ID B8MFI6_TALSN Unreviewed; 1064 AA.
AC B8MFI6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 ORFNames=TSTA_017940 {ECO:0000313|EMBL:EED16720.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED16720.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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 EMBL; EQ962656; EED16720.1; -; Genomic_DNA.
DR RefSeq; XP_002483954.1; XM_002483909.1.
DR AlphaFoldDB; B8MFI6; -.
DR STRING; 441959.B8MFI6; -.
DR GeneID; 8109050; -.
DR VEuPathDB; FungiDB:TSTA_017940; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; B8MFI6; -.
DR OMA; EFAVMLC; -.
DR OrthoDB; 169393at2759; -.
DR PhylomeDB; B8MFI6; -.
DR Proteomes; UP000001745; 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 ECO:0000313|EMBL:EED16720.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 470..688
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 117669 MW; 67E2994B5066AB37 CRC64;
MAPKKKGNKR QEEDWEAELG ESVPAATETP AEANGDAAAN GDDDQMGGGL LAALKKNRSK
KAKKGKALDN DFVEGEDPTQ ADTNGDAAVD LSSKAPQEAT FDDEDDVFTG KPKKGKAAPA
PPKLEPAEEA EEGGKVKSKK EKEKEKKERE KQRKKEQAAK KKAATPAAPV KEEPVKAAPE
VKAEPTPAPA AKIEPAGKKK KIPAHLAAIQ KQQEALRKAQ EEEERLRAEA EAAEAERIRK
LEEEEKKKEE ARQRKKEKER EKKEQLRKEG KLLTKAQKEA KERNELRMKQ MLAAGVGHVA
GLEERGEPSE KKKMVVTNRK KKGPKKDEVD LEAAAAAARA QREAEDEKRR KEEEDLAKAQ
AAKDEADLED DWEAAAKAEV GDDVKDSWDA ESDEEQQDNK QVDQEQKTAK QANGTAKSED
SESEEETSSD EEDEEATAAQ KAIAQRKAEA AERRKKQHEE ALAARSKDNL RSPICCILGH
VDTGKTKLLD KIRQTNVQEG EAGGITQQIG ATYFPVDALK QKTAVVNRDG SFEFKIPGLL
IIDTPGHESF SNLRSRGSSL CNIAILVVDI MHGLEPQTLE SMRLLRDRKT PFIVALNKID
RLYGWKKIDN NGFQESLAMQ SKGVINEFRS RVEQTKLAFA EQGFNSELYW ENKSMARNVS
LVPTSAHTGE GIPDMLKLLT TLTQERMTNS LMYLSEVECT VLEVKVIEGL GTTIDVVLSN
GILREGDRIV LCGLNGPIAT NIRALLTPAP LKELRLKSQY VHNKEVKAAL GVKIAANDLE
HAIAGSRLMV VGPDDDEEDL EEEVMSDLEN LLSKVSKDQR GVSVQASTLG SLEALLEFLR
VSKIPVSNIS IGPVFKRDVM LAGTMLEKGL KEYAVMLCFD VKVDKEAQAY ADDVGVKIFT
ADIIYHLFDD FTKHMAELNE QRKEESKMHA VFPCVLKTVA VFNKKDPIVV GVDVVEGSLR
LLTPIAVVKQ NAAGQKEIIQ LGRVASIERD HKAIQVCKRG QPSVAVKIDG ANQPAYGRQL
EESDTLYSEI SRKSIDTLKE FYRSDVTMEE WALIKKMKPL FDIP
//