ID A0A0D2DQY0_9EURO Unreviewed; 1594 AA.
AC A0A0D2DQY0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=BTB domain-containing protein {ECO:0000259|PROSITE:PS50097};
GN ORFNames=Z517_06856 {ECO:0000313|EMBL:KIW80241.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW80241.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW80241.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW80241.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846972; KIW80241.1; -; Genomic_DNA.
DR RefSeq; XP_013284049.1; XM_013428595.1.
DR AlphaFoldDB; A0A0D2DQY0; -.
DR STRING; 1442368.A0A0D2DQY0; -.
DR GeneID; 25306346; -.
DR VEuPathDB; FungiDB:Z517_06856; -.
DR HOGENOM; CLU_002285_0_0_1; -.
DR OrthoDB; 318368at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 343..396
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 397..456
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 909..984
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 200..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1594 AA; 174413 MW; A37ECB33B94AC141 CRC64;
MSYNLWRSFF EDDVDAFRQY LANATFSSAA PRTPGAGQVG SAALKIGSPG NLAVSPKTPF
KFRKSSGTTP LSATPGKNVA LVLTRAEVNT KDSFGRTILH HAASSQSDDA LAFVKALLEM
PFLDLYAQDL ESGWTPLHRA LYFGNISVAH ALMARDIQNA TDYTTNAQHS LAGGLVKIKD
HEGNSPFEVF GLTIAPRSLQ QDSSTLPPGI RDDDSINGVD DSGEHQDHDR ARRHVTPLID
LAGDEVYAFG SNKNLSLGLG DGDDRHFPER LHFERPDHLL RRLLDDHLAE RRKSWVHEDL
ADSVGDLQSH SDLPAIIRYR PITIQNVVMS KLHTAVLTSD PISNLYICGY GPGGRLGTGD
ENTSFTYRCI QAGGLAKRRI SSIALGQDHS VAVCSQGEVY TWGSNRFGQL GYALPEVSKN
EVPTQLIPRQ LFGYIKKEVI IGAAASAIHS AIYTASAMYT FGKNEGQLGL TDAEARSLEM
QVLPRRVGVS ILQSPIKSVS AIDRATIVLL ENHDVFVFTH YGWTKLTFPL ETFTNYYMGN
NLSTRFNMES NYIKQITSGG NTICAMSSFG EVYSIDVPKV PETVPSNMST TNPTKARNAL
PAPSRLWSLR KDHMSAIDVA VGQDGSIILC TASGSAWRKE KRANIKTVRD TKLSPGRPKD
YKFVRIPNLT GVIAVRSNAF GAFTAVRKDV STTRDQIVLA PPSLWRDAFR LLPFREYGVS
QTVPVAEVDA CHVAQAVISR SSAETDILNM CQRHEPLSQS QYDVWITSTV TDVRIPIHSF
MLKGRSRVMR TALAEVQETY YYSIPDVMSI EYGQDGQIQV SFQGADFLTL MNLVLYLYTD
NLVDVWHYTS KALQSAARFR SVRVELMKIA SHLEMRSLER AVRVMINPAR SLTNDMELAV
VDPDFFSDAD VIVELADDAE LPAHSVLLCN RCPFFDGLFN GRAGGMWMAS RRSNAEDQAA
AVRVDLKHID EKIFVMVLRH LYADTGEELF DDVVTSSLDE FVDIVIELMS VANELMLDRL
AQICQKTLGR HVNLRNVCPM VNIVAECTVD SFKNAALEYI CLNLESMLEL KLLDDLDEDL
LVELDKVVQA NQLAFLPFAR SNRAATELLE NYPELLGQIE AGRQTRIDSM RLRSRLIEDE
GRFAASMRSR YGSLERASCS PHNKNSLPTP VDSSPPSTPS RSPAIKANDA EDDLPFDMDG
EDPELPPASN SEKTLHAPGR KDLSLGRAAS SATTKLPVND SPPLLTRSRE AISSSLRFSD
EDSPESAVIG TATNGFAAQR TAWRVPTQGV KKDGLKDIME QASAARVSNL TQAMQTASTG
SKANTKVSQK ERKRQQQQTK EQSTNPSGLS AVKSTTNSPS SPWQAIAKTT KPNSSPTVFA
PIEAVKEAAM KQPMTMRQTV ARGTSTTGSS PKGSAGAGPA IGLTAPSKPA APQIQSIRHT
PLPTRASAVD ARTSMAEILA QQQIEKIAVK EAIAKKSLQE IQQEQEFQEW WDNESRRVQE
QEAQANAAAT ARRGKGGRAR GGHRRGGPQG KASTVIEAGE QQKKSSMGSA SVRQESGSGR
GIGPSNGQRG SASSARARGQ GKPQHSHRGA RHQS
//
