ID A0A2K6DCR6_MACNE Unreviewed; 1221 AA.
AC A0A2K6DCR6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=EIF5B {ECO:0000313|Ensembl:ENSMNEP00000033706.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000033706.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000033706.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6DCR6; -.
DR Ensembl; ENSMNET00000058153.1; ENSMNEP00000033706.1; ENSMNEG00000040038.1.
DR GeneTree; ENSGT00940000162583; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000040038; Expressed in multicellular organism and 13 other cell types or tissues.
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; IEA:UniProtKB-KW.
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:UP000233120}.
FT DOMAIN 630..847
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..570
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 138694 MW; FEB3C4A0A629E2CC CRC64;
MGKKQKNKNE DSAKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK
ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD
SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKVKERSRV
NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD SSFKIKTVAQ KKAEKKERER
KKRDEEKAKL RKLKEKEELE TGKKDLSKQK ESQRKSEEET VKSKVTLDTG VIPASEEKAE
TPTAAEDDNE GDKKKKDKKK KKGEKEDKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR
EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE
ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC APVEVTEQGV
PEKEETPPPV EPGGKEDTED AGLDDWEAMA SDEETEKVEG NTVHIEVKEN PEEEEEEEEE
EEEEDEESEE EEEEEGESEG SEGDEEDEKV SDEKDSGKTL DKKPSKEMSS DSEYDSDDDR
SKEERAYDKA KRRIEKRRLE HSKNVNTEKL RAPIICVLGH VDTGKTKILD KLRHTHVQDG
EAGGITQQIG ATNVPLEAIN EQTKMIKNFD RENVRIPGML IIDTPGHESF SNLRNRGSSL
CDIAILVVDI MHGLEPQTIE SINLLKSKKC PFIVALNKID RLYDWKKSPD SDVAATLKKQ
KKNTKDEFEE RAKAIIVEFA QQGLNAALFY ENKDPRTFVS LVPTSAHTGD GMGSLIYLLV
ELTQTMLSKR LAHCEELRAQ VMEVKALPGM GTTIDVILIN GRLKEGDTII VPGVEGPIVT
QIRGLLLPPP MKELRVKNQY EKHKEVEAAQ GVKILGKDLE KTLAGLPLLV AYKEDEIPVL
KDELIHELKQ TLNAIKLEEK GVYVQASTLG SLEALLEFLK TSEVPYAGIN IGPVHKKDVM
KASVMLEHDP QYAVILAFDV RIERDAQEMA DSLGVRIFSA EIIYHLFDAF TKYRQDYKKQ
KQEEFKHIAV FPCKMKILPQ YIFNSRDPIV MGVTVEAGQV KQGTPMCVPS KNFVDIGIVT
SIEINHKQVD VAKKGQEVCV KIEPIPGESP KMFGRHFEAT DILVSKISRQ SIDALKDWFR
DEMQKSDWQL IVELKKVFEI I
//