ID G4V1G2_NEUT9 Unreviewed; 1121 AA.
AC G4V1G2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 03-MAY-2023, entry version 39.
DE RecName: Full=Formin GTPase-binding domain-containing protein {ECO:0000259|SMART:SM01140};
GN ORFNames=NEUTE2DRAFT_117146 {ECO:0000313|EMBL:EGZ67846.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ67846.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ67846.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL891269; EGZ67846.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V1G2; -.
DR STRING; 510952.G4V1G2; -.
DR eggNOG; ENOG502RXE8; Eukaryota.
DR HOGENOM; CLU_008022_0_0_1; -.
DR OMA; QTWATAK; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06371; Drf_GBD; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 482..791
FT /note="Formin GTPase-binding"
FT /evidence="ECO:0000259|SMART:SM01140"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 122998 MW; 4C5E403FC8FDFADB CRC64;
MPPAADLYGG VSAYRTGSGD GMRDRNYNNN NNNNNSDNSD NNNNNNNNND LPPFFPLQNQ
NQVQPQQRPK SSYLRQLMSH KRSNTVGAGQ VQLPPAVFST DFQKSSDSDH HHVMSSSAAS
VIDPDSPELL RPPNKINPDL VAQRHSCDMN LTGYQRHQFA AALCELRPNQ LDDQPPRSPE
KKSNPFTTIS LKSPFGLRDS SKASKNKGDQ SPTKPKKVKS AANIGQLLRP KSDKNLRQQE
QEEEENSRRR NKDKENRAPS AIDTSPPPPI YAQFARGSPF ALPPELNSST KPVPSPLDYR
NPFWDSGKPL PADPDRPGTG GTRSSIAESQ HLKSEAENRE RDRNNSRSKS RPKTFHQYFA
SNSQQDEKRT PSDSSTDTRY KQPQSDNQNQ SSPQEKQERS WKRQTWATAK TSDLAAGGSS
GSDRSSQRLN VKSMFSSSGN GGGSSSSAGG ERSKSGATAA AAAAATQSTS MERQQSAPPL
LQQHIDPKDI DKHLEAMLDR RNIPENQRYK MRNLNDTIKL EFIRQDWAEM QAKMVNQNAS
NTSLEKGGNA GSVNGGAGSE REDQQQQQQS SSSSRREDGN SKDKDNERTG RTKKKGFGLS
LGKGAASKAQ SSPTKSIGRH FRSKSNDSSM NERPSFGDVN GNSGGNGVGG FLGMKGGKSQ
QVPADFVAYL QKVHKPELVE VGKLHKLRLL LRNETVAWTE EFIKQGGMKE IVDLLHRIMA
VEWREEHEDA LLHENLLCLK ALCTTALALQ YLHTIHATLF PALLHLIFDP EKKGPSEFTT
RNIITSILLT YIECATPQER ITRAQTILQF LRDPETEEEK KPVNFILEMR RERPYRVWCK
EAVSVTKEVF WIFLHNMNIV SLPPADSSLS GSSGAGGGSS GINGEQKDTQ QQQLYQAGII
DPSALTRNDT ESGGEDSETA TPAQLAYMSR HFPQERPPVP AAPYVGGVEW DATNYLASHL
DLMNAIIACT GPTATERNAL RAQLRISGWE RCLGGSLRMC KEKFYGSVHD GLRTWVAAAA
EDGWDVRDVR FGPPPEGRGY SPMKKTPGKK PREEAPPKIE IPKLDFHIGG ADSPGIGVSP
GGLGVGMVAA SVANINGNGG GGGRSPMPVS PAVRAPDYWL S
//