ID A0A2K3P3E3_TRIPR Unreviewed; 1388 AA.
AC A0A2K3P3E3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Translocase of chloroplast 132 chloroplastic-like protein {ECO:0000313|EMBL:PNY09779.1};
GN ORFNames=L195_g006336 {ECO:0000313|EMBL:PNY09779.1};
OS Trifolium pratense (Red clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY09779.1, ECO:0000313|Proteomes:UP000236291};
RN [1] {ECO:0000313|EMBL:PNY09779.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY09779.1};
RX PubMed=24500806; DOI=10.3732/ajb.1300340;
RA Istvanek J., Jaros M., Krenek A., Repkova J.;
RT "Genome assembly and annotation for red clover (Trifolium pratense;
RT Fabaceae).";
RL Am. J. Bot. 101:327-337(2014).
RN [2] {ECO:0000313|EMBL:PNY09779.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY09779.1};
RX PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT (Trifolium pratense) Breeding.";
RL Front. Plant Sci. 8:367-367(2017).
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:PNY09779.1}.
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DR EMBL; ASHM01003368; PNY09779.1; -; Genomic_DNA.
DR STRING; 57577.A0A2K3P3E3; -.
DR EnsemblPlants; Tp57577_TGAC_v2_mRNA28780; Tp57577_TGAC_v2_mRNA28780; Tp57577_TGAC_v2_gene27837.
DR Gramene; Tp57577_TGAC_v2_mRNA28780; Tp57577_TGAC_v2_mRNA28780; Tp57577_TGAC_v2_gene27837.
DR Proteomes; UP000236291; Unassembled WGS sequence.
DR ExpressionAtlas; A0A2K3P3E3; baseline.
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:SF135; GTP-BINDING PROTEIN A; 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:UP000236291};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 754..983
FT /note="AIG1-type G"
FT /evidence="ECO:0000259|PROSITE:PS51720"
FT REGION 68..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1035
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1388 AA; 151914 MW; 2B1291FB46A36838 CRC64;
MDNEGERVRV DVGVSEESVK NFEGEEVFEE AMDPIKRFDD LGGDAVVGED DVVTDTVSEL
PSDLVDEVAD KKEESDTFRE SVGVDDEEEL EVIANQEVRE DQQGQLYNKE AEGGVSCDES
YSIKDDFSGG KELSDSNADG SVVFQEGRDL VNGESGLLSE KGEGEDLEYV TPRQNGGLIS
ENGSTDKVDF AVEEFRTESG SDEEMKNKDA DGGYLKEDGL DPDLRDDKIE EERNDSGDPS
SEIQDGTDDL EHHHEIFVEM EDETIGTDAI HKDTNGKETG VSDSQSTESK VYSNHETKDD
DAESNSEHLE TIGETGGSSP AVNESEVVET AGSSSLSENS LANEMPTVQA TAADSEVGST
KVYQSQISTE ENQGNYENLS VVDRSEVIET GGSSPTLDER KVTETVVNSS ISENSSANEI
PTVQTTAADS EEGSAKVYQS QISNEENQGN SEISSVVDRS EVIETLRSSP ALDEVKVAET
VGSSPPSENS FANELPTVQA TAADSVKETS KVYPSKISNA ENQGNYEKSS VVGEPEKIPE
NNTKEKQTTQ IIKEQNSELD SSSGKSVAPG TPLDRPVGLG PVAPLLRPTP RVVQQPRVNN
TKEKQTTQIT KEHNSELDSS SGKSVPTSTP LVRPAGLGSA APLLEPSPRV VQQPRVNNTV
SNVQSPKMED SSTGEAEEYD ETREKLQMIR VKFLRLAKRF GQTPHNVVVA QVLYRLGLAE
QLRGRNGGRV GAFSFDRASA MAEQLESAGQ EPLDFSCTIM VLGKTGVGKS STINSIFDEV
KFNTDAFQMG TKKVQDVVGT VQGIKVRVID TPGLLPSWTD QQHNEKILHS VKRFIKKTPP
DIVLYLDRLD MQSRDFSDMP LLRTITDVFG PTIWFNAIVV LTHAASAPPD GPNGTPSSYD
MFVTQRSHVV QQAIRQAAGD MRLMNPVSLV ENHSACRTNT AGQRVLPNDQ VWKPHLLLLS
FASKILAEAN ALLKLQDNPR EKPYTARARA PPLPFLLSSL LQSRPQLKLP EEQFSDDDGL
NDDLDEPSDS GDETDPDDLP PFKPLTKAQI KNLSRAQKKA YLDEVEYREK LFMKKQLKYE
KKQRKMMKEM AESAKDLPTE YGENVEEESE GASSVPVPMP DMSLPASFDS DTPTHRYRYL
DSSNQWLVRP VLETHGWDHD VGYEGLNVER LFVLKDKIPV SFSGQVTKDK KDANVQMEMA
SSVKHGEGKA TSLGFDMQTV GKDLAYTLRS ETKFLNFRRN KGTAGLSFTL LGDALSAGVK
VEDKLIANKR FKLVIAGGAM TGRDDVAYGG SLEAQLRDKN YPLGRSLSTL GLSVMDWHGD
LAVGCNLQSQ IPIGRYTNLV ARANLNNRGA GQISIRLNSS EQLQIALIGL IPLLQKVVGY
SQQLQYGQ
//
