ID R1E594_BOTPV Unreviewed; 1559 AA.
AC R1E594;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative cytokinesis protein sepa protein {ECO:0000313|EMBL:EOD42863.1};
GN ORFNames=UCRNP2_10388 {ECO:0000313|EMBL:EOD42863.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD42863.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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DR EMBL; KB916932; EOD42863.1; -; Genomic_DNA.
DR RefSeq; XP_007589614.1; XM_007589552.1.
DR STRING; 1287680.R1E594; -.
DR KEGG; npa:UCRNP2_10388; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_001313_1_0_1; -.
DR OMA; NHYWKAR; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000013521; 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:UP000013521}.
FT DOMAIN 106..505
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 833..1254
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1268..1300
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..606
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 649..706
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 30..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1559 AA; 174125 MW; A020FA221F93EDCA CRC64;
MSDKTRQSSG GKSFFSRRKN KDDVPETPGL PSNLNPQSSR HQHRSSVNSI NGGSPSQRPI
SYLPEHIHSA GVLTSIPYDS VPPDGRSPVA VDFLPKDTSA AAAAARREPL PHHLNKGGVD
FHQLAEWQGE QRRRQNARQT QFSVDGMGIL GRADEEGSPE WYVRKVLDNS ITAKQLQSLS
VSLRTQPIGW VKAFVEAQGQ IALTNVLNKI NRRQGQGPAP SGSQSNTDKD LDREYDIVKC
LKALMNNKYG ADNALSYPQI VTSLAASLIS PRLNTRKLVS EVLTFLCHWA NGQGHEKVLQ
ALDQLKQAQG ENGRFDAWMR IVEVTVDGRG KMGSLVGASD EARSGGIGFE NLLMEYAVAS
LFLVNMIVDA PERDLQLRVH LRAQFTACGI KRILTKMEGF QYEVIDKQVE RYRTNEAIDY
EDLLERENSS MVDSIEGEVK DMNDPSQIVD AIQNKIHGTR AQDYFLSAMQ HLLLIRDNEG
EDRLRLFQLV DSMLSYVAMD RRLPDMDLKQ SLNFTVQSLL DKLYTDSEAR QARDEAIEAR
QIADAAVAER DEMRAQLELG ADGVVGKLQK QMEEQNALLE LRGRQIKQLK AELSDLQTVR
AKELQRNELE TRELYLMLRD AQDVAASAAA KKGKDGKPGQ ADPIIMQGIL DREKLLDKLE
MQLERSKTQA KLEGKVWQAV DPGDKLRELR EKMDGYEEEN NKADFSRADY TNSFLGTVNR
KPVPKRPTGD DTDAEYEDED MVVEKPRLVE LRRPKMSSTQ QGALLGEIAS KVKKLDDSDD
EADAEGDGVT TGPTHPSVDS ESPKTPADGE KFNARRGPGF LPQPGYAGTQ KVGLAVARPK
KKLKALHWDK VDTPQVTMWA SHAPTYEAKE EKYKELSKRG VLDEVEKLFL AKEIKQIGKK
QSAKNDKKQL ISNDLVKGFH VALSKFNQHS ADEVVRMIIH CDKPILENDV VIEFLQRTEL
CNIPENVSKQ MAPYAKDWTG PDAANATRES DPAELTREDQ IYLYTAYELH HYWKSRMRAL
ELTRTYEAEY DDIFTKLQEV VRVSDSLRDS VSLMNVLGLI LDIGNYMNDA NKQATGFKLS
SLARLGMVKD DKNESTFADL VERIVRNQYP EWEGFVDEIT GVIAAQKINV EQLTLDAKKY
IDNIKNVQGS LDSGNLSDPK KFHPEDRVSI IVQRCMKDAR RKAEAMADYL EDMKKTYDDI
LTFYGEDPTD ENARREFFAK LAVFVNEWRK SREKNIKWEE TRRRNEENMR RKAQQAPRSP
TADGPLLSPA STGAMDTLLE KLRAAAPQTR DQRDRRRRAR LKDRHQVRVA SGQKMPELPG
VSVDGEEGSS AGANGLLSPN SIASGDNSGD TGGEGDEREK GDKNGGNSEG EDIADRAAVM
LQGLRGDEVS EVPGRDDSIR IRRRRENAGN ERESRRRRRA RQGGSTADET IKEEPGSPRA
GDGDTDSRPG TGYSRPGTAH TNATTDSVAD SEQTKPDTEP DMEADGEKTA LPSPPPEKQD
EDEPMPDADA DVEASTKEAG KDDDRPESPL PTPVTIVSPP SPGREDKNDL PPVPPKDEE
//
