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Database: UniProt
Entry: A0A059BDB2_EUCGR
LinkDB: A0A059BDB2_EUCGR
Original site: A0A059BDB2_EUCGR 
ID   A0A059BDB2_EUCGR        Unreviewed;      1217 AA.
AC   A0A059BDB2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=AIG1-type G domain-containing protein {ECO:0000259|PROSITE:PS51720};
GN   ORFNames=EUGRSUZ_G01765 {ECO:0000313|EMBL:KCW64108.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW64108.1};
RN   [1] {ECO:0000313|EMBL:KCW64108.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW64108.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid,
CC       chloroplast outer membrane {ECO:0000256|ARBA:ARBA00023766}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00023766}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC       TOC159 subfamily. {ECO:0000256|ARBA:ARBA00023775}.
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DR   EMBL; KK198759; KCW64108.1; -; Genomic_DNA.
DR   RefSeq; XP_010066259.1; XM_010067957.2.
DR   RefSeq; XP_010066260.1; XM_010067958.2.
DR   AlphaFoldDB; A0A059BDB2; -.
DR   STRING; 71139.A0A059BDB2; -.
DR   EnsemblPlants; KCW64108; KCW64108; EUGRSUZ_G01765.
DR   GeneID; 104453412; -.
DR   Gramene; KCW64108; KCW64108; EUGRSUZ_G01765.
DR   KEGG; egr:104453412; -.
DR   eggNOG; ENOG502QR60; Eukaryota.
DR   InParanoid; A0A059BDB2; -.
DR   OMA; KECLIVP; -.
DR   OrthoDB; 4210585at2759; -.
DR   GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045036; P:protein targeting to chloroplast; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd01853; Toc34_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR006703; G_AIG1.
DR   InterPro; IPR045058; GIMA/IAN/Toc.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR024283; TOC159_MAD.
DR   InterPro; IPR005690; Toc86_159.
DR   NCBIfam; TIGR00993; 3a0901s04IAP86; 1.
DR   PANTHER; PTHR10903:SF135; GTP-BINDING PROTEIN A; 1.
DR   PANTHER; PTHR10903; GTPASE, IMAP FAMILY MEMBER-RELATED; 1.
DR   Pfam; PF04548; AIG1; 1.
DR   Pfam; PF11886; TOC159_MAD; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51720; G_AIG1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Plastid {ECO:0000256|ARBA:ARBA00022805};
KW   Plastid outer membrane {ECO:0000256|ARBA:ARBA00022805};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          583..812
FT                   /note="AIG1-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51720"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..865
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1217 AA;  132827 MW;  04EA21F291916641 CRC64;
     MEYAARDVDG PPRVEEEVNG EAGVLEERVE ERVGSAAGDD SKVVEGEEVF EEAVVDAHDD
     SSREEGLKVV SVAGVPGPDT DDVAGVDPSS EVSNENASAG HEDEKFEEAI GTPAKIENNE
     EIVKEVDVEE KVEGLVGGES IGGALVADGV DEGGTHEKVP VKEDDGLMSN GEDAVREIAE
     LHVDEEMHND VDGSSPTHGV ALKKLDNGTE DELENGNVSM EGLLDTEHKG TSSVEVLYAG
     DQHEELVDTD LATEGKLIID RELEIAPAAN HPDDLDEGNA TLATENKGDV KVETKSVTAS
     FESVYHDADG EVKKSFSSTD TEYQNDVNKE VKDATNGPDS SQGKISEQDP TSIDRPSSTS
     DEPVTHESGI LTTSEELKSE KDEQITAGTI EIDQEDVTSR TQQPVENVQE NHHKHTSAEK
     LEKKDSDSGG DGKKVIRENG IPAAKEVASS GRLMNHASVP ARPAGLGRAA PLLEPAPRVS
     QQSRVNGAVS HAQAQHIEES ANGESEDHDE TREQLQMIRV KFLRLAHRLG QTPHNVVVAQ
     VLYRLGLAEQ IRGRNGGRVG AFSFDRASAM AEQAEASGQE PLDFSCTIMV LGKTGVGKSA
     TINSIFDEVK FSTDAFDTGT KKVQDVVGTV QGIKVRIIDT PGLLPSLTDQ RQNEKILHSI
     KRFIKKTPPD IVLYLDRLDM QTRDLGDMPL LRTITEIFGP SIWFNAIVVL THAASAPPDG
     PNGTASSYDM FVTQRSHVVQ QAIRQAAGDM RLMNPVSLVE NHSACRTNRA GQRVLPNGQV
     WKPHLLLLSF ASKILAEANA LLKLQDSPPG KPFASRSRAP PLPFLLSTLL QPRPQPKLPE
     EQYGDDDGMD DDLDESSDSD DESEYDELPP FKRLTKAQVS KLTRAQKKAY FDELEYREKL
     FMKKQLKEER RRRRMMKKMA AAAKDQPSEY VENAEEESGG AASVPVPMPD LALPASFDSD
     NPTHRYRYLD NSTQWLVRPV LDTHGWDHDV GYEGINLERL FVVKDKIPIS FSGQVSKDKK
     DANVQMEVAS SLKHGEGKST SLGFDMQTVG KDLAYTVRSE TRFSNFRKNK ATAGLSFTLL
     NDALTAGLKV EDKLIVNKWL RLVMTGGAIT ARGDVAYGGS LDATLRDKDY PLGRSLFTLG
     LSVMDWHGDL AVGGNIQSQL PIGRFTNLIA RANLNNRGAG QVSLRVNSSE QLQIALLGLI
     PLFKRLLEFP QQWQLGQ
//
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