ID A0A165NJV6_9APHY Unreviewed; 1368 AA.
AC A0A165NJV6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAEQUDRAFT_729658 {ECO:0000313|EMBL:KZT67056.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67056.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT67056.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT67056.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429081; KZT67056.1; -; Genomic_DNA.
DR STRING; 1314783.A0A165NJV6; -.
DR OrthoDB; 1334285at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR47775; BUD SITE SELECTION PROTEIN 14; 1.
DR PANTHER; PTHR47775:SF1; BUD SITE SELECTION PROTEIN 14; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 69..130
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 629..761
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 21..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 149167 MW; E49265422E514C83 CRC64;
MQRPAQQDTF DLRDQILADD HNSQMMDHAY PSDEEHSVLE DDSDTDDRDE FMVDDDDGSS
SLSIPNESID FDLVYALHSF AATVEGQANV VKGDSLFLMD DSNSYWWLVR VLKTQEVGYI
PAENIETPFE RLARLNKHRN VDLASATHAE LEETRDRLRE NVSRGAPSPS PTPTPAGARS
SRHARGVSFT AAFSVHRYPP AVWNEEDEED EDVEWDDEGY EDEDPELAEE QEERERTMMT
EGSGGEGGIP GMEPDDDMSW EDGAVEQVQA KEREAAAAAA AAATAAAAAE AERVRQQLQQ
QEQELREQQQ RELQAQSLRK QPSREHMQAQ PSGVEVLPNS PTKTMDPAHV TETRKLTMTP
PVARVDDARS LTTDDRKRAR EEEEEVARKK ASSLAADRAK AGLGPTPGAR PASAGGKLRK
ERDSTDDESG KDKDKKKKSG GMFGGIFGRK KDKDKGKDKG VDSSSVASGG SDRDPSRESE
ESGKSLKDSA PAPEPASPVT AMARQQQQQQ QSGYRASPVR QQAQLQPQQQ TPQTPPQAAI
ASISQHASQL RQRDQQQQAL YQQYLNRSPS TPPEAQPSYG LQSASAVLQG SASFTSSISS
GSGLTTGGGR PRPGSLVLSP SGMDGLLPDL SVVRVFAGSN LQTEATFKTV LLNTSTTAQD
LVRQAIQRFR LPAGEDEKDY YLTIKQVEGS SADLLPHEKP LGVFESLVEA ALELPKVKRS
SVGSISSVAS NLSMHPAIKK LSMNDFTDDS AVKFYLNRRG GEELSIGGEG DETLLAESVQ
GEDPESPRSK SQYLTVTPTS PTNGVTLERF SSPSYRFPLQ LVIYPDDLPD DMVFDPQTEA
IIFKNTLRDR PQVGPSPGLQ QNLRKKVFVF PRNVTVAEVI ELGLERFGIL EGVVDGGDEI
EDKLTKRRSS SRVRYGLTVD VGGKERELTP SSKVIDAFPR PPTYRAMQFG NSKRRSADSA
QLLGSLDDVS PDDPVFILRR AVAYRATSRH RLSAPLDEIA LQRMQRNSAS SSSAGSDSTV
GPAEDTRSQT SQTSKQAIIA AQRAATRASQ RAILSAQANE SRGLDVALPS GAIVRSLRGE
VDNRMRYSYV EPDGETYDIS NIVEEEWRGE VGPLTRSDTT ADDLLHGVLA RGKDGLGAKL
DRVLSKIKHE KDAARGGSAQ SNSDVFTDVG AVRTQSPSTY STADEGASRA ATAIPTASGR
ASAAVQRVPS SLSRISSYRT ASPGESSDSH GKRSVTPNAN QRRGLLHERQ GSALSEASAH
RTTTPTSHHV ASAGRYQTPL PTPRLVLPRD DFGLAQMMAV IELRASQQKD VPESTPQDRV
DELLFGKPND MNALHPQIRD IYSGSFKQLE EMDQTLDQLL HLVIPSRQ
//
