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Database: UniProt
Entry: A0A2G5HQC3_CERBT
LinkDB: A0A2G5HQC3_CERBT
Original site: A0A2G5HQC3_CERBT 
ID   A0A2G5HQC3_CERBT        Unreviewed;       676 AA.
AC   A0A2G5HQC3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=VMS1 {ECO:0000313|EMBL:PIA94725.1};
GN   ORFNames=CB0940_08365 {ECO:0000313|EMBL:PIA94725.1};
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:PIA94725.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA94725.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA94725.1,
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family.
CC       {ECO:0000256|ARBA:ARBA00009262}.
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:PIA94725.1}.
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DR   EMBL; LKMD01000104; PIA94725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HQC3; -.
DR   OrthoDB; 8371at2759; -.
DR   Proteomes; UP000230605; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047139; ANKZ1/VMS1.
DR   InterPro; IPR041175; VLRF1/Vms1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR16036; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR16036:SF2; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF18826; bVLRF1; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          72..94
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REPEAT          501..534
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          32..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  74698 MW;  462616A4E8AC0C7A CRC64;
     MAAPNGHADQ LLKRPLYVFD LPDEILYTLQ LKSQPTAGAD PDLTTPPPPT PASPSLTATE
     NQEGAPSKAT SCALCGLSFA SLLEQRSHIR SDLHGYNIKQ KQRNKKPVSE AEFEQLVGQL
     DESISGSDTS DTEDDEDDKH ESTLSALLKR QAKITDGDAD DAPTLKRKRG SGKPPMIWFS
     SSKLPLNTSL GVYRSIFTSK EQDQEDKLLD VIKQKQLAPK PQPSHQKKQQ SKDEEEDGGV
     ALPASMIQRG TSADGPHYFL CMIGGGHFAA MVVSLTPKLT KKAGIEDRSA TVIAHKTFHR
     YTTRRKQGGS QSANDNAKGN AHSAGSSIRR YNESALIQEV RDLLAEWKPL IDTSELLFIR
     ASGTTNRRTL FGPYEEQVLN SRDDRIRGFP FNTRRATQSE LMRAFVELTR VKVSEVDEAA
     LARQAEEDQA KATAKAEALA NSKNNAPKAA KISKEDEEAA LHTQQLQALI RRSKAPGLLS
     YIQSNKLSPD LRFVPAEHNH HAPTPLHLAA ASNSPACVST LLIKLGADPT TRNEDGKSAF
     DIAGDRATRD AFRLARAQLG EDKWSWEDAG VAAALSQADA QARAAREKEE KAAEDAAEKQ
     RRQAEIERLR KEDTQKRNDQ QEKKFGKGHM LAKPQLTAEE RRAEEARGMT DEMRMRLERE
     KRARAAEERM KRLAGK
//
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