ID G9MYS3_HYPVG Unreviewed; 1054 AA.
AC G9MYS3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 ORFNames=TRIVIDRAFT_112883 {ECO:0000313|EMBL:EHK20252.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK20252.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK20252.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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}.
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:EHK20252.1}.
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 EMBL; ABDF02000080; EHK20252.1; -; Genomic_DNA.
DR RefSeq; XP_013954450.1; XM_014098975.1.
DR AlphaFoldDB; G9MYS3; -.
DR STRING; 413071.G9MYS3; -.
DR EnsemblFungi; EHK20252; EHK20252; TRIVIDRAFT_112883.
DR GeneID; 25786912; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_112883; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; G9MYS3; -.
DR OMA; EFAVMLC; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000007115; 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; 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:UP000007115}.
FT DOMAIN 460..678
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..424
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1054
FT /evidence="ECO:0000313|EMBL:EHK20252.1"
SQ SEQUENCE 1054 AA; 116214 MW; D21C1E5D78B27FB4 CRC64;
MAPKKKGNKN AQEDWEAELG ESIAPAGDAP PAAEQNGEDD EAAGGGGLMA IMRKNKEKRK
KKGIVDEEPA PEPVEEDLSA KAPVEASLDD DEFALPQKKG KGGKGKPAPA AAAKDDKDDL
EEPGRILTKA EKEKLKKERE KQRKKEQAAK KKTPAPAKAP EPAKTTAKDE PAAEPAAAPA
PAPAETGGKK KKIPAHLALI QKQQEELRRR QEEAVRLEAE AKALAEEEEK RLAEENKRKE
EQKALKKQRE KERIEQLKKE GKFLTKAQKE EKARNELKLQ QMLAAGIKIG PQEEEGAPKK
KVVYDSKKKR GKNDKKDEEA ALAEAAERAR LQAEKALKEA EEKAAKEKAE AEAKAAASKA
ARESDVEDDW EAAANSEGED VKDSWDADSD EEAEKKAAAK DKKEEEDEEE EDESESEEED
SEDEAVSKAQ QLEAQRKKEA AERREKAHQA ALAARSKDNL RSPICCILGH VDTGKTKLLD
KIRQTNVQEG EAGGITQQIG ATYFPVDAIR QKTAVVNKDS EFEFKVPGLL VIDTPGHESF
SNLRSRGSSL CNIAILVVDI MHGLEPQTLE SMRMLRERKT PFIVALNKID RLYGWKKVDN
NGFQDSLALQ SKAVQNEFKN RLEQTKLAFA EQGFNSELFY QNKSMAKFVS LVPTSAHTGE
GIPDMLKLIL QLTQERMVGS LMYLSEVQAT VLEVKAIEGF GMTIDVILSN GILREGDRIV
LCGTEGAIVT NIRALLTPAP LRELRLKSAY VHNKEVKAAL GVKISAPGLE GAIAGSRLMV
IGPDDDEDDI IDEVESDLAN LLSRVETSGR GVSVQASTLG SLEALLDFLK DCKIPVANVG
IGPVYKRDVM QCGIMLEKAP DYAVMLCFDV KVDKEAQQYA EDQGIKIFTA DIIYHLFDNF
TKHMDEMLEK KKEESKMLAV FPCVLKPVAI FNKTAPIVIG VDVVEGQLKI NAPIAAVKTN
PTTNAKEVVA LGRVTSIERD HKQIPVCKKG QPSVAVKIEM GGHQPIYGRH LEEADTLYSQ
ISRASIDTLK EFYRKEVTNE EWQLIIKLKP LFDI
//
