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Conserved domains on  [gi|153791380|ref|NP_001028597|]
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zinc finger and SCAN domain-containing protein 10 isoform 1 [Mus musculus]

Protein Classification

SCAN and COG5048 domain-containing protein( domain architecture ID 11578208)

SCAN and COG5048 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 39-123 5.07e-35

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


:

Pssm-ID: 153421  Cd Length: 85  Bit Score: 127.76  E-value: 5.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380  39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 153791380 119 EGVPR 123
Cdd:cd07936   81 EDLLA 85
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
366-767 3.78e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.58  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 366 HPNLQPHPssRSFRCLWCGKTFGRSSILKLHMRTHTDERPHACHLCNRRFRQS--SHLTKHLLTHSSEPAFRCA------ 437
Cdd:COG5048   24 LKSLSNAP--RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSkslpls 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 438 ----------ECNQGFQRRSSLMQHLLAHAQGKNLTPNPEGKTKVPEmaaVLCSHC-GQTFKRRSSLKRHLRNHAKDKDH 506
Cdd:COG5048  102 nskasssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRN---NPLPGNnSSSVNTPQSNSLHPPLPANSLSK 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 507 LSSEDPGSLSSSQESNPYVCSDCgKAFRQSEQLMIHTRRVHTRERPFSCQVCGRCFT---------QNSQLISHQQIHTG 577
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSE-NSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQlspksllsqSPSSLSSSDSSSSA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 578 EKPHACPQCSKRFVRRAGLARHLLTH-GSLRPYHCAQCGKSFRQMRDLTRHVRC--HTGE--KPCRCNE--CGEGFTQNA 650
Cdd:COG5048  258 SESPRSSLPTASSQSSSPNESDSSSEkGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRND 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 651 HLARHQRIHTGEKPHACDICGHRFRNSSNL-------ARHRRSHTGERPYSC--PTCGRSFRRNAHLQRHLITHTGSKqe 721
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFR-- 415

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 153791380 722 kEVPQECPECGKSFNRSCNLLRHLLVHTGARPYSCALCGRSFSRNS 767
Cdd:COG5048  416 -PYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 39-123 5.07e-35

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 127.76  E-value: 5.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380  39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 153791380 119 EGVPR 123
Cdd:cd07936   81 EDLLA 85
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 39-120 1.56e-31

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 117.97  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380   39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ..
gi 153791380  119 EG 120
Cdd:pfam02023  81 ED 82
SCAN smart00431
leucine rich region;
39-125 9.16e-31

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 116.64  E-value: 9.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380    39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80


                   ....*..
gi 153791380   119 EGVPRDI 125
Cdd:smart00431  81 EDLEREL 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
366-767 3.78e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.58  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 366 HPNLQPHPssRSFRCLWCGKTFGRSSILKLHMRTHTDERPHACHLCNRRFRQS--SHLTKHLLTHSSEPAFRCA------ 437
Cdd:COG5048   24 LKSLSNAP--RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSkslpls 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 438 ----------ECNQGFQRRSSLMQHLLAHAQGKNLTPNPEGKTKVPEmaaVLCSHC-GQTFKRRSSLKRHLRNHAKDKDH 506
Cdd:COG5048  102 nskasssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRN---NPLPGNnSSSVNTPQSNSLHPPLPANSLSK 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 507 LSSEDPGSLSSSQESNPYVCSDCgKAFRQSEQLMIHTRRVHTRERPFSCQVCGRCFT---------QNSQLISHQQIHTG 577
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSE-NSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQlspksllsqSPSSLSSSDSSSSA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 578 EKPHACPQCSKRFVRRAGLARHLLTH-GSLRPYHCAQCGKSFRQMRDLTRHVRC--HTGE--KPCRCNE--CGEGFTQNA 650
Cdd:COG5048  258 SESPRSSLPTASSQSSSPNESDSSSEkGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRND 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 651 HLARHQRIHTGEKPHACDICGHRFRNSSNL-------ARHRRSHTGERPYSC--PTCGRSFRRNAHLQRHLITHTGSKqe 721
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFR-- 415

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 153791380 722 kEVPQECPECGKSFNRSCNLLRHLLVHTGARPYSCALCGRSFSRNS 767
Cdd:COG5048  416 -PYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
568-592 2.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.67e-04
                          10        20
                  ....*....|....*....|....*
gi 153791380  568 LISHQQIHTGEKPHACPQCSKRFVR 592
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
PRK00481 PRK00481
NAD-dependent deacetylase; Provisional
 592-643 7.47e-03

NAD-dependent deacetylase; Provisional


Pssm-ID: 234777  Cd Length: 242  Bit Score: 39.01  E-value: 7.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153791380 592 RRAGlARHLL-THGSLRPYHCAQCGKSFRQMRDLtrhvrchtGEKPCRCNECG 643
Cdd:PRK00481 106 ERAG-SKNVIeLHGSLLRARCTKCGQTYDLDEYL--------KPEPPRCPKCG 149
 
Name Accession Description Interval E-value
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 39-123 5.07e-35

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 127.76  E-value: 5.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380  39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:cd07936    1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                 ....*
gi 153791380 119 EGVPR 123
Cdd:cd07936   81 EDLLA 85
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 39-120 1.56e-31

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 117.97  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380   39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALA 80


                  ..
gi 153791380  119 EG 120
Cdd:pfam02023  81 ED 82
SCAN smart00431
leucine rich region;
39-125 9.16e-31

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 116.64  E-value: 9.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380    39 PEVAHQLFRCFQYQEDMGPRASLGRLRELCNHWLRPALHTKKQILELLVLEQFLSVLPPHVLSRLHGQPLRDGEEVVQLL 118
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80


                   ....*..
gi 153791380   119 EGVPRDI 125
Cdd:smart00431  81 EDLEREL 87
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
366-767 3.78e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 78.58  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 366 HPNLQPHPssRSFRCLWCGKTFGRSSILKLHMRTHTDERPHACHLCNRRFRQS--SHLTKHLLTHSSEPAFRCA------ 437
Cdd:COG5048   24 LKSLSNAP--RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrpLELSRHLRTHHNNPSDLNSkslpls 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 438 ----------ECNQGFQRRSSLMQHLLAHAQGKNLTPNPEGKTKVPEmaaVLCSHC-GQTFKRRSSLKRHLRNHAKDKDH 506
Cdd:COG5048  102 nskasssslsSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRN---NPLPGNnSSSVNTPQSNSLHPPLPANSLSK 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 507 LSSEDPGSLSSSQESNPYVCSDCgKAFRQSEQLMIHTRRVHTRERPFSCQVCGRCFT---------QNSQLISHQQIHTG 577
Cdd:COG5048  179 DPSSNLSLLISSNVSTSIPSSSE-NSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQlspksllsqSPSSLSSSDSSSSA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 578 EKPHACPQCSKRFVRRAGLARHLLTH-GSLRPYHCAQCGKSFRQMRDLTRHVRC--HTGE--KPCRCNE--CGEGFTQNA 650
Cdd:COG5048  258 SESPRSSLPTASSQSSSPNESDSSSEkGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRND 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 651 HLARHQRIHTGEKPHACDICGHRFRNSSNL-------ARHRRSHTGERPYSC--PTCGRSFRRNAHLQRHLITHTGSKqe 721
Cdd:COG5048  338 ALKRHILLHTSISPAKEKLLNSSSKFSPLLnneppqsLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFR-- 415

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 153791380 722 kEVPQECPECGKSFNRSCNLLRHLLVHTGARPYSCALCGRSFSRNS 767
Cdd:COG5048  416 -PYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
551-775 3.54e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.46  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 551 RPFSCQVCGRCFTQNSQLISHQQIHTGEKPHAC--PQCSKRFVRRAGLARHLLTHG------------------------ 604
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHnnpsdlnskslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 605 -----SLRPYHCAQCGKSFRQMRDLTRHVRCHTGEKPCRCNECGEGFTQ----------------------NAHLARHQR 657
Cdd:COG5048  112 ssssnSNDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNtpqsnslhpplpanslskdpssNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 658 IHTGEKPHACDICGHRFRNSSNLARHRRSHTGERPYSCPTCgrSFRRNAHLQRHLITHTGSKQEKEVPQECPECGKSFNR 737
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTN--SQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTAS 269

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 153791380 738 SCNL---LRHLLVHTGAR-PYSCALCGRSFSRNSHLLRHLRT 775
Cdd:COG5048  270 SQSSspnESDSSSEKGFSlPIKSKQCNISFSRSSPLTRHLRS 311
zf-H2C2_2 pfam13465
Zinc-finger double domain;
568-592 2.67e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.67e-04
                          10        20
                  ....*....|....*....|....*
gi 153791380  568 LISHQQIHTGEKPHACPQCSKRFVR 592
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 754-776 3.71e-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: 3.71e-04
                          10        20
                  ....*....|....*....|...
gi 153791380  754 YSCALCGRSFSRNSHLLRHLRTH 776
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 507-599 3.78e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791380 507 LSSEDPGSLSSSQESNPYVCS--DCGKAFRQSEQLMIHTRRVHtrerpfscqvCGRCFTQNSQLISHQQIHTGEKPHACP 584
Cdd:COG5189  333 RNIDTPSRMLKVKDGKPYKCPveGCNKKYKNQNGLKYHMLHGH----------QNQKLHENPSPEKMNIFSAKDKPYRCE 402

                         90
                 ....*....|....*
gi 153791380 585 QCSKRFVRRAGLARH 599
Cdd:COG5189  403 VCDKRYKNLNGLKYH 417
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 693-715 4.65e-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: 4.65e-04
                          10        20
                  ....*....|....*....|...
gi 153791380  693 YSCPTCGRSFRRNAHLQRHLITH 715
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 480-500 2.23e-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: 36.12  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|.
gi 153791380  480 CSHCGQTFKRRSSLKRHLRNH 500
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
393-417 2.79e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*
gi 153791380  393 LKLHMRTHTDERPHACHLCNRRFRQ 417
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 665-687 3.47e-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: 35.35  E-value: 3.47e-03
                          10        20
                  ....*....|....*....|...
gi 153791380  665 HACDICGHRFRNSSNLARHRRSH 687
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 553-575 4.62e-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: 34.97  E-value: 4.62e-03
                          10        20
                  ....*....|....*....|...
gi 153791380  553 FSCQVCGRCFTQNSQLISHQQIH 575
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
707-737 6.81e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.81e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 153791380  707 HLQRHLITHTGSKqekevPQECPECGKSFNR 737
Cdd:pfam13465   1 NLKRHMRTHTGEK-----PYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
623-648 6.95e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.95e-03
                          10        20
                  ....*....|....*....|....*.
gi 153791380  623 DLTRHVRCHTGEKPCRCNECGEGFTQ 648
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK00481 PRK00481
NAD-dependent deacetylase; Provisional
 592-643 7.47e-03

NAD-dependent deacetylase; Provisional


Pssm-ID: 234777  Cd Length: 242  Bit Score: 39.01  E-value: 7.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 153791380 592 RRAGlARHLL-THGSLRPYHCAQCGKSFRQMRDLtrhvrchtGEKPCRCNECG 643
Cdd:PRK00481 106 ERAG-SKNVIeLHGSLLRARCTKCGQTYDLDEYL--------KPEPPRCPKCG 149
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 727-748 7.93e-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: 7.93e-03
                          10        20
                  ....*....|....*....|..
gi 153791380  727 ECPECGKSFNRSCNLLRHLLVH 748
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
 
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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