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Database: UniProt
Entry: A0A166D9J3_DAUCS
LinkDB: A0A166D9J3_DAUCS
Original site: A0A166D9J3_DAUCS 
ID   A0A166D9J3_DAUCS        Unreviewed;      1492 AA.
AC   A0A166D9J3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZN04966.1};
GN   ORFNames=DCAR_005803 {ECO:0000313|EMBL:KZN04966.1};
OS   Daucus carota subsp. sativus (Carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN04966.1};
RN   [1] {ECO:0000313|EMBL:KZN04966.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaf {ECO:0000313|EMBL:KZN04966.1};
RX   PubMed=27158781; DOI=10.1038/ng.3565;
RA   Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA   Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA   Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA   Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT   "A high-quality carrot genome assembly provides new insights into
RT   carotenoid accumulation and asterid genome evolution.";
RL   Nat. Genet. 48:657-666(2016).
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}.
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:KZN04966.1}.
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DR   EMBL; LNRQ01000002; KZN04966.1; -; Genomic_DNA.
DR   STRING; 79200.A0A166D9J3; -.
DR   EnsemblPlants; KZN04966; KZN04966; DCAR_005803.
DR   Gramene; KZN04966; KZN04966; DCAR_005803.
DR   Proteomes; UP000077755; Chromosome 2.
DR   GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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; GTPASE, IMAP FAMILY MEMBER-RELATED; 1.
DR   PANTHER; PTHR10903:SF120; TRANSLOCASE OF CHLOROPLAST 159, CHLOROPLASTIC; 1.
DR   Pfam; PF04548; AIG1; 1.
DR   Pfam; PF11886; TOC159_MAD; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000077755};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          885..1010
FT                   /note="AIG1-type G"
FT                   /evidence="ECO:0000259|Pfam:PF04548"
FT   DOMAIN          1216..1480
FT                   /note="Translocase of chloroplast 159/132 membrane anchor"
FT                   /evidence="ECO:0000259|Pfam:PF11886"
FT   REGION          601..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1105..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1191..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1139
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1492 AA;  159939 MW;  C389637D2CC61CE3 CRC64;
     MESTAEAASN SLLSADPFTG SVETSSFLDK NVVNDTNVLN GSDDIDSISS VSDDGFVSGE
     EDFDVEKKSF LDYPDDKYKT VDVNSGDPFV DFETPIAGGE EKSFKDVVLE SGEGLNGVVE
     RIGDGVEKSF KDVVAESGES LNGVVEGNGD VVEKSFKDVV ESGESLNGVV EGSGDGVKES
     FKDVVVESGD GVLGNVDVVT EGGLREDKVT EFSEGLGSDL NGVVEKNGGV GKSFKDVVVE
     GGEGLTGNVD VGAEGGFVEE EVRGFTEGLG SGVEENSLES EEVLEVKKME GVSQVVEKHV
     VESSESEQVG DVVVESGSGV EVTREGDTVV ETINVDLLEP GVAVVGEMEG NGTAYRSMNL
     NAESDQVSAG TVEEGSGENI IVSAESDNPS LENGSDKVIV GTFEENEVQN IGAPSNSQLS
     DIDNAKITLD GDSVGKDLHV NMAVSGVAVG IEKEEVDGVL SGAGQVHGEI VSFVKDGNFL
     HSNANIVEPN TFADVKTTPE GDSVVENIKV DMSEPGVAVV GNIEEDGQAD ANVGNNQENE
     KEHVNQIEGV EVVSTRNFVG DDGSDAAVDA LLPVSSIPTN AEEHKRDDDL SLSVQDEITE
     NGVSEKSLAN DSAESNPLQN KEIEVKDDAN FVKNETSEDD LEGSGSDEGD SDGMIFGSSE
     AAKQFIEELE RGSEGNSNSG AESFHDNAQR IDGQIVTDSE EEDSDEEGEG KELFNSAALT
     ALLKAATGAG SDGGNITISQ DGSGRFSIER PAGLGSSTHS LRPAARANRS NFFNPSIFAG
     GEETEDNLTA EEKGKIEKLQ SIRVKFLRLV QRLGMSSGDS VASQVLYRLA LVAGRQTGQL
     FNLDNAKQTS LQLEDEKADL DFSLSILVLG KSGEEKAPVD AFQPATTAVK EIIGVVDGVK
     IRVFDTPGLK SSVVDQSFNR SILSSVKKFT KKNPVDIVLY VDRLDAQTRD LNDIPLLRTI
     TSSLGSPIWR SVIVTLTHAA SAPPEGPSGS PFSYDSFVSQ RSNVVQQSIG QASGDLRMLS
     PSLMNPVCLV ENHSSCRRNR EGQKVLPNGQ SWRPQLLILC YSTKILSEAN SISKPQDSFD
     SRRLFGYRTR SPPLPYMLSS MLQSRVHPKL SSEQGGDNGD SDVDLADLSD SDQEDEDEYD
     QLPPFKPLRK SQLAKLSVEQ RKAYFEEYDY RVKLLQKKQW REELKRLKEM KMKGKDSAND
     QGYNEEDPDA GSAAPVSVPL PDMALPPTFD GDNPAHRYRF LEPTSQFLAR PVLDTHGWDH
     DCGYDGVNLE QSLAILSQFP AVVSVQLTKD KKEFTVNLDS SIAAKHGENG SSMAGFDIQN
     MGKQLAYIIR GETKFKNFRK NKTAAGISVT FLGENVVTGL KVEDQISFGK QYSLVASGGT
     VRSQQDVAYG ANIELQRREL DYPIGQVQST LGLSIIKWRG DLALGFNSVA NFSIGRNSKV
     AVRGSLNNKL SGQISVRTSS SEHLSLALAS ILPVAVTIYK KLFPVGDKYS TY
//
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