ID A0A319A3M6_ASPLB Unreviewed; 568 AA.
AC A0A319A3M6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Protein kinase activator Bem1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO96DRAFT_481190 {ECO:0000313|EMBL:PYH53714.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH53714.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH53714.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH53714.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ821361; PYH53714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319A3M6; -.
DR OrthoDB; 1368965at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd05992; PB1; 1.
DR CDD; cd06890; PX_Bem1p; 1.
DR CDD; cd11878; SH3_Bem1p_1; 1.
DR CDD; cd11879; SH3_Bem1p_2; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR035550; Bem1/Scd2_PX.
DR InterPro; IPR035548; Bem1/Scd2_SH3_1.
DR InterPro; IPR035549; Bem1/Scd2_SH3_2.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15706:SF2; BUD EMERGENCE PROTEIN 1; 1.
DR PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 9..74
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 128..190
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 290..410
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 491..568
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT REGION 232..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 63150 MW; 369C15DAB92B7F2A CRC64;
MKSAIAILPP KKVIKALYDY QPEPGNSQEL AFSKGDFFHV ISREDDLDWY EACNPLIPSA
RGLVPVSFFE VIGKNERHSA GSVDHHKKKE PHDSGFSDRA AFPGTDFISN SSRNSFQPRM
SQLGKGSSAM VYGIVQYDFQ AERPDELDAK AGEAIIVIAQ SNQEWFVAKP IGRLGGPGLI
PVSFLELRDM QTGQAVTDPL EAVRRAGVPK VEEWKKMTAE YKNSSITLGK IDSAGGSSMQ
SVTSSMDKMS IGRQSQMSQN GQSQGYHTRN ASKGSLVQQV SHQSQQSYHQ SLMAPIAASI
PRYCFDNDKY WYIIEAKMED GRCWELARYY HDFYDFQIAL LTQFEEEAGN RGKPRTLPYM
PGPVTHVTDA ISNGRRQNLD EYIKKLLAMP PHISRCQLVR QLFAPRAGDF EIDPNAFGEE
TRFSGGSHHS SANEPSRSVS RQSSQAPIAV HTERNSHQRG QPSLSLSNGG PPPMNRQPSS
LTQVSTSSGG AMKVKVFFQD DLIAIRVPND ISLQQLKEKL MDRLKIQDEI MVQYKDEPSG
TYVDLATDSD LDTAIQRNSK LTLYVGLA
//
