ID A0A316UD48_9BASI Unreviewed; 990 AA.
AC A0A316UD48;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCV69DRAFT_280374 {ECO:0000313|EMBL:PWN22764.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN22764.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN22764.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN22764.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819322; PWN22764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UD48; -.
DR STRING; 1684307.A0A316UD48; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000245942; 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 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:UP000245942};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 22..275
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 926..990
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 319..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 105241 MW; AC03D26E90336051 CRC64;
MAAEGAEGSR RYAAEGELEE SPSFCNAFWG NGDAGYEAIN GRMKTASRTM EEIRALYKER
AEIEADYAKR LGKLAKSIVG KDETGSTRQA LEVVRGELDM TSRVHGDLSV MIKKDLEGAI
TEYQTKSQGA RKTAAASIEK LFKNKQAQET YVNKSRERYE QDCIKINGYT AQSSLVQGRD
LDKVTSKLDK AQSTVQANDK DYQNFVRALK DTTLRWNTEW KAYLDQCQDI EEERLDFIKS
NLWNYANAIS AVCVADDEGC ERIRVALENC ETPKDIAVFV QQRGTGAVIP DAPEYINYAR
GQHGSGRPSS QIANFVRQTT RPAQPPPPPP SQSYGGGSGT GSGRDGGSGG QSDVGNGVSY
QSVQGNGAPA AEALPPSQSQ YKPGAPPSGG VGLPGMGLPE QTGPSYQQLP QHQPPVATPP
KPERRMSAKN FLARTPSNRT GGASAYGGSA TSYNNSAAPQ SASLPPSVAP DADEDPIAKA
LASLRLKSGG KSPAPSHQGR PTQSSGPPPS TLSTSSHRYS QLPPGRASSP GPSLNGSVVV
PTSPSAAFMQ GPQRSHSPLP VEDIMSSYGQ SFPGERKSIS LSRRGSVSSA VSSTRVNVAA
TQPAQPPRGR SPAPSGEGFA GVGARGRSPS PQPYQGDFRH QATPSQDGRT PRHQAQSSIS
APQHPPQRAG TPLGISLDAS GSVTHDQMAQ EYMQRTGSVP PPQQPAAPAP YQQQAPSQQY
QQYQQQPAQG GGYGPPSSHQ RPSSVVHGQQ QHGGYSAPPP PSQAAPSQYH GQPSPGQHGY
QQSNAQYGQG APPFQRQDSS SAVGYNNYGQ QQGAAAPHSY GPGRGSTPGP SAGGETPASA
YMHQYQRQSN LASSTVGQQH EPQRWSQHGG GGSQPPPQQN GGYAAPAPVV QQPPPQQQQQ
APPPAQQQNQ QPAIAPTGQY SDTGKPILFY VKAMYDYTAT TEEEFSFTLG DIIAVTQTDP
DGWWQGELLD EARRKRGANT FPSNFTNLLT
//