ID A0A2G5HZG3_CERBT Unreviewed; 584 AA.
AC A0A2G5HZG3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=RING-CH-type domain-containing protein {ECO:0000259|PROSITE:PS51292};
GN ORFNames=CB0940_06031 {ECO:0000313|EMBL:PIA97934.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA97934.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA97934.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA97934.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PIA97934.1}.
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DR EMBL; LKMD01000102; PIA97934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HZG3; -.
DR OrthoDB; 2730627at2759; -.
DR Proteomes; UP000230605; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR46283:SF2; AT07234P-RELATED; 1.
DR PANTHER; PTHR46283; E3 UBIQUITIN-PROTEIN LIGASE MARCH5; 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|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 71..145
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 65578 MW; 70B135C1F00F0D77 CRC64;
MASLPARQSS RPRRASPSEQ SQASTTQPQE SPAQVRSQSE DSQTIFVNKP AEEEAELEQE
KSLPAETAAG QDEDEVMRCW ICMSDSTEDG PDTSPWRDPC PCALVAHEEC LLDWIADIES
PKNAHNRSRS GKIECPQCKA EIKLSRPRDY IVDAMRGLER MTDRAVIPVS GLALSSAMVH
ISQYVGVHTI YAIFGADDGN RLLEPLWRWA TQPSVEVYAS EPEKVWEILS TLFLDRLKHW
RLIVGLPLIT PVLVLSRTSL ADSVLPVLPI VFFASQAHSP SDALDFASWP PSASFAFAVL
PYVRSLYNAY YKRVWAEKEK QWLEAVKPRV SQQNEQDAAA NNGQNPAEAE GDGNVFEVRI
EQEVWEDDWE QEDQRLVQQA ADRQPAAHNE AQQPGLQIEQ NNDEDANAPQ QAAGEVPQQA
QAPQRDLPQE GGFPRGENDA APAPVVPRDR LEDFARRRQE AQGQHNNAGN VQNVERRLSL
SLTGMAETFL GALFFPTIAG LAGEALKLVL PHRWVTPPPM RIFRETWAAG FWQRKWARSL
VGGCLFVVCK DFLRLYVCWR AAQLHKDRRV LDVDRRKGRG SFRP
//
