ID A0A3A2ZUW1_9EURO Unreviewed; 841 AA.
AC A0A3A2ZUW1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=GTPase binding protein Rid1 {ECO:0000313|EMBL:RJE23074.1};
GN ORFNames=PHISCL_04603 {ECO:0000313|EMBL:RJE23074.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE23074.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJE23074.1}.
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DR EMBL; MVGC01000137; RJE23074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A2ZUW1; -.
DR Proteomes; UP000266188; 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:UP000266188}.
FT DOMAIN 327..607
FT /note="Formin GTPase-binding"
FT /evidence="ECO:0000259|SMART:SM01140"
FT REGION 29..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 94480 MW; C0A7EB4E68B2F5A3 CRC64;
MTPITHAPNI FEDVPRSPTK PSALRAFLSS KAHKRNPTAD DAIVPHAIHR DAPSGGPSMY
RGEGANSNPP QFPLGERAAN RDAADGLLPL TKSTTKDGKH TLHKKTKSAV SLKSLKNYME
RKDTKSDESP EDDSGELKPK KAKSANSLTA ILKRSQRGRK GGDEKEVRDK ENRSPTDLSD
NAPDSSWAYR PSHSEEQARP RSYMDKRRTF EEEVSLYTPK GYSPSHQRNF YDYHQPSLTK
RSGLKPRPKS DCLSGDRSVK DYIAPQRTPS DNGPVDVQRT AHRRPRGWSR PGSYSEEQRQ
ESNPKAMSRV QAAISVFNAK SQEADLQKRL DSKDLESEFE KLLDARNIPH NMRDKMRSLD
TNIKADFIQK DRTDTMPHSA NGSMSTNDSS RRGRGKEQKE DRPREGKSRS RSRSRGFSFT
KGSSPTKKHR PESGTFHRRP KSIELAQPIN LSRVLSPSTS TTSLSGAAAV DTAADPSDFV
HYLREIQKPE MVDVGKLHKL RILLRNETVS WVDDFLEEGG MDEVVQLLYR IMKIEWRGEH
EDTLLHETLL CLKALCTTSA ALKRLTEIES DLFPALLRML FDEDKKGPSE FTTRGLIINL
MFTQLSTAPS PEVAATRARR ILSYLSDPTP PEENQPLSFI ANIYQSRPYR VWCKEVTNVS
KEVFWIFLHH LNVIRVVSSD KPTFLERHFP VPRPPVPAAP YVGGVEWDAT NYLAAHLDLM
NGIIACLPTS DERNHLRTEL RASGFEKVMG GSLRTCKEKF YSSIHDCLRT WVAAAVEDGW
PHIFVREGPP KPEPGSPSKS PIKRGSPKKG AVNDNPPKLE LGLGLDIPEP QSKGDVFGDW
L
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