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Database: UniProt
Entry: A0A2B7WRS5_9EURO
LinkDB: A0A2B7WRS5_9EURO
Original site: A0A2B7WRS5_9EURO 
ID   A0A2B7WRS5_9EURO        Unreviewed;      1068 AA.
AC   A0A2B7WRS5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=GX51_06391 {ECO:0000313|EMBL:PGG99197.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGG99197.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGG99197.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGG99197.1,
RC   ECO:0000313|Proteomes:UP000224080};
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:PGG99197.1}.
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DR   EMBL; PDNC01000104; PGG99197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7WRS5; -.
DR   STRING; 2060905.A0A2B7WRS5; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000224080; 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:PGG99197.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224080}.
FT   DOMAIN          474..692
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..469
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        27..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  117891 MW;  896AE61193F90ECA CRC64;
     MAPKKKGSKK QQEDWEAELG ETIPPTTGTD DAATGEDGND AANNANDNNN NDDDGMSGGL
     LATLKKNRNK KAKKGKGGDN DFVEGEDPTA AAAAAESKQP QEASFEDDED DVFSGTAAAR
     QRAKDKAAAM KEKAKEAEEE GGKLKSKKEK EKEKKEREKQ RKREQAAKKK ATTTPAAAPA
     TNAEPAKPAV EEKPAAPAAP AAAPAADTAG KKRKLPAHLA AIQKQQEALR KQQEEIARLE
     AEEKAAAEEH QRRLEEEERK KEEARQRKKE KEREKKEQLR REGKLLTKAQ KEAQQRNELR
     KQQMLAAGAV VPGLEEPLEK KKPVYENRKK RPVKKQEDDL EAAAARAEAQ RLELEAEKAK
     KAEEERKRAE EKAAAKAAAQ AAAKEAEDDD IKESWDMSSD EEGGEKREAD QDEESGANGA
     AKGETSPEES EEESSEDEEA TAAQRALAQK KAEAAERRRR QHEEALAARS TDNLRSPICC
     ILGHVDTGKT KLLDKVRQTN VQEGEAGGIT QQIGATYFPT ESLKQKTAVV NKDGSFEFKV
     PGLLVIDTPG HESFSNLRSR GSSLCNIAIL VVDIMHGLEQ QTLESMRLLR DRKTPFIVAL
     NKIDRLYGWK KIDNNGFQDS LALQSKGVQN EFRDRVEKTK LAFAEQGFNS ELYWENKSMA
     RNVSLVPTSA HTGEGVPDML KLLVSLTQER MTKQLMYLTE VECTVLEVKV IEGLGTTIDV
     VLSNGVLREG DRIVMCGLNG AIATNIRALL TPAPLKELRL KSQYVHNKEV RAALGVKIAA
     NDLEHAIAGS RLLVVGPNDD EEDLEDEVMS DLENLLSKVS KDNRGVSVQA STLGSLEALL
     EFLRASKIPV ANISIGPVYK RDVMRAGTML EKAKQFAVML CFDVKVDKEA QAYADEVGIK
     IFTADIIYHL FDDFTKHMEQ IAEQKKEESK LLAVFPCVLN TVAVFNKKDP IVIGVDVVEG
     SLRLLTPIAA VKANPVTGVK EIINLGRVQS IEREHKQIPL CKKGQPSVAI KIEGPNQPLY
     GRQLEEKDTL YSLISRPSID TLKEFYRADV SMDEWVLIKK LKPLFDIP
//
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