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Database: UniProt
Entry: A0A0M3I8S6_ASCLU
LinkDB: A0A0M3I8S6_ASCLU
Original site: A0A0M3I8S6_ASCLU 
ID   A0A0M3I8S6_ASCLU        Unreviewed;      1215 AA.
AC   A0A0M3I8S6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 2.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE   AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001378001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0001378001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (MAY-2016) 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}.
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DR   WBParaSite; ALUE_0001378001-mRNA-1; ALUE_0001378001-mRNA-1; ALUE_0001378001.
DR   Proteomes; UP000036681; Unplaced.
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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          640..862
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          964..1023
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        15..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..519
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..602
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1215 AA;  136829 MW;  42749D0E821E40F9 CRC64;
     MQKYSQFVIF QLGSDDESTD KESASDSANE KPVEKVAVPT RKEQKKGKEA KKDESSDQVA
     KETNATVKAK ETGKGKAKKG KKSAKEDEDL DALLADLDKP IERPIGKGKK KGAAKEEPTR
     ETNTAAVVEP EITPAFEAGD LDAHHQGDAK AEEEGDAAAK KKDKKKKKKK GGAEKEKSEE
     PVTTQEVQRE LALQEDKGEQ PNEQEAMKEE QLDGEXVRIN EAFEDSKKRD KEAGDLDAHQ
     QEDAKAEEEG DAATKKKEKK KKKKKGGAEK EKSEEPVTTQ EVQGELALQE DKGEQPNEEE
     AMKEEQLDGE AAEGGEESAA DKKKEKKKKK EKEKKAKEGD KKETKKKKHV DLIKQLLREK
     QEAEERLLRE QREEEERLAA IQRAKEEEER LAREKKEREK QRKKERDERL KAEGKYLTPA
     QKEKLRKQQA MLASMNVILP AALREGGQES APAKRPVYGK KKQRRGQQQE NKGSTPDSSA
     QPSEVPSREI SVEPKKPKIE EEKVADSWDD LIVDEKPQEV PDDWEQESEE RYEKLENESE
     KVTAPNEERN ATAEVKKTST DVREVPRVEK EDEAESSSEG ESEESSSEEE SSEEEEEESS
     EDEQTTRESK EQLKERVRAR LKANFKRKEA AEAKRTVDDL RAPVICVLGH VDTGKTKMLD
     TIRRTNVQDG EAGGITQQIG ATQVPAAAIK ERTKMVREFD GDKMKIPGFL IIDTPGHESF
     SNLRSRGSSL CDYAILVVDL MHGLEQQTLE SLKLLRKRET PFVIALNKID RLYDYESNPR
     KDVYQHLKSQ PINAQLQFKE LKDKVVLQFA EQFAEQGVNV ALANENPDPN EYVSMVPTSA
     FLGDGIGNLM AYIVIESQTR LARKLAFCEE LECIVMEVKS LPGLGTTIDV ILVNGTLRVG
     DVIVLTGTEG AIMTQIRELL MPQPLRELRV KNAYEHFQSI KAAQGVKILA KGLEKALAGL
     PIFVANKEDE LDVLKEESEA QLSKALMAIK KKPEGVYVQA STLGSLEALL EFLKKAAAML
     ERKEEYACIL AFDVRVDRDA EQFAATEGVR IFSADIIYHL EESFLKYREE LRLRRRRENE
     HLAIFPCKLR ILPQHVFNAR NPIVVGVSVE AGQLKRGTPL CVPSKDCIFI GTVSSIERNH
     EQVDLAKTGD EVCVKIENTT GEAPKLYGRH FNHEDALVSR ISRETIDVCK AHFRDDLSKA
     DWQLIVQLKK LLDIM
//
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