ID W7LVX6_GIBM7 Unreviewed; 1745 AA.
AC W7LVX6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cytokinesis protein {ECO:0000313|EMBL:EWG43378.1};
GN ORFNames=FVEG_04885 {ECO:0000313|EMBL:EWG43378.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG43378.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG43378.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7600 {ECO:0000313|EMBL:EWG43378.1}, and M3125 / FGSC 7600
RC {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2] {ECO:0000313|EMBL:EWG43378.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=7600 {ECO:0000313|EMBL:EWG43378.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2013) 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; DS022246; EWG43378.1; -; Genomic_DNA.
DR EMBL; DS022246; EWG43379.1; -; Genomic_DNA.
DR RefSeq; XP_018749569.1; XM_018892802.1.
DR RefSeq; XP_018749570.1; XM_018892803.1.
DR STRING; 334819.W7LVX6; -.
DR GeneID; 30062918; -.
DR KEGG; fvr:FVEG_04885; -.
DR VEuPathDB; FungiDB:FVEG_04885; -.
DR eggNOG; KOG1922; Eukaryota.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000009096; Chromosome 4.
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; 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:UP000009096}.
FT DOMAIN 241..669
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1093..1515
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1535..1565
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 729..763
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1384..1457
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1074
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1745 AA; 195633 MW; 270B8D655CFDF846 CRC64;
MSDKTRQSSG GRSLFSRSKH KDKRLTEESR YPADDAASFR SSRHKRESSA ISLDRPESSD
GGINQMAGVI TSIPYDAVGG GSRSPIPVEY LPKGEQMPVR REPLPHHLNK NGLDFHQYPS
WDGTSAQSGA HSPGRQPLGY GYGNVTMAST GRQTQYQQWG PPRGSSSHSN NPPNPRYDSY
MSSNARGSAD NLSIQSAMPS ASSQSSYAAS QHSNRDSHRF TKFPSGPPPG QSDPQGGFYF
PKPDDDNVVE QMFLQLMQKR GWHNLPEQAR RQMMAYPAQK KWTLIYQDRL TEWQGEQKRR
QTARPNQYTA TPDITTYSDE EGTPEWYVRR VMEDRLDTKG MGSLEVNLRT QQIGWVKRFV
ECQGQVALMT LLLKINRRTA QGPVQDNTRI DKNLDREYDI IKCVKALMNN KFGADDALIH
QKVMVALASS LISPRLTTRK LVSEIITFLC TWGENAEGHL KVIQALDEVK TASGENGRFD
AWMRLVEVTI DGRGKMGSLV GASEELRTGG IGMENLLMEY AVATLMLVNM IIDSPERDLE
LRIHIRAQFT ACGIKRILTK MEEFQYELLD KQIERFRTNE AIDYEDMLER ENSSIKDDVE
GEVKDLTDPV QIADAIQQRL HGTKTNDYFI SALQHLMLIR ANDGEERLRM FQLVDSMLSY
VAMDRRLPNM DLKQSLNFTV QSLLDKLHTD SEARQAQDEA LESRQIAEAA MAERDETKAQ
LELGADGLVA KLQKQLDEQS RFIDAQRRQA DGLKAELDSM QTMRAKEAQR YELETRELYL
MLRDAQDVAA SKAIKSAAAA SASSKVAGPE DPARMQGILD RERLMERLQM QIERQKTQYK
LEGRVWGDAV GPSDRLRALR EEMDDRPGTP PGGGTPPRDF TNSVLGSIHR NTKIPRKPLK
RRSDGEVIDE DDETEGEDGV IFEKPRIVEM KRPTIDPKQQ AGLLGEIGSK VKKFDASDSE
DDTTGPSHPS METSSPITPP GDSETPKIEV TGAAPPPPPP PPPPPMPGQI PGAPPPPPPP
PPPPMPGQLP GAPPPPPPLP GMLMPGGGPP PPPPPPLPGA GGMPPPPPPP LPGAMSGHFL
ARQPAFGAAP SIGLPVVRPK KKLKALHWEK VDAPETSHWA AHTPSAEARE EKYQELSKKG
ILDEVEKLFM AKEIKKIGIG NSSKKDDKKQ IISSDLRKAY EIAFAKFSQY SVEKIVQMII
HCDPEILDNA VVMDFLQKDD LCNIPDNTVK QMAPYSKDWT GPDAKSQDRE LDPSELTRQD
QLYLYTAFEL HHYWKSRMRA LALTRSFEQE YEEINEKIRQ VVTVSESLRD SVSLMNVLGL
ILDIGNYMND ANKQARGFKL SSLARLGMVK DDKNESTLAD LVERIVRNQY PEWETFADDI
NGVMTAQKIN IEQLQADAKK YIDNIRNIQM SLDSGNLSDP KQFHPQDRVS QIVQRIMKEA
RRKSEQMELY LEEMMKTYKD IMVFYGEDPA DDGARRDFFA KLALFVGEWK KSRDKNVQVE
ETRKRNEASM KRKHTAQLKL TNANANAEAG PTSPSNTGAM DSLLEKLRAA APQARDQRDR
RRRARLKDRH QVRVASGQKI PDLDEIPEVE AGLKNKEEPT EDESKMLSPG LSSPREGEDD
VADRAAALLQ GMRGGDGADD NDPERRETLR KARRQTAEEE RRLRRRRRER ATTNQSEENP
DEQKEEPREE PKVEEGEAAK EPPKEEETPI EDDVPTPRAA TTSDGAPEEE QGEKAQAQAQ
AQAQA
//
