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Conserved domains on  [gi|1958746637|ref|XP_038953666|]
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centromere protein T isoform X1 [Rattus norvegicus]

Protein Classification

CENP-T family protein; histone H3 family protein( domain architecture ID 11241258)

CENP-T family protein similar to C-terminal region of centromere protein T, a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation| histone H3 family protein similar to histone H3-like centromeric protein that is specifically found in centromeric nucleosomes

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 ...
 1-375 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: 584.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   1 MADLSSPDGDPTIRTLLRHVLDTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTSTRKHSHGTGSVGRLARVQGHG 80
Cdd:pfam16171   1 MADSSSPDSEPTTRTLLRRVLDTADSRTPRRPRSARAGAQRRLLETPSSRRLSSQTKTSARRRSHGARSIGRLAHVQASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  81 HLEEQTPRTLLQNILLTAPESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLELQLPELDPPSTLAPGLKAPGKRKQKLRL 160
Cdd:pfam16171  81 HLEEQTPRTLLKNILLTAPESSIVMPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 161 SVFQQEVNQQLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNIGAFLQNLENKSLTSALPGDS 240
Cdd:pfam16171 161 SVFQQGVDQGLPLSQEPRGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLALAPPGDS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 241 HRTPVAALPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSR--AGFGASPLPFS 318
Cdd:pfam16171 241 HRTPVATLPTDTVLEDTQPFSQPLVGCSPSVHHSLPCPSHTGAEDAERAVGRRTQSSGPGLQNNSPGkpAEVDALALPFP 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746637 319 EPQPQS-PELREAVGSKEAEEPKDLEGSSGDEETSGMPASRELSSSAQDLLLAEEPHQ 375
Cdd:pfam16171 321 NTQPEGhTEVTEAEGSQEAVEAKEPEGSSGDEDTSGRPASPELASSTPEFLQARRPHQ 378
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 483-586 4.46e-43

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: 149.89  E-value: 4.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 483 RHHQDPY--KAGLSHYVKLFSFH--TKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLV 558
Cdd:pfam15511   1 RGHEVPSlpTAVVKRLAQRFARTsgSKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQI 80

                          90       100
                  ....*....|....*....|....*...
gi 1958746637 559 TDQVSLHVLVERYLPLEYRQQLIPCAFR 586
Cdd:pfam15511  81 TSQTTLFSLAQRYLPRELLQELRMPPPA 108
 
Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-375 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: 584.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   1 MADLSSPDGDPTIRTLLRHVLDTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTSTRKHSHGTGSVGRLARVQGHG 80
Cdd:pfam16171   1 MADSSSPDSEPTTRTLLRRVLDTADSRTPRRPRSARAGAQRRLLETPSSRRLSSQTKTSARRRSHGARSIGRLAHVQASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  81 HLEEQTPRTLLQNILLTAPESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLELQLPELDPPSTLAPGLKAPGKRKQKLRL 160
Cdd:pfam16171  81 HLEEQTPRTLLKNILLTAPESSIVMPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 161 SVFQQEVNQQLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNIGAFLQNLENKSLTSALPGDS 240
Cdd:pfam16171 161 SVFQQGVDQGLPLSQEPRGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLALAPPGDS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 241 HRTPVAALPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSR--AGFGASPLPFS 318
Cdd:pfam16171 241 HRTPVATLPTDTVLEDTQPFSQPLVGCSPSVHHSLPCPSHTGAEDAERAVGRRTQSSGPGLQNNSPGkpAEVDALALPFP 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746637 319 EPQPQS-PELREAVGSKEAEEPKDLEGSSGDEETSGMPASRELSSSAQDLLLAEEPHQ 375
Cdd:pfam16171 321 NTQPEGhTEVTEAEGSQEAVEAKEPEGSSGDEDTSGRPASPELASSTPEFLQARRPHQ 378
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 483-586 4.46e-43

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: 149.89  E-value: 4.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 483 RHHQDPY--KAGLSHYVKLFSFH--TKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLV 558
Cdd:pfam15511   1 RGHEVPSlpTAVVKRLAQRFARTsgSKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQI 80

                          90       100
                  ....*....|....*....|....*...
gi 1958746637 559 TDQVSLHVLVERYLPLEYRQQLIPCAFR 586
Cdd:pfam15511  81 TSQTTLFSLAQRYLPRELLQELRMPPPA 108
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 493-582 1.57e-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: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 493 LSHYVKLFSFHTKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLVTDQVSLHVLVERYL 572
Cdd:cd22920     5 KSLVKKLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYL 84

                          90
                  ....*....|
gi 1958746637 573 PLEYRQQLIP 582
Cdd:cd22920    85 PLELLDELIP 94
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
509-550 6.61e-04

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


Pssm-ID: 441639  Cd Length: 67  Bit Score: 38.27  E-value: 6.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958746637 509 EKAALEMVEKcLDEYFQRLCNDLEVFAAHAGRKTVKPKDLEL 550
Cdd:COG2036    21 EDAVEALAEI-LEEYAEEIAKEAVELAKHAGRKTVKAEDIEL 61
PHA03247 PHA03247
large tegument protein UL36; Provisional
 22-381 7.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   22 DTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTstrkhshgTGSVGRLARVQGHGHLEEQTPRTLLQNILLT---- 97
Cdd:PHA03247  2655 DPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPT--------VGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpa 2726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   98 -------APESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLElQLPELDPPSTLAPGLKAP-GKRKQKLRLSVFQQEVNQ 169
Cdd:PHA03247  2727 aarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA-PAPPAAPAAGPPRRLTRPaVASLSESRESLPSPWDPA 2805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  170 QLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNI--GAFLQNLENKSLTSALPGDSHRTPVAA 247
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapGGDVRRRPPSRSPAAKPAAPARPPVRR 2885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  248 LPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSRAgfgASPLPFSEPQPQSPEL 327
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT---TDPAGAGEPSGAVPQP 2962

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746637  328 RE-AVGSKEAEEPKDLEGSSGDEETS---------GMPASReLSSSAQDLLLAEEPhqlfEPPP 381
Cdd:PHA03247  2963 WLgALVPGRVAVPRFRVPQPAPSREApasstppltGHSLSR-VSSWASSLALHEET----DPPP 3021
 
Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-375 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: 584.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   1 MADLSSPDGDPTIRTLLRHVLDTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTSTRKHSHGTGSVGRLARVQGHG 80
Cdd:pfam16171   1 MADSSSPDSEPTTRTLLRRVLDTADSRTPRRPRSARAGAQRRLLETPSSRRLSSQTKTSARRRSHGARSIGRLAHVQASG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  81 HLEEQTPRTLLQNILLTAPESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLELQLPELDPPSTLAPGLKAPGKRKQKLRL 160
Cdd:pfam16171  81 HLEEQTPRTLLKNILLTAPESSIVMPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 161 SVFQQEVNQQLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNIGAFLQNLENKSLTSALPGDS 240
Cdd:pfam16171 161 SVFQQGVDQGLPLSQEPRGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLALAPPGDS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 241 HRTPVAALPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSR--AGFGASPLPFS 318
Cdd:pfam16171 241 HRTPVATLPTDTVLEDTQPFSQPLVGCSPSVHHSLPCPSHTGAEDAERAVGRRTQSSGPGLQNNSPGkpAEVDALALPFP 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746637 319 EPQPQS-PELREAVGSKEAEEPKDLEGSSGDEETSGMPASRELSSSAQDLLLAEEPHQ 375
Cdd:pfam16171 321 NTQPEGhTEVTEAEGSQEAVEAKEPEGSSGDEDTSGRPASPELASSTPEFLQARRPHQ 378
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 483-586 4.46e-43

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: 149.89  E-value: 4.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 483 RHHQDPY--KAGLSHYVKLFSFH--TKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLV 558
Cdd:pfam15511   1 RGHEVPSlpTAVVKRLAQRFARTsgSKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQI 80

                          90       100
                  ....*....|....*....|....*...
gi 1958746637 559 TDQVSLHVLVERYLPLEYRQQLIPCAFR 586
Cdd:pfam15511  81 TSQTTLFSLAQRYLPRELLQELRMPPPA 108
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 493-582 1.57e-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: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637 493 LSHYVKLFSFHTKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLVTDQVSLHVLVERYL 572
Cdd:cd22920     5 KSLVKKLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYL 84

                          90
                  ....*....|
gi 1958746637 573 PLEYRQQLIP 582
Cdd:cd22920    85 PLELLDELIP 94
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 503-554 5.36e-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: 56.03  E-value: 5.36e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958746637 503 HTKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRR 554
Cdd:cd22919    19 EKGVTVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKLLARR 70
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 511-554 6.46e-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: 47.19  E-value: 6.46e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958746637 511 AAL-EMVEKCLDEYFQrlcnDLEVFAAHAGRKTVKPKDLELLMRR 554
Cdd:pfam15630  32 AALtELVYKQLENLAK----DLEAFAKHAGRSTITTDDVKLLARR 72
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 508-553 4.56e-06

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: 44.13  E-value: 4.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958746637 508 VEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMR 553
Cdd:cd00076    18 VSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 503-550 3.13e-04

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: 39.06  E-value: 3.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958746637 503 HTKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLEL 550
Cdd:cd22909    14 AGAERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIEL 61
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
509-550 6.61e-04

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


Pssm-ID: 441639  Cd Length: 67  Bit Score: 38.27  E-value: 6.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958746637 509 EKAALEMVEKcLDEYFQRLCNDLEVFAAHAGRKTVKPKDLEL 550
Cdd:COG2036    21 EDAVEALAEI-LEEYAEEIAKEAVELAKHAGRKTVKAEDIEL 61
HFD_H4 cd22912
histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component ...
 520-556 9.91e-04

histone-fold domain found in histone H4 and similar proteins; Histone H4 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467037 [Multi-domain]  Cd Length: 79  Bit Score: 38.35  E-value: 9.91e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958746637 520 LDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQG 556
Cdd:cd22912    38 LKDFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQG 74
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 508-552 1.50e-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: 37.20  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958746637 508 VEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLM 552
Cdd:pfam00808  21 ISQDAKELIAECVEEFIEFVASEAAEICNKAGRKTINPEHIKQAV 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 22-381 7.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   22 DTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTstrkhshgTGSVGRLARVQGHGHLEEQTPRTLLQNILLT---- 97
Cdd:PHA03247  2655 DPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPT--------VGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpa 2726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   98 -------APESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLElQLPELDPPSTLAPGLKAP-GKRKQKLRLSVFQQEVNQ 169
Cdd:PHA03247  2727 aarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA-PAPPAAPAAGPPRRLTRPaVASLSESRESLPSPWDPA 2805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  170 QLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNI--GAFLQNLENKSLTSALPGDSHRTPVAA 247
Cdd:PHA03247  2806 DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapGGDVRRRPPSRSPAAKPAAPARPPVRR 2885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  248 LPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSRAgfgASPLPFSEPQPQSPEL 327
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT---TDPAGAGEPSGAVPQP 2962

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746637  328 RE-AVGSKEAEEPKDLEGSSGDEETS---------GMPASReLSSSAQDLLLAEEPhqlfEPPP 381
Cdd:PHA03247  2963 WLgALVPGRVAVPRFRVPQPAPSREApasstppltGHSLSR-VSSWASSLALHEET----DPPP 3021
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 98-389 8.05e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637   98 APESSTVMPNPVVKPAQVPEVARPSRRGSSRGSlelqlPELDPPSTLAPGLKAPGKRKQKLRLSVFQQEVNQQLPLPQEQ 177
Cdd:PHA03307    83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-----PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGA 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  178 RGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNIGAFLQNLENKSLTSALPGDSHRTPVAALPTDVVFEDT 257
Cdd:PHA03307   158 SPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746637  258 QPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTP-STGTRPQSQMSRAGFGAsplPFSEPQPQSPelreAVGSKEA 336
Cdd:PHA03307   238 DSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWnGPSSRPGPASSSSSPRE---RSPSPSPSSP----GSGPAPS 310

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958746637  337 EEPKDLEGSSGDEETSGMPASRELSSSAQDLLLAEEPHQLFEPPPSPGVAAVS 389
Cdd:PHA03307   311 SPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPS 363
 
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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