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Conserved domains on  [gi|1333139713|ref|XP_023544738|]
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transcription initiation factor TFIID subunit 12 [Cucurbita pepo subsp. pepo]

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 ...
 378-451 1.83e-37

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: 132.27  E-value: 1.83e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333139713 378 SRILSKRSIGELVNQIDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNITL 451
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 ...
 378-451 1.83e-37

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: 132.27  E-value: 1.83e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333139713 378 SRILSKRSIGELVNQIDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNITL 451
Cdd:cd07981     1 NPLLSKRKLQELVREVDPNERLDPDVEELLLQLADDFVDDVVTFACKLAKHRGSDTLEVKDVQLHLERNWNIRV 74
TFIID_20kDa pfam03847
Transcription initiation factor TFIID subunit A;
382-449 7.88e-31

Transcription initiation factor TFIID subunit A;


Pssm-ID: 367691 [Multi-domain]  Cd Length: 68  Bit Score: 114.00  E-value: 7.88e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333139713 382 SKRSIGELVNQIDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNI 449
Cdd:pfam03847   1 SKRKLQDLVQQIDSTTKLDEDVEDLLLEIADDFVESVTTFACKLAKHRKSDKLEVRDIQLHLERNWNM 68
COG5624 COG5624
Transcription initiation factor TFIID, subunit TAF12 [Transcription];
379-485 2.52e-20

Transcription initiation factor TFIID, subunit TAF12 [Transcription];


Pssm-ID: 227911 [Multi-domain]  Cd Length: 505  Bit Score: 93.99  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333139713 379 RILSKRSIGELVNQ-IDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNITLPGFCSD 457
Cdd:COG5624   382 RLDSKRKLEELQHGgVDEEEKIENEVEELLLSRADGFVEPVTEFSCRLAKHRKSDTLEVRDGQLHLERNWNIRCPGFVDD 461

                          90       100
                  ....*....|....*....|....*....
gi 1333139713 458 EI-KIFRKPLTNDTHRERLAAVKKSIVAS 485
Cdd:COG5624   462 IIhMSYRKQKPTVEYCQKKLAIKTEKGIE 490
 
Name Accession Description Interval E-value
HFD_TAF12 cd07981
histone-fold domain found in transcription initiation factor TFIID subunit 12 (TAF12) and ...
 378-451 1.83e-37

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: 132.27  E-value: 1.83e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333139713 378 SRILSKRSIGELVNQIDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNITL 451
Cdd:cd07981     1 NPLLSKRKLQELVREVDPNERLDPDVEELLLQLADDFVDDVVTFACKLAKHRGSDTLEVKDVQLHLERNWNIRV 74
TFIID_20kDa pfam03847
Transcription initiation factor TFIID subunit A;
382-449 7.88e-31

Transcription initiation factor TFIID subunit A;


Pssm-ID: 367691 [Multi-domain]  Cd Length: 68  Bit Score: 114.00  E-value: 7.88e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333139713 382 SKRSIGELVNQIDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNI 449
Cdd:pfam03847   1 SKRKLQDLVQQIDSTTKLDEDVEDLLLEIADDFVESVTTFACKLAKHRKSDKLEVRDIQLHLERNWNM 68
COG5624 COG5624
Transcription initiation factor TFIID, subunit TAF12 [Transcription];
379-485 2.52e-20

Transcription initiation factor TFIID, subunit TAF12 [Transcription];


Pssm-ID: 227911 [Multi-domain]  Cd Length: 505  Bit Score: 93.99  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333139713 379 RILSKRSIGELVNQ-IDPSERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLEKNWNITLPGFCSD 457
Cdd:COG5624   382 RLDSKRKLEELQHGgVDEEEKIENEVEELLLSRADGFVEPVTEFSCRLAKHRKSDTLEVRDGQLHLERNWNIRCPGFVDD 461

                          90       100
                  ....*....|....*....|....*....
gi 1333139713 458 EI-KIFRKPLTNDTHRERLAAVKKSIVAS 485
Cdd:COG5624   462 IIhMSYRKQKPTVEYCQKKLAIKTEKGIE 490
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 381-444 2.19e-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: 42.20  E-value: 2.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333139713 381 LSKRSIGELVNQIDPsERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILLHLE 444
Cdd:cd00076     1 LLRSAVARILKSAGF-DSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 380-441 3.50e-03

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: 35.98  E-value: 3.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333139713 380 ILSKRSIGELVNQIDPsERLDPEVEDLLVDLAEEFVESITTFGCSLAKHRKSTTLEAKDILL 441
Cdd:cd22909     1 ELPKAPVKRIIKKAGA-ERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIEL 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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