ID A0A0D0E0X7_9AGAM Unreviewed; 1421 AA.
AC A0A0D0E0X7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
GN ORFNames=PAXRUDRAFT_10306 {ECO:0000313|EMBL:KIK97216.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK97216.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK97216.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK97216.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., 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:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
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; KN824946; KIK97216.1; -; Genomic_DNA.
DR STRING; 930991.A0A0D0E0X7; -.
DR HOGENOM; CLU_005863_0_0_1; -.
DR InParanoid; A0A0D0E0X7; -.
DR OrthoDB; 2787019at2759; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR024982; Rax2-like_C.
DR InterPro; IPR048266; Rax2-like_second.
DR InterPro; IPR048265; Rax2-like_third.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR31778; BUD SITE SELECTION PROTEIN RAX2; 1.
DR PANTHER; PTHR31778:SF2; BUD SITE SELECTION PROTEIN RAX2; 1.
DR Pfam; PF12768; Rax2; 1.
DR Pfam; PF20842; Rax2_2; 1.
DR Pfam; PF20843; Rax2_3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054538};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1421
FT /note="SH3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002209352"
FT TRANSMEM 1240..1268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1364..1421
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1322..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 147250 MW; A5B54D6F54231B43 CRC64;
MSPSLQTCPL VALLIISVAH FAFASLPLVD FDRMGQVGLA GAFAGLTLFD NSTTVAFDPS
TSSLLSRTPQ GALTPLGNTN PGGSISSGCL IKEVYYFGGS FSSIGNISAG YVASYSPSSG
TFSALGPNGP NGPISAVYCD LSSDNLWVGG HFSSPGASVA VWSTNSKSWS PPPFQGFTGA
HAQVMAITSN VFDTSLFFAG SFLTAFTGGT NNTNNTNNPN VPYSPGASPF SSSLVPIPLQ
GAEIVGAPSS TNPSFSNIQT ILCPAGPDGP GNTWLAADGN AALITVRAFA SISAYGIRLG
NTFQNGYGTT AFSATSIPDN TVQTLSYVDP STGNNITCTS SCPLSTDPSI LYQDFLFTTP
VTLTGVQITL SAWQGTAPGL HMMQLLSSGA FASAVGSQNA QSCFAPNPSN ITMTGSWTSK
NANTNIPATL QTVLVSTVPV GTPASQAPTF TWMPYVSASG QYDVNLIIPG CANFQDCALR
TSVRVTVFPG DGSQPYVSTV SQQVQNDAMV LVYSGPIVPS SSNFVTTVTM SLADQPTGDG
QNGEYELVAG DVELILTSAN VSSSSSTSLS NGSTGTGTQH GFGFFEWPLN SNTTIDATSV
VPNTSETSLD MVGIDLYNAL GAATAGSVVI SAVLQHPSGA IFLGGSFTLT TGSVNGASNI
VAYKDGSLFS LPNNGLNGAV TSFALYGDEL YIGGSFSDTQ NTSTQGKIMG IAMYNVKTNL
WSTLGAGVNG FVASIALANT QIQVAGNFTE IRAMSGPSTT VGGFATWDIK RGSWVNSGGF
VMGNLTFVGN GTSSSQGESQ FLAGNIQTVA EYGATGLVVL SNGDNNGPVV SPLGIQLGTA
TNSSVPAATA RKRSSHYRRG PAAWISNLKI STLFSRQSAT SPSTLPPSPP APAPAVLAGV
FWSNSSSSHE VAIIGGNFSF PTSSSAMSQA VAIYDPVSSS VTALAGAQVY GVVRSLYVDA
ESYLYVGGEF NLSDAKGNGF AIYDLIAQQW FTTVVQPLQA ISGSSVVVRS ITTSTYKPNA
VIVAGSFAQA GTVRCQGICL FDTTLNQWSA LGSNMQGSIS SVSYAGNNQE LLIAAGAITL
SDGTSANVAQ YSFANTTWTA IGNPTAIPGP VTAVEVNNGN LSSIFAAGRT ADGSLPFMVF
WNGVSWSDIG SGLQENSNIS QLLMVPLQNT HNSNSVIESD RMLMISGALS DTSFGLASSV
LFDGQTFIPY IASVSAQGTM GYISSLFYSI TSFSFSQQHF LATGVVILIS IAIAAGVVFL
LALVGILWTL LSRRDDKLVG YENDDEDDDS VQHRPSSLLE HINAATRTTI LGTQSSFNNF
SVEKEETARE GGATEPDPFG PDASNYLRAE TPSDAVVGTM AAEEVSRPAH VRYGFDGTGE
GELPLTVGIE IEVLDDRDNA WWYARNPQTG QEGVVPASYL Y
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