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Conserved domains on  [gi|693582852|ref|NP_001289058|]
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histone H3-like centromeric protein A isoform 2 [Mus musculus]

Protein Classification

histone H3 family protein( domain architecture ID 11269512)

histone H3 family protein similar to histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes

PubMed:  8121801
SCOP:  4000793

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
H3 smart00428
Histone H3;
3-105 2.14e-58

Histone H3;


:

Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 174.94  E-value: 2.14e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852     3 GSQTLRR-RQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLS 81
Cdd:smart00428   2 GKTKHRRyRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGVDLRFQSSAIMALQEAAEAYLVGLFEDTNLLA 81
                           90       100
                   ....*....|....*....|....
gi 693582852    82 LHAGRVTLFPKDIQLTRRIRGFEG 105
Cdd:smart00428  82 IHAKRVTIMPKDIQLARRIRGERL 105
 
Name Accession Description Interval E-value
H3 smart00428
Histone H3;
3-105 2.14e-58

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 174.94  E-value: 2.14e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852     3 GSQTLRR-RQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLS 81
Cdd:smart00428   2 GKTKHRRyRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGVDLRFQSSAIMALQEAAEAYLVGLFEDTNLLA 81
                           90       100
                   ....*....|....*....|....
gi 693582852    82 LHAGRVTLFPKDIQLTRRIRGFEG 105
Cdd:smart00428  82 IHAKRVTIMPKDIQLARRIRGERL 105
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
8-102 2.36e-48

histone-fold domain found in histone H3 and similar proteins; Histone H3 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: 467036  Cd Length: 95  Bit Score: 149.23  E-value: 2.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852   8 RRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRV 87
Cdd:cd22911    2 RYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKTK-DLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80
                         90
                 ....*....|....*
gi 693582852  88 TLFPKDIQLTRRIRG 102
Cdd:cd22911   81 TLMPKDMQLARRIRG 95
Histone pfam00125
Core histone H2A/H2B/H3/H4;
3-101 1.56e-41

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 132.94  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852    3 GSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSrgVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSL 82
Cdd:pfam00125  30 KKKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTK--TDLRISADAVVALQEAVEDFLVELFEEANLLAI 107
                          90
                  ....*....|....*....
gi 693582852   83 HAGRVTLFPKDIQLTRRIR 101
Cdd:pfam00125 108 HAKRVTLTPKDIQLARRLR 126
PLN00161 PLN00161
histone H3; Provisional
3-102 3.70e-35

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 117.02  E-value: 3.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852   3 GSQTLRRRQKF----MWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLALQEAAEAFLIHLFEDAY 78
Cdd:PLN00161  25 RQELDKKPHRYrpgtVALREIRKYQKSTELLIRKLPFARLVREISNEMLRE-PFRWTAEALLALQEATEDFLVHLFEDCN 103
                         90       100
                 ....*....|....*....|....
gi 693582852  79 LLSLHAGRVTLFPKDIQLTRRIRG 102
Cdd:PLN00161 104 LCAIHAKRVTIMPKDMQLARRIRG 127
 
Name Accession Description Interval E-value
H3 smart00428
Histone H3;
3-105 2.14e-58

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 174.94  E-value: 2.14e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852     3 GSQTLRR-RQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLS 81
Cdd:smart00428   2 GKTKHRRyRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGVDLRFQSSAIMALQEAAEAYLVGLFEDTNLLA 81
                           90       100
                   ....*....|....*....|....
gi 693582852    82 LHAGRVTLFPKDIQLTRRIRGFEG 105
Cdd:smart00428  82 IHAKRVTIMPKDIQLARRIRGERL 105
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
8-102 2.36e-48

histone-fold domain found in histone H3 and similar proteins; Histone H3 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: 467036  Cd Length: 95  Bit Score: 149.23  E-value: 2.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852   8 RRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRV 87
Cdd:cd22911    2 RYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKTK-DLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80
                         90
                 ....*....|....*
gi 693582852  88 TLFPKDIQLTRRIRG 102
Cdd:cd22911   81 TLMPKDMQLARRIRG 95
Histone pfam00125
Core histone H2A/H2B/H3/H4;
3-101 1.56e-41

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 132.94  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852    3 GSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSrgVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSL 82
Cdd:pfam00125  30 KKKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTK--TDLRISADAVVALQEAVEDFLVELFEEANLLAI 107
                          90
                  ....*....|....*....
gi 693582852   83 HAGRVTLFPKDIQLTRRIR 101
Cdd:pfam00125 108 HAKRVTLTPKDIQLARRLR 126
PLN00161 PLN00161
histone H3; Provisional
3-102 3.70e-35

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 117.02  E-value: 3.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852   3 GSQTLRRRQKF----MWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLALQEAAEAFLIHLFEDAY 78
Cdd:PLN00161  25 RQELDKKPHRYrpgtVALREIRKYQKSTELLIRKLPFARLVREISNEMLRE-PFRWTAEALLALQEATEDFLVHLFEDCN 103
                         90       100
                 ....*....|....*....|....
gi 693582852  79 LLSLHAGRVTLFPKDIQLTRRIRG 102
Cdd:PLN00161 104 LCAIHAKRVTIMPKDMQLARRIRG 127
PTZ00018 PTZ00018
histone H3; Provisional
16-102 1.72e-33

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 113.08  E-value: 1.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852  16 LKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFwwQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQ 95
Cdd:PTZ00018  49 LREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRF--QSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQ 126

                 ....*..
gi 693582852  96 LTRRIRG 102
Cdd:PTZ00018 127 LARRIRG 133
PLN00121 PLN00121
histone H3; Provisional
8-102 1.01e-32

histone H3; Provisional


Pssm-ID: 177733 [Multi-domain]  Cd Length: 136  Bit Score: 110.91  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852   8 RRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSrgVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRV 87
Cdd:PLN00121  41 RYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK--TDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRV 118
                         90
                 ....*....|....*
gi 693582852  88 TLFPKDIQLTRRIRG 102
Cdd:PLN00121 119 TIMPKDIQLARRIRG 133
PLN00160 PLN00160
histone H3; Provisional
16-102 1.61e-28

histone H3; Provisional


Pssm-ID: 165727  Cd Length: 97  Bit Score: 98.97  E-value: 1.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582852  16 LKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVdFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQ 95
Cdd:PLN00160   8 LKEIKMYQKSTDLLIRRLPFARLVREIQMEMSREA-YRWQGSAILALQEAAEAHLVGLFEDSNLCAIHGKRVTIMPKDMQ 86

                 ....*..
gi 693582852  96 LTRRIRG 102
Cdd:PLN00160  87 LARRIRG 93
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
55-97 2.58e-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: 38.74  E-value: 2.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 693582852  55 QAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQLT 97
Cdd:cd00076   19 SKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELA 61
 
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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