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Database: UniProt
Entry: V8NV23_OPHHA
LinkDB: V8NV23_OPHHA
Original site: V8NV23_OPHHA 
ID   V8NV23_OPHHA            Unreviewed;      1187 AA.
AC   V8NV23;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-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};
DE   Flags: Fragment;
GN   Name=EIF5B {ECO:0000313|EMBL:ETE65518.1};
GN   ORFNames=L345_08720 {ECO:0000313|EMBL:ETE65518.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE65518.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE65518.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE65518.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE65518.1}.
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DR   EMBL; AZIM01001864; ETE65518.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8NV23; -.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
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   ECO:0000313|EMBL:ETE65518.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT   DOMAIN          596..813
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          25..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..474
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..526
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE65518.1"
SQ   SEQUENCE   1187 AA;  135214 MW;  C0C37A3072E0F717 CRC64;
     MRLYPLRRVL KTEDDILKEL EELSLETQGG RVEKEPVVAK VENENEELGL SKQDKKKKGK
     NKKASLEEED GSEETEEKEK KSKKSLKPKK ELLSESDDDD DDFDLKKRRG KVQKSGNKHE
     FSEEDETGIV KKSKELAHPV SSGESEDELD EGSQAKKGQK KNQKVKLVAE TESGDDLNDS
     SFKIKTVAQK KAEKKEREKK KREEEKAKLR KQKEKEDLEA NKEQAKMKKT DKRTASDQLS
     TSATLEKGET PEAAEVNDNE GEKKKKDKDK KKKKGEKDEK EKEKKKGPSK ATVKAMQEAL
     AKLKEEEERA KREEEERIRQ LEELEAKRKE EERLEQEKKE RKKQKEKERK ERLKKEGKLL
     TKSQRESKAR AEVTLKLLQA QGVEVPSKDS IPKKRPIYED KKKKKQQQQE SREGDKCCLW
     ITVNTETDIT ELASPVEEAA EIVVPEQEEI NLQAEPVSEE KEEEPEDGGL DDWEAMASDE
     EREKERKTVH IEVKEQNDED EDEDEDEDED MEESEEYEEG ESEGSEEEKT SDEKESDPQA
     SAKHSVEKKL NKEISSDSES DSDDDRTKEE RSYDKAKRRI EKRRIENNKN ANTEKLRAPV
     ICVLGHVDTG KTKILDKLRH THVQDSEAGG ITQQIGATNV PLEAINEQAK MVKTFDRETV
     KIPGMLIIDT PGHESFSNLR NRGSSLCDIA ILVVDIMHGL EPQTIESINL LKSKKCPFIV
     ALNKIDRLYD WKKSPDTDVA VTLKKQKKNT KDEFEERAKA IIVEFAQQGL NAALYYENKD
     PRTFVSLVPT SAHTGDGMGS LIALLVELTQ TMLNKRLAHC EELRAQVMEV KALPGMGTTI
     DVILINGRLK EGDTIIVPGV EGPIVTQIRG LLLPPPMKEL RVKNQYEKHK EIIAAQGVKI
     LGKDLEKTLA GLPLLVAYKE DEIPVLKDEL IHELKQTLNA IKLEEKGVYV QASTLGSLEA
     LLEFLKTSEV PYAGINIGPV HKKDVMKASV MLEHDPQYAV ILAFDVRIER DAQEMADSLG
     VRIFSAEIIY HLFDAFTKYR QDYKKQKQEE FKHIAVFPCK MKILPQFIFN SRDPIVMGVV
     VDAGQVKQGT PICVPSKNFI DIGIITSIEI NHKQVDVAKK GQEVCVKIEP IPGEAPKMYG
     RHFEATDILV SKISRQSIDA LKDWFRDEMQ KSDWQLIVEL KKVFEII
//
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