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Database: UniProt
Entry: A0A087SF12_AUXPR
LinkDB: A0A087SF12_AUXPR
Original site: A0A087SF12_AUXPR 
ID   A0A087SF12_AUXPR        Unreviewed;      1373 AA.
AC   A0A087SF12;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=F751_3034 {ECO:0000313|EMBL:KFM24316.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM24316.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM24316.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM24316.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
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; KL662107; KFM24316.1; -; Genomic_DNA.
DR   RefSeq; XP_011397204.1; XM_011398902.1.
DR   STRING; 3075.A0A087SF12; -.
DR   GeneID; 23614425; -.
DR   KEGG; apro:F751_3034; -.
DR   eggNOG; KOG1144; Eukaryota.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000028924; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd03703; aeIF5B_II; 1.
DR   CDD; cd16266; IF2_aeIF5B_IV; 1.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
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   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:KFM24316.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00209};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00209}.
FT   DOMAIN          139..249
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   DOMAIN          778..995
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..134
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..653
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..713
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..749
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1373 AA;  147288 MW;  8C11EA00BCF80B3E CRC64;
     MPPKKKNRNL DDWEKDFAAL DENGELKEPE EALTKPVTKT KKKDKKKGKK AAAFDSDDEA
     VPAVLTPAAG AAGVESEDDE PTIGPTKASR GRKAAPVSVF ELLGEEDEGS GAEGEEEEAA
     EEEEVAEEEE GKGATDETPE LRPVPIVAKI VGLKQHPKAD RLRVVKLAAG PLLGDVQVVT
     NAPNLTKQQL VALAPVGCKT PGTGMEIAHT KLRGVESAGM ICSAQDLDAE EETMLELESK
     KKRKGKKSKA ATDALFAALA GALTLGADEL QLGPKKKSKK KTARAELDLD ALLADNGGDK
     AVTPLTEPTP SETSKGKDRE KEEPAASDAE LDALLAEIDA PAPAAPVPAP TGGGKKKKKG
     KGGKGKADGE EEDLDALLAE LGVELPASAA GVGSAAASAP GGPSDATEEN GGGGEGGPAT
     SAAAKRRAKK KARDAAKKSG GAVEAEGGEE PAAEESSEPA SASAKGGKKG APKVSAAVKR
     MQAALEAQRR AAEEAARLAE EQRLREEEEE RAAEEAERQK AEAAERRKAE KLARREQLKK
     EGKLLTGKAK AEAERLARVR EQFLKQAGID VDAGAPKKKP VYTNRKRTQP RKQVNPEAEG
     PVSAAAEEEP APAPEPESEV PADEPAAPAD EPVEGAVEET WEATVDDWEA MDEDTLVLPG
     QQPAAPVATA AGTPQAEVAE QNGEAATSEK AVEEAVAEEE ESDEEEEEGE TSSSDASESG
     SGTETESESE SESSSEYSSS EEESTDSEAE MEERIAAQRE KRAERRKLAM ALRNPADLRS
     PICCILGHVD TGKTKILDNI RRTNVQDGEA GGITQQIGAT YIPGDAILTR TEELRRGKSF
     DLKLPGLLVI DTPGHESFSN LRSRGSGLCD IAVLVVDLMH GLEQQTIESL NLLRMRKTPF
     VIAMNKVDRL YGWKSVPNSP IIDALERQAE HVCTEFEQRM DKIMLQLNEQ GMNVALYWRN
     KDPRSFISIV PTSAHTGEGI PDLLQILVKL TQTAMAEKLT FVNDLQCTVL EVKSIEGLGT
     TIDVVLINGQ LQEGDTIVVC GLGGAIVTPI RALLTPQPLR EMRVKGTYVH HKEVRAAMGI
     KLAAHNLETA VAGTQLFVVR PDDDLEALKA EVMEDMQDIF ASVDKTGEGV CVQASTLGSL
     EALLAFLKTP EVNIAVSAIN IGPVHKRDVM RANVMIERGV KKYGVILAFD VPVNKEAREM
     AEELGVNIFT ADIIYHLFDQ FTAYLKHVKE EEQEAARLEA VFPCVLRIMP TCVFNKKDPI
     VVGVEIAEGI ARIGTPICVP SQGGFELGRI ASMEKDHKAV DTAKRGDAVA MKIEATNPDQ
     AARLYGRHFD HKDDLVSKIT RKSINVLKDM FRDDLTKDDW RLVVRLKKVF NID
//
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