ID A0A2C9UC21_MANES Unreviewed; 1415 AA.
AC A0A2C9UC21;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=MANES_15G012200 {ECO:0000313|EMBL:OAY27743.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY27743.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY27743.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY27743.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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; CM004401; OAY27743.1; -; Genomic_DNA.
DR STRING; 3983.A0A2C9UC21; -.
DR EnsemblPlants; OAY27743; OAY27743; MANES_15G012200.
DR Gramene; OAY27743; OAY27743; MANES_15G012200.
DR OMA; HASHEFT; -.
DR OrthoDB; 4210585at2759; -.
DR Proteomes; UP000091857; Chromosome lg15.
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:UP000091857};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 770..1004
FT /note="AIG1-type G"
FT /evidence="ECO:0000259|PROSITE:PS51720"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1415 AA; 154701 MW; 994ACAC6B3B787F2 CRC64;
MASFPRVSLS KTQGSPSFSN SLLLSPAGSF PIRAPITPDD DSSDFESISH TDHGYSDTSI
SIDNGSESDE YVSGEEYESF SEKLFAGDPD EESPDEESGR LDKNKLSRPF VPNPDKVTLG
NSVTDEESAV TGQYSPFVET NSPYLQRNMP VAQLTMDDND FEELTSDDGI VSGATEDSRF
SAMISAPRVK VSDFEEDKED EPWVQRDSSV INKIELLQGA DSLGNFVGAE HGVLSSEDNV
LGSVSVKLIK HDSHVFTMDA QVEPLMENKG NSQMKEDAKH VVDDPASVES VEDDGQVVPD
SEFLVDSKED VLGKYSQLGD DGKQLVEERL QLENLEEEQI KPNFTEGHNG KSMENDFMDN
VSDQCIGSHV KEQISENGCG GAYESQLNQV ENIAPDITEL KVDGVVLQKE QTSEIVNSSN
ETFVTVINPV DESLQKIVAE LQEMELEVLG VEAEKTTDFV NGYHSCVFNG SDALEEGNGS
EKLKGKSGPE TGMTFESLAL EDDIRVESAD GAFESNGTVD LLEDIALPEM SGVDRLEAAS
QGNTNSFGIG EEANHDSEKI GGHGGLLSDE DVEELIFGGS GSIEHNMSEL EKSAAFSPFP
AADDRQYRID GQIILDSEEE LETDKEHEEE KLFDSAALAA LLKAATGVEL DGGSVMATSA
SSEVFSAQQC AGSGSSFDIK QASQLSMVKD VVNDSAGEEE KMIIEKIQHI RVKFLRLVQR
LGHSPEDSIV AQVLQRSVLA AGLHASHEFT LESSKRMAMQ LEAEGKDDLD FGLNIFVIGK
TGVGKSATIN SLFGEKKVMI NAFEPATTRV KEIVGTIDGV RIRILDTPGL RSPVKEEAIN
RKIFASIKRL IKKFPPDVVL YVDRLDTHAR DLNDLPLLAS LTNSLTASIW QNAIVTLTHA
AAPPPDGLSG SPLSFEVFVA QRSHIVQQAI SQAVGDLRLM YPSMMHPVSL VENHPSCPKN
EKGESILPNG QSWRTHLLLL CYSLKILSEV SSLTKTPDLF DSKKLFGIRL RPLPLPHLVS
SLLQSRPHPK LAAEQGGDDV DSDMELLDLS DSDEEDEYEQ LPPFKPLKKS QVNELSKEQR
KAYFSEYAYR VKLLQKKQWR EEVKKLKELK KKSKDSKSKH DSTGEDVDQE DGGPPTVPFP
IPDFVLPPSF DCDNPSYRYR MLEPASQLLV RPVLDSQGWD HDCGYDGVSL ERNLAIADQF
PGAIAVQITK DKKVFNLHLD SSICAKHGEN GSIMAGFDIQ TIGRQLGYIL RSETKFRNYK
INKTSAGISI TMLNKNVATG LKIEDQIAIG NRLSLVGNAG AVRSGGDTAY GGNFEVRLKS
KDFPVEQDQS TLGLSLVNWR GELGVMANLQ SQFSVGHNSK IAIHIGMNNR QSGQITIKTS
SSELQLALIS IIPMAISILK SLYPGGAARK SNMLD
//
