ID A5DRR5_LODEL Unreviewed; 996 AA.
AC A5DRR5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=GBD/FH3 domain-containing protein {ECO:0000259|PROSITE:PS51232};
GN ORFNames=LELG_00051 {ECO:0000313|EMBL:EDK41873.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK41873.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK41873.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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DR EMBL; CH981524; EDK41873.1; -; Genomic_DNA.
DR RefSeq; XP_001527531.1; XM_001527481.1.
DR AlphaFoldDB; A5DRR5; -.
DR STRING; 379508.A5DRR5; -.
DR KEGG; lel:LELG_00051; -.
DR VEuPathDB; FungiDB:LELG_00051; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_300538_0_0_1; -.
DR InParanoid; A5DRR5; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000001996; 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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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 SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SUPFAM; SSF48371; ARM repeat; 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:UP000001996}.
FT DOMAIN 32..511
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 630..726
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..909
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 111167 MW; A043747D2E6D4805 CRC64;
MVKSALQTTQ ISYMPSEPSP GVSNVAITDY RDKRPDDKVV NYLFEKLLSV RNFSAHAIDS
LRKQTIDRKW ELVVREHETN ASFDMSNLPK LSSLLEASST GHLQLRQQSY QIPRGNESQS
TFNSSSEDAV SLLHRDNSNS DQSNTFKKLN QIAKLENDKH KDGTPEWYVS RIMAGKLTVK
DLKKLEKRLN IENITTEQSA TWIQSFLIAQ GESALAVILA KIGKKTIKSN EEFDKEYLLV
KCLLHIINFE SGEEMGKVVL NDKDVLRNKS ILVKALIHAI ISPRLTTRIL VTQVLATLLH
YCHSEVYHVI VHQFRSLQTD SHYNNSNNNN KSSKEHGHNR IGLRFQTWIA TFEATLSKGT
WSSKFSANLR NYITITLVLI NYIVNLAGSV KNRMSVRHEL NDAHILKVFE KIKKFGDEKI
TNELECYEYY AIEDNELLLE EKKRLNRKGL PQLPTAVNAE ELFENISLSE YDSLLEEASS
GSYSSTTLDL PYVENIAVQV VQQLLHQQLP QQHLQQQPQQ HLQQLPQQHL QQLQLLLPLR
QPSGYDGTEV PETLEPPKSL NRRLGDVFTK LVELEDTTPP NTSNYATKNI IALMECMLDQ
LTTGTLTKNG EISSVTIQRL IDGLSSEMIA RTAVAESRKL EREVQRLKEI NIHLSKTLKE
TKLNSKQVQE KLQLQLQLQE QLKEQVNIPI EYTYQAEEIA QQKKQISLLQ RQVKTLEEDR
SRIFRNKTVN TSLDDLSSNR LGKDTLNKSG VANIESLANE FKVGELSDRS GTIQRPPTPP
GLFMKKTNSR SSKNSASSST QGSPVRSNQR LNAGSPLILE HAFFAHIRNE RKNPLNKEGN
LPVNASSSKS TSNNGLSQLE LLSNVDSNEQ QATVQTNSTD ALRTTLTPSS ALSFVPPAPP
APPIPGFMKV SSSPPSSSHP QPLGNATPIG NQASPPQPQP PSPPPPPPPP PPSLIPFGAS
PPPPPPPPPP PPPPPPHSPS SPSSTSSSAT FTTAYF
//
