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Database: UniProt
Entry: A0A2B7X4J3_9EURO
LinkDB: A0A2B7X4J3_9EURO
Original site: A0A2B7X4J3_9EURO 
ID   A0A2B7X4J3_9EURO        Unreviewed;       984 AA.
AC   A0A2B7X4J3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Translation initiation factor aIF-2 {ECO:0000313|EMBL:PGH03780.1};
GN   ORFNames=AJ80_08650 {ECO:0000313|EMBL:PGH03780.1};
OS   Polytolypa hystricis UAMH7299.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX   NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH03780.1, ECO:0000313|Proteomes:UP000224634};
RN   [1] {ECO:0000313|EMBL:PGH03780.1, ECO:0000313|Proteomes:UP000224634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH03780.1,
RC   ECO:0000313|Proteomes:UP000224634};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PGH03780.1}.
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DR   EMBL; PDNA01000207; PGH03780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7X4J3; -.
DR   STRING; 1447883.A0A2B7X4J3; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000224634; 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; 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   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; 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   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:PGH03780.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224634}.
FT   DOMAIN          470..688
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..452
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        128..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..434
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   984 AA;  108319 MW;  2A6A9366AEBD29DB CRC64;
     MAPKKKGGKK QQDDWEADLG ESITPTNEAA QDASPPADDN AAGEEDGMGG GLLAALKKNR
     SKKAKKGKVV NDFVEGEDAA DGNTPDGEGT ATPVDLASKA PQEASFDDEE EDVFSGNAKK
     GKQAAKGGNK KAQKDEEEGN TVKSKKEKEK ERKEREKQRK REQAAKKKSA TPAPAPTPKA
     EAKPVAEAKP ADAPADESAG KKRKVPAHLA AIQRQQELLR QQQEEEARRT EEEKRLEAEF
     KQKLEEEEQK KEEARQRKRE KEREKKEQLR KEGKLLTKAQ REAKERNELR MKQMLAAGAT
     VAGLEAPTDE KKKPVYDNRK KRAPRKQEEV DLEAAAARAE EERKAAEEEK LKREAEEKAR
     AEAEAAAAAA AAAEESDDDV KDSWDMDSDQ EAEEKASKKT KEVVVDGHAK PGANGAAADG
     EEGESEEESE SEDEESTATQ RAIAQRKAEA AERRKKQYEE ALAARSKDHL RSPICCILGH
     VDTGKTKLLD KVRQTNVQEG EAGGITQQIG ATYFPVDALK QKTAVVNKDG TFEFKVPGLL
     IIDTPGHESF SNLRSRGSSL CNIAILVVDI MHGLEPQTLE SMRLLRDRKT PFIVALNKID
     RLYGWKKIDN NGIQDSLAFQ GKGTQAEFRD RVEKTKLAFA EQGFNSELYW ENKSMARNVS
     LVPTSAHTGE GVPDLLKLLL QLTQERMTNS LMYLSEVECT VLEVKVIEGL GTTIDVVLSN
     GVLREGDRIV LCGLNGPIAT NIRALLTPAP LKELRLKSQY VHNKEVKAAL GVKIAANDLE
     QAIAGSRLLV VGPDDDEEDL EEEVMSDLEN LLSRVSKDNR GVTVQASTLG SLEALLEFLR
     VSKIPVCNIS IGPVFKRDVI RCSTMLEKAK QFAVMLCFDV KVDKEAQAYA DEMGIKIFTA
     DIIYHLFDDF TKHMEEVALQ KKEENKLLAV FPCVLNPVAV FNKTNPIVVG VDVVEGALRL
     LTPIVAVKQN PVTGAKEIIN LGRV
//
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