ID A0A1E1L4P8_9HELO Unreviewed; 1744 AA.
AC A0A1E1L4P8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Probable cytokinesis protein SepA {ECO:0000313|EMBL:CZT05459.1};
GN ORFNames=RCO7_08485 {ECO:0000313|EMBL:CZT05459.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT05459.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZT05459.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZT05459.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-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; FJUW01000035; CZT05459.1; -; Genomic_DNA.
DR STRING; 914237.A0A1E1L4P8; -.
DR InParanoid; A0A1E1L4P8; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000178129; Unassembled WGS sequence.
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; SSF81995; beta-sandwich domain of Sec23/24; 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:UP000178129}.
FT DOMAIN 281..710
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1110..1531
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1546..1578
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1709
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1744 AA; 193920 MW; E79DA7D028D6CFBC CRC64;
MSSADSKSRQ SSGGKSFFSR SSKKDRRHAS DEGSLGAELV KTSTTGSRSS RHARDSSVAS
IERPNSPGAD LRGLNQMAGV ITSIPYESVM ADGKSPIPVD YLPRSDQLPV GREPLPHHLN
KKGVDYHQYP AFDPATTSHG SSHPSGPRPP PLTGNITMAS TGDRRTQLQQ WGPGRASNAS
TLNGTHNSRY DSYSTAPTSA YARTSFDHSS LDSSTDRSSV FSSGSSSRTA LPASQSTSSF
NSNLSPSHPS SRESHRITKF PNHHMSGSPS GSFGGEGSGI NKPTDDRVIE EQFLALMQKR
GWHNLPDQAR RQMMAYPAAK KWTLVHQDRL TELQGEQKRR TNARNTGQYG REMEMLANAE
EEGTPEWFVR KVMDNSISAK QLQSLAVSLR TQPIGWVKTF VECQGQVALT NVLGKINRRQ
AQGPAPADGS TSDRDLDREY DIVKCLKALM NNKFGADDAL HHQQVIVALA TSLISPRLTT
RKLVSEVLTF LCHWADGQGH FKVIQAMDHV KNQQGENGRF DAWMRVVEVT VDGRGKMGSL
VGASEEVRSG GIGMENLLME YAVATLFLIN MVVDAPERDL QLRVHIRAQF TACGIKRILT
KMEGFQYDVI DKQIERFRTN EAIDYEDLLE RENSSIKDNV EGEVKDLSDP TQIVDAIMQK
VQGSRTQDYF VSALQHLLLI RDNDGEERLR MFQLVDSMLS YVAMDRRLPD MDLKQSLNFT
VQSLLDKLHT DSEARQALDE ALESRQIADS AMAERDEMKS QIELGADGMV AKLQKQLEEQ
AQIIEIQRRQ IEGLKSDLES VQGLRAKEAQ RNELETRELY LMLRDAQDIA ASNAAKGVGG
AALGESDPSQ MKGILDREKL MDRLEMQIER QKTQYKLEGR VWGDAAGPSD RLRALREEMD
GDSRAGAGAT PPRDFTNSML GSVSRQTRIP RKPVNSQGQD MLFEDDDDIA DDGEEGIVFE
KPRVVEMRRP KKAPGYLEEM NSKVKRYDAS DDEDGDGVTT GPSHPSLESD SPRTPSDETL
PKTEGFDGPP PPPPPPPPMP GLTPGFNGPP PPPPPPPPPP GSMGGPPPPP PPPPPPMLGG
MMPPPPPPMP GKKSGGFLNQ SSYNSAPTLG LPVARPKKKL KALHWEKVDT TMTTHWASHA
PTAAEKEEKY AELSRKGVLD EVEKLFLAKE IKQIGMGASK KTDKKQIISS DLMRTFQISL
AKFSSYSVER IVQMVIHCDK EVLDNAVVMD FLQKEDMCNV PENTAKLMAP YSKDWTGPDA
NKDNREMDPT ELTREDQIYL QTAYELHHYW KSRMRALALT RTFEAEYDEV SAKLKQVVAV
SESLRDSVSL MNVLGLILDI GNYMNDSNKQ ASGFKLSSLA RLGMVKDDKN ESTFADLVER
IVRTQYPEWE GFTDDIGGVV TSQKLNVEQL QQDARRYVDN IKNVQMSLDS GNLSDPKKFH
PQDRVSQIVQ RSMKDARRKA EQMQLYLEDM IRTYDDIMVF YGEDPADENA RRDFFSKLAI
FVTEWKKSRE KNVVLEATRK RNEASMKRKH AQLKITGPAD GSAPPSPVST GAMDSLLEKL
RAAAPQARDQ RDRRRRARLQ NRYQVRVASG QHIPDPDEIP EIEDALKSPE SVSTEGLMSP
EIGGVPKEGS EDDVAERAAL LLQGMRGTDG ANDAEETERR DSVRRARRRD NAEEERKARR
KRREKASSFS EAAEGDALPE EEDTPQTVEA IEEDEGKEKV PTPTTVVRPP SPEGSRTKPI
ELDE
//