ID A0A1Y2D2Q0_9FUNG Unreviewed; 1185 AA.
AC A0A1Y2D2Q0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=FH2-domain-containing protein {ECO:0000313|EMBL:ORY53477.1};
GN ORFNames=BCR33DRAFT_756813 {ECO:0000313|EMBL:ORY53477.1};
OS Rhizoclosmatium globosum.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Rhizoclosmatium.
OX NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY53477.1, ECO:0000313|Proteomes:UP000193642};
RN [1] {ECO:0000313|EMBL:ORY53477.1, ECO:0000313|Proteomes:UP000193642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL800 {ECO:0000313|EMBL:ORY53477.1,
RC ECO:0000313|Proteomes:UP000193642};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY53477.1}.
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DR EMBL; MCGO01000001; ORY53477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2D2Q0; -.
DR STRING; 329046.A0A1Y2D2Q0; -.
DR OrthoDB; 1331062at2759; -.
DR Proteomes; UP000193642; Unassembled WGS sequence.
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 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; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR PANTHER; PTHR45691:SF6; PROTEIN DIAPHANOUS; 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|ARBA:ARBA00023054};
KW Reference proteome {ECO:0000313|Proteomes:UP000193642}.
FT DOMAIN 41..404
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 629..1030
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1054..1086
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..574
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 130183 MW; 4F50044A1E93F5CA CRC64;
MNRRVSALMV SSPSAAGLPR NNSGLPQSPS TASFTAAYDQ VPMPPLAAIT TMLELLMEDL
NLTEDKKQVL RLLSQERKWI MLQQHLGERY RDNAARDLQQ EISDIRKLNN PDRDLLTDLV
VSLRSRPIRW ISNFIDNGGL SILLSNLKGL GLENRHDEFE ELYIKCLKSL MNNKIGLSAV
LDNEGSMNII AMSLRSPALR TRSLVLEIFG AVCLIPGGHR CVLEGMESLA ELAALRFRFE
AVVSTLWLSC QGVSQQEKEL QVACMSFINA VICGGPGVNL EFRMHLRYEF LHLGLMQLID
KIGHIENELL QTQIDVWIAG LEADEEELFG RLGVAIDEDV NLDNTEELFD VVYENMKLSS
CVEPLHSVLR HVALLPPNPF QKMKYMFIID KVVQQICLQT TGGDAADPAA ALLDLDIRGL
VTEFGDPTKS RELEEKLRKA LEKSRKLEKD LDSAKGTTVA ADSAKKDEEI RNLSASLAAA
RRDIDTLNNA LKDKLLNAEG GAEVLAKVQA NWSSKTSAPP PPPAPPVSFA PPPPPPPMMG
GPPPPPPPMM GGPPPPPPPM MGGGPPPPPP PMMGGGKKLI FMKIPDHVPT IGPPPPPPPM
MGGPPPPPGF GPPPPPGAPV APGLQLPPSK PTNLSSKPLK ALNWTKIPPL KIKETVFATL
DDAEIHEQLK DSYIEFEDLF AAKELKEMKK DVTKGSSESI NTSGPKEITF LDTKRSQNTN
IMLKAIKMSP ATIAQAVESC DLTTLKQFII NELLKVVPTD DEIQSIKLYE NEVENLAVAE
RFFQAMSGIS SYEQKLRAMY FQSSYDELLD DVENMIGWLK RATWDVRDSK KFKELLAIIL
ALGNYMNSGQ RGGAYGFKLN TLLKLIDTKS SIQNRKHTLL HYLTEIMPKK FPEVIGFQEE
LSHVDDGAKV TIPQIRQIVV SIRDNLSSIK GLLSKLENDP TATKFYETLN KFYADAFATY
QDVEIRFKNA EKEFEAIVVL YGEDAKTTTP EEFFGIFSKF VAAYNQAKLD NELAAAKVIE
EEKKEAVKRT MEERRKKKRE ATTRVKETTS SGLDATDGPL DDLISAIRTG KAFGGFSDAP
ARKRAANSTS SAREGSPSER ISAADGRKGS VTLLAALGTQ DNLNRGAAKT RELATKASTS
TLNGSGGSLE SVRSRSPDKD LLAALVGGKK GRVRAESRSR SPLRE
//
