ID A0A165QI76_9AGAM Unreviewed; 952 AA.
AC A0A165QI76;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEOLEDRAFT_1119526 {ECO:0000313|EMBL:KZT22466.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT22466.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT22466.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT22466.1,
RC ECO:0000313|Proteomes:UP000076761};
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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV425595; KZT22466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QI76; -.
DR STRING; 1314782.A0A165QI76; -.
DR InParanoid; A0A165QI76; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000076761; 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; NOSTRIN, ISOFORM H; 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 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:UP000076761};
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 889..952
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 289..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 104014 MW; 9FD2860B950240B3 CRC64;
MAARRQASTT SLAKFARANE TDLSQPSLDF CNAFWGAGDG GVDVLFARMR GAARTMEELR
SFWKERAAIE EDYAKRLAKL TKLPLGRDEI GELRNSLDTL RLETDKQAGF HLQMGQQIRT
DLEGQTATFC ARQAHHRKTF QSAIEKSFKI KQAQESHVNK AREKYEADCM RINGYTAQST
LVQGKDLEKI HQKLERVQQT VQANERDFAN FARALQETAR QWELDWKAFC DSCQDMEEER
MDFMKDNVWA YANAVSTVCV HDDESCEKIR LALEQFEPEK DMENFVRDYG TGASIPEPPQ
FVNYTDPDAV MNSSSRPTNH SARFTRTTQR RAQQQAPPPA PPEDEEPPVN TAGRGAGGGR
GPSPMDGMNN STHALARNQT HSRASTREEP TTNGQPNVRR GDTMSFRPPN EPHAEPIDPT
SKTMIKIGDN AYEVDPAQDP QQQGRASRRV PAQNGAPKPG VGDDSDPLAR AMTELRNQAG
TVRRNPTRKD TDSSRPGTSR GPTSSQGLAS SSNVNLVAPQ SSGSANGGSQ NHGNRWRNSA
EIVVGSYPLS SSPRPASPNP PTAAFMSPNR PPSTVGDSNL PVEDVLKGYQ QSFPGERKSL
SRQNSRRSSV SGMSQNDQGQ RIGRPVSREG HAGIGAHGRS PSPGLPISRS ASPSLMNVAP
PVNDSRNSLT SPPRQVVRAG SSASSTRGPQ RAPSPNPVGI ALDPSGRVAM DSMADRYAAE
QQRRQQQQQQ QQPAYQNPPQ ANQIRRTSTY VSPTGPPNGQ QLSYGAPPPV GPPPPAPAPA
PAPAPVGYQP PQQSYGHPSQ QYYPPPPPHV HQPQPHMGYG NTPADLQRGA SLSYGGPPSH
LQQPGYAGYG YQPHHSGPIA RTPSPQAPQM VPISQAPPPT NQYTEEGKPV LFYVKALFDY
SATIEEEFDF QAGDIIAVTA TPEDGWWSGE LLDEARRQPG RHIFPSNFVC LF
//