ID A0A067FZU8_CITSI Unreviewed; 1109 AA.
AC A0A067FZU8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=AIG1-type G domain-containing protein {ECO:0000259|PROSITE:PS51720};
GN ORFNames=CISIN_1g036930mg {ECO:0000313|EMBL:KDO71655.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO71655.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO71655.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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; KK784888; KDO71655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067FZU8; -.
DR STRING; 2711.A0A067FZU8; -.
DR PaxDb; 2711-XP_006489085-1; -.
DR eggNOG; ENOG502SMC8; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
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 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:SF127; AIG1-TYPE G DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 468..702
FT /note="AIG1-type G"
FT /evidence="ECO:0000259|PROSITE:PS51720"
FT REGION 89..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 120885 MW; 74C50561643577B7 CRC64;
MESEGEEDEP FSESMSPEKF VDSSVSSKFI GVGDVSVSSS AESIAVNDFA EDSVSAELVE
DKGDGVTAES HNESFVDRKG DVFKFVENSI EQGPELRNSV PEKIESEDQD RTQEHSAELS
HFEELMVEVE GVNAEEPSDS QNNPRSSFDD SGGVSLDQDS GNDNLESKTE PEIDSEVHLY
DPLVFISAES ADGTMKGKKI QALDSHSLEP NSSLQNGDLL GTVEGDGLED AESSASRSLK
SETETDDVIE RAEGRQKGSL SNEDIEELIF GSSRTTRQIT HGLEERLASS SITESEDFQG
HSQRIDGEIV TESDDEPDAK MSGEGNELFD SATLIALLKS ATGAASDGGG LPSNRADGSN
VFTYQHHAGS GSLFPSLSPG PSINLEGDVT KDKLSDEEKR KIEKIQILRV KFLRLVQRLG
HSFDDSVVAQ VLYRLALALG GHSSQAVSIE AAKRVAEQHE IEDKDDMDFS LNILVLGKTG
VGKSATINSI FGEEKSTINA FEPATSSVKV IAGLVHGVKI RIFDTPGLRS PAIGRTVNKK
TLASIRKSIK KFPPDVVLYV DRLDTHTRDH NDLPLLKSLT SSLGSSVWQN AILCLTHAAS
EPPDGPSGLP LSYEVFVGQQ SHAIQQRISQ AIGDPHLMNL NMMHPVSLVE NHQSCQKNRI
GEIVLPNGQS WRPQLLLLCF SLKILSEANS VSKSQGPAPK KFFGFRRPAP LSYFLSSLLQ
SHTHPKLSAD QGGDGVESDV ELVDFSGSDL EDEDEYDQLP PFKPLRKSQV AKLSKEQRKA
YFEEYDYRVQ LLQKKQWKEE VKRLREMKKK GYRSNNDDER EDGNLEDDPP ATVPAMLPDF
ALPPSFDGDS PAYRYRLLEA TSQLLARPVL DSPSWDHDCG FDGVSLERNF VIANQFPGAF
AFQITKDKKE FNIHLDSSIS AKFAESGSTM AGLDIQTVGR QLAYIFRSET KFRSFKMNKT
SGGVSITLLG ENVATGLKIE DEIAVGKRLV LSGNAGAVQC RGDTAYGANL ELRLKDKDFP
IGNNNSSLGL SLMNWRGDLN LMANVQSQFS VGRSSKMAVC IGLNKQRSGQ VTVKLSSSEQ
LQMALIGIVP IALSGFRSIC PGSAGQSTS
//
