ID A5DSH8_LODEL Unreviewed; 1940 AA.
AC A5DSH8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK42136.1};
GN ORFNames=LELG_00314 {ECO:0000313|EMBL:EDK42136.1};
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:EDK42136.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK42136.1, 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; EDK42136.1; -; Genomic_DNA.
DR RefSeq; XP_001527794.1; XM_001527744.1.
DR STRING; 379508.A5DSH8; -.
DR GeneID; 5235845; -.
DR KEGG; lel:LELG_00314; -.
DR VEuPathDB; FungiDB:LELG_00314; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_001313_1_0_1; -.
DR InParanoid; A5DSH8; -.
DR OMA; TPSIKMK; -.
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; 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; 2.
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:UP000001996}.
FT DOMAIN 274..710
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1319..1735
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1759..1791
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1799..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 781..826
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1055..1093
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..961
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1854..1883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1940 AA; 220362 MW; 9D2B0CE41DF98F81 CRC64;
MSSNSKASHG SSNRKSTNSI FSVIRNRDSQ RDKDRERDRE REAHTRNESQ SDFSSSETAS
ILSGGTQYSS NSRRLTHNNH LIQSFQQQPG QPFQEQLYHL PLQILLLLHT NPYQTQTHTS
PYTSTSTINN HHHPHEQQQQ QQQQSPYARK SSVYSISTLG SGKPSSIKQH PVNPYDTTAT
GAGLSRQSTN FTSPNASTSL SRKSTNVSIN SLGRSTKNPY TDTSSSYPAA SVSSLQDSNG
STNHNNNYYN NNNANNNNNI IDNYNNNNNN NFPLEKPSPL EIDRMFKNLL EKLNIKGMAP
QSARELLNSD TERKWMLLVQ NHKAEQERQV RHANEKETHT PKLYAQLLIL KSITKQQLNE
LWVQLRSEPI NWLRVFVYDC QGDTLLATTL LKLHEDMAQR GVSNIEDERF DEEHYIMRCL
KCVLNQKLGA ERIRTDVDIF VNAVCGCLLS PRLLTRKLAT DALTFIITYN LKDSGRYHKV
LRAIDSLNDK VRFDFEEYDE NNSNKKRHLI RKPPPSLGSK RFEVWLSLVE RTVDAKGKFN
SNVGEREEVR SQYIGTTSKG NHFPDYCIAT LLLISIIVQY GADFRVRIHL RAQLQAAGLN
RLLAKFQDLR LESLLNILDQ YLDLARADEE EMKFTQNIDE NLNFNDPVEL MRSLWENIRD
SEAQDHFLST IQHLYLAQSE RKNDQRELGH SLRVLDNIVQ NLSSVQTSDE NTAINIAINR
LTSSMSTDDQ YRRALEEVKY YRKVAEEATA ERDEISKQLS MGADGLITSL TNDLKERDLV
ISRFRRINEE TREEMNELKT KYMKEKQELE LEMRELLILL NSSELETSKS RKGKTTTVSL
STSNAELADR LKRQIHRRRA ESRLDNKQLG TQVEPLKRLR ALRDQMGDIE NMARELEMTE
FENYTGEIAD EAKSLSEPEI AESASESEVE EGNKEEEEEE NEEEEEKEEE EEEEEEEEKL
EELYLPPTPP SPENKRPVRS DDLIKLDNLR KKLSNLQSES NDIMKFNSSS ILNKQKYLAM
ERLRELEQNF KDFNIDFSLS DEDDQFAFTE LAQVDDNMKD KTKEVLSEVE RLRNELRKQL
AAAQKTAQQK SSKTQKSTLK RDSIMKKIED KYVKGQVKTE SMGTPVSGSV SKEYKKANRT
TTIGGMDPLF LKELSNKVKM TEAISTSSDV NEEEGSVSSS KGQVHDKAVE EPNLSAGITS
ASSVQEKSLP SIPPPPPPPP APPLPSFSNG KVTGGVASLL PPPPPPPLPP LHYGSQNSLA
PGPPPPPPPP PPPPPGLSVG SNIAGPPPPP PPPPPFPASA SKTRKSPFGT PESLSSPQFE
HVPRPKRKLK QLHWEKIDHN EATSSFWKNQ STSTLASDLM SKGVFDEIEI IFAAKEIKKL
ATKKKEDIDK ISFLSRDVAQ QFSINLHAFN QLSDEEFVAK VLRCDKDIIT NHSVLEFFSK
DEITEITNSA ARNFEPYSTD YKVEDITKPE KDPSELKRPD RIFLELMYNL QHYWKSRNRA
LTIVAHYEKD YEDLVSKLRA IDESVDSIKN SNSLRGVFEI ILTVGNYMND TSKQAKGFKL
NSLQRLSFMK DEKNSMTFLH YVEKLIRTQY PELQQFLDDL AKCNDIAKFS IESIYNDCKD
YARAVKNIQT SIDIGNLSDI SKFHPLDRVL KVVLPTLPRA SHKAQLLIDQ ANFTIKQFDD
LMIYFGEDPS DQFVKNSFVS KFTNFMREYK RVQAENVKRE EEIRIYEQRR KLLETPKKVS
AELGERRNDN ASENDEDNEN GDEGVMDSLL EKLKAAGPAR GEPTSARKKA MLRRQILENQ
RKFANSSTSP SKDGRDSEIS EDDLTLLQES ESTDSVDSKQ TEVRSSRAKN LLQELRGANE
DDSEESVSLA QKYRQERLKK KLTIDSSSSS SSSSAAATTT ATTNMASANI DATTPTTTDN
HNNGDKSDND ANTDATKILD
//
