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Conserved domains on  [gi|290999757|ref|XP_002682446|]
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histone H3 [Naegleria gruberi]

Protein Classification

histone H3( domain architecture ID 10794185)

histone H3 is a core component of the nucleosome that wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00018 PTZ00018
histone H3; Provisional
 1-138 1.47e-85

histone H3; Provisional


:

Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 245.97  E-value: 1.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757   1 MARTKQTARKSTGGKAPRKQLASKAARKSAkqPSTGGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:PTZ00018   1 MARTKQTARKSTGGKAPRKQLASKAARKSA--PVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 290999757  81 YKSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIRGERT 138
Cdd:PTZ00018  79 FKTDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS 136
 
Name Accession Description Interval E-value
PTZ00018 PTZ00018
histone H3; Provisional
 1-138 1.47e-85

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 245.97  E-value: 1.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757   1 MARTKQTARKSTGGKAPRKQLASKAARKSAkqPSTGGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:PTZ00018   1 MARTKQTARKSTGGKAPRKQLASKAARKSA--PVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 290999757  81 YKSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIRGERT 138
Cdd:PTZ00018  79 FKTDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS 136
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 42-135 1.95e-62

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: 185.82  E-value: 1.95e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757  42 HRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDYK-SDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRV 120
Cdd:cd22911    1 RRYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKtKDLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80

                         90
                 ....*....|....*
gi 290999757 121 TIMQKDMQLAKRIRG 135
Cdd:cd22911   81 TLMPKDMQLARRIRG 95
H3 smart00428
Histone H3;
36-138 2.22e-56

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 171.09  E-value: 2.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757    36 GGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDYK--SDLRFQSNAVLALQEASEAYLVSLFEDTNLC 113
Cdd:smart00428   1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTtgVDLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                           90       100
                   ....*....|....*....|....*
gi 290999757   114 AIHAKRVTIMQKDMQLAKRIRGERT 138
Cdd:smart00428  81 AIHAKRVTIMPKDIQLARRIRGERL 105
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-134 3.22e-48

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 151.05  E-value: 3.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757    1 MARTKQTARKSTGGKAPRKQLASKAARKSAKqpstgglkKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:pfam00125   1 MARNKNKANPRRGGTAPEKKISQKSSSSSKK--------KTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQS 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 290999757   81 YKSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIR 134
Cdd:pfam00125  73 TKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
 
Name Accession Description Interval E-value
PTZ00018 PTZ00018
histone H3; Provisional
 1-138 1.47e-85

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 245.97  E-value: 1.47e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757   1 MARTKQTARKSTGGKAPRKQLASKAARKSAkqPSTGGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:PTZ00018   1 MARTKQTARKSTGGKAPRKQLASKAARKSA--PVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 290999757  81 YKSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIRGERT 138
Cdd:PTZ00018  79 FKTDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS 136
PLN00121 PLN00121
histone H3; Provisional
 1-138 8.20e-76

histone H3; Provisional


Pssm-ID: 177733 [Multi-domain]  Cd Length: 136  Bit Score: 221.47  E-value: 8.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757   1 MARTKQTARKSTGGKAPRKQLASKAARKSAkqPSTGGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:PLN00121   1 MARTKQTARKSTGGKAPRKQLATKAARKSA--PATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 290999757  81 YKSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIRGERT 138
Cdd:PLN00121  79 FKTDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 136
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 42-135 1.95e-62

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: 185.82  E-value: 1.95e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757  42 HRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDYK-SDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRV 120
Cdd:cd22911    1 RRYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKtKDLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80

                         90
                 ....*....|....*
gi 290999757 121 TIMQKDMQLAKRIRG 135
Cdd:cd22911   81 TLMPKDMQLARRIRG 95
H3 smart00428
Histone H3;
36-138 2.22e-56

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 171.09  E-value: 2.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757    36 GGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDYK--SDLRFQSNAVLALQEASEAYLVSLFEDTNLC 113
Cdd:smart00428   1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTtgVDLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                           90       100
                   ....*....|....*....|....*
gi 290999757   114 AIHAKRVTIMQKDMQLAKRIRGERT 138
Cdd:smart00428  81 AIHAKRVTIMPKDIQLARRIRGERL 105
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-134 3.22e-48

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 151.05  E-value: 3.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757    1 MARTKQTARKSTGGKAPRKQLASKAARKSAKqpstgglkKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:pfam00125   1 MARNKNKANPRRGGTAPEKKISQKSSSSSKK--------KTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQS 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 290999757   81 YKSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIR 134
Cdd:pfam00125  73 TKTDLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
PLN00161 PLN00161
histone H3; Provisional
 1-135 4.01e-46

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 146.30  E-value: 4.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757   1 MARTKQtarkstgGKAPRKqlASKAARKSAKQPSTGGLKKPHRYKPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQD 80
Cdd:PLN00161   1 MARRLQ-------GKRFRK--GKKPQKEASGVTRQELDKKPHRYRPGTVALREIRKYQKSTELLIRKLPFARLVREISNE 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 290999757  81 YKSD-LRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLAKRIRG 135
Cdd:PLN00161  72 MLREpFRWTAEALLALQEATEDFLVHLFEDCNLCAIHAKRVTIMPKDMQLARRIRG 127
PLN00160 PLN00160
histone H3; Provisional
 45-136 5.61e-37

histone H3; Provisional


Pssm-ID: 165727  Cd Length: 97  Bit Score: 121.69  E-value: 5.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290999757  45 KPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDY-KSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIM 123
Cdd:PLN00160   2 RPGEKALKEIKMYQKSTDLLIRRLPFARLVREIQMEMsREAYRWQGSAILALQEAAEAHLVGLFEDSNLCAIHGKRVTIM 81

                         90
                 ....*....|...
gi 290999757 124 QKDMQLAKRIRGE 136
Cdd:PLN00160  82 PKDMQLARRIRGQ 94
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 72-134 5.38e-04

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: 36.76  E-value: 5.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 290999757  72 RLVREIAQDYkSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDM-QLAKRIR 134
Cdd:cd22920    6 SLVKKLFKHF-LKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVeLLMKRQR 68
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 70-130 1.90e-03

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: 34.50  E-value: 1.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 290999757  70 FQRLVREIAQDYkSDLRFQSNAVLALQEASEAYLVSLFEDTNLCAIHAKRVTIMQKDMQLA 130
Cdd:cd00076    2 LRSAVARILKSA-GFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELA 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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