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Database: UniProt
Entry: A0A067FIT9_CITSI
LinkDB: A0A067FIT9_CITSI
Original site: A0A067FIT9_CITSI 
ID   A0A067FIT9_CITSI        Unreviewed;       768 AA.
AC   A0A067FIT9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=CISIN_1g004202mg {ECO:0000313|EMBL:KDO67248.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO67248.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO67248.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KK784897; KDO67248.1; -; Genomic_DNA.
DR   EMBL; KK784897; KDO67249.1; -; Genomic_DNA.
DR   RefSeq; XP_006483588.1; XM_006483525.2.
DR   RefSeq; XP_006483589.1; XM_006483526.2.
DR   RefSeq; XP_006483590.1; XM_006483527.2.
DR   STRING; 2711.A0A067FIT9; -.
DR   PaxDb; 2711-XP_006483588-1; -.
DR   GeneID; 102609501; -.
DR   KEGG; cit:102609501; -.
DR   eggNOG; KOG0458; Eukaryota.
DR   OrthoDB; 470716at2759; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd04093; HBS1_C_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR029459; EFTU-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT   DOMAIN          338..563
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          193..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   768 AA;  83571 MW;  367C94AE449C1B2A CRC64;
     MPHKVNYEDY DYGDYYEYED YDDYDYDVED NGEAPTPASE SKQETSKPRV WSCAICTYDN
     EEGMSVCDIC GVLRTPLVNN NRKTAGGICK DSGASVMAKS LFASLPPRTP KKAVVIQRQN
     DGSLMEEGNN CHKLGNTKGK FHEFHEAFSS HSHSKFNIAP FKFDVPSPDD LVSNGLHSSK
     TGSKGNFLDL KSSRVSSSVS EKNGSVNTRS SAKKSDIANV LMPKDKQDSV DERNSLKNEV
     RASSRISDSS SVVMAKDRLG TIDEGNCSNH GTVDDSISSS VDGTESSSHT GNLTSNMKNM
     SSTAKSGNST NVSARKTNSH TQYKPEKWML PDKKGDRMTQ LNLAIVGHVD SGKSTLSGRL
     LFLLGRITQK QMHKYEKEAK LQGKGSFAYA WALDESAEER ERGITMTVAV AYFDSKNYHV
     VVLDSPGHKD FVPNMISGAT QSDAAILVID ASVGSFEVGM NTAKGLTREH AQLIRSFGVD
     QLIVAVNKMD AVQYSKDRFD SIKVQLGTFL RSCGFKDASL TWIPLSALEN QNLVTAPDDG
     RLLSWYKGPC LLDAIDSLRP PPREFSKPLL MPICDVLKSQ HGQVSACGKL EAGALRSGLK
     VLVLPSGEVG TVHSIERDSQ SCSVARAGDN IAVSLQGIDV SRVMSGGVLC HPDFPVAIAT
     HLELKVLVLD FAPPILIGSQ LECHIHHAKE AARIVKITSL LDTKTGKVTK KSPRCLTAKQ
     SAIVEVALQE PVCVEEFSNC RALGRAFLRS SGRTIAVGIV TRIIEDQQ
//
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