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Database: UniProt
Entry: A0A1Y2UL68_9PEZI
LinkDB: A0A1Y2UL68_9PEZI
Original site: A0A1Y2UL68_9PEZI 
ID   A0A1Y2UL68_9PEZI        Unreviewed;       296 AA.
AC   A0A1Y2UL68;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=RING-CH-type domain-containing protein {ECO:0000259|PROSITE:PS51292};
GN   ORFNames=M434DRAFT_83823 {ECO:0000313|EMBL:OTA83621.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA83621.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA83621.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA83621.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR   EMBL; KZ112605; OTA83621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2UL68; -.
DR   STRING; 1001938.A0A1Y2UL68; -.
DR   Proteomes; UP000194361; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16495; RING_CH-C4HC3_MARCH; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46347; RING/FYVE/PHD ZINC FINGER SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR46347:SF1; RING_FYVE_PHD ZINC FINGER SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        128..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..116
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  33696 MW;  E49B0D8530D591DA CRC64;
     MADDQTSSGT ATGNDHSQNQ ESRPKTNSDQ PKKRIRMCWI CHDEVEATYE EPSFLDGIGN
     RRPKRQYISE NGDRLINPCN CKGSVKYVHE GCLKDWLSHN PEALQCSRCR YEYRMERLNW
     ANRIRSPVVA LGLTIVILLI TIFLLGFIAD PLLKLWLDPA NTIAETITTG HIISVEDEDD
     PFPEESGLFT HFLKGFFSLG LLGFIKVFLV ASPWQWWNLR TSGVIGGGGR RGGTGRDRMQ
     NINLTLVLIG VITFLYSVWK VTRQWTKDTL DKASQRILNV QRDNDDDDDD SDDEDD
//
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