ID A0A0C9YN99_9AGAR Unreviewed; 729 AA.
AC A0A0C9YN99;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=BAR-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=K443DRAFT_671339 {ECO:0000313|EMBL:KIK09438.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK09438.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK09438.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK09438.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KN838538; KIK09438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YN99; -.
DR STRING; 1095629.A0A0C9YN99; -.
DR HOGENOM; CLU_008936_0_0_1; -.
DR OrthoDB; 1331687at2759; -.
DR Proteomes; UP000054477; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0051666; P:actin cortical patch localization; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR CDD; cd07593; BAR_MUG137_fungi; 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; IPR004148; BAR_dom.
DR InterPro; IPR046982; BIN3/RVS161-like.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR47174; BRIDGING INTEGRATOR 3; 1.
DR PANTHER; PTHR47174:SF3; BRIDGING INTEGRATOR 3; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..245
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 428..486
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 80583 MW; A43BCB56619A6661 CRC64;
MASKQIGKFR QWAGEVISSK EKTTVAEEFR ELKRDIDLRK DGMQRLTVAS EAYHHYLSKK
KANEALGEAE KLLPIDTLGI VMIHHGEDFG DESPYGASLV KLGRAHCKVA TLQEAFALTF
KDTFLASIER FKEDIKEYEA LRKKLDSRRL SYDAAISKLE KVSKGNKKEK EKREAEDEMD
RAKQRYEETA EDLRAHMHAI QENEFSQLKD LGSFLDLEIN FVQQYFDVLR EVKSEWPEKS
STSYLQAFRS ARNISPSPSR LNRQSVKVSP DLSSEDERYG KRRRSGSTAS KTPSNSRPAS
RLSRKRTNST SASTMMTPDL QKDSAKPDSS ADKEKEKNRR MSVAGWASSA VESVTSRGKK
NKDTEAFSAL GDDDEPSTGS LGESSSLKKS SSFRSLGRQP PSRNKSIENV PGVSPKVTPR
ILRPPSVQER KVVRALYDFS GSSDELSFKA GSEILVLNEV LDDWWLGELE GRSGLFPTTY
VETLSISAST PQRAATTTSK NSNGLSLLVP SSAFGPGSGG EEEYPSDMDD EFGTHPMMVQ
RSPFYGGFND ALSVTSSQAE EEQEGHPLQL DRLLPAPQQK QAQTALDDED YYVPKPKAKS
ILHSLDTAQQ PLLSRSISEA PPDTTSGRTL FNQATGPSIK KVPPPPPPRR HTTIAVSSVG
PPIPERRLPP PFASKTSVTT TSTPASSISG HGYDTSPFES ASEDSGCGKF RQNPFKPKGM
CSNCLEFHD
//
