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Conserved domains on  [gi|285811935|tpg|DAA12480|]
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TPA: Rsc8p [Saccharomyces cerevisiae S288C]

Protein Classification

RSC8 family protein( domain architecture ID 11474203)

RSC8 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 26-557 0e+00

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


:

Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 735.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935  26 STNTPSFPHLAQEQAKEESATLGAevaHKKINYEQEAQKLEEKALRFLAKQTHPVIIPSFASWFDISKIHEIEKRSNPDF 105
Cdd:COG5259    1 KTNSVDKKHDSGEERNEQSAEIMD---HSKSANEKKTTILRVEAETFLMEQTHPIIIPSYAEWFDGSKIHEIEKRSNPEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 106 FNDSSRFKTPKAYKDTRNFIINTYRLSPYEYLTITAVRRNVAMDVASIVKIHAFLEKWGLINYQIDPRTKPSLIGPSFTG 185
Cdd:COG5259   78 FNGRSPSKTPEVYKDYRNFMINSYRLNPNEYLTVTACRRNVAGDVAAIVRVHRFLEKWGLINYQVDPGTRPSTIGPPLTS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 186 HFQVVLDTPQGLKPFLPENVIKQEVEGGDGAEPQVKKEFPVNLTIKKNVYDSAQDFNALQDESRNSrqihkVYICHTCGN 265
Cdd:COG5259  158 HFQDLHDTPRGLSPFLPWGPINQRVLGAKEIEYETHKEENYSPSLKSPKKESQGKVDELKDHSEKH-----PSSCSCCGN 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 266 ESINVRYHNLRARDTNLCSRCFQEGHFGANFQSSDFIRLENNGNSVKKNWSDQEMLLLLEGIEMYEDQWEKIADHVgGHK 345
Cdd:COG5259  233 KSFNTRYHNLRAEKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIRDKNWSRQELLLLLEGIEMYGDDWDKVARHV-GTK 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 346 RVEDCIEKFLSLPIEDNYIREVVGSTLNGKGGDSRDGS-----VSGSKLMECVNDAVQTLLQGD-DKLGKVSDKSREIS- 418
Cdd:COG5259  312 TKEQCILHFLQLPIEDNYLSKGDGKGDNSKGRLPFDGSenpvlSTISFLAGIVNPRVQSEKQRAiIKSGKISHINRESQe 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 419 --EKYIEESQAIIQELVKLTMEKLESKFTKLCDLETQLEMEKLKYVKESEKMLNDRLSLSKQILDLNKSLEELNVSKKLV 496
Cdd:COG5259  392 hiEEVIEYALDSGKEKAKLQATNEERKMERLRNVLIQAQLEKLKMKLGHLKELEKSTSLERQELDANLLLRRLNAEEKLF 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811935 497 LISEQVDSGIQLVEKDQeGDDEDGNTATGHGVKRVGKEGEEVGEGDSIAKLQPQVYKPWSL 557
Cdd:COG5259  472 AIDEVLSKCLNLISDDQ-GKNPDNKPSTETGENHLGQEISNETDVKPISKEAPQFYRYWSL 531
 
Name Accession Description Interval E-value
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 26-557 0e+00

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 735.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935  26 STNTPSFPHLAQEQAKEESATLGAevaHKKINYEQEAQKLEEKALRFLAKQTHPVIIPSFASWFDISKIHEIEKRSNPDF 105
Cdd:COG5259    1 KTNSVDKKHDSGEERNEQSAEIMD---HSKSANEKKTTILRVEAETFLMEQTHPIIIPSYAEWFDGSKIHEIEKRSNPEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 106 FNDSSRFKTPKAYKDTRNFIINTYRLSPYEYLTITAVRRNVAMDVASIVKIHAFLEKWGLINYQIDPRTKPSLIGPSFTG 185
Cdd:COG5259   78 FNGRSPSKTPEVYKDYRNFMINSYRLNPNEYLTVTACRRNVAGDVAAIVRVHRFLEKWGLINYQVDPGTRPSTIGPPLTS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 186 HFQVVLDTPQGLKPFLPENVIKQEVEGGDGAEPQVKKEFPVNLTIKKNVYDSAQDFNALQDESRNSrqihkVYICHTCGN 265
Cdd:COG5259  158 HFQDLHDTPRGLSPFLPWGPINQRVLGAKEIEYETHKEENYSPSLKSPKKESQGKVDELKDHSEKH-----PSSCSCCGN 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 266 ESINVRYHNLRARDTNLCSRCFQEGHFGANFQSSDFIRLENNGNSVKKNWSDQEMLLLLEGIEMYEDQWEKIADHVgGHK 345
Cdd:COG5259  233 KSFNTRYHNLRAEKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIRDKNWSRQELLLLLEGIEMYGDDWDKVARHV-GTK 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 346 RVEDCIEKFLSLPIEDNYIREVVGSTLNGKGGDSRDGS-----VSGSKLMECVNDAVQTLLQGD-DKLGKVSDKSREIS- 418
Cdd:COG5259  312 TKEQCILHFLQLPIEDNYLSKGDGKGDNSKGRLPFDGSenpvlSTISFLAGIVNPRVQSEKQRAiIKSGKISHINRESQe 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 419 --EKYIEESQAIIQELVKLTMEKLESKFTKLCDLETQLEMEKLKYVKESEKMLNDRLSLSKQILDLNKSLEELNVSKKLV 496
Cdd:COG5259  392 hiEEVIEYALDSGKEKAKLQATNEERKMERLRNVLIQAQLEKLKMKLGHLKELEKSTSLERQELDANLLLRRLNAEEKLF 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811935 497 LISEQVDSGIQLVEKDQeGDDEDGNTATGHGVKRVGKEGEEVGEGDSIAKLQPQVYKPWSL 557
Cdd:COG5259  472 AIDEVLSKCLNLISDDQ-GKNPDNKPSTETGENHLGQEISNETDVKPISKEAPQFYRYWSL 531
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 89-168 1.05e-31

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 117.28  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935   89 FDISKIHEIEKRSNPDFFNDSSrfKTPKAYKDTRNFIINTYRLSPYEYLTITAVRRNVAMDVASIVKIHAFLEKWGLINY 168
Cdd:pfam04433   1 SDPDKLHPIEKRLLPEFFNGKS--KTPEVYLEIRNFILNLWRENPKEYLTKTDARRALKGDVNLISRIHEFLERWGLINF 78
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 258-302 1.67e-22

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 90.46  E-value: 1.67e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 285811935 258 YICHTCGNESINVRYHNLRARDTNLCSRCFQEGHFGANFQSSDFI 302
Cdd:cd02336    1 YHCFTCGNDCTRVRYHNLKAKKYDLCPSCYQEGRFPSNFQSSDFI 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 254-297 4.89e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 66.31  E-value: 4.89e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 285811935   254 IHKVYICHTCGNESINVRYHNLRARDTNLCSRCFQEGHFGANFQ 297
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
 
Name Accession Description Interval E-value
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 26-557 0e+00

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 735.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935  26 STNTPSFPHLAQEQAKEESATLGAevaHKKINYEQEAQKLEEKALRFLAKQTHPVIIPSFASWFDISKIHEIEKRSNPDF 105
Cdd:COG5259    1 KTNSVDKKHDSGEERNEQSAEIMD---HSKSANEKKTTILRVEAETFLMEQTHPIIIPSYAEWFDGSKIHEIEKRSNPEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 106 FNDSSRFKTPKAYKDTRNFIINTYRLSPYEYLTITAVRRNVAMDVASIVKIHAFLEKWGLINYQIDPRTKPSLIGPSFTG 185
Cdd:COG5259   78 FNGRSPSKTPEVYKDYRNFMINSYRLNPNEYLTVTACRRNVAGDVAAIVRVHRFLEKWGLINYQVDPGTRPSTIGPPLTS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 186 HFQVVLDTPQGLKPFLPENVIKQEVEGGDGAEPQVKKEFPVNLTIKKNVYDSAQDFNALQDESRNSrqihkVYICHTCGN 265
Cdd:COG5259  158 HFQDLHDTPRGLSPFLPWGPINQRVLGAKEIEYETHKEENYSPSLKSPKKESQGKVDELKDHSEKH-----PSSCSCCGN 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 266 ESINVRYHNLRARDTNLCSRCFQEGHFGANFQSSDFIRLENNGNSVKKNWSDQEMLLLLEGIEMYEDQWEKIADHVgGHK 345
Cdd:COG5259  233 KSFNTRYHNLRAEKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIRDKNWSRQELLLLLEGIEMYGDDWDKVARHV-GTK 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 346 RVEDCIEKFLSLPIEDNYIREVVGSTLNGKGGDSRDGS-----VSGSKLMECVNDAVQTLLQGD-DKLGKVSDKSREIS- 418
Cdd:COG5259  312 TKEQCILHFLQLPIEDNYLSKGDGKGDNSKGRLPFDGSenpvlSTISFLAGIVNPRVQSEKQRAiIKSGKISHINRESQe 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 419 --EKYIEESQAIIQELVKLTMEKLESKFTKLCDLETQLEMEKLKYVKESEKMLNDRLSLSKQILDLNKSLEELNVSKKLV 496
Cdd:COG5259  392 hiEEVIEYALDSGKEKAKLQATNEERKMERLRNVLIQAQLEKLKMKLGHLKELEKSTSLERQELDANLLLRRLNAEEKLF 471

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811935 497 LISEQVDSGIQLVEKDQeGDDEDGNTATGHGVKRVGKEGEEVGEGDSIAKLQPQVYKPWSL 557
Cdd:COG5259  472 AIDEVLSKCLNLISDDQ-GKNPDNKPSTETGENHLGQEISNETDVKPISKEAPQFYRYWSL 531
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 89-168 1.05e-31

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 117.28  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935   89 FDISKIHEIEKRSNPDFFNDSSrfKTPKAYKDTRNFIINTYRLSPYEYLTITAVRRNVAMDVASIVKIHAFLEKWGLINY 168
Cdd:pfam04433   1 SDPDKLHPIEKRLLPEFFNGKS--KTPEVYLEIRNFILNLWRENPKEYLTKTDARRALKGDVNLISRIHEFLERWGLINF 78
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 258-302 1.67e-22

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 90.46  E-value: 1.67e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 285811935 258 YICHTCGNESINVRYHNLRARDTNLCSRCFQEGHFGANFQSSDFI 302
Cdd:cd02336    1 YHCFTCGNDCTRVRYHNLKAKKYDLCPSCYQEGRFPSNFQSSDFI 45
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 254-298 9.87e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 68.28  E-value: 9.87e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 285811935  254 IHKVYICHTCGN-ESINVRYHNLRARDTNLCSRCFQEgHFGANFQS 298
Cdd:pfam00569   1 IHKVYTCNGCSNdPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 254-297 4.89e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 66.31  E-value: 4.89e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 285811935   254 IHKVYICHTCGNESINVRYHNLRARDTNLCSRCFQEGHFGANFQ 297
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 258-302 1.09e-10

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 56.67  E-value: 1.09e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 285811935 258 YICHTCGNESINVRYHNLRARDTNLCSRCFQEGHFG-ANFQSSDFI 302
Cdd:cd02249    1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGKKGhPPDHSFTEI 46
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 312-357 7.46e-08

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 48.65  E-value: 7.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 285811935  312 KKNWSDQEMLLLLEGIEMYEDQWEKIADHVGGhKRVEDCIEKFLSL 357
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLGNRWKKIAKLLPG-RTDNQCKNRWQNY 45
SWIRM-assoc_1 pfam16495
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
 426-486 1.81e-07

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 48.67  E-value: 1.81e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 285811935  426 QAIIQELVKLTMEKLESKFTKLCDLETQLEMEKLKYVKESEKMLNDRLSLSKQILDLNKSL 486
Cdd:pfam16495  23 QRLVALLVETQLKKLELKLKQFEELEKLLERERRQLERQRQQLFLERLAFKKQRLEVAEKL 83
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
312-357 8.55e-07

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 45.68  E-value: 8.55e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 285811935   312 KKNWSDQEMLLLLEGIEMY-EDQWEKIADHVGGhKRVEDCIEKFLSL 357
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYgKNNWEKIAKELPG-RTAEQCRERWRNL 46
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 314-357 1.39e-06

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 45.26  E-value: 1.39e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 285811935 314 NWSDQEMLLLLEGIEMY-EDQWEKIADHVGGhKRVEDCIEKFLSL 357
Cdd:cd00167    1 PWTEEEDELLLEAVKKYgKNNWEKIAKELPG-RTPKQCRERWRNL 44
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
258-363 1.02e-04

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 45.06  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285811935 258 YICHTCGNESIN-VRYHNLRARDTNLCSRCFQEG-HFGANFQSSDFIRLENNGNSV-KKNWSDQEMLLLLEGIEMYE-DQ 333
Cdd:COG5114    6 IHCDVCFLDMTDlTFIKCNECPAVDLCLPCFVNGiETGVHSPYHGYRIIETNSYPIgEEGWGADEELLLIECLDTLGlGN 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 285811935 334 WEKIADHVGGHKRvEDCIEKFLSLPIEDNY 363
Cdd:COG5114   86 WEDIADYIGSRAK-EEIKSHYLKMYDESKY 114
Myb_DNA-bind_6 pfam13921
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 315-356 7.72e-03

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 372817 [Multi-domain]  Cd Length: 60  Bit Score: 34.98  E-value: 7.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 285811935  315 WSDQEMLLLLEGIEMYEDQWEKIADHVgGHKRVEDCIEKFLS 356
Cdd:pfam13921   1 WTEEEDEKLLKLVEKYGNDWKQIAKEL-GRRTPKQCFDRWRR 41
 
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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