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Database: UniProt
Entry: A0A0C2YH15_HEBCY
LinkDB: A0A0C2YH15_HEBCY
Original site: A0A0C2YH15_HEBCY 
ID   A0A0C2YH15_HEBCY        Unreviewed;      1090 AA.
AC   A0A0C2YH15;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M413DRAFT_19503 {ECO:0000313|EMBL:KIM40392.1};
OS   Hebeloma cylindrosporum h7.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM40392.1, ECO:0000313|Proteomes:UP000053424};
RN   [1] {ECO:0000313|EMBL:KIM40392.1, ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RA   Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., 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:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
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.
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DR   EMBL; KN831783; KIM40392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2YH15; -.
DR   STRING; 686832.A0A0C2YH15; -.
DR   HOGENOM; CLU_004415_0_0_1; -.
DR   OrthoDB; 2025446at2759; -.
DR   Proteomes; UP000053424; 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:UP000053424};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          28..281
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          1027..1090
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          306..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..827
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..904
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  120112 MW;  86A139A1A958E681 CRC64;
     MSARRQSSTT SLSKFARTHS PILQNRSLDF CNSFWGFGDG GVDVLFARMR GAARTMEELK
     AFWKERASIE EEYAKRLAKL AKMTLGRDEI GDLRKSLDAV RTETERQAGF HLDLAQQFRS
     EFEVPTTAFH ARQLHHKKTY QAGIEKEFKT KQTQESYVNK AREKYEQDCV RINSFTAQAS
     LVQGKDLEKI NLKLERTQQT VQTNEREFSN FSKALHETVM KWEQDWKSFC DSCQDMEEDR
     MDFMKDNLWH YANAVSTVCV ADDASCESIR VALEQMEAEK DMENFVREYG TGNQIPDPPA
     FVNYQAPDAI PSSSARPTSR AAQFNRSTAR EVPVRQYSMP PEEEPMVNTA GIGAGGGGAA
     ASRRNDPYAS ESVSDVSRQP TRNSTQAQTI PYTNGTSHHH HAGPSTSPSN AASSPNQAIR
     RQSTLSSPLA QAQQQQLQRV LQDPYAEPID PNAETYIKVG YHAYKVDLSN DPQAQQHPGP
     SSSIRQTTNN QLTASPTKQN GSVDPLMKQL EELQNAVSTS GSVRRNTIQK PKQSSIIEQQ
     KSGHVSSLSA ASRAAATGAA GSSSLSLPTQ GSSLAVGGPS PGQQHQQRRS PSPARDYRNS
     AESVVGAHPS VSRPTSPNPP TAAFMVPNSG QPAGAEVVQD VLADYHQSLP GERKSISRSN
     STARGRAPSV SAVSIGGGGS GAPSPAGHIQ GQNLSRPPSQ LGHAGIGAHG SRSNSPQPVS
     RGPSPAPSHG RNSFIQPPVQ VGQALARTPS PNTVGIALDP SGRVLHDEMA QRYQQQQQHP
     PPQQYHQQQQ QQQRAPPPLQ TQHPAYNAPP PMQQQQMAPP PPQQPVQQQQ QQPHRRNSYI
     SPNTIAPPIA AQAYGVSPPP PAMYHTPSPQ PSYIQQQQQQ PPAPVYNPPP PVQYQPPPQQ
     QQQPRYSAPP QQQPVQVSYG SVNGLQRNPT SATATSGSYY GNHTPPQQQQ MQPVQQSQQQ
     MLAVQQQQQQ QQQQQQQRMV QQTQQSQQQQ QQQQQRAYQQ QLYHDPTPVR RSPSPQPPPQ
     STDDGNTVLF YVKALYDYTA TIEEEFDFQA GDIIAVTATP EDGWWSGELL DEARRQKGRN
     VFPSNFVCLF
//
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