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Conserved domains on  [gi|1696027606|gb|TPX76857|]
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hypothetical protein CcCBS67573_g01861 [Chytriomyces confervae]

Protein Classification

histone H2A( domain architecture ID 11487859)

histone H2A is a core component of the nucleosome which plays a central role in DNA double strand break (DSB) repair

CATH:  1.10.20.10
Gene Ontology:  GO:0003677|GO:0030527|GO:0000786|GO:0006281
PubMed:  8121801|35331626|31965982|24647359
SCOP:  4000793

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 327-446 1.04e-77

histone H2A; Provisional


:

Pssm-ID: 185399  Cd Length: 134  Bit Score: 238.11  E-value: 1.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 327 GGKGKSsGKAKTGAK---SRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTR 403
Cdd:PTZ00017    2 GGKGKT-GGGKAGKKkpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1696027606 404 IIPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKS 446
Cdd:PTZ00017   81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKS 123
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 327-446 1.04e-77

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 238.11  E-value: 1.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 327 GGKGKSsGKAKTGAK---SRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTR 403
Cdd:PTZ00017    2 GGKGKT-GGGKAGKKkpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1696027606 404 IIPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKS 446
Cdd:PTZ00017   81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKS 123
H2A smart00414
Histone 2A;
342-447 5.74e-74

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 227.60  E-value: 5.74e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606  342 SRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 421
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 1696027606  422 LLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
325-447 9.42e-64

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 202.40  E-value: 9.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 325 MAGGKGKSSGKAKtGAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRI 404
Cdd:COG5262     2 VSGGKGGKAADAR-VSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1696027606 405 IPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:COG5262    81 IPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSK 123
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 341-429 3.23e-58

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the 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 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: 467020  Cd Length: 89  Bit Score: 186.20  E-value: 3.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 341 KSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN 420
Cdd:cd00074     1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                  ....*....
gi 1696027606 421 KLLGSVTIA 429
Cdd:cd00074    81 KLFKGVTIA 89
Histone_H2A_C pfam16211
C-terminus of histone H2A;
417-447 1.02e-16

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 73.34  E-value: 1.02e-16
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1696027606 417 EELNKLLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTK 31
 
Name Accession Description Interval E-value
PTZ00017 PTZ00017
histone H2A; Provisional
 327-446 1.04e-77

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 238.11  E-value: 1.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 327 GGKGKSsGKAKTGAK---SRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTR 403
Cdd:PTZ00017    2 GGKGKT-GGGKAGKKkpvSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1696027606 404 IIPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKS 446
Cdd:PTZ00017   81 ITPRHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKS 123
H2A smart00414
Histone 2A;
342-447 5.74e-74

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 227.60  E-value: 5.74e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606  342 SRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 421
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 1696027606  422 LLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PLN00157 PLN00157
histone H2A; Provisional
 325-447 3.83e-71

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 221.26  E-value: 3.83e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 325 MAGGKGKSSGKAKTGAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRI 404
Cdd:PLN00157    1 MSGRGKRKGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1696027606 405 IPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:PLN00157   81 VPRHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSG 123
PLN00156 PLN00156
histone H2AX; Provisional
 323-446 3.45e-64

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 203.66  E-value: 3.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 323 TSMAGGKGKSSGkakTGAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKT 402
Cdd:PLN00156    5 GTTKGGRGKPKA---TKSVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1696027606 403 RIIPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKS 446
Cdd:PLN00156   82 RIVPRHIQLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKV 125
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
325-447 9.42e-64

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 202.40  E-value: 9.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 325 MAGGKGKSSGKAKtGAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRI 404
Cdd:COG5262     2 VSGGKGGKAADAR-VSQSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1696027606 405 IPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:COG5262    81 IPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSK 123
PLN00153 PLN00153
histone H2A; Provisional
 325-447 2.50e-59

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 190.70  E-value: 2.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 325 MAG-GKGKSSGKAktgAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTR 403
Cdd:PLN00153    1 MAGrGKGKTSGKK---AVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1696027606 404 IIPRHLQLAIRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:PLN00153   78 IVPRHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKTK 121
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 341-429 3.23e-58

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the 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 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: 467020  Cd Length: 89  Bit Score: 186.20  E-value: 3.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 341 KSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN 420
Cdd:cd00074     1 QSRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELN 80


                  ....*....
gi 1696027606 421 KLLGSVTIA 429
Cdd:cd00074    81 KLFKGVTIA 89
PLN00154 PLN00154
histone H2A; Provisional
 321-447 1.59e-45

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 155.10  E-value: 1.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 321 PKTSMAGGKGKSSGKAKTgakSRSSRAGLQFPVGRIHRLLRKGNYA-QRVGAGAPVYLAAVLEYLGAEILELAGNAARDN 399
Cdd:PLN00154   12 AKTTAAAAKKDKDKKKPT---SRSSRAGLQFPVGRIHRQLKQRVSAhGRVGATAAVYTAAILEYLTAEVLELAGNASKDL 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1696027606 400 KKTRIIPRHLQLAIRNDEELNKLLGSvTIAQGGVLPNIQPSLLPKKSE 447
Cdd:PLN00154   89 KVKRITPRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINKSTK 135
PTZ00252 PTZ00252
histone H2A; Provisional
 335-445 3.17e-34

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 125.07  E-value: 3.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 335 KAKTGAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDN--KKTRIIPRHLQLA 412
Cdd:PTZ00252   10 KASKSGSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPRTVTLA 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1696027606 413 IRNDEELNKLLGSVTIAQGGVLPNIQPSLLPKK 445
Cdd:PTZ00252   90 VRHDDDLGSLLKNVTLSRGGVMPSLNKALAKKH 122
PLN00155 PLN00155
histone H2A; Provisional
 325-384 1.17e-22

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 90.92  E-value: 1.17e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1696027606 325 MAG-GKGKSSGKAktgAKSRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYL 384
Cdd:PLN00155    1 MAGrGKGKTSGKK---AVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 351-424 3.83e-18

second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat.


Pssm-ID: 467040  Cd Length: 75  Bit Score: 78.43  E-value: 3.83e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696027606 351 FPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLG 424
Cdd:cd22915     2 FPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLFG 75
Histone_H2A_C pfam16211
C-terminus of histone H2A;
417-447 1.02e-16

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 73.34  E-value: 1.02e-16
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1696027606 417 EELNKLLGSVTIAQGGVLPNIQPSLLPKKSE 447
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTK 31
Histone pfam00125
Core histone H2A/H2B/H3/H4;
310-414 4.72e-15

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 71.70  E-value: 4.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 310 PLRRGHYDNAIPKTSMAGgKGKSSGKAKTGAKSRSSRAGLQFPVGRIHRLLRKGNYA-QRVGAGAPVYLAAVLEYLGAEI 388
Cdd:pfam00125  20 KISQKSSSSSKKKTRRYR-PGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKTdLRISADAVVALQEAVEDFLVEL 98

                          90       100
                  ....*....|....*....|....*.
gi 1696027606 389 LELAGNAARDNKKTRIIPRHLQLAIR 414
Cdd:pfam00125  99 FEEANLLAIHAKRVTLTPKDIQLARR 124
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 342-423 2.34e-12

histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, which has implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). This subfamily also includes BTB/POZ domain-containing protein 11 (BTBD11), also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11. It is a BTB-domain-containing Kelch-like protein with unknown function.


Pssm-ID: 467038  Cd Length: 105  Bit Score: 63.09  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696027606 342 SRSSRAGLQFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK 421
Cdd:cd22913    10 SKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAELWG 89


                  ..
gi 1696027606 422 LL 423
Cdd:cd22913    90 LL 91
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
350-422 2.23e-06

Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];


Pssm-ID: 227572  Cd Length: 113  Bit Score: 46.49  E-value: 2.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1696027606 350 QFPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 422
Cdd:COG5247    23 RFPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFL 95
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
351-402 2.03e-05

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


Pssm-ID: 441639  Cd Length: 67  Bit Score: 42.13  E-value: 2.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1696027606 351 FPVGRIHRLLRKgNYAQRVGAGAPVYLAAVLEYLGAEILELAGNAAR-DNKKT 402
Cdd:COG2036     2 LPVAPVDRIIKK-AGAERVSEDAVEALAEILEEYAEEIAKEAVELAKhAGRKT 53
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 351-414 2.27e-05

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: 42.15  E-value: 2.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1696027606 351 FPVGRIHRLLRKGNyAQRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIR 414
Cdd:cd22909     2 LPKAPVKRIIKKAG-AERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
HFD_DRAP1 cd22906
histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, ...
 351-422 6.43e-05

histone-fold domain found in Dr1-associated protein 1 (DRAP1) and similar proteins; DRAP1, also called Dr1-associated corepressor or negative cofactor 2-alpha (NC2-alpha), acts as a corepressor for Dr1 (down-regulator of transcription 1)-mediated repression of transcription. It forms a heterodimer with Dr1. The association of the Dr1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. DRAP1 can bind to DNA on its own. It also binds TATA-binding protein-associated factor 172 (BTAF1).


Pssm-ID: 467031 [Multi-domain]  Cd Length: 75  Bit Score: 40.97  E-value: 6.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1696027606 351 FPVGRIHRLLRK----GnyaqRVGAGAPVYLAAVLEYLGAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKL 422
Cdd:cd22906     4 FPAARIKKIMQSdeevG----KVAAAVPVLISKALELFLEDLLTKAAEVAKERNAKTITPSHLKQCVESEEKFDFL 75
CBFD_NFYB_HMF pfam00808
Histone-like transcription factor (CBF/NF-Y) and archaeal histone; This family includes ...
 351-413 3.15e-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: 36.05  E-value: 3.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1696027606 351 FPVGRIHRLLRKGNYAQRVGAGAPVYLAAVLEYLgaeILELAGNAAR----DNKKTrIIPRHLQLAI 413
Cdd:pfam00808   3 LPIARVKRIMKSDPDAGRISQDAKELIAECVEEF---IEFVASEAAEicnkAGRKT-INPEHIKQAV 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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