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Conserved domains on  [gi|693582859|ref|NP_001289061|]
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histone H3-like centromeric protein A isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HFD_SF super family cl45933
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 28-90 3.22e-30

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.


The actual alignment was detected with superfamily member smart00428:

Pssm-ID: 480273 [Multi-domain]  Cd Length: 105  Bit Score: 103.68  E-value: 3.22e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693582859    28 VGSQTLRR-RQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQE 90
Cdd:smart00428   1 GGKTKHRRyRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGVDLRFQSSAIMALQE 64
 
Name Accession Description Interval E-value
H3 smart00428
Histone H3;
28-90 3.22e-30

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 103.68  E-value: 3.22e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693582859    28 VGSQTLRR-RQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQE 90
Cdd:smart00428   1 GGKTKHRRyRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGVDLRFQSSAIMALQE 64
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-92 3.93e-23

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 86.33  E-value: 3.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582859    1 MGPRRKPQTPRRRPSSPAPGPSRQ-SSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSrgVDFW 79
Cdd:pfam00125   1 MARNKNKANPRRGGTAPEKKISQKsSSSSKKKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTK--TDLR 78

                          90
                  ....*....|...
gi 693582859   80 WQAQALLALQETL 92
Cdd:pfam00125  79 ISADAVVALQEAV 91
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 34-90 2.08e-22

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: 83.74  E-value: 2.08e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 693582859  34 RRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLALQE 90
Cdd:cd22911    2 RYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKTK-DLRFQSSALLALQE 57
PLN00161 PLN00161
histone H3; Provisional
 13-90 3.86e-15

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 66.18  E-value: 3.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582859  13 RPSSPAPGPSRQSSSV-GSQTLRRRQKF----MWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLA 87
Cdd:PLN00161   8 KRFRKGKKPQKEASGVtRQELDKKPHRYrpgtVALREIRKYQKSTELLIRKLPFARLVREISNEMLRE-PFRWTAEALLA 86


                 ...
gi 693582859  88 LQE 90
Cdd:PLN00161  87 LQE 89
 
Name Accession Description Interval E-value
H3 smart00428
Histone H3;
28-90 3.22e-30

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 103.68  E-value: 3.22e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693582859    28 VGSQTLRR-RQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQE 90
Cdd:smart00428   1 GGKTKHRRyRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTGVDLRFQSSAIMALQE 64
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-92 3.93e-23

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 86.33  E-value: 3.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582859    1 MGPRRKPQTPRRRPSSPAPGPSRQ-SSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSrgVDFW 79
Cdd:pfam00125   1 MARNKNKANPRRGGTAPEKKISQKsSSSSKKKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTK--TDLR 78

                          90
                  ....*....|...
gi 693582859   80 WQAQALLALQETL 92
Cdd:pfam00125  79 ISADAVVALQEAV 91
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 34-90 2.08e-22

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: 83.74  E-value: 2.08e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 693582859  34 RRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLALQE 90
Cdd:cd22911    2 RYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKTK-DLRFQSSALLALQE 57
PLN00161 PLN00161
histone H3; Provisional
 13-90 3.86e-15

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 66.18  E-value: 3.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582859  13 RPSSPAPGPSRQSSSV-GSQTLRRRQKF----MWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGvDFWWQAQALLA 87
Cdd:PLN00161   8 KRFRKGKKPQKEASGVtRQELDKKPHRYrpgtVALREIRKYQKSTELLIRKLPFARLVREISNEMLRE-PFRWTAEALLA 86


                 ...
gi 693582859  88 LQE 90
Cdd:PLN00161  87 LQE 89
PTZ00018 PTZ00018
histone H3; Provisional
 8-90 4.72e-14

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 63.39  E-value: 4.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582859   8 QTPRRRPSSPAPGPSRQSSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFwwQAQALLA 87
Cdd:PTZ00018  15 KAPRKQLASKAARKSAPVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRF--QSSAVLA 92


                 ...
gi 693582859  88 LQE 90
Cdd:PTZ00018  93 LQE 95
PLN00121 PLN00121
histone H3; Provisional
 2-90 1.51e-13

histone H3; Provisional


Pssm-ID: 177733 [Multi-domain]  Cd Length: 136  Bit Score: 62.38  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693582859   2 GPRRKPQTPRRRPSSPAPGPSRQSSsvgsqtlRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSrgVDFWWQ 81
Cdd:PLN00121  16 APRKQLATKAARKSAPATGGVKKPH-------RYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK--TDLRFQ 86


                 ....*....
gi 693582859  82 AQALLALQE 90
Cdd:PLN00121  87 SSAVLALQE 95
PLN00160 PLN00160
histone H3; Provisional
 42-90 1.03e-09

histone H3; Provisional


Pssm-ID: 165727  Cd Length: 97  Bit Score: 51.20  E-value: 1.03e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 693582859  42 LKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVdFWWQAQALLALQE 90
Cdd:PLN00160   8 LKEIKMYQKSTDLLIRRLPFARLVREIQMEMSREA-YRWQGSAILALQE 55
 
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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