ID A0A165FUX1_XYLHT Unreviewed; 1886 AA.
AC A0A165FUX1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FH2-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=L228DRAFT_269789 {ECO:0000313|EMBL:KZF21410.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF21410.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF21410.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF21410.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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DR EMBL; KV407461; KZF21410.1; -; Genomic_DNA.
DR RefSeq; XP_018186965.1; XM_018335316.1.
DR STRING; 1328760.A0A165FUX1; -.
DR GeneID; 28900453; -.
DR InParanoid; A0A165FUX1; -.
DR OMA; NHYWKAR; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProt.
DR Gene3D; 6.10.30.50; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR47102; PROTEIN BNI1; 1.
DR PANTHER; PTHR47102:SF2; PROTEIN BNI1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT DOMAIN 294..727
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1200..1621
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1640..1670
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 758..828
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1490..1517
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1886 AA; 207985 MW; 5E6362A38B7BB7A7 CRC64;
MPATTPPADS KSRQGSAGKS FFSRKLHKDK SSFHRSPSDD NHLLPELPGR GSAHGSQSSR
YSDRSSMMSI DRPQSFGGDP SGLAMHTGVI TSIPYESVAS DAKSPIPVEY LPRTEHQIPR
KEPQPHHLNT RGADFHQYPA FSPSQAANKH SQPTGPRPPP HASNSGGTSS PYSADKAAAQ
QYSRSGSVAS GLNGFSHGNS YSYSTANSST NPRTSFDQAS VYSSISSATR GSTLFSSNNS
SQTAIAQSPG HQTPPRSSHG YPNQQQPALY ANSPSSSSSF NTNAAFSPDG FHLHPPSDVR
VIEEQFLALM NKRGWQNMPE QAKRQMLAYP ADKKWTLVYQ DRLTEWQGEK RRRQNARQTL
TGPDGQNGPL ARADEEGSPE WYVRKVMNDT ITSQELASLS VSLRTQPIGW VKSFVEAQGQ
VALTNILSKI SRRQTHGGAA TTRSGNIEQD LDREYDILKC IKAVMNNQYG TEDALTHQQI
IVALATSLTS ARLTARRIVS EILTFLSHCN GGDGHVKVLQ AMDYVKNMQG ETGRFDAWMR
LVEVTIDGRG KMGSLVGASD EVRSGGIGME NLLMEYAVAT LLLVNMLVDA PEGDRNLPLR
CHIRAQFTSC GIKRILTKME SFHYETIDKQ IERYRTNEAI DYEDLLEREN SSMKDSIEGE
LKDLNDPAQI VDAIMSKVNG TRAQDYFVSS MQHLLLIREN GGEDRLRMFQ LVDAMLSYVA
MDRRLPDMDL KQSLNFTVQS LLDKLHTDSE ARQALDEAVE ARQIADSAIA ERDEMKAQVE
LGADGVVGKL QKQIEEQAAI INLQQRQNDG LKAELADLQQ IRAQELQRNE LETRELYLML
RDAQDVASSV ARKAGKDGLA QNDPVHMQGI LDRERLMDRL EMQLERAKTQ CQLEGKIWQQ
VGPSDKLREL REKMDGDFER QPELDQSPQQ MLEGSALGSV RRTRTVNRGS RRAAADAFAG
ELSSVIGRRN AEEEDDEDVY YEKPRLVELT RPKVHGKHPS TATAEIASQL QRFDGSEGEE
PEDEGDGVTT GPSHPSAGSE APKTPVDEIP SADEKFGQPA PPPPPPLPTL PGNGTAAPPP
PPPLPSLPGA ASAIPPAPPL PGADAIPPPP PLPGTTAIPP PPPPPPLPGT SAIPPPPPPP
PLPGALPGGP PPPPPPPLPG MPMPPPPPPP PPMPGAPPLP GARKGGFLPQ PAFTSTPSVG
LAVARPKKKL KALHWEKVDT PQITMWASHA PTHEEKEKKY LELSKRGVLD EVEKLFLAKE
VKKIGGKSSK KDDKKQIISN DLRKQYQISM SKFSQFSVDE VIRMIIHCDK DVLDNNVVMD
FLQKNDLCNI PDNTAKAMAP YSKDWTGPDA ANTSREQDPA ELTREDQIYL QTAFELHHYW
KSRMRALALT RSFEAEYDEV SEKLREVVRV SESLRDSVSL MNVLGLILDI GNYMNDSNKQ
ATGFKLSSLA RLGMVKDDKN ESTFADLVER IVRTQYPEWE GFLDDISGVV AAQKLNVEQL
QTDAKKYIEN IKNVQSSLDS GNLSDPKKFH PQDRVSQVVQ RSMKDARRKA EQMQLFLEEM
IRSYDDIMTF YGEDNTDENA RRDFFAKLAL FVVEWKKSRE KNVTLEETRR RNEISMRRKN
ANAAALLNAS TGTETATTAH NTGAMDTLLE KLRAAAPQAR DQRDRRRRAR LKDRHQVRIA
SGQTLPELPE IKNSSYESEG NQQQQQQQNQ QQDEDGEPNG ELHVPEPGHT TLDGISEGED
IADRAANLLQ GLRGDGEGEN ESMGRDSSLR VRRRRDAEDE RRQRRKRRAA GAHMSTASTA
TTISTLGEEQ LPNPDDSMSV EGSSLIEGTS VVEDAADSQR EAPEDEAEGS DDKAAPLPPA
SPTTPKTPTT IVSPPSPEQP TSRENQ
//
