ID   C5DK76_LACTC            Unreviewed;      1976 AA.
AC   C5DK76;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=KLTH0F02376p {ECO:0000313|EMBL:CAR23877.1};
GN   OrderedLocusNames=KLTH0F02376g {ECO:0000313|EMBL:CAR23877.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR23877.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR23877.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00037935}.
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DR   EMBL; CU928170; CAR23877.1; -; Genomic_DNA.
DR   RefSeq; XP_002554314.1; XM_002554268.1.
DR   STRING; 559295.C5DK76; -.
DR   GeneID; 8292506; -.
DR   KEGG; lth:KLTH0F02376g; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_001313_1_0_1; -.
DR   InParanoid; C5DK76; -.
DR   OMA; NHYWKAR; -.
DR   OrthoDB; 1118745at2759; -.
DR   Proteomes; UP000002036; Chromosome F.
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:UP000002036}.
FT   DOMAIN          167..676
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          1332..1750
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1779..1809
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1751..1779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1791..1814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1836..1976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          703..773
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          899..926
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1005..1024
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1039
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1211..1225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1263
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1311
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1838..1879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1924..1943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1944..1960
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1961..1976
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1976 AA;  218910 MW;  B8B71221DD2DB3FA CRC64;
     MNRSSNSKSS KAPHNRSASS SSGNGGIFSN LKRLTTGSGN SSVSHNTQKL DISDISSPKK
     INLPDTGEFS HKPLSKQSTL NMASLSAYTD AVGAHNRSAS NASVGSPTKY SYSRRASQWS
     NNNSAVSGSK LSRQQTNQSM SSASIFSQGS FSNLSKFVGP DGAVRLERPR DPKEIEELFE
     EVLYKRNVYQ SLPASAQREL NNYDLEKKWL MVRQDLQSEV KKFMNSKNAS KSSTVVGGSS
     SAVPDSPSAS NFTSSTSPNG SFTGLSRPKI STSSVNTSEQ FYSSNLGTSS TTTLSQDPSH
     LSPDYYVRKI ICNDISAKRL NDLWVSLRTE QLDWVQGFLE AQGQVAIANV ILKTCYRESP
     DNLLGDEVLD KEFAYFKCLK TSLNLREGAD EAVMSNSARI IVSAIVEGLL SLRVATRRVA
     SELLISLSQW SLPHGFNHVM DALDQESRFC DNVHLQARLI TQSASKDPKK GSSIAPTPDG
     DGDRVMRKFE QWMLVVEYTL DGRGKMGSLV GASEDFRTSG GENAIMEYAY LTLLLINHLC
     QTPVDVKQRT VLRARLKNAG LPRILNKMKL LNYEKVDEQL ARFDDSTTDD FDALYSQEST
     GEGVDMKDPV SMTQNLWNLC KGTDAEQHLT SLLQNLLIST GELGSKNKDD PTQRTKQLKL
     IDALVSNVSM ASVDMQSSFN SAIQRLYDAM QTDEIARRAI LENRDWVKRY EEIKADRDNL
     KEKLSNAEGG LVGQLQDEVR QRDHILEKSQ RVNAQLQHEL DESKKKLILA KHEHEVELRK
     TLTAMNSNFE GSHNMRDEKG SENPRPLRPE RKLAIQKALQ AKLEKTSKEI NVESKRLGLS
     LEPNKRLKLL RSRMEDIENQ ARELEMTNFS DYQKDDIKEP EVSNEDDHKA VSESEEKAQQ
     ISALKLEELR KKLASLQQES NDISKFNVEG RFHEMFSGQK SLALDRLKKL ETDYKGFGIN
     FDPDSPLGQA LAGKSVSSDD KARTLDPKEA LNIVEEVSNI LSGLDSSKAA EKSNETPLRT
     ATSSDSSEDE MDDKNGDKIA ADSTLPTSSF LESLSQKYGG AQNSLSNRHS FAGGEINYPG
     SGYHRKSFMN RVKRTGAVPY LGELSGKIGS SSYIKPSEAE ENVGIGIMVD EKPLSRRVQE
     DAAGVSQLES NEEKPALSHD LDKNTTHSKP ITIGENLAAA KTAGKQQAHE DEGTTEGSST
     DKDSHEIASA TSAPPPPPPP PMDLFAKNGA PVKTDNPDPA VSDTKSAAAP PPPPPPPPIP
     PMLASSSSGS TSKAGAPPPP PPPPPPPPAL LSQSSNNGPP PPPPPPPPFG ASVSRNKSAT
     PSPMLPQSPS LFDRYPRPSK KLKQLHWEKI DDAEDSIWRD AKAEKFADDL YEKGVLSRLE
     KAFAAREIKS LASRKKKDSD KLSFLSRDVS QQFGINLHMY SSLSVEEVVS KILRCDRDFL
     STPSVIDFLS KQEIVEVSNN LARNFAPYTI DWEGVSSVEN AKPPEKDPTE LQRADRLYLE
     LFVNLQTYWS SRMRALKVIT TYEKDYSDLV HKLSMIDKAT CSIQQSENLR NVLDVILAVG
     NFMNDSSKQA QGFRLATLQR LTFIKDDKNS MTFLNYVEKI IRETYPEFND FLKELEPVVA
     AVKISIEQVA QDCREFSQSV INVERSVDIG NLSDPTKFHP SDRVLLKVLP TLPEARKKGD
     LLMDEMKLTL LEFDNLMRLF GEDAMDKFAR NSFFKKFADF LLEYKKAQVY NLKLEEEERA
     YERRKKLVED QLKRTRESES KNKGTTDAGG DSVRNEVNED RDVMDRLLEK LKNAGPAKSD
     PSSARKRAVA RKRLLQGSSS NSTILDNFDI EDSDGKSLVY SPDNNSSEVQ LNEADTSPTP
     ERRVRDSNAT SPASHDTGSS DLTDRARNLL IELRGPESPG VKMSAQHQRL SKLRARRKND
     SSSSGSENRL NFVGAGQAEN SDEQNEPEVL KSKPESANDD DNGEQSDSSD GEFLDA
//