ID A0A0C3CYN4_HEBCY Unreviewed; 1618 AA.
AC A0A0C3CYN4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M413DRAFT_15198 {ECO:0000313|EMBL:KIM48956.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM48956.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM48956.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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DR EMBL; KN831768; KIM48956.1; -; Genomic_DNA.
DR STRING; 686832.A0A0C3CYN4; -.
DR HOGENOM; CLU_000718_1_0_1; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000053424; 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:UP000053424}.
FT DOMAIN 204..603
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1077..1478
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1492..1521
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 625..652
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 686..713
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1452..1486
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 182107 MW; 77D0C5DBAC1E66D1 CRC64;
MDTLFGRKKA RPRQSSVSVQ DLNERSVPYD KLSGPARSPV SVTTSNQGIL GISAPNTNPA
LTASGTELNK FTMQRSKRER DRVYEQHLHQ DSSTTSVSTA DSSTLYDDPG LSNKSLPPPH
PQTARIRRSE ASSSPRSQNT DFGQFPHTSA YATVRPISGT TSRSENHRNS KYAASLTSSE
PGSHHSHLSH FYHRHQSSET FQFSRPETDE EIEVLFENVK RTRDLGDIPN LPTEQKWQMV
YNDEHIRWRE ERQREEQSRR QNEIGQPAAI IAESPEWYVK KFLDKTITAK QAGSLLVSLR
SKELSWFHKF ISIQGTSVLA QTLQHISRKG PSRREADTNL EYEVVKCLRH ILNNAAAANE
ALTHTSIVTQ IASSLNSPHL PTRKSLLDLL TFLAYWNEGE AHPLVITALE VLSSSNNEAG
GCYEYWFKSM EQSLSGRGKM GSLVGASEEV KRTGGVDSSL NEYALSNLVL IHGVLAFVDD
FDLRLHHRSQ MESAGLKRIL ELCANFGVSS IDKLINKLQT LFADDEKKLR ERLDQEILRD
LTNPQDVFNA IYSKTQGTRA RDYFLSMMQH LLLIREEGQP MVHYYQLLDS IVTDVVLDKK
LAGAEHRMGY SVERIIAQFN EADRYQAAED EAAEARALAV RLKLEKEALE EEISQGHEGL
IGALKTQLAS MEEKLSVSRE TTSRLHGQLE HQKATYEDKI QQLEAQIMEL FRMLKEVGKG
VETILDGGNG MDRKALVQTL ERNFQRRKTI SILEGKEGHN RRKGRPSGGN AIEEEDEEDT
DATPGKSGLR KPNAAGVVGK KLFHHLYGQE KIVVDERGRV SQFMDADEAD AREQVQQQLA
AGVKLYSPQI GIVSGSRSIR GSPRRGDGFK LNGLLAPKTE DTFSNDSADL SRSSSPANDD
ESEYDRSSRS GFTNRTEDTV FTSVSSDSSG ENPRVPAPGS LAEQLNKHYL SRTKSTSSQN
GSPVNPPALA MLSKETTSEG LPPPPPPPPP PPPPPPPPPP PPPPPPGFNT LIPSTSGPPL
PPPPPPPPPP PGMKSMIPTA MFGAPPPPPP PSNPSSARSS ARTSLLGSHL NFMNLRKEIA
ITPSTKMKQL QWDKLPQQQV NKTLWKEDEP QKEQEMLQKL QMDGVWMEME EDFKAKQLVI
NLMARQKRAE LRSVLDDKIR RRVEILIQLF RRLEPEEIAR KIQQFDPETC TQVFLSELRP
LLPTPEQVGK LNVYRNADPA ELAELHPSDR LMVQLIKIDR LGPRIEGMLY KVTFEDTWTL
LDEGARKLSE AGRDLLDAKY FKELLSLILL IGNYMNGTGI KGGAFGFRVS SINKLVDTKS
VNNTTLLHFL EKTVNRHFPE MEEFLEELEK PAEAYRVNLQ DIRKGLAELR DGLSRIHEEL
LEHFADLDEN DRYGKQMWSF YNKSNVQLED LVDDVKNADS TFTDAIRYYG EEDKNMSSSE
FYGIFKTFVI SYKKCKQENQ TSAEEKRALE RRKLAIEETR ANRQRELETS APDEDDNALE
RLIENLRNGD TITRKARRRR PGAEKDSTMT GNLTLDLLRP ADDPTMVARD MLARLQSDGF
VAPPSPTMST HQRRRRRRTE RALQNEKEIP NSPLAMEILD IETDELIATE EDFSTLPP
//
