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Database: UniProt
Entry: A0A1U8B0Y8_NELNU
LinkDB: A0A1U8B0Y8_NELNU
Original site: A0A1U8B0Y8_NELNU 
ID   A0A1U8B0Y8_NELNU        Unreviewed;      1605 AA.
AC   A0A1U8B0Y8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Translocase of chloroplast 159, chloroplastic-like {ECO:0000313|RefSeq:XP_010269518.1};
GN   Name=LOC104606150 {ECO:0000313|RefSeq:XP_010269518.1};
OS   Nelumbo nucifera (Sacred lotus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010269518.1};
RN   [1] {ECO:0000313|RefSeq:XP_010269518.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_010269518.1; XM_010271216.2.
DR   STRING; 4432.A0A1U8B0Y8; -.
DR   GeneID; 104606150; -.
DR   KEGG; nnu:104606150; -.
DR   eggNOG; ENOG502QR60; Eukaryota.
DR   InParanoid; A0A1U8B0Y8; -.
DR   OrthoDB; 4210585at2759; -.
DR   Proteomes; UP000189703; Unplaced.
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   Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          960..1194
FT                   /note="AIG1-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51720"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1234..1252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1605 AA;  172091 MW;  7C5F904713356F53 CRC64;
     MDSKASVPLY ATEEAPLPAE TSQQHHHPPV KVSLSRSPGI RAPPFYFDIE NDEDNVGDKK
     SNGSSVSSRS TEGSYESEGF VSGEDEFETA SERPFIADPD EEAIEVAMEG EDAGISFVRD
     GQVEEVTVPF FQSALGSSSF SPPKTVMPIA KPSREDDDVE DEGLVSEVED DGVSGVARVP
     SSEELQGSGG MVETPTPKVK VLGDEGGEED ESSLGRDSAP SEGLTSGFVQ SGLGRDGVPE
     PLGVAGNDSE TIEEGSGTEN PKPEAGVLDS AEKEPTGEAN SVSDELGEDQ VPISTNSCVE
     DSAASEQDNL PESAKLNEDA NPAGQGSPVP EKHELEGTEL KDILEENKND ALGGSYTVEV
     HSSIEGEFSV DSKQNSNVIA KNPSLDGEAD QSVPVIEESV DSNFIKADNT NSVTGGDLVV
     ETRQPILLGS ESGVVGDKEE NDASEVKIVE QPVGPESGVV GDKEENEASE TEVVERLLDS
     ESCVDGHTEE YKASETEGVE RLLGSESGVV GDNGDYKASK TEEVEQPAEK SVRLGTGSDQ
     SSHVVEEPIL SKLIEADTGV AKIEEVNAVE HEAATNPVHE AKELGSLEPI TNKAGVVEVD
     VLDTGSTSVD TIMAVSADVH EGERDGAGAD ESICLDEDEN TGISELESEQ QTAASGADAD
     ESTLDSAING VAINSTGPVA EESKHLENGD ASIAAQGYEL EDGISSKLNR PQSMVPVSIL
     DPEIKQEAEV QDLEGGDDDE GPVSDEEAEG VMFGSSEAAK RIMELVQGTG TGSHFSSESF
     LDHSQRIDGQ IATDSDEEVE TDEESDGKEL FDSAALAALL KAATNAGSDG GSITITSSDG
     SRLFSVERPA GLGSSIRSLK PDSRPNRPSI FTPSGLTAEG ESEDNLSEEE KKKLEQLQLI
     RVKFLRLVQR LGHSPEDSIV SQVLYRMVLA AGRRTGQVFN LEAAKTTAMQ MEAEGKDDLI
     FSLNILVLGK TGVGKSATIN SIFGEKMSVI DAFEPATTTV KEIVRSVDGV KIRIIDTPGL
     RPSVMEQSFN RKVLSSIKKF TKKCPPDIVL YVDRLDTQTR DLNDLPLLRS ITSSLGSSVW
     RSAIVTLTHA ASAPPDGPSG SPLSYEVFVA QRSHVVQQCI GQAVGDLRLM NPSLMNPVSL
     VENHPACRKN REGQRVLPNG QSWRPQLLLL CYSMKILSEV SSLSKPQDPF DQRKLFGFRI
     RSPPLPYLLS SLLQSRAHPK LSADQGGENG DSDVDLGDLS DSDQEEEEDE YDQLPPFKPL
     RKAQVANLSK EQRKAYFDEY DYRVKLLQKK QWKEEVKRMK EMKKGKASDD DYGYMGEDVD
     QENGSPSAVP VPLPDMVLPP SFDGDNPAYR YRFLEPTSQL LARPVLDTHG WDHDSGYDGV
     SLEQNLAIAG QFPAGVAVQI TKDKKEFNIH LDSSVSAKHG ENGSTLAGFD IQTIGKQLAY
     ILRGETKFKN MKKNKTTAGI SVTLLGENVA TGLKIEDQIA IGNRLVLVGS TGAVRSQGDV
     AYGANLEARL REKDFPIGQD QSTLGLSLMK WRGDLALGAN LQSQFSVGSN SKMAVRVGLN
     NKLSGQITVR TSTSEQLQIA LMGILPIATA IFRTIWPANE TYSAY
//
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