ID A0A2J6SUW3_9HELO Unreviewed; 1570 AA.
AC A0A2J6SUW3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=BTB domain-containing protein {ECO:0000259|PROSITE:PS50097};
GN ORFNames=K444DRAFT_539396 {ECO:0000313|EMBL:PMD54565.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD54565.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD54565.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD54565.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ613859; PMD54565.1; -; Genomic_DNA.
DR STRING; 1095630.A0A2J6SUW3; -.
DR InParanoid; A0A2J6SUW3; -.
DR OrthoDB; 318368at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR CDD; cd18186; BTB_POZ_ZBTB_KLHL-like; 1.
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; PF13637; Ank_4; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF13540; RCC1_2; 1.
DR SMART; SM00248; ANK; 3.
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; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 327..380
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 381..441
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 441..497
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 914..985
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 195..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1570 AA; 172780 MW; 77FCDBC00FFE7ADA CRC64;
MSNLLWRYYH NGEVDRFRHL LSNGSHSTQY TPKNYGAGLG AHTVCGSVGS PSGFATSPRA
VVKGRKVSGQ AGNFGAGKVG NSGLGRAEVN SRDHAGLTIL HRAVSSPSES AISFAIALLE
HPTIDLYIQD TENGWTALHR ALYFGNITMA HAIIEKDIRD PGSQGSSVIK VKDYEGNSPF
DVYNATIARR NLQLTGDGTE SDDGSNDDTE FVQAESCSDP NSMQTSIDGD EVFTWGSSRN
HGLGFKDQDD RQHPEKITLR RPDHLLFRFY REHLESNGAA NSANDTSLSL PKSVSELPTL
IANRPIIIQD VALSKLHSAI LTTDPESNLY ICGFGPGGRL GTRDEMTRFS YVPIEGGALA
GKKVTKIALG QNHSLAVTSE GSLLSWGTNT FGQLGYTLPR PALKDEEPIC ATPRQIFGPL
KREFIVGAAA SALHSVAHTS TSLFTWGKNE GQLGLMDSDS RSLEVQSVPR KVAASLFKAS
ITMVSAINSA TIVLLANHTV CVFTHYGYNI VKFPLDEGFT NYHLKSNPLT TRYDTVSNHI
SQVTAGGDTI AAISTRGDLY TLTVRKHDNT SATSTTNPSK IKDSLSTPER VWALRKGNWD
GIKSAGITEN GSVIVCTQAG AVWHRVKRAK IKDAFTGSRS FNRKDFKFQR IPGLTKVAAI
RSTAFGVYAA IRKDCDVTKT QIAVEQRSLW EDIAPLLSLR GLEASKPLLD DEDTETPRSW
TPVLPKDLFD PMKRAVLTSP DLDADIARHL LGQDLDGYDI DICTTTSDVR IPTHGFILAR
SPVMRNALSQ FRRSGAASIP DVLSISSGSV EGRTEIGAGD PKPRIMFQGL DLIVVVNLII
YLYEDTIIDV WHFTRHCPSM AFRYRQVRIE LMKTAGHLKL NKLEAAVRLM TEPERQLNVD
LNRATHDPRF FDDGDAIIEL DGSELRVHSA LLCQRCPFFE GMFNGRAAGQ WLASRREDIS
EAVRIDLKHI EPETFRLVLR FLYADVGPEL FDDVVSADID EFSELLLDVM AASNELMLNR
LSQICQQVIG RFVSTRNVCS LLNVISPCSV KLFKDSALEY VCLQLESMLE NHLLNDLDEE
LLLELSNVVR ANQLNCLPFA KSGRAELLLH ERHPSLAEDI HEEKQRRLRD MTFRANLKDD
DSRLSSSFRT RVGSLDDMMS FSPSQDKAGR KSKAARNAPF SPSIRPKDST VDLMFDMDDE
DPLGSPKSPL LNATTEVASP HQTDSTGPKL PWNELESRSV PDQELSLPFS NTPGLGIQNM
PENAPPSTKT WSSPALPSSK LDMREIMAQA SSTRISALSM SLSAQKSKEA AASKQSTPKL
SQKERKKQQQ QAMRLSMNQP RIELFDHKVD GKTSSPWQVA SSGPKMSLKD VLNQPIHSSP
PVHNKNLGPP IPSKPMTTRR TASPDTRFSG QNRSASNKNI TKMQPRSVGP SKAATPPPSS
KSMPIIPHSK SYTQPAGKAE PSLQLSMADI IGQQRREQEV VREAVAKRSL QEIQEEQAFQ
EWWDQESRRA QEEEAAKANN STSSLRRGGK TRGGSRGKSG GRERGGRGRG DDRAGRGRGR
GQEKTSNVMQ
//
