ID A0A2G5IBQ3_CERBT Unreviewed; 1155 AA.
AC A0A2G5IBQ3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=NuA3 HAT complex component NTO1 {ECO:0000313|EMBL:PIB02205.1};
GN ORFNames=CB0940_00534 {ECO:0000313|EMBL:PIB02205.1};
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:PIB02205.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB02205.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB02205.1,
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 -!- 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:PIB02205.1}.
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DR EMBL; LKMD01000100; PIB02205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5IBQ3; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 428..478
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 482..598
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 896..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 993..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 128182 MW; 1D4B1ACB174B7520 CRC64;
MAGSDTSPRR AVRTPRALAS IEPTTEPAQK KQRLRFEPGG PGGGGRYIDE QGNEMTRAEA
VERGLISSAP RSRSRRPVGA RPNIVAKAPK HRTSAATDGH TPSVTRPSMT TRPRRERPER
YAPPPTTPRP RYSNAAAAAA ASQASDGYKP REERSWDEFH PELDLAAGLM VFSADEVDGR
TSKHDPKLQN LKLNGLEVNG DVDMQDASDD ERSGRNGTPN RRRPGRPPRR PESMLSGLGS
PPAPRIQPLA THNPKERLNL PKPSYRHYNH FLQYEEDQLQ NKVNYVDRTM AGVGYQESDR
FELPPNVLIR LAENQHVEDE ADVSLRLASD GPAEVGLGHP VVGKVEYDMD EQDVAWLEEL
NEHRKAEELP AIKPAIFEIT MTQIEKEYHA LEKRIPKPQP RHAQTHRPRS SSQAAVNGDP
NPPGDEPDSK CSICDDGDCE NANAIIFCDG CDLAVHQECY GVPFIPEGQW FCRKCKEIGR
GTPTCIFCPN VDGAFKQTST LRWSHLLCAI WIPEVNIANM TFMEPIQDVD KVPKGRWKLS
CYICNQKMGA CIQCGNKNCY QAFHVTCARR ARLFLKMKSQ TQGGIDTSAL KAFCDKHVPQ
EWRRNNDTDN ATIEAKRWYK HAFKDRKWAD SQTAALELGA PPTPDGGLGG DAHGTEDTIA
VSKRRNKKDQ KCSWRLASGA PVVPQVVYTT VEASLTRFTI RKKKEFVEKV CRYWTLKREA
RRGAALLKRL QLQLEGFSSM EVTRRSFAGM GAAGGPRLQR RIDFAEMLQK DMSFLKDLTA
QVKQREELRL REVELLRELV DTVYFPIPPL LRPILLRAQK LDEKTRSFRT GFDMLAQRLR
ERYYTSVSDF SRDLSKIFAE ALAAVGTSGE PSEADIEAIH NQLNEVKVGS AAHMALTQEQ
KDLKRLAKRI VKAVKEPLEA AMKKEAELRG LELEEQLRKL DSMGIFASAT SKSGDADGAE
EQDNVDTDMP DAGAVEQEVE PAIAKDSMLP FANDTHTPAS KAASHASSNL NMSSKTRSDK
PTTEPLSPPI SRSSSRPSGA PASASGESSN ANGENHDVFA QGGVPWYLEP FDPIGTTIHE
ERYTGRAVLR AMSEELSDMD EDTLGELAGM STDATPNEKV NGGSHAASSS VSGSGTRARA
NSNRKKRPKR SHWSR
//
