ID G0WBV2_NAUDC Unreviewed; 972 AA.
AC G0WBV2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Protein BOI2 {ECO:0008006|Google:ProtNLM};
GN Name=NDAI0E04050 {ECO:0000313|EMBL:CCD25222.1};
GN OrderedLocusNames=NDAI_0E04050 {ECO:0000313|EMBL:CCD25222.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD25222.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD25222.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE580271; CCD25222.1; -; Genomic_DNA.
DR RefSeq; XP_003670465.1; XM_003670417.1.
DR AlphaFoldDB; G0WBV2; -.
DR STRING; 1071378.G0WBV2; -.
DR GeneID; 11498971; -.
DR KEGG; ndi:NDAI_0E04050; -.
DR eggNOG; ENOG502QPMX; Eukaryota.
DR HOGENOM; CLU_003845_0_0_1; -.
DR OMA; WLAALIK; -.
DR OrthoDB; 164125at2759; -.
DR Proteomes; UP000000689; Chromosome 5.
DR CDD; cd09535; SAM_BOI-like_fungal; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR PANTHER; PTHR12844:SF42; CONNECTOR ENHANCER OF KSR PROTEIN CNK; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..64
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 169..233
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 788..902
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 110078 MW; 5CA2AA8460CE5747 CRC64;
MSQILLVQNK YLKQMEDELD LKIGDKIKVI TDDGKYNDGW YLGENLKTKE KGLFPVQFTK
PYIANNQRNV HENANNTIDN TMNDIDKALR ELQMDSFLDI SNNNDFTTTI NTNANTPGLN
IIFNNNGRYS MNDAQFSNHS APSLNENTTL INRSTHNNVD MDLMNVLNWS PHHVMEYFLK
LGFDPKLIQN FGKHKISGKI LLQLELNHLK ELDINSFGSR FEIFKEIQYI KNFYQNTYCK
MKITKFTITS TTFDKKPINL SFTIIVIGNK KTTTYKEKIS SNDIITTSSS PYSRSPRRLQ
SDNNNFIKGI DRKKSGILDT YSYDSLPMIS KNFVAEGAFE SPGKAPKPPS YPSPIQLKQS
PKNNNSNKFR HSSIDLYSSS LPLANNNTDF IFPQSIELND NNNMISNKNL CTNSTLSSSN
TVDMTATSIL TEITPISDSA VINSKGTIPN SNTNTNTSTN KHHRKTSSTV TSSSLKRNSV
VYTGHKKNQS GGSFIELFNR ISTLSPGPMN IKTTTTFENN EIELPQRPAS TIYTSSPIHY
SHQPYYLRQS SSSNTRTRHH HSHHSRSTST AAATNSYSFP KSPYSNVTNL QYTNNNNSSS
NDNRRPHHTR SISNLEVSYS RNISSSSTTP KDRNNNERRQ QPQHKRNSSL LSFFTSFDHD
KTVNVDERKT SSSTTVTSAR QNSNNLNSLR TPTPLHQRNS SLITSPTKQR QQPSNKNVRS
LSSNNILPSP SKDSSTTLTS PNHLRSTSDA TNRINKSNHN NSKLKGKQQT SAFQEGRRTI
KVEDSIITSN CSGWMYKKSS NKLAIWKKRF FTLHGTRLSY FYDYNDTMER GLIDITSHQV
IPLNNESISL LKPSGKYCFK LIPPQPGSKK GLTFTQPRIH YFAVNSKDDM RSWLAALIKA
TIDIDTDVPV ITSVSIPTVS LNEAKRMLKE AREITLECER NRELNEEDED NMSWDSPPTP
KELIATEQSR II
//
