219521356 251 RVHLGYRPHSC--SVCGKSFRDQSELKRHQKIHQNQEPVDGNQECTLR 296
Cdd:COG5048  409 ITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFR 456
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 259-281 2.80e-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: 38.05  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|...
gi 219521356  259 HSCSVCGKSFRDQSELKRHQKIH 281
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 202-279 3.81e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 202 TNSCSQCGKLFRSPKSLSYHRRMH--LGERPFCCTL--CDKTYCDASGLSRHRR---------------VHLGY----RP 258
Cdd:COG5189  319 TNSSSNGKLAHGGERNIDTPSRMLkvKDGKPYKCPVegCNKKYKNQNGLKYHMLhghqnqklhenpspeKMNIFsakdKP 398

                         90       100
                 ....*....|....*....|.
gi 219521356 259 HSCSVCGKSFRDQSELKRHQK 279
Cdd:COG5189  399 YRCEVCDKRYKNLNGLKYHRK 419
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 102-250 8.55e-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: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 102 EQWREFVHLPNTEGLSEGK-KKELREqhPSLRDEGTSDDKvfLACRGAGQCPLSAPAG--TMDRTRVLQASQAGPPFFCY 178
Cdd:COG5189  278 ELFEESSLGFDYEFIHKSVgNKEIRG--GISTGEMIDVRK--LPCTNSSSNGKLAHGGerNIDTPSRMLKVKDGKPYKCP 353

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521356 179 T--CDKCFSRRSYLYSHqfvhnpKLTNSCSQCGKLFRSPKSlsyHRRMHLGERPFCCTLCDKTYCDASGLSRHR 250
Cdd:COG5189  354 VegCNKKYKNQNGLKYH------MLHGHQNQKLHENPSPEK---MNIFSAKDKPYRCEVCDKRYKNLNGLKYHR 418
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
174-449 2.12e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 174 PFFCYTCDKCFSRRSYLYSHQFVHNPKLTNSCSQ--CGKLFRSPKSLSYHRRMHLGERPFCC------TLCDKTYCDASG 245
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskslplSNSKASSSSLSS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 246 LSRHRRVHLGYRPHSCSVCGK----SFRDQSELKRHQKIHQNQEPVDGNQECTLRIPGTQAEFQTPIARSQGSIQGLLDV 321
Cdd:COG5048  113 SSSNSNDNNLLSSHSLPPSSRdpqlPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLISSNV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 322 NHaPVARSQEPIFRTEGPMAQNQASVLKNQAPVTRTQAPITGTLCQ-----------------------------DARSN 372
Cdd:COG5048  193 ST-SIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPksllsqspsslsssdssssasesprsslpTASSQ 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 373 SHPVKPS-------RLNVFCCPHCSLTFSKKSYLSRHQKAHLTEPPNY----CFH--CSKSFSSFSRLVRHQQTHWKQKS 439
Cdd:COG5048  272 SSSPNESdsssekgFSLPIKSKQCNISFSRSSPLTRHLRSVNHSGESLkpfsCPYslCGKLFSRNDALKRHILLHTSISP 351

                        330
                 ....*....|
gi 219521356 440 YLCPICDLSF 449
Cdd:COG5048  352 AKEKLLNSSS 361
PHA00733 PHA00733
hypothetical protein
 196-277 2.50e-03

hypothetical protein


Pssm-ID: 177301  Cd Length: 128  Bit Score: 38.32  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521356 196 VHNPKLTNSCSQCGKLFRSpKSLSyhrrmhlgerPFCCTLCDKTYCDASGLSRHRRvhlgYRPHS--CSVCGKSFRDQSE 273
Cdd:PHA00733  50 IYNPQLLDESSYLYKLLTS-KAVS----------PYVCPLCLMPFSSSVSLKQHIR----YTEHSkvCPVCGKEFRNTDS 114


                 ....
gi 219521356 274 LKRH 277
Cdd:PHA00733 115 TLDH 118
 
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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