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Database: UniProt
Entry: G9NU18_HYPAI
LinkDB: G9NU18_HYPAI
Original site: G9NU18_HYPAI 
ID   G9NU18_HYPAI            Unreviewed;       480 AA.
AC   G9NU18;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Zinc finger PHD-type domain-containing protein {ECO:0000259|SMART:SM00249};
GN   ORFNames=TRIATDRAFT_283222 {ECO:0000313|EMBL:EHK45555.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK45555.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK45555.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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:EHK45555.1}.
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DR   EMBL; ABDG02000023; EHK45555.1; -; Genomic_DNA.
DR   RefSeq; XP_013943840.1; XM_014088365.1.
DR   AlphaFoldDB; G9NU18; -.
DR   STRING; 452589.G9NU18; -.
DR   GeneID; 25779603; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   HOGENOM; CLU_020879_0_0_1; -.
DR   OMA; RPRYMNP; -.
DR   OrthoDB; 5491784at2759; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47793; HISTONE DEACETYLASE COMPLEX SUBUNIT CTI6; 1.
DR   PANTHER; PTHR47793:SF1; HISTONE DEACETYLASE COMPLEX SUBUNIT CTI6; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          19..85
FT                   /note="Zinc finger PHD-type"
FT                   /evidence="ECO:0000259|SMART:SM00249"
FT   REGION          102..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  53513 MW;  7F3C299835C6AB55 CRC64;
     MSNELDPLQD EEDEAVRCIC GCEDYPGRPP VDGSDANFLA SIELTEDVTG FFVQCDICKV
     WQHGACVGIF SAESSPEEYF CEQCRKDLHK IHTANNGQKY SKYLPLSRPA RTASRATSVA
     KDGARSPRLG SSKSARSQST SHISKRRSTM NSRDAAYDDE QLRRAIEASK EEVAQDGTET
     TNRRTKRGRS NSEENNVIVK RQRTNSQSTT PPPRPMDTIS QENTDDENGG RNGLKRPRTY
     KVTERSEREE KDRLRQETIS KRKGRADRRR TEDSDVSEDV NPLSSKAPNN SGAETSGFED
     PTPAVPSPVP GTPPASHSSA ANSNKRTSRS NHKKGKGKNQ YTKDRTTDIE RSPARSVSRD
     TQRANNATTA AHSRHVGDHK NSSRTKIGMA GKMSMLDMKR RVAAIMDFIS RTQVDLAAEA
     ALDRSNNSTQ SPLDPTKSPM EKDAKEQRDS PESKVFKELS CMEMMDVLTR DMVKWQNQYA
//
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