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Database: UniProt
Entry: A0A022RBT9_ERYGU
LinkDB: A0A022RBT9_ERYGU
Original site: A0A022RBT9_ERYGU 
ID   A0A022RBT9_ERYGU        Unreviewed;      1188 AA.
AC   A0A022RBT9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
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   ORFNames=MIMGU_mgv1a000394mg {ECO:0000313|EMBL:EYU37802.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU37802.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU37802.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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   EMBL; KI630513; EYU37802.1; -; Genomic_DNA.
DR   RefSeq; XP_012837054.1; XM_012981600.1.
DR   AlphaFoldDB; A0A022RBT9; -.
DR   STRING; 4155.A0A022RBT9; -.
DR   GeneID; 105957653; -.
DR   KEGG; egt:105957653; -.
DR   eggNOG; KOG1144; Eukaryota.
DR   OMA; APNQNED; -.
DR   OrthoDB; 561106at2759; -.
DR   PhylomeDB; A0A022RBT9; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
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:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 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:UP000030748}.
FT   DOMAIN          597..813
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..506
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..523
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  132853 MW;  B7E26526AFE375FC CRC64;
     MGRDNVELKN NKSTSMGGKK SKKNGFLIDD NEYSIGTELS EYSVLVPESK VAPLGKQMKT
     DLNNEDEQVE DDYDVPVIKF DGRNKSKGKK SACFSASSFE LLGEDEDEND YGRNDNDEEL
     GSPVIAFSGK KKHSKSGCGV SSAFDLLGKD KDDSSKEEDE DIGITFTGKK KKSSKGLNKA
     SGNSFSAAVL DEENGEDASV SNESSKIWNG DASSDFVEPE KRSDDSKIKK QTGEDPTDTS
     KNKKKKKKKN KGGKTGDEED DLDKILAELG VVLPESTCIA APTVVQHRGE LEEAADADKE
     NEDEGPVGSV TSKKKKKKKK KDKEKEKKAA HEKQEETKIE TNSNVLGKKV PKHVREILAK
     QKEAEEKKKQ EKEERQRKEE EEQRRVEEEQ EEQRLMEEKK RLKREKEKEK LLKKKQEGKI
     LTAKQKEEVR KREAMRTQFL ANAGGLQLPS GEPSAKRPLY QKKKAKAQQA QPNGASASDN
     VEITDSKEIQ HEFSLARDSD AVDLVEENGV HDEEEDEEWD ANSWDDSDLK LPGKSAFEDE
     DVDTKPEPKE IKNSRNATQD VELASITTKP RDFIEEKKNI KQVPKEESPN SDDKNELRSP
     ICCIMGHVDT GKTKLLDYIR GTNVQEGEAC GITQQIGVTY FPAENIRERT RELKADAKLN
     VPGLLVIDTP GHESFTNLRS RGSGLCEIAI LVVDIMHGLE PQTIESLNLL KMRNTDFIVA
     LNKVDRLYGW KTCRNAPIAK AMKQQSKQVQ MLFNDRLIQI ITQFKEQGLN TELYYKNKDR
     GDTFNIVPTS AISGEGIPDI LLLLVQWTQK TMIERLTFSK EVECTVLEVK VIEGHGTTID
     VVLVNGVLHE GDQIVVCGLQ GPIVTTIRSL LTPHPMKELR VKGTYLHHKE IKAAQGIKII
     AQGLEHAIAG TSLYVVGPDD DLEDVKNKTM EDMKSVMSRI DKSGEGVYVQ ASTLGSLEAL
     LELLKTPVNI PVRGISIGPV HKKDVMKASV MLEKINEYAT ILAFDVKVTQ EARELADELG
     VRIFTADSIY QLLEQFKAYI NNLKEERKRE AAEEAVFPCV LKIVPNCVFN KKDPIVLGVD
     VVEGTLKIGT PICVPQKEFI EIGRIASIEN NHKPVDYAKK GQSVAIKIVG SNSEDQQKTF
     GRHFDIDDEL VSKISRSSLD ALKQNYKDEV SQDEKNLLFK LKRLFKIP
//
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