ID M1D1A0_SOLTU Unreviewed; 1337 AA.
AC M1D1A0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN Name=102604773 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079119};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079119, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400079119}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400079119};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
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DR RefSeq; XP_006356684.1; XM_006356622.2.
DR STRING; 4113.M1D1A0; -.
DR PaxDb; 4113-PGSC0003DMT400079119; -.
DR EnsemblPlants; PGSC0003DMT400079119; PGSC0003DMT400079119; PGSC0003DMG400030793.
DR GeneID; 102604773; -.
DR Gramene; PGSC0003DMT400079119; PGSC0003DMT400079119; PGSC0003DMG400030793.
DR KEGG; sot:102604773; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_2_1_1; -.
DR InParanoid; M1D1A0; -.
DR OMA; INEVQCT; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1D1A0; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF16; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B-LIKE; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT DOMAIN 744..961
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..648
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 147875 MW; 3BBC06EF50FF3B7D CRC64;
MGRKKPVREN ESLESSKQGG GGGGKSKKKN RVIDDDDYSV GTELSEDTVV LEDKAELVPE
ISKKRGKKGK KSGARDEDVE ETEDKLVRKE EDDEKKKLGG GEKNLAKQVG GGGKSKKKNV
AIDDDEYSIG TEISAETQEE ELAPAVAFGK KKSKKGKKGG VSTSDYGSLG QDDDDEDVSG
LSRDRDGVVG DSDREAESVA SVTGKTKNLR LGKSSASLSV TSAFHAIDDQ DNETGQLSEE
DEESTVAFTG RSSGISFSAA LLDEENDADT SLKLETEANE EDDAPGIIFS GKKKSSKKKN
KSASSTIDTA FRNDSTNVVD QDHCNLGVNR EDADDNRGKK QTTDVLETSK NKTKKKKSGH
ASKILADLGE GSTITTPAQP ANASLPQEEK SQQQSQLGDD TGEREAVEEA VKSAAAKKKK
KKEKEKEKKA AVAVSEMEEK QEGTKNDTRA KLADKKQSKQ VREMQERLKK MKEVEESKKK
EEEERLRKEE EEHLRLEELE RLAEEKKHLK KEREKEKLLK KKLEGKLLTG KQKEEARRLE
AMRKQFLASG GALPLSTGES RKDATKRPIY QSKKSKSQAW ANGKVQEESV ESTEVQENQQ
EIVSEVDSMK TEKAEDIDLV SVEEKSEVAD AEENRVEEEE DEEEWDARSW DDADLKLPRK
SAFEDEELDS DPQPIITKAA RSVVSDTGPL PVAAKSVIPT QKAVASVPDV TKNDGSKKRE
PVVVVSGKGT EKPGASSSKS EDNLRSPICC IMGHVDTGKT KLLDCIRGTN VQEGEAGGIT
QQIGATYFPA ENIRERTKEL KADAKLKVPG LLVIDTPGHE SFTNLRSRGS SLCDIAILVV
DIMHGLEPQT IESLNLLKMR NTEFIVALNK IDRLYGWKVC RNAPIVKAMK QQSKDVQFEF
ITRLTQIVTQ FKEQGINTEL YYRNKEMGKD TFSIIPTSAI SGEGIPDLLL LLVQWTQKTM
VERLTYSSEV QCTVLEVKAI EGHGTTIDVV LINGMLHEGD QIIVCGMQDP IVTSIRALLT
PHPMKELRIK GSYVHHKEIK AAQGIKINAQ GLEHAIAGTS LYVVGPDDDV ENIKEAAMED
MRSVMSRIDR SGEGVYVQAS TLGSLEALLE FLKTDEVRIP VSGIGIGPVH KKDVMKASVM
LEKKIEYATI LAFDVKVTQE ARELADEAGV KIFIADIIYH LFDQFKAYID NLKEEKKKEV
AEEAVFPCSL KIVPNHVYNK KDPIVVGVDV LEGIARVGTP ICIPQREFID IGRIASIENN
HRPVDSAKKG QRVSIKIVGS NSEEKQKMFG RHFEIEDELV SKVSRRSIDI LKANFRNDLS
IEDWKLVKTL RDLFKIQ
//
