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Database: UniProt
Entry: F0XL26_GROCL
LinkDB: F0XL26_GROCL
Original site: F0XL26_GROCL 
ID   F0XL26_GROCL            Unreviewed;      1035 AA.
AC   F0XL26;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:EFX01604.1};
GN   ORFNames=CMQ_8070 {ECO:0000313|EMBL:EFX01604.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX01604.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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DR   EMBL; GL629788; EFX01604.1; -; Genomic_DNA.
DR   RefSeq; XP_014171086.1; XM_014315611.1.
DR   AlphaFoldDB; F0XL26; -.
DR   STRING; 655863.F0XL26; -.
DR   GeneID; 25981685; -.
DR   eggNOG; ENOG502QPS1; Eukaryota.
DR   HOGENOM; CLU_293559_0_0_1; -.
DR   InParanoid; F0XL26; -.
DR   OrthoDB; 5489296at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06449; ACCD; 1.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005965; ACP_carboxylate_deaminase.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   NCBIfam; TIGR01274; ACC_deam; 1.
DR   PANTHER; PTHR31668; GLUCOSE TRANSPORT TRANSCRIPTION REGULATOR RGT1-RELATED-RELATED; 1.
DR   PANTHER; PTHR31668:SF10; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          59..91
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          97..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1035 AA;  113023 MW;  B25917EB93C725A3 CRC64;
     MVTVSRTFAV AESFLRQQAI AGSIWIPVDM AAEAAAVGTS ENVDPLVSAR PYRSHKIPAC
     DFCRRRKSRC DRVRLDEPCS LCRAHWRTCT SRSADHAVLT RPMTPRQRRP RKDHKTHRPS
     AVPPSSPPET VAVVDKTVDG RLSAHGSPHR PSPHAAEAAP NLESTVVPET NLSGHIVGPT
     LARDAQMLEQ YISPRDNVAV SHVHPNPYSV YSDDPLNPVV YMKVPRQRSR VSSGNGTPGF
     KQFEVIDKIC ESLGPNLVDL YFDIVHPPFP ILDQTAIVKA YEQGVLPHAL TCEIYAVALV
     FWQLSDKIAA TSRPPPDIRY IWNLTVSAMH EDFLSPCFST VVACILDLLG RPITSITYNA
     INVGSAVALA QSLGLNRNPA SWNLESPQKN LRIRTWWALL IHDYWASLCH GTPCHIHRDQ
     WDVVLPTMGT ILDGAVSENS STVSEARRKG AQSFIGLCRL TKILGELLST IYCLRHEPLE
     NVLRNLRRIE TSIDDWQESL PPWLNPEHGD FERDQPGSLN LRLSFLAVKM CICRVALQGR
     CVKAGNSLIQ FVTSLSTDET RMFWLPYAAY HFASAVTLML RCALEAHTEN VGVTCVKSAR
     KLIDYLRRMK TEADWDLADI CLGQCETTVK QMSDGGYAEF WKRTGGAGRL LSDSVRDHVA
     QPGQDEVEDG SGLVGGIADA ASTSAAVAAV DPVQLPETFA AIPRESLLFG LSPIQALPRI
     SKALGGKVNI YAKREDCNSG FAYGGNKTRK LEYFVPEILS SGSDTLISIG GVQSNHTRQV
     AALATRLGLK AALVQEKWVN WDDVVYEKAG NIQLSRLMGA DVRLDPSPFG IEHKPTLKNL
     EKELQAAGAK PYYIPAGASD HPLGGLGFAR WAFEVIQQEK EAGVFYDAII VCAVTGSTMA
     GIVAGFKLAE KLGGKPRKVI GIDASATVEQ TAAQVLRIAK ATGVKIGLED GDITEKDIIL
     DGRYHAGTYG IPDKTTIDAI KFGASTEAFI TDPVYEGKSL AGMMDLVRNG EIAEGSNVLY
     AHLGGQLALN AYTSM
//
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