ID A0A1D6FUE3_MAIZE Unreviewed; 1207 AA.
AC A0A1D6FUE3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Translocase of chloroplast 159 chloroplastic {ECO:0000313|EMBL:AQK95090.1};
GN ORFNames=ZEAMMB73_Zm00001d010852 {ECO:0000313|EMBL:AQK95090.1};
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:AQK95090.1};
RN [1] {ECO:0000313|EMBL:AQK95090.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK95090.1};
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; AQK95090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6FUE3; -.
DR SMR; A0A1D6FUE3; -.
DR IntAct; A0A1D6FUE3; 5.
DR STRING; 4577.A0A1D6FUE3; -.
DR ExpressionAtlas; A0A1D6FUE3; baseline and differential.
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; 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 567..796
FT /note="AIG1-type G"
FT /evidence="ECO:0000259|PROSITE:PS51720"
FT REGION 1..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..475
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 195..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..410
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 129751 MW; 154CE1EEBD3AC08B CRC64;
MATTTDAAPV APVEEGNAAP AAAEEEPPKK VEAAVATTDA APVAPASVED ENPALAAAAE
EELTEKFESA AAAAAEEEVD DREAPKQVVA DVGEREEEEE EVEKGEEVGS GSAVGGELSD
EEEVEVSPSP LGEEVAEVAE PQDKVAHVSE ANGELGDGKE ASDDVVALGG GEASEESANK
DADGDDVVAQ GGEEALEEST KKDADVEDEA IRPEPPSEAT AVVMNDGSIE ELAPASAEEI
IDSVREDSPQ KEQSAEDQAV AGEVVEDVGV DKPTEVENVD ATSADGILSR ELAPESIKET
NGTGEIEGAT EVVDHEEEAA DNDIIEAVPD DADGDGNEAE DDDDGTNSDT SPARVAILES
SEAAKQIMKE LAEGSSSGSI SRDFTNSMDG QIMLDDSEDD DDDNDDDGDE KGFDSAALAA
LLKAATGGSS GGDITVTSQD GSRIFTMDRP AGLGSSAPSL RPTAPRQSAR SNLFSPSELA
VTADPTEEMT EEEKKLHDKV ELIRVKFLRL VYRLGATPEE TVAAQVLYRL SLAEGIRHGR
QTNRAFSLDN ARRKALLLEA EGKEDLNFSC NILVLGKTGV GKSATINSIF GEEKSRTDAF
SSATTNVREI VGDVDGVKIR IIDTPGLRPN VMDQGSNRKI LAAVKNYTKK CPPDIVLYVD
RLDSLSRDLN DLPLLKTITA VLGSSIWFNA IVALTHAASA PPEGLNGAPM TYEVLMAQRS
HIIQQSIRQA AGDMRLMNPV ALVENHPSCR KNREGQKVLP NGQSWRHQML LLCYSSKILS
EANSLLKLQD PNPGKLFGFR FRSPSLPFLL SSLLQSRAHP KLSAEQGGNE GDSDVELDDY
SDVEQDDDEE EYDQLPPFKP LTKAQLARLT KEQKNAYFDE YDYRVKLLQK KQWKDEIRRL
KEMKKRGKTD LDDYGYANIA GENDQDPPPE NVSVPLPDMV LPPSFDCDNP TYRYRFLEST
STVLARPVLD AHGWDHDCGY DGVSVEETLA ILSRFPANVA VQVTKDKKEF SIHLDSSIAA
KHGENASSLA GFDIQTVGRQ LAYILRGEAK IKNIKKNKTT GGFSVTFLGD IVATGLKVED
QLSLGKRLSL VASTGAMRAQ GETAYGANLE ARLKDKDYPI GQSLSTLGLS LMKWRRDLAL
GANLQSQFSI GRGSKMAVRL GLNNKLSGQI TVRTSTSEQV QIALLGLVPV AASIYRSFRP
SEPSFAY
//
