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Database: UniProt
Entry: A0A2S6C1H2_9PEZI
LinkDB: A0A2S6C1H2_9PEZI
Original site: A0A2S6C1H2_9PEZI 
ID   A0A2S6C1H2_9PEZI        Unreviewed;       318 AA.
AC   A0A2S6C1H2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=RING-CH-type domain-containing protein {ECO:0000259|PROSITE:PS51292};
GN   ORFNames=CBER1_00285 {ECO:0000313|EMBL:PPJ53585.1};
OS   Cercospora berteroae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ53585.1, ECO:0000313|Proteomes:UP000237631};
RN   [1] {ECO:0000313|Proteomes:UP000237631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT   mechanisms and extends production to the genus Colletotrichum.";
RL   bioRxiv 0:0-0(2017).
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:PPJ53585.1}.
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DR   EMBL; PNEN01000578; PPJ53585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6C1H2; -.
DR   STRING; 357750.A0A2S6C1H2; -.
DR   OrthoDB; 2718337at2759; -.
DR   Proteomes; UP000237631; 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:UP000237631};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        168..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..153
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35688 MW;  2FA444A467B15EF7 CRC64;
     MAAYSTGASW SFPADLPGAF EQQFSPEPPL AGVDDPSMNG SHHTADSETK PAAEPEPNRR
     RTHYRARKCR ICLEEVEPTF HYDPDSTLPA SMQPPPRVTY ESEDGGRLLS PCKCKGSQKY
     VHEECLGAWR RADPLQQRNY WECPTCRYKY KLQRLTWSAW ISSTSAQLGL TAVILVASIF
     LLGFVADPII NLYIDPYTTI ATGGGPRDSL LFEDEPTTWF EHMLKGLASL GLVGFAKFLF
     TLSPFQWFNV RTSFGRNTVG GNGRDRLQQI SWITILIGII TASYAIYKLV RAWSRRTLES
     ASERVMDVGG NDDEDEDD
//
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