IF2P_PONAB
ID IF2P_PONAB Reviewed; 1220 AA.
AC Q5RDE1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3;
DE AltName: Full=Translation initiation factor IF-2;
GN Name=EIF5B; Synonyms=IF2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in translation initiation. Translational GTPase
CC that catalyzes the joining of the 40S and 60S subunits to form the 80S
CC initiation complex with the initiator methionine-tRNA in the P-site
CC base paired to the start codon. GTP binding and hydrolysis induces
CC conformational changes in the enzyme that renders it active for
CC productive interactions with the ribosome. The release of the enzyme
CC after formation of the initiation complex is a prerequisite to form
CC elongation-competent ribosomes. {ECO:0000250|UniProtKB:P39730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P39730};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site.
CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also
CC act as a transition state stabilizer of the hydrolysis reaction.
CC {ECO:0000250|UniProtKB:G0S8G9};
CC -!- SUBUNIT: Interacts with ANXA5 in a calcium and phospholipid-dependent
CC manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH90216.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR857972; CAH90216.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q5RDE1; -.
DR SMR; Q5RDE1; -.
DR STRING; 9601.ENSPPYP00000013483; -.
DR PRIDE; Q5RDE1; -.
DR eggNOG; KOG1144; Eukaryota.
DR InParanoid; Q5RDE1; -.
DR Proteomes; UP000001595; Unplaced.
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; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Hydrolase; Initiation factor; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1220
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000354072"
FT DOMAIN 629..846
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..645
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 663..667
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 702..705
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 756..759
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 824..826
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
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..417
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 488..512
FT /note="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..569
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 638..645
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 134
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GUV7"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60841"
SQ SEQUENCE 1220 AA; 138687 MW; D946A64E6A76BCE6 CRC64;
MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK
ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD
SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKIKERSRV
NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD SSFKIKTVAQ KKAEKKERER
KKRDEEKAKL RKLKEKEESE TGKKDQSKQK ESQRKSEEET VKSKVTLDTG VIPASEEKAE
TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR
EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE
ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC AAVEVMEQGV
PEKEETPPPV EPEEEEDTED AGLDDWEAMA SDEETEKVEG NTVHIEVKEN PEEEEEEEEE
EEEDEESEEE EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT
KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK LRHTHVQDGE
AGGITQQIGA TNVPLEAINE QTKMIKNFGR ENVRIPGMLI IDTPGHESFS NLRNRGSSLC
DIAILVVDIM HGGEPQKMKP TNLPKPKKCP FMVALNKIDR LYDWKKSPDS DVAATLKKQK
KNTKDEFEER AKAIIVEFAQ QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE
LTQTMLSKRL AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ
IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA YKEDEIPVLK
DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT SEVPYAGINI GPVHKKDVMK
ASVMLEHDPQ YAVILAFDVR IERDAQEMAD SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK
QEKFKHIAVF PCKMKILPQY IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS
IEINHKQVDV AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD
EMQKSDWQLI VELKKVFEII
