TF2H2_ARATH
ID TF2H2_ARATH Reviewed; 421 AA.
AC Q9ZVN9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=General transcription factor IIH subunit 2 {ECO:0000305};
DE Short=AtGTF2H2 {ECO:0000303|PubMed:16623910};
DE AltName: Full=TFIIH basal transcription factor complex p44 subunit {ECO:0000305};
DE Short=Atp44 {ECO:0000303|PubMed:15645454};
GN Name=GTF2H2 {ECO:0000303|PubMed:16623910}; Synonyms=P44 {ECO:0000305};
GN OrderedLocusNames=At1g05055 {ECO:0000312|Araport:AT1G05055};
GN ORFNames=T7A14.8 {ECO:0000312|EMBL:AAC97995.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH XPD.
RX PubMed=16623910; DOI=10.1111/j.1365-313x.2006.02705.x;
RA Vonarx E.J., Tabone E.K., Osmond M.J., Anderson H.J., Kunz B.A.;
RT "Arabidopsis homologue of human transcription factor IIH/nucleotide
RT excision repair factor p44 can function in transcription and DNA repair and
RT interacts with AtXPD.";
RL Plant J. 46:512-521(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP COMPONENT OF TFIIH CORE COMPLEX, AND NOMENCLATURE.
RX PubMed=15645454; DOI=10.1002/em.20094;
RA Kunz B.A., Anderson H.J., Osmond M.J., Vonarx E.J.;
RT "Components of nucleotide excision repair and DNA damage tolerance in
RT Arabidopsis thaliana.";
RL Environ. Mol. Mutagen. 45:115-127(2005).
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 (By similarity). Can restore UV resistance
CC in the NER-deficient ssl1-1 yeast mutant (PubMed:16623910).
CC {ECO:0000250|UniProtKB:Q13888, ECO:0000269|PubMed:16623910}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of XPB,
CC XPD, TFB1/GTF2H1, GTF2H2/P44, TFB4/GTF2H3, TFB2/GTF2H4 and TFB5/GTF2H5,
CC which is active in NER. The core complex associates with the 3-subunit
CC CDK-activating kinase (CAK) module composed of CYCH1/cyclin H1, CDKD
CC and MAT1/At4g30820 to form the 10-subunit holoenzyme (holo-TFIIH)
CC active in transcription (By similarity). Interacts with XPD
CC (PubMed:16623910). {ECO:0000250|UniProtKB:Q13888,
CC ECO:0000269|PubMed:16623910, ECO:0000305|PubMed:15645454}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}.
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DR EMBL; AF499443; AAM90909.1; -; mRNA.
DR EMBL; AC005322; AAC97995.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27784.1; -; Genomic_DNA.
DR EMBL; AK229479; BAF01337.1; -; mRNA.
DR PIR; E86184; E86184.
DR RefSeq; NP_683275.2; NM_148434.4.
DR AlphaFoldDB; Q9ZVN9; -.
DR SMR; Q9ZVN9; -.
DR STRING; 3702.AT1G05055.1; -.
DR PaxDb; Q9ZVN9; -.
DR PRIDE; Q9ZVN9; -.
DR ProteomicsDB; 232755; -.
DR EnsemblPlants; AT1G05055.1; AT1G05055.1; AT1G05055.
DR GeneID; 839332; -.
DR Gramene; AT1G05055.1; AT1G05055.1; AT1G05055.
DR KEGG; ath:AT1G05055; -.
DR Araport; AT1G05055; -.
DR TAIR; locus:504956103; AT1G05055.
DR eggNOG; KOG2807; Eukaryota.
DR HOGENOM; CLU_028556_1_2_1; -.
DR InParanoid; Q9ZVN9; -.
DR OMA; CMCHIEN; -.
DR OrthoDB; 768809at2759; -.
DR PhylomeDB; Q9ZVN9; -.
DR PRO; PR:Q9ZVN9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVN9; baseline and differential.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:InterPro.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IGI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IGI:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:TAIR.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR007198; Ssl1-like.
DR InterPro; IPR004595; TFIIH_C1-like_dom.
DR InterPro; IPR012170; TFIIH_SSL1/p44.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07975; C1_4; 1.
DR Pfam; PF04056; Ssl1; 1.
DR PIRSF; PIRSF015919; TFIIH_SSL1; 1.
DR SMART; SM01047; C1_4; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR TIGRFAMs; TIGR00622; ssl1; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..421
FT /note="General transcription factor IIH subunit 2"
FT /id="PRO_0000435434"
FT DOMAIN 83..272
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 362..408
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46978 MW; 20A863C08776F4E4 CRC64;
MSNQRKRSND EREEEDDEDA EGIGEWERAY VDDRSWEELQ EDESGLLRPI DNSAIYHAQY
RRRLRMLSAA AAGTRIQKGL IRYLYIVIDF SRAAAEMDFR PSRMAIMAKH VEAFIREFFD
QNPLSQIGLV SIKNGVAHTL TDLGGSPETH IKALMGKLEA LGDSSLQNAL ELVHEHLNQV
PSYGHREVLI LYSALCTCDP GDIMETIQKC KKSKLRCSVI GLSAEMFICK HLCQETGGLY
SVAVDEVHLK DLLLEHAPPP PAIAEFAIAN LIKMGFPQRA AEGSMAICSC HKEVKIGAGY
MCPRCKARVC DLPTECTICG LTLVSSPHLA RSYHHLFPIA PFDEVPALSS LNDNRRKLGK
SCFGCQQSLI GAGNKPVPCV TCRKCKHYFC LDCDIYIHES LHNCPGCESI HRPKSVSLME
E
