ID A0A2G5IDI9_CERBT Unreviewed; 1558 AA.
AC A0A2G5IDI9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=BTB/POZ domain-containing protein 1 {ECO:0000313|EMBL:PIB02584.1};
GN ORFNames=CB0940_00785 {ECO:0000313|EMBL:PIB02584.1};
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:PIB02584.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB02584.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB02584.1,
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:PIB02584.1}.
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DR EMBL; LKMD01000100; PIB02584.1; -; Genomic_DNA.
DR OrthoDB; 318368at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
DR CDD; cd18186; BTB_POZ_ZBTB_KLHL-like; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR22872:SF2; BTB_POZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR22872; BTK-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50012; RCC1_3; 2.
PE 4: Predicted;
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 331..384
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 385..444
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 910..978
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 32..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1558 AA; 171233 MW; 8B22026C7D43E1D1 CRC64;
MSSLLWQAFY DDSIDAFERC LEAAAQNARS VHVSRGGPSH GSSATIGSPD YASSPSTLAR
SRKSHTPRTP AVGAVVLSKA DINGRDNQGM TLLHHVASCT TENAVAFATA LIDHPLIDLY
VQDLENGWTA LHRAFYFGNV TIARLILERD SGNIFASKQV NQLLKVKDRE GLGPLDLYAA
TIKDRTLRPE ATGRRRSASD ASEEDIPGPD GEDESTSSRI QSTEIGGDQL FSFGSGSNNN
LGLGDQDDRA FPERVTLRRP EHLLRRFYSE YLKQHDLKWA MHDPTYQREA IDIRGMWIED
MPWVIRSRPL VIQDVFMSKL HSAVLTSDPI SNLYMCGHGQ GGRLGTGDER TRFTYVCVEG
GALTGKHVAT VALGLNHSLA LDEAGEIYSW GNNAYGQLGF SLPKTSGDED PISTVPRQIF
GSLKRETVQG IAASRFHSVA HTSTSLFTFG KNEGQLGIVD SDARSLEFQT TPRKVAASLF
SSPISAVAAI DRATVCLLDN HDVWVFANYG YAKIQFPLDG FTNYFLKQSF LVTTYDTAPN
RVIKITAEGD TICALSSRGE IFTVSISQRA DDRSSVSTTN PAKIRSAISQ PQRIWSPKKS
NMAARDVGLD ADGSVILSTD EGSVWKRTRR AKIKDSTVTA ASEYRPKDYK FSRIPGLTRV
LAVRASGSGA YSALRYDCDV LRKQIVIEDP SLWKHVFPLM SFGDFGDNDR RSDDDDTRPR
FWQGPKKHDR LAAVKKAILG SADIDADLRA YFANASATSD HSFNACIATT TSDVQIPVHR
FMLTARSRVL RRGFRDLCEA STFTIPDLCQ SEINEHGQLV LTFQGVDLLT IVDLAMYLYT
DDVVPFWNFT KAAPKMAYSY KEVRAELMKI SHKLEMRALE PAVRQMVSPH PCLNMDLELA
YADPAFFYDA DIVVELEDDE EIKLHSALVC ARCPFFEGLF MGRSRGAWIA GRADGDHVKV
DLKHVSAKTF AMVLRHIYCE AGVELFDDIV STDTDDFLDT VTDVLSCANE LMLDRLSQVA
QSVAGQYVNV RNVCGLLNAM APSAVREFLD AGLEYLCLNL EAMLQGHYLN ELDPDLLEEL
DEVVRANQLA CMPFAKSGRA EQLLHDRHPA LAEAIDRNRR RKIDAVALRA KFNDVLSPGV
FNDASSNSPA HHRARRRSSQ VAKPESVREV PSLKAKASTK DMMFDMDEDQ DQASARLSPV
IRPMMSPRGL DATFQNTPPD ETWFDSRGKA VPSPKLAPHS TTPGAITPRT PKSPLLGANA
GKPWSLAALS SKVDMKDILQ QTSTSDRTSN LTQGLASAAS PPQNVPAPFS LPAPKMSQKE
RKRMQQAQLQ GAVSVSPANQ AQGEPAKPFS WQTISSQKRP TLKNVMESET STPSGSPNSR
SNSTPQMTMR QTVANPKHAK QAIGPRVVQQ RSVSDSKQVS LVSGPQGTNQ GKVQTLPVSQ
PSSSRPIPQS IRHQPMVEVD LGLSMSEIVA QQQIEKEIIR EAVAKRDLQD IQAEQEFQEW
WDKESARVQQ AAQQDSAGPA KGSRRGRGRG GARGRGKKPG GEGNAKGTTQ ATKVDGKK
//
