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Conserved domains on  [gi|688591487|ref|XP_009290705|]
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transcription initiation factor TFIID subunit 12 isoform X1 [Danio rerio]

Protein Classification

transcription initiation factor TFIID subunit 12( domain architecture ID 10168398)

transcription initiation factor TFIID subunit 12 is a component of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC), and may be essential for mediating regulation of RNA polymerase transcription

CATH:  1.10.20.10
Gene Ontology:  GO:0005669|GO:0003677|GO:0042789|GO:0003713|GO:0006352|GO:0017025|GO:0046982|GO:0140297|GO:0006355
PubMed:  31751889|14969724|19308322
SCOP:  4000797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HFD_TAF12 cd07981
histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and ...
 56-129 8.78e-46

histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and similar proteins; TAF12, also called TATA Binding Protein (TBP) associated factor 12, transcription initiation factor TFIID 20/15 kDa subunits, TAFII-20/TAFII-15, or TAFII20/TAFII15, is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAFs are essential for mediating regulation of RNA polymerase transcription. TAF12 interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes. It is important for RAS-induced transformation properties of human colorectal cancer cells; its levels are increased in the cells harboring the RAS mutation. Also, TAF12 interacts with activating transcription factor 7 (ATF7) and contributes to the hypersensitivity of osteoclast (OCL) precursors to 1,25-dihydroxyvitamin D2 (1,25-(OH)2D3; also known as calcitriol) in Paget's disease (PD), a disorder of the bone remodeling process, in which the body absorbs old bone and forms abnormal new bone.


:

Pssm-ID: 467025 [Multi-domain]  Cd Length: 74  Bit Score: 144.21  E-value: 8.78e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688591487  56 PQVLSKKKLQDLVREIDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWI 129
Cdd:cd07981    1 NPLLSKRKLQELVREVDPNERLDPDVEELLLQLADDFVDDVVTFACKLAKHRGSDTLEVKDVQLHLERNWNIRV 74
 
Name Accession Description Interval E-value
HFD_TAF12 cd07981
histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and ...
 56-129 8.78e-46

histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and similar proteins; TAF12, also called TATA Binding Protein (TBP) associated factor 12, transcription initiation factor TFIID 20/15 kDa subunits, TAFII-20/TAFII-15, or TAFII20/TAFII15, is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAFs are essential for mediating regulation of RNA polymerase transcription. TAF12 interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes. It is important for RAS-induced transformation properties of human colorectal cancer cells; its levels are increased in the cells harboring the RAS mutation. Also, TAF12 interacts with activating transcription factor 7 (ATF7) and contributes to the hypersensitivity of osteoclast (OCL) precursors to 1,25-dihydroxyvitamin D2 (1,25-(OH)2D3; also known as calcitriol) in Paget's disease (PD), a disorder of the bone remodeling process, in which the body absorbs old bone and forms abnormal new bone.


Pssm-ID: 467025 [Multi-domain]  Cd Length: 74  Bit Score: 144.21  E-value: 8.78e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688591487  56 PQVLSKKKLQDLVREIDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWI 129
Cdd:cd07981    1 NPLLSKRKLQELVREVDPNERLDPDVEELLLQLADDFVDDVVTFACKLAKHRGSDTLEVKDVQLHLERNWNIRV 74
TFIID_20kDa pfam03847
Transcription initiation factor TFIID subunit A;
60-127 1.53e-36

Transcription initiation factor TFIID subunit A;


Pssm-ID: 367691 [Multi-domain]  Cd Length: 68  Bit Score: 120.55  E-value: 1.53e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688591487   60 SKKKLQDLVREIDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNM 127
Cdd:pfam03847   1 SKRKLQDLVQQIDSTTKLDEDVEDLLLEIADDFVESVTTFACKLAKHRKSDKLEVRDIQLHLERNWNM 68
COG5624 COG5624
Transcription initiation factor TFIID, subunit TAF12 [Transcription];
6-156 2.52e-27

Transcription initiation factor TFIID, subunit TAF12 [Transcription];


Pssm-ID: 227911 [Multi-domain]  Cd Length: 505  Bit Score: 106.31  E-value: 2.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688591487   6 AQTSRSNFYTVVKAEASSTPPLSSSMANSTVAPGKLP----GTPGPAGRLSPEGP------------QVLSKKKLQDLVR 69
Cdd:COG5624  315 AQRSRFPGTCSIYPENPGKRWCSTKYPQPLVHKGDRDtetgGCAAPDGGLATPGRdkgplyerddlwRLDSKRKLEELQH 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688591487  70 E-IDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWIPGFGSDEIRP-YKKACTTE 147
Cdd:COG5624  395 GgVDEEEKIENEVEELLLSRADGFVEPVTEFSCRLAKHRKSDTLEVRDGQLHLERNWNIRCPGFVDDIIHMsYRKQKPTV 474


                 ....*....
gi 688591487 148 AHKQRMALI 156
Cdd:COG5624  475 EYCQKKLAI 483
 
Name Accession Description Interval E-value
HFD_TAF12 cd07981
histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and ...
 56-129 8.78e-46

histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and similar proteins; TAF12, also called TATA Binding Protein (TBP) associated factor 12, transcription initiation factor TFIID 20/15 kDa subunits, TAFII-20/TAFII-15, or TAFII20/TAFII15, is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAFs are essential for mediating regulation of RNA polymerase transcription. TAF12 interacts with TAF4 and makes a novel histone-like heterodimer that binds DNA and has a core promoter function of a subset of genes. It is important for RAS-induced transformation properties of human colorectal cancer cells; its levels are increased in the cells harboring the RAS mutation. Also, TAF12 interacts with activating transcription factor 7 (ATF7) and contributes to the hypersensitivity of osteoclast (OCL) precursors to 1,25-dihydroxyvitamin D2 (1,25-(OH)2D3; also known as calcitriol) in Paget's disease (PD), a disorder of the bone remodeling process, in which the body absorbs old bone and forms abnormal new bone.


Pssm-ID: 467025 [Multi-domain]  Cd Length: 74  Bit Score: 144.21  E-value: 8.78e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688591487  56 PQVLSKKKLQDLVREIDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWI 129
Cdd:cd07981    1 NPLLSKRKLQELVREVDPNERLDPDVEELLLQLADDFVDDVVTFACKLAKHRGSDTLEVKDVQLHLERNWNIRV 74
TFIID_20kDa pfam03847
Transcription initiation factor TFIID subunit A;
60-127 1.53e-36

Transcription initiation factor TFIID subunit A;


Pssm-ID: 367691 [Multi-domain]  Cd Length: 68  Bit Score: 120.55  E-value: 1.53e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688591487   60 SKKKLQDLVREIDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNM 127
Cdd:pfam03847   1 SKRKLQDLVQQIDSTTKLDEDVEDLLLEIADDFVESVTTFACKLAKHRKSDKLEVRDIQLHLERNWNM 68
COG5624 COG5624
Transcription initiation factor TFIID, subunit TAF12 [Transcription];
6-156 2.52e-27

Transcription initiation factor TFIID, subunit TAF12 [Transcription];


Pssm-ID: 227911 [Multi-domain]  Cd Length: 505  Bit Score: 106.31  E-value: 2.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688591487   6 AQTSRSNFYTVVKAEASSTPPLSSSMANSTVAPGKLP----GTPGPAGRLSPEGP------------QVLSKKKLQDLVR 69
Cdd:COG5624  315 AQRSRFPGTCSIYPENPGKRWCSTKYPQPLVHKGDRDtetgGCAAPDGGLATPGRdkgplyerddlwRLDSKRKLEELQH 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688591487  70 E-IDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWIPGFGSDEIRP-YKKACTTE 147
Cdd:COG5624  395 GgVDEEEKIENEVEELLLSRADGFVEPVTEFSCRLAKHRKSDTLEVRDGQLHLERNWNIRCPGFVDDIIHMsYRKQKPTV 474


                 ....*....
gi 688591487 148 AHKQRMALI 156
Cdd:COG5624  475 EYCQKKLAI 483
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 58-124 1.62e-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: 38.69  E-value: 1.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688591487  58 VLSKKKLQDLVREIDpNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQ 124
Cdd:cd22920    2 SLPKSLVKKLFKHFL-KRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQ 67
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 59-122 2.13e-04

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: 37.58  E-value: 2.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688591487  59 LSKKKLQDLVREIDPnEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLE 122
Cdd:cd00076    1 LLRSAVARILKSAGF-DSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
Histone pfam00125
Core histone H2A/H2B/H3/H4;
67-119 3.54e-03

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 35.49  E-value: 3.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688591487   67 LVREIDPNEQLDEDVEEM---LLQIA-DDFIESVVTAACQLARHRKSSTLEVKDVQL 119
Cdd:pfam00125  65 VVREVVQSTKTDLRISADavvALQEAvEDFLVELFEEANLLAIHAKRVTLTPKDIQL 121
ATP-synt_F1_alpha_C cd18113
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ...
 61-95 7.48e-03

F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.


Pssm-ID: 349748 [Multi-domain]  Cd Length: 126  Bit Score: 34.65  E-value: 7.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 688591487  61 KKKLQDLVREIDPNEQLDEDVEEMLLQIADDFIES 95
Cdd:cd18113   91 RSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
 
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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