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Conserved domains on  [gi|126722969|ref|NP_079358|]
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centromere protein T [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-415 0e+00

Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This family represents the N-terminus of CENP-T.


:

Pssm-ID: 465039  Cd Length: 378  Bit Score: 557.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969    1 MAD-HNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASG 79
Cdd:pfam16171   1 MADsSSPDSEPTTRTLLRRVLDTADSRTPRRPRSARAGAQRRLLETPSSRRLSSQTKTSARRRSHGARSIGRLAHVQASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969   80 HLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 159
Cdd:pfam16171  81 HLEEQTPRTLLKNILLTAPESSIVMPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  160 SVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLA------- 232
Cdd:pfam16171 161 SVFQQGVDQGLPLSQEPRGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLAlappgds 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  233 --------PPNIVLEDTQPFSQPMVG-SPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAqflageaeEV 303
Cdd:pfam16171 241 hrtpvatlPTDTVLEDTQPFSQPLVGcSPSVHHSLPCPSHTGAEDAERAVGRRTQSSGPGLQNNSPGKPA--------EV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  304 NAFALGFLSTssgvsgedeveplhdgveeaekkmeeegvsvsemeatgaqgpsrveEAEGHTEVTEAEGSQGTAEADGPG 383
Cdd:pfam16171 313 DALALPFPNT----------------------------------------------QPEGHTEVTEAEGSQEAVEAKEPE 346

                         410       420       430
                  ....*....|....*....|....*....|..
gi 126722969  384 ASSGDEDASGRAASPESASSTPESLQARRHHQ 415
Cdd:pfam16171 347 GSSGDEDTSGRPASPELASSTPEFLQARRPHQ 378
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 460-549 1.48e-35

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


:

Pssm-ID: 467045  Cd Length: 94  Bit Score: 128.44  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969 460 LSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHL 539
Cdd:cd22920    5 KSLVKKLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYL 84

                         90
                 ....*....|
gi 126722969 540 PLEYRQLLIP 549
Cdd:cd22920   85 PLELLDELIP 94
 
Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-415 0e+00

Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This family represents the N-terminus of CENP-T.


Pssm-ID: 465039  Cd Length: 378  Bit Score: 557.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969    1 MAD-HNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASG 79
Cdd:pfam16171   1 MADsSSPDSEPTTRTLLRRVLDTADSRTPRRPRSARAGAQRRLLETPSSRRLSSQTKTSARRRSHGARSIGRLAHVQASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969   80 HLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 159
Cdd:pfam16171  81 HLEEQTPRTLLKNILLTAPESSIVMPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  160 SVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLA------- 232
Cdd:pfam16171 161 SVFQQGVDQGLPLSQEPRGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLAlappgds 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  233 --------PPNIVLEDTQPFSQPMVG-SPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAqflageaeEV 303
Cdd:pfam16171 241 hrtpvatlPTDTVLEDTQPFSQPLVGcSPSVHHSLPCPSHTGAEDAERAVGRRTQSSGPGLQNNSPGKPA--------EV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  304 NAFALGFLSTssgvsgedeveplhdgveeaekkmeeegvsvsemeatgaqgpsrveEAEGHTEVTEAEGSQGTAEADGPG 383
Cdd:pfam16171 313 DALALPFPNT----------------------------------------------QPEGHTEVTEAEGSQEAVEAKEPE 346

                         410       420       430
                  ....*....|....*....|....*....|..
gi 126722969  384 ASSGDEDASGRAASPESASSTPESLQARRHHQ 415
Cdd:pfam16171 347 GSSGDEDTSGRPASPELASSTPEFLQARRPHQ 378
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 460-549 1.48e-35

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 128.44  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969 460 LSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHL 539
Cdd:cd22920    5 KSLVKKLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYL 84

                         90
                 ....*....|
gi 126722969 540 PLEYRQLLIP 549
Cdd:cd22920   85 PLELLDELIP 94
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 457-551 2.37e-35

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 434768  Cd Length: 108  Bit Score: 128.32  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  457 KAGLSHYVKLFSFYA--KMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVL 534
Cdd:pfam15511  10 TAVVKRLAQRFARTSgsKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQITSQTTLFSL 89

                          90
                  ....*....|....*..
gi 126722969  535 VERHLPLEYRQLLIPCA 551
Cdd:pfam15511  90 AQRYLPRELLQELRMPP 106
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 354-474 2.50e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  354 GPSRVEEAEGHTEVTEAEGSQGTAEADGPGASSGDEDASGRAASPESASSTPESLQARRHHQFLEPAPAPGAAVLSSEPA 433
Cdd:PHA03307  311 SPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 126722969  434 EPLLVRHPPRPRTTGPRPRQDPHKAGLSHYVKLFSFYAKMP 474
Cdd:PHA03307  391 RAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
502-517 2.86e-03

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 36.35  E-value: 2.86e-03
                         10
                 ....*....|....*.
gi 126722969 502 AAHAGRKTVKPEDLEL 517
Cdd:COG2036   46 AKHAGRKTVKAEDIEL 61
 
Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-415 0e+00

Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This family represents the N-terminus of CENP-T.


Pssm-ID: 465039  Cd Length: 378  Bit Score: 557.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969    1 MAD-HNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASG 79
Cdd:pfam16171   1 MADsSSPDSEPTTRTLLRRVLDTADSRTPRRPRSARAGAQRRLLETPSSRRLSSQTKTSARRRSHGARSIGRLAHVQASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969   80 HLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 159
Cdd:pfam16171  81 HLEEQTPRTLLKNILLTAPESSIVMPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  160 SVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLA------- 232
Cdd:pfam16171 161 SVFQQGVDQGLPLSQEPRGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLAlappgds 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  233 --------PPNIVLEDTQPFSQPMVG-SPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAqflageaeEV 303
Cdd:pfam16171 241 hrtpvatlPTDTVLEDTQPFSQPLVGcSPSVHHSLPCPSHTGAEDAERAVGRRTQSSGPGLQNNSPGKPA--------EV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  304 NAFALGFLSTssgvsgedeveplhdgveeaekkmeeegvsvsemeatgaqgpsrveEAEGHTEVTEAEGSQGTAEADGPG 383
Cdd:pfam16171 313 DALALPFPNT----------------------------------------------QPEGHTEVTEAEGSQEAVEAKEPE 346

                         410       420       430
                  ....*....|....*....|....*....|..
gi 126722969  384 ASSGDEDASGRAASPESASSTPESLQARRHHQ 415
Cdd:pfam16171 347 GSSGDEDTSGRPASPELASSTPEFLQARRPHQ 378
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 460-549 1.48e-35

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 128.44  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969 460 LSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHL 539
Cdd:cd22920    5 KSLVKKLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYL 84

                         90
                 ....*....|
gi 126722969 540 PLEYRQLLIP 549
Cdd:cd22920   85 PLELLDELIP 94
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 457-551 2.37e-35

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 434768  Cd Length: 108  Bit Score: 128.32  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  457 KAGLSHYVKLFSFYA--KMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVL 534
Cdd:pfam15511  10 TAVVKRLAQRFARTSgsKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQITSQTTLFSL 89

                          90
                  ....*....|....*..
gi 126722969  535 VERHLPLEYRQLLIPCA 551
Cdd:pfam15511  90 AQRYLPRELLQELRMPP 106
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 472-521 7.68e-10

histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also called MHF1, apoptosis-inducing TAF9-like domain-containing protein 1 (APITD1), FANCM-associated histone fold protein 1, FANCM-interacting histone fold protein 1, or Fanconi anemia-associated polypeptide of 16 kDa (FAAP16), is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-S, together with CENP-X, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-S acts as a crucial cofactor for FANCM, in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-S also forms a discrete complex with FANCM and CENP-X, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-X (CENP-T-W-S-X heterotetramer), CENP-S is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, CENP-S binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-X. It does not bind DNA on its own.


Pssm-ID: 467044  Cd Length: 77  Bit Score: 55.26  E-value: 7.68e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 126722969 472 KMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRR 521
Cdd:cd22919   21 GVTVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKLLARR 70
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 497-521 2.45e-07

CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


Pssm-ID: 464782  Cd Length: 76  Bit Score: 48.34  E-value: 2.45e-07
                          10        20
                  ....*....|....*....|....*
gi 126722969  497 DLEVFAAHAGRKTVKPEDLELLMRR 521
Cdd:pfam15630  48 DLEAFAKHAGRSTITTDDVKLLARR 72
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 475-520 3.38e-05

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 41.82  E-value: 3.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 126722969 475 MERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMR 520
Cdd:cd00076   18 VSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 354-474 2.50e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126722969  354 GPSRVEEAEGHTEVTEAEGSQGTAEADGPGASSGDEDASGRAASPESASSTPESLQARRHHQFLEPAPAPGAAVLSSEPA 433
Cdd:PHA03307  311 SPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 126722969  434 EPLLVRHPPRPRTTGPRPRQDPHKAGLSHYVKLFSFYAKMP 474
Cdd:PHA03307  391 RAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
502-517 2.86e-03

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 36.35  E-value: 2.86e-03
                         10
                 ....*....|....*.
gi 126722969 502 AAHAGRKTVKPEDLEL 517
Cdd:COG2036   46 AKHAGRKTVKAEDIEL 61
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 501-517 3.42e-03

histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation.


Pssm-ID: 467034  Cd Length: 64  Bit Score: 35.98  E-value: 3.42e-03
                         10
                 ....*....|....*..
gi 126722969 501 FAAHAGRKTVKPEDLEL 517
Cdd:cd22909   45 LAKHAGRKTVKAEDIEL 61
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 479-519 6.36e-03

Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes archaebacterial histones and histone like transcription factors from eukaryotes.


Pssm-ID: 395650  Cd Length: 65  Bit Score: 35.28  E-value: 6.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 126722969  479 ALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLM 519
Cdd:pfam00808  25 AKELIAECVEEFIEFVASEAAEICNKAGRKTINPEHIKQAV 65
 
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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