ID A0A2T4BIE3_9HYPO Unreviewed; 1018 AA.
AC A0A2T4BIE3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB69096.1};
GN ORFNames=BBK36DRAFT_1193140 {ECO:0000313|EMBL:PTB69096.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB69096.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ680209; PTB69096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BIE3; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000241546; 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; 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:UP000241546};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 13..266
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 958..1018
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 316..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 111889 MW; 9DFD5C0A72CC922C CRC64;
MPAAIADAPA VAMSFANNFW GKDDAGVGPL LERMINSKQT CDELKNFYGV RAAIEDEYSR
KLLNLSKKNL GSHETGTLKA SLDTVRGELE AMAKQHQNIA AQMKTELEEP LAAFAGGIKE
RRKIIQNTVE KLLKVKIQQT NHVNKTRDKY EQECLKIKGY LAQGHMVMGQ EERRNKAKLE
KTQISLATSN TEYENAVKVL EETTTRWNRE WKAAADKFQD LEEERLDFTK NSLWTFANIA
STVCVSDDAS CEKIRLSLES MDVETDIITF INERGTGQEI PEAPKYINFV RGDVHDDQSE
ASDDDNNYTV AQFPRSINPA FRSSSPQPST FESHHDPNSP LANDLAHRPP PKPTGREGAA
TPQKSPQKLL PAGRPSMDDP YRKQQPPSMD DRYRKQPPAV EDQYRRQQQP PAPDDQYRRQ
LPPAEEQQQQ PHGRQPPAAD DPYRRQQPGA DDQYRRPPPG AEDQFRRSQT GSQPPSPYDN
LHQSPKPTTP HDPYPKDGMT MLCRPGAPSA SSPQIQSARP SSRDSRSEYS DPTSISSQEP
QAGKMSPVKQ DAPTSSSPDK RMMKKKSGFF QNHSPFRRKS TKDLQAAAAA GSPQPGNRNT
WHPSQSQSQT STSPVRRPAP YGNSEPQTRN LLKERTASPE PIDANASLAL GVGQNVLPVT
TPDTNRQKPQ QPVQKAEPAD PIAAALAELK NVNVNKQASV RMSADHYHGI STPVPTNDAA
AMTRAFPAPG SHDAAAAARG TPPPSYQAQT QVTRLGVPPP AVTSRAMKEA TQKITGQARS
IFGDDGRRGS VSNPASPISR PGTRGNDASG SVSPGGNRGA SPQPQRRMSN DPRQMGRNSV
SPNPYIDHRR NGSQASLAQQ NQGYYRGASP HGSTRGSTRG ASPNPYQGDY SHSPSRPQSS
YGGSEMAMQL AGDDRYGSTR SRSSMRPGSR AMGLYDGGHQ RSKSVADPSR QYNRDGRPIL
HMARALYMYQ AAIPEELGFA KGDYLAVFRH QDDGWWEAEV HGGNGQVGLV PSNYLQPC
//
