ID A0A2B4S6M2_STYPI Unreviewed; 394 AA.
AC A0A2B4S6M2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=General transcription factor IIH subunit 3 {ECO:0000256|RuleBase:RU368090};
DE AltName: Full=General transcription factor IIH polypeptide 3 {ECO:0000256|RuleBase:RU368090};
GN Name=Gtf2h3 {ECO:0000313|EMBL:PFX24719.1};
GN ORFNames=AWC38_SpisGene10685 {ECO:0000313|EMBL:PFX24719.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24719.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- FUNCTION: Component of the general transcription and DNA repair factor
CC IIH (TFIIH) core complex, which is involved in general and
CC transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC and, when complexed to CAK, in RNA transcription by RNA polymerase II.
CC In NER, TFIIH acts by opening DNA around the lesion to allow the
CC excision of the damaged oligonucleotide and its replacement by a new
CC DNA fragment. In transcription, TFIIH has an essential role in
CC transcription initiation. When the pre-initiation complex (PIC) has
CC been established, TFIIH is required for promoter opening and promoter
CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC subunit of RNA polymerase II by the kinase module CAK controls the
CC initiation of transcription. {ECO:0000256|RuleBase:RU368090}.
CC -!- SUBUNIT: Part of a TFIID-containing RNA polymerase II pre-initiation
CC complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1,
CC GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2,
CC ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10,
CC TAF11, TAF12 and TAF13. Component of the 7-subunit TFIIH core complex
CC composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and
CC GTF2H5, which is active in NER. The core complex associates with the 3-
CC subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H,
CC CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription. Interacts with RARA; the interaction requires prior
CC phosphorylation of RARA on 'Ser-369' which then enhances interaction of
CC RARA with CDK7. {ECO:0000256|RuleBase:RU368090}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368090}.
CC -!- SIMILARITY: Belongs to the TFB4 family. {ECO:0000256|ARBA:ARBA00005273,
CC ECO:0000256|RuleBase:RU368090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX24719.1}.
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DR EMBL; LSMT01000169; PFX24719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4S6M2; -.
DR STRING; 50429.A0A2B4S6M2; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
DR InterPro; IPR004600; TFIIH_Tfb4/GTF2H3.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12831:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 3; 1.
DR PANTHER; PTHR12831; TRANSCRIPTION INITIATION FACTOR IIH TFIIH , POLYPEPTIDE 3-RELATED; 1.
DR Pfam; PF03850; Tfb4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU368090};
KW DNA repair {ECO:0000256|RuleBase:RU368090};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU368090};
KW Nucleus {ECO:0000256|RuleBase:RU368090};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU368090};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU368090}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|RuleBase:RU368090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368090}.
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 394 AA; 43888 MW; B55238A2BA9B893F CRC64;
MADENISNLL VVILDANPVW WGRTSNEEQQ RISLTHCVDS LMVFCNAHLM MQHSNCLSFI
ISHTNTSKFV FPKEDSGEDI SGNGQKELLT DGKYEGFAEV NDAIITEMKS LLSTEDLTDS
QSTELPPTLL ANALTMALCL LWPEGRPVIG NVANFVRGYK PKAPCQVFPY AYLGSTFTQV
FINIYTVTAL PEVLKAAPDV STQYMPIMNC IFAAQKSNTM IDACVVDEHS GFLQQAADIT
GGMYLKVPQT LALLQYLLNT MIDACVVDEH SGFLQQAADI TGGMYLKVPQ TLALLQYLLF
IASLFLSVSL AKAKLKPTFE WLLKKYFRNY YSKGGITGQC NFCTWTESQF SFLAILLSVE
TPQELCYQRT RFKLPALPLA RPKKKKKENT APGK
//