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Database: UniProt
Entry: A0A1E1L4P8_9HELO
LinkDB: A0A1E1L4P8_9HELO
Original site: A0A1E1L4P8_9HELO 
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
//
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