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Database: UniProt
Entry: A0A1E3QRF1_9ASCO
LinkDB: A0A1E3QRF1_9ASCO
Original site: A0A1E3QRF1_9ASCO 
ID   A0A1E3QRF1_9ASCO        Unreviewed;      1642 AA.
AC   A0A1E3QRF1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ODQ80275.1};
GN   ORFNames=BABINDRAFT_35416 {ECO:0000313|EMBL:ODQ80275.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ80275.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) 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; KV454430; ODQ80275.1; -; Genomic_DNA.
DR   RefSeq; XP_018985603.1; XM_019131713.1.
DR   STRING; 984486.A0A1E3QRF1; -.
DR   GeneID; 30149566; -.
DR   OrthoDB; 1118745at2759; -.
DR   Proteomes; UP000094336; 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:UP000094336}.
FT   DOMAIN          24..466
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          1011..1431
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1450..1482
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          882..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1427..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1488..1514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1576..1642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          487..557
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          606..658
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        948..996
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1592..1608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1609..1627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1628..1642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1642 AA;  185243 MW;  C66E5FABD8E3550A CRC64;
     MHSVSKKLVR HGTTQSLHSE FVLGKPSDPR EIEAMFRVLM EKRDFRSLPL VARKEMSHYS
     VDKKWMLIYQ DALTEYKKQE RQFLKGDDNI TPEFYVRKIM DKSITDTQLN NLWVSLRTEP
     VTWVKGFVAA QGEVALARVL GQLTNSHSSL LDTELDKELL MVKCFRSVLN VLEGAHRIYK
     AKTCMETITN SLFSPRMQTK KIVTDILCFY ANWGKHGGES FHRILTILSA TPQGFDKSGV
     LDETDDMGPV LEQMRPSETA LSLMSRRQLV MNQQSSMTRL ELWMRTVQKT LDGRGLMGSM
     VGASAELRGA QGENQLNEYC LSTMILIKSF TTNHKDIRVR THLRAQMRSF GLPKILEAFY
     RLEYDVLSNW IKEFENAMAD DYAVLSRHKN LQDQSVNLND PVSLIGKMWE NVKNTEVEGY
     FMSAIQHLFL AQLDPLVKPD NPELIRSFRI LDGVISGISM RSSLDDESTV NVAIQKLYST
     LQTDEVARKA VAELREAKRV ANEASAERDE LAKQVRMGGE GMVSKLSVQL QEQEMVLQRQ
     RKLNDEMTSE LEDLKRKRVL DRHQQELEMR EMFIMLNNSA TTTVSEKSNA ASGMSVSIET
     TNQDLITKLQ SRLANKKDEY RSETRRWGKP TVEPSSRLRA LRDKMDDIEQ QARELEMTDF
     QNYSGPAAMV TPSPKRTRKI KTVKEVEKKV PKKHVASPSP VKLGPARPWQ EDDLAKLSSL
     RKKLVSLQSE SNDILKYNQD LKDQELYNKQ KYLAMERLRE LEENFKNFNI DFTAPNRDSR
     LVDMDPKMMA KIHAELAEAE SLRATLESRL APVQHQVSDD DQPTNFLALE AKYVNGQKAT
     PVADVTNSQS QYQPATALSP GMLLNFLNEL SSKVSRKSAI DDTALPQGSA PPPLPNGTSS
     NIVPSVAAGV PLLLGAPPPP PFPPLLGTTN VPKLLPSFEI PSLPDMPSRS VSPSPPPPPP
     PPPPPPPPPL MSPLLMSPTM TGGPPPPPPP MPGMKSHPMT PVAISRSPSP FDNFPRPKRK
     LKQLHWEKFE NTENSFWEKH APSEALASEL QEKGVFDEIE NIFAAKEFRK FATKKGKDEK
     DKISFLARDI SQQFGINLHG FNTMSDQDLV LSVLNCDKRV FENVSILEFL GKDELTEIPN
     GVGRNLEPYS TDYTRGVEDG GTTKPDKDPA ELARADRVYL ELIYNLQHYW KSRIRALQTV
     ISFEKDYSDL VAKLRVVDIA CESVQNSSHL RGLFDIILMV GNYMNDSTKQ AQGFKLSTLQ
     RLTFMKDENN SITFLHYVEK IVRNKFPEMM AFMDELIVTV DAAKLSMVQI AADCRQYSQS
     IMNVQSLIDF GNLSDPTKLH PEDRVLKKVL PVLPEARRKG ELLTDQSKYT IAEFDKVMRF
     FGEEPEDEFA RNSFFRKFAN FLLDFKKVNK ENLQREEEER AYEARKKMLE GPKRSQARNG
     HLGGDSEPSE DVDGALMDTL LEKLKAVGPA KSDPLSARRR AIARKQLLEN TRKNQDDDGD
     TSQSLDIPDS DSSSLVDLLD EGMVSPASDM LTEEETTPDV GSRARNLLKE LRGPSTGPGP
     EDKLTPAQKL RMMKRKKELG ASTSDVSLRD LSDVVSDSDL RSSDHEQTAS DVDVTVTPGQ
     VDTTRETGSP LSEDEAHDIL EE
//
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