ID A0A1L9VP92_ASPGL Unreviewed; 920 AA.
AC A0A1L9VP92;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPGLDRAFT_45703 {ECO:0000313|EMBL:OJJ85700.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ85700.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR EMBL; KV878894; OJJ85700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9VP92; -.
DR STRING; 1160497.A0A1L9VP92; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_45703; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR CDD; cd07651; F-BAR_PombeCdc15_like; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF7; CYTOKINESIS PROTEIN 2; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 13..266
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 860..920
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 351..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 100578 MW; 8E6210CD04DCEE66 CRC64;
MPGTLADGPS VSLSFANNFW GKDDAGVPPM LDRMHSAKVT CDELKNFYTL RAAIEDEYSR
KLLALCRKSL GAGETGSLRS SLDVVRTETE SIGKAHAAIA GQMKQELEEP LTAFAGGSKE
RRKIIQNGIE RLLKTKIQQT QLVNKTRDRY EQDCLRIKGY LAQGHMVMGQ EERKNKAKLE
KTQIQLASSS SEYEAAVKIL EDTTGRWNKE WKAACDKFQD LEEERLDFAK SSLWTYANIA
STVCVSDDAS CEKIRLALED CEVERDIVSF IKERGTGQEI PDPPKFINFC RGDINDTSSE
ASAEEDGYSV AQFQRTINPA FRSSSPQPST YESHHDPSAE IANMMGQIEA PPQTSREASV
TPQKPTQQPA PLDLRRGGQP PPNYDPNQHG EIAKVPHNAY PTDGMTMFCR TGPPSERSSG
TNSGYRPSSR DSQSELSNPT SMSSQEPPSA RQSSTKPTNG VALPGTSPDK QVQKKRSAFF
SNSPFRRKSR HDKDRGSGPS QPPSRGTWDS SSKHTSPVKA APQQQPQAQP QQQPPPQPQL
LAQSQPQPPA VMGPGDRAPS PEPVDPRANF QLNVGNNVFD VASPEKRKSL QQSKSADDDL
DPIARALADL KTSGKSPSSR VSADRYHGIA SPAPSTAGAP PAYNDPSMKR LDAPQPAHTS
AQMQRTTQKY IGQGQNMYRN RGSSPGPVSR NSVQSQDSAR ARSPTPRRSA SPNVSPRVDT
RMTQYNRGTS PSPSTHQSSS VRSRYSQSPS VATPPQRPGD AAYSPREYAP RSPNMAPRAV
SPQPQYRQQS RPSSAGGMEL QLSRGDMYGG GSGREAYSAR GRDTARPISY YGDVASTGRS
RSRTLAAAEP GRQFSRDGRP ILHFARAMYS YAAAIPEELG FTKGDVLSVL RLQDDGWWEA
EIASAPRRTG LVPSNYLQII
//
