ID A0A395HUR1_ASPHC Unreviewed; 1015 AA.
AC A0A395HUR1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Polarized growth protein Boi2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO97DRAFT_406216 {ECO:0000313|EMBL:RAL11259.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL11259.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL11259.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL11259.1,
RC ECO:0000313|Proteomes:UP000248961};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ824289; RAL11259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HUR1; -.
DR STRING; 1450537.A0A395HUR1; -.
DR VEuPathDB; FungiDB:BO97DRAFT_406216; -.
DR OrthoDB; 164125at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd09535; SAM_BOI-like_fungal; 1.
DR CDD; cd11886; SH3_BOI; 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; IPR035551; Boi1/2_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037370; Pleckstrin.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12092:SF16; PH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12092; PLECKSTRIN; 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; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 11..75
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 244..310
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 731..886
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 74..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 110131 MW; BB0386086D2AE3D5 CRC64;
MALAAPPRNV VPGDLLLVVH DFDARGPDEL TLRRGEKIEL VELDEGFGDG WYLGKDLTTG
STGLFPGVYT TAAPKIRTRP STETAQQQPA AAHPTATDGT TLDAETVPQS GESTPQVSRH
TSISDLRATE VPRSPPQQQQ PQQRSASSPL PTAKMTLEIR QALEGQHRNG QDSPVMNETL
SVIDEHITDL STPRHSVADQ ELSVLNDSAS EYSSHIDHRR SYINGHETDE EEERQPQEAQ
VRRWSPAYAA RQLRQLGIED RHCDIFEEQE ISGDVLLDMN QDFLFMKEFD FGVMGRRLKT
WHKIRTFQDQ VKVGRKPQSP AVSPSQPRSS LAAGPSSPER TRSRTGQTAP LLPRIPTLRT
SNTPHPRLVS NTVSSSSSGS PIPPQTPPYM DHSRRPSAAS VREINHSRRH SSIDATTCYS
GVVDGSPGPT QRGSFDRAWS LSTGPQQRLP TRPGTSAGTS TGTSPAFETG FVPTGHHPNE
SNGSDAVAAT RDDLDRGYFS GPEGDTRKNR RLLQKRQSAT GSADARISPV PGEPLRVAKR
HSRISSMDSI REKAAQPIAP PNKSYTAPAP KRRLRSLSTR LVDRRAPQSA PVSAIEDRSG
GSSLFGPLFG GKSENDASRS SQQTAKIGGP KFFRAVGLRA MSDVVNKGAE TAAPPSPIRD
RDPAPARTGS TTPSTTKSSE RLSTDGSGKG TEGGLWPRSR PSVKTGPKSK KDTSAYMRGL
EKKSPQEQMT GCDYVGWMKK KSPNLITTWK PRLFVLRGRR LSYYYSEQDT EERGLIDITA
HRVLRADHDP MIALHATITG STGSPTAPAP SVQLADGTSS TDPIPTTEAP RVSKAGNEGP
FFFKLVPPKS GSSRTVQFTK PAVHYFQVDN VQEGRRWMAA LMKATIERDM DLPVETTNKQ
RTISLKEAQL MNQRPPALMA GAAAGVADGA PPEAMEKEVA SLKTPSESTE AETAAETPEA
SEAPEERGLM IKGLDFDGEP ARRDGNEEGS RLSNPLGEVD TGPASLLPES IRNSQ
//
