ID A0A1D6FUE4_MAIZE Unreviewed; 1038 AA.
AC A0A1D6FUE4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Translocase of chloroplast 159 chloroplastic {ECO:0000313|EMBL:AQK95091.1};
GN ORFNames=ZEAMMB73_Zm00001d010852 {ECO:0000313|EMBL:AQK95091.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK95091.1};
RN [1] {ECO:0000313|EMBL:AQK95091.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK95091.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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; CM000784; AQK95091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6FUE4; -.
DR eggNOG; ENOG502QR60; Eukaryota.
DR ExpressionAtlas; A0A1D6FUE4; baseline and differential.
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 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; 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.
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 398..627
FT /note="AIG1-type G"
FT /evidence="ECO:0000259|PROSITE:PS51720"
FT REGION 1..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 111782 MW; 88011903CE28B0CA CRC64;
MATTTDAAPV APVEEGNAAP AAAEEEPPKK VEAAVATTDA APVAPASVED ENPALAAAAE
EELTEKFESA AAAAAEEEVD DREAPKQVVA DVGEREEEEE EVRLEAKSEG VAGPEAENGK
AEGVVVGGHD GRDVNEAEED RRVGKLGAAT AVKDGGGEEP ASEDGEAAAS VSAPVSEVES
KSENGESGEG DPSLASPDAP ESDEKGELQE EEQHDEERGA AVEVNVVDKI AEDVESPVAE
EEKLVPEVEK GEEVGSGSAV GGELSDEEEV EVSPSPLGEE VAEVAEPQDK IMKELAEGSS
SGSISRDFTN SMDGQIMLDD SEDDDDDNDD DGDEKGFDSA ALAALLKAAT GGSSAQVLYR
LSLAEGIRHG RQTNRAFSLD NARRKALLLE AEGKEDLNFS CNILVLGKTG VGKSATINSI
FGEEKSRTDA FSSATTNVRE IVGDVDGVKI RIIDTPGLRP NVMDQGSNRK ILAAVKNYTK
KCPPDIVLYV DRLDSLSRDL NDLPLLKTIT AVLGSSIWFN AIVALTHAAS APPEGLNGAP
MTYEVLMAQR SHIIQQSIRQ AAGDMRLMNP VALVENHPSC RKNREGQKVL PNGQSWRHQM
LLLCYSSKIL SEANSLLKLQ DPNPGKLFGF RFRSPSLPFL LSSLLQSRAH PKLSAEQGGN
EGDSDVELDD YSDVEQDDDE EEYDQLPPFK PLTKAQLARL TKEQKNAYFD EYDYRVKLLQ
KKQWKDEIRR LKEMKKRGKT DLDDYGYANI AGENDQDPPP ENVSVPLPDM VLPPSFDCDN
PTYRYRFLES TSTVLARPVL DAHGWDHDCG YDGVSVEETL AILSRFPANV AVQVTKDKKE
FSIHLDSSIA AKHGENASSL AGFDIQTVGR QLAYILRGEA KIKNIKKNKT TGGFSVTFLG
DIVATGLKVE DQLSLGKRLS LVASTGAMRA QGETAYGANL EARLKDKDYP IGQSLSTLGL
SLMKWRRDLA LGANLQSQFS IGRGSKMAVR LGLNNKLSGQ ITVRTSTSEQ VQIALLGLVP
VAASIYRSFR PSEPSFAY
//