GenomeNet

Database: UniProt
Entry: F9X3H2_ZYMTI
LinkDB: F9X3H2_ZYMTI
Original site: F9X3H2_ZYMTI 
ID   F9X3H2_ZYMTI            Unreviewed;       445 AA.
AC   F9X3H2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=General transcription and DNA repair factor IIH {ECO:0000256|PIRNR:PIRNR015919};
GN   ORFNames=MYCGRDRAFT_37615 {ECO:0000313|EMBL:EGP89828.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP89828.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP89828.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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 TFIIK, in RNA transcription by RNA polymerase
CC       II. {ECO:0000256|PIRNR:PIRNR015919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR015919}.
CC   -!- SIMILARITY: Belongs to the GTF2H2 family.
CC       {ECO:0000256|ARBA:ARBA00006092, ECO:0000256|PIRNR:PIRNR015919}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001197; EGP89828.1; -; Genomic_DNA.
DR   RefSeq; XP_003854852.1; XM_003854804.1.
DR   AlphaFoldDB; F9X3H2; -.
DR   STRING; 336722.F9X3H2; -.
DR   EnsemblFungi; Mycgr3T37615; Mycgr3P37615; Mycgr3G37615.
DR   GeneID; 13403598; -.
DR   KEGG; ztr:MYCGRDRAFT_37615; -.
DR   VEuPathDB; FungiDB:ZTRI_2.360; -.
DR   eggNOG; KOG2807; Eukaryota.
DR   HOGENOM; CLU_028556_2_0_1; -.
DR   InParanoid; F9X3H2; -.
DR   OMA; INWVEVP; -.
DR   OrthoDB; 276422at2759; -.
DR   Proteomes; UP000008062; Chromosome 2.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   CDD; cd01453; vWA_transcription_factor_IIH_type; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR013083; Znf_RING/FYVE/PHD.
DR   NCBIfam; TIGR00622; ssl1; 1.
DR   PANTHER; PTHR12695; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2; 1.
DR   PANTHER; PTHR12695:SF2; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2-RELATED; 1.
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; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR015919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR015919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR015919};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR015919};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR015919};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          85..294
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   ZN_FING         315..332
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015919-1"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  48526 MW;  87F88E903F0D60BA CRC64;
     MADSDGEYDG HGSDDEIATN GGRAMPSRSK GRAQASWEAG ATRAWELKEA PDGSIEGVLG
     GIEEASKRKR LLKDTTPLQR GIIRHTILML DLSVAMLEKD LRPTRHLLTI TYTIAFIREF
     FEQNPISQLG ILGMREGLAI RVSDMSGNPN DHIAAVRALR GTDPKGNPSL QNGLDMARAA
     LYHTPSHGTR EVVIILGALL TSDPGDIHDT IKACIKDRIR VTIIGLAAQM HICAEICRKT
     NAGDDNCYNV AVDEVHFREL LMGITTPPVV RSTDAEAQKL NQAALLMMGF PSRIVEEHAT
     LCACHGNLTR GGYLCSRCKA KVCSLPATCP TCDLTLILST HLARSYHHLF PLQNWVEVSW
     QRAADRGSEQ CFGCLSPFPR VHGATNGDDA DKTYSKRAEG ASESSRYECE SCQNHFCIDC
     DCFNHETSHN CPGCTSSTHL PGAEG
//
DBGET integrated database retrieval system