ID A0A165BIT5_EXIGL Unreviewed; 1641 AA.
AC A0A165BIT5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Actin-binding FH2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=EXIGLDRAFT_845323 {ECO:0000313|EMBL:KZV80728.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV80728.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV80728.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV80728.1,
RC ECO:0000313|Proteomes:UP000077266};
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 -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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DR EMBL; KV426456; KZV80728.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165BIT5; -.
DR InParanoid; A0A165BIT5; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000077266; 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; 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; 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:UP000077266}.
FT DOMAIN 230..633
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1082..1486
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 655..685
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 719..753
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..826
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 181268 MW; 6CCFE7E24359C105 CRC64;
MDSLFRKKNR PRQSSISNGD NLGDKSVPYD KIQSSGRAPS TVGSSRSGLQ ISAPITNPNL
TAEGTDLNVN QLHKKRAERE REYAQYAIDD AAAAARPASP GPSLASSRRS GARSPSPPPA
MPIISTQPSS PSIPRTPRSA NLSDFGGGGH YSQSRTSTHS TASSANSRHL SSRSAPDSRR
GGGTPRPSAQ SIAAPSIRQS VASLAASAYA HTTHHRNSSV DAGAGEFYFP RPQSDEEIEA
LFEHVRNTRD LGPLDTKLTL DQKWLIVYND EQLRWREDKK RLEEETYSRT VARETGGNVQ
GMYSKDSPEW YLKKFMDNTI TPKHVASLCV SLRTMPIGWL EAFLSLQGVS VLGRHLNSIN
RKGPMRREND IQLEYEILKC FRIISNNKAG ADDIAAHQQA IQYIACSFST PHLPSRRLIA
DMLCYFAYEN PGPDAVLLAL EALSSANNET GRFDYWFKSL EATLTGRGKM GSKVGASEDL
KRNGGLESSL NEYAFMNLTL VNGLVVTNDD FEMRVHIRSQ MEAAGIRSIL EKCKEFRFPA
LDQQILQYEN SAEEDQRRLL ERFDQDILRD MQDPYDVYRA IISSVEGTKA FAYFLSAMQH
LLLIREEGEA RVRYYQLIDT LITSVVLDNK QGFSGGLFNT VGVSVARLVA QFGEQEQAQL
AIEEAAQARA ELQRVQVEKD ALADEVAQGE GGLVGTLKAK LANTEDKLKV SRQTSDVLTA
RLEDQKRTYE EQIHQLELQI AELFKMLREA RGLDALEALN VSGMSRQELV STLEKQMERK
KTISILEGRL GRKQKKLAKL KAGMTADQLQ DDDDDDDSED DEDDEETTAD GKKKTKKRTK
SGVPRTSQFM DAEEERVRAH IEQSLTAGAE LMSPPRNNHL FGARSMRNSP RKATTRKLAE
GKAALPPRFL DGLDPRERRI VTDPGPGAGA DTDVGSESSM SRISEAGTDG TPATSISGVS
DLARARTLMG EQLANKLASM GKNASDGEMA GADGAAPPPP PPPPPPPPPG LMGPPPPPPP
PPPPPPPGYI PPIPTSMSGI PPPPPPPPPG PRSVPGSMPG SARSSVATTV ANNFSSAFGS
RKDVPIVAST KMKQLQWDKL PQQAVGRTLW NEEEPDKEKD WMQKLQMDGV WREMEDDFRA
KEFVKNLLAK KKAAELKSVL DPQTKKHVEI IMQRVKQLSP EEIATKILEY DPDVCSEVFL
DGLKTLLPTP DQVAKLASYK TSTIEELSEL HVADRLMVAL IKIERLGPRI KGMTYRAKFE
ETAQMLEEDT KKLIAAGDAL QNCPHFKELL SLILLIGNYM NGTGNKGGAF GFRVSSINKL
ADTKSSNSTT LVHFLERTVA KHFPEMESFL DELAAPADAY RINLQDVRKR FGELREGLAA
IRQELDTHFA DLSALPPEDR YAKKMWRFAG ECGDRLDDIN DSLTLADSSF TEVLRYYGED
ERNLTSSEFY GIFKTFVATY KNCKKQNQTV AEERAQAEKR RQLQEDRRAA HAKQDTATTD
PAETDVLDNL VKKLLAGEGV SRKHKRHRPT PSQRNLTPLT LPAEGSETAE VARNMLMALK
DDGFQLFTPT SPRVPSTRRS RLRSEIRSED EGDEPMTPRS GDAPSDNEDP TVRLHSRQSS
FAREGSGSPA AESFAANETQ E
//
