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Database: UniProt
Entry: B6K2T4_SCHJY
LinkDB: B6K2T4_SCHJY
Original site: B6K2T4_SCHJY 
ID   B6K2T4_SCHJY            Unreviewed;      1034 AA.
AC   B6K2T4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=tif52 {ECO:0000313|JaponicusDB:SJAG_03732};
GN   ORFNames=SJAG_03732 {ECO:0000313|EMBL:EEB08574.1};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08574.1, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB08574.1, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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; KE651167; EEB08574.1; -; Genomic_DNA.
DR   RefSeq; XP_002174867.1; XM_002174831.2.
DR   AlphaFoldDB; B6K2T4; -.
DR   STRING; 402676.B6K2T4; -.
DR   EnsemblFungi; EEB08574; EEB08574; SJAG_03732.
DR   GeneID; 7052248; -.
DR   JaponicusDB; SJAG_03732; tif52.
DR   VEuPathDB; FungiDB:SJAG_03732; -.
DR   eggNOG; KOG1144; Eukaryota.
DR   HOGENOM; CLU_002656_1_0_1; -.
DR   OMA; EFAVMLC; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:EnsemblFungi.
DR   GO; GO:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:EnsemblFungi.
DR   GO; GO:0042256; P:cytosolic ribosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:EnsemblFungi.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblFungi.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   CDD; cd03703; aeIF5B_II; 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   ECO:0000313|EMBL:EEB08574.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT   DOMAIN          437..655
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1034 AA;  114983 MW;  661A10DFA130BEE4 CRC64;
     MGKKGKKNAY ADWEDDLGTD ISGQNAYKEP EPVEEEVEEK MEKLDLTETA PSKKKKGKKG
     KKNTPSPPVE EELEEPEEPV KTGPVELTAG VISEDEFAPI KPKKNKKKKA NKVVEPVEEE
     VDVAVPEIRI KSKKEKERER KEREKLRKKQ QQAAKKGTPS SQTPVTGTSS PLDSSATEES
     ATPKEAPVKT GKGKRKGPNV AALQKMLEQQ RAREEELKRE KEEEERRIAE EQRRLEEEER
     KKEEAKQRKK EKEKRKKEEL KAQGKYLTKK QKEAMALAER RKKQMLEAGY VVAGLAEKAE
     GEKKEKKKKK PVYDNRKRSG KSNASSASSS VILTPTTTEA QTPSETPASP VPSKLKEEEK
     AAEDEAMFDS WEAALDEPEP ASWEEQLQEE EKPTEDSKSS EDSKAKAKDG KKETKNDVDA
     IPEAEGNTDS NVSSSNMRSP ICCILGHVDT GKTKLLDNLR RSNVQEGEAG GITQQIGATY
     FPIDALKEKV KVMEKESKID YQIPGLLIID TPGHESFTNL RSRGSSLCNI AILVIDIMHG
     LEPQTIESIR LLRERKTPFI VALNKVDRLY GWHSIKDNAF QDSLKKQKKA IQREFQDRVK
     SVILQLNEQG LNAALYYENK NMGRYVSLVP TSAVSGEGVP DLLKLLITLT QSRMSENLKY
     LSKLECTVLE VKVIEGLGAT VDVVLSNGVL REGDRIILCG MSGPIITTVR ALLTPQPLKE
     MRIKSAYVHH KEIKAAMGVK ICANDLDKAV AGSRLLVVGP DDDEEELADE IMEDLEDLLG
     RIDTSGVGVS VQASTLGSLE ALLEFLKQME IPVSSVSVGP VYKKDIMRSA TMLEKAPEYA
     IMLCFDVKID KDAEELAEQM GIKIFSANII YHLFDAFTAH QKQLMEKKRE EGKGVAVFPC
     VLRTVAAFNK RDPIILGVDV VEGILRTGTP IVAVKPGPDG ENQVVELGTV ASIESNHKPV
     EKVKKGQAGA GVAVKLESNG SQILFGRQVD EKDMLYSHIS RRSIDALKDP AFRNEVSREE
     WQLIIQLKKV FGII
//
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