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Database: UniProt
Entry: A0A0A2VXT4_BEABA
LinkDB: A0A0A2VXT4_BEABA
Original site: A0A0A2VXT4_BEABA 
ID   A0A0A2VXT4_BEABA        Unreviewed;      1717 AA.
AC   A0A0A2VXT4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Cytokinesis protein sepA {ECO:0000313|EMBL:KGQ05564.1};
GN   ORFNames=BBAD15_g9162 {ECO:0000313|EMBL:KGQ05564.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05564.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ05564.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05564.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00037935}.
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:KGQ05564.1}.
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DR   EMBL; ANFO01000936; KGQ05564.1; -; Genomic_DNA.
DR   STRING; 1245745.A0A0A2VXT4; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_001313_1_0_1; -.
DR   Proteomes; UP000030106; 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   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   DOMAIN          227..654
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          1089..1510
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1525..1557
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1590..1717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..951
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..982
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1050
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1492..1509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1594..1610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1637..1684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1717 AA;  190768 MW;  6B7AB1FAC23CA091 CRC64;
     MSDKTRQSSG GRSIFSRNKN KDKRNTDNDS YDALSTLSSR SSRHTRDSSA ISFDGLASPD
     PSMGMMPGAI TSIPYDATAP GSRSPIPVDY LPKADQVPVR REPLPHQLNK GHDFHQYPTF
     DPSVANAASH TSRLGPPATN VTMASTGRNT QYQLWGPSRG SMASTINGSH TSRYDSLLSP
     NNRVSDASVY SIQPSASSTS SYGIPHRESH RLTKFPGPGA HDTFHFPKPD DVNVIEQMFA
     HLMHRRGWHN LPDQARRQMM AYKPDKKWTL LHQDRLGEWQ DEQKRRMTAR VSQFAQPDVT
     TYSDEEGTPE WYVRRVMEDK LDGKGMGSLE VNLRTQQIGW VRRFVECQGQ VALVTLLLKI
     SRKIANAPAN ESSKVEKGLD REYDIIKCLK TLMNNKFGAD DALMQQKVLL ALGTSLVSPR
     LTTRKLVSEI LTFLCTWGDN GEGHYKVIQA LDEVKAQSGA NGRFDDWMQL VEATVDGRGK
     MGSMVGASDD IRTGGVGMEN LLMEYSVASI ILVNMMVDAP EKDLQLRVHI RAQFTACGIK
     RILSKMEAFQ YELLDKQIER FRTNEAIDYE DMLERENSSI KDSIEGEVKD LSDPVQIADA
     IQQRLQGSRT NDYFVSALQH LLLMRANDGE ERLRMFQLVD AMLSYVAMDR RLPNMDLKQS
     LNFTVQSLLD KLHTDSEARQ AQDEALESRQ IAEAAMAERD EMRSQLALGA DGLVAKLQKQ
     LDEQGRFIDA QRRQAEGLKA ELDSVQTLRA KEAQRNELET RELYLMLRDA QDIAASNAAK
     GAALNSPMGA SNGTSPEQMQ GILDRERLME RLQMQLERQK TQYKLEGRVW GEAAGPSDRL
     RALREEMEDD EADAASAAAP RDLTNSVLGS IHRQTRIPRK PVNTNGDVSD KETIEEASEM
     EEEDGVVYER PRIVEFKRPV IDAKQQAVLV DELGSKVKKY DGSDEEDEGV TTGPSHPSMD
     SSAPLTPADT DTLKTGSTTA VTPAGAAPPP LPPPPPPMPG QLAGPPPPPP PPPPPMPQQI
     PGAPPPPPMP GQIPGAPPPP PPPPPMPGMR LPAIGTDGTS MPPPPPPMPG PKTGGFLPQP
     TYSATPSVGL PVARPKKKLK ALHWEKVDAP ETSHWAAHTP SAEAREEKYI ELSRKGILDE
     VEKLFMAKEI KKIGAATGRK DDKKQIISAD LRKAYEIALA KFSQHSVEKI VQMIIHCDVE
     VLDNVVVMDF LQKDDLCNIP DNISKQMAPY SRDLTGPDAA TQARELDPAD LTRQDQIYLY
     TAFELHHYWK SRMRALALTR SFEAEYEEIY AKMHQVISVS ESLRDSVSLM NVLGLILDIG
     NYMNDANKQA RGFKLSSLSR LGMVKDDKNE SSLADLVERI VRSQYPAWEN FASEIGGVIP
     AQKMNVEQLE TDAKKYISNI RNVQTSLDSG NLSDPKKFHP EDRVSLIVQR CMKEARRKAE
     QMQLYLDEMI RTFKDIMIFY GEDPADENAR RDFFPKLANF LSEWKKSREK NIQLEETRKR
     NEASMKRKHA AQKAALAASE PGSASATSTG AMDSLLEKLR AAAPQARDQR DRRRRARLKD
     RHQVRVASGQ KIPDLNEIPE VEVGLKTSEQ TIEEEEGMTA STTGPAGLAS PDRTQSREGD
     DDVADRAAAL LQGMRGGDAE DSEKRESLRK ARRQTAEDER RMRRRRREKA SVSNAEDVGK
     PADMAEEDTS AAGQDESAQI SAAGPSENGE AGEEGKS
//
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