ID A0A0D2H1R8_9EURO Unreviewed; 1097 AA.
AC A0A0D2H1R8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=Z517_08397 {ECO:0000313|EMBL:KIW78559.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW78559.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW78559.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW78559.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846973; KIW78559.1; -; Genomic_DNA.
DR RefSeq; XP_013282367.1; XM_013426913.1.
DR AlphaFoldDB; A0A0D2H1R8; -.
DR STRING; 1442368.A0A0D2H1R8; -.
DR GeneID; 25307887; -.
DR VEuPathDB; FungiDB:Z517_08397; -.
DR HOGENOM; CLU_002656_1_0_1; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000053029; 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:KIW78559.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT DOMAIN 503..721
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..485
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 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 120664 MW; F9BAF1D9B6666952 CRC64;
MAPKKKGGKK QADDWENELG ETVDPIAQAT EDAKRAETEN DAAEEVNGGG GLMAALRKNK
DRRAKKGKPV VNDFVEGEDA DGVTPVQPEN DLHAKAPTEA TFDDEDDDVF AGNAHKKTKG
GKKQQEKDEQ PANADGEDAG EGVKSKKEKE REKKEREKQR KKEQAAKKKT VAPASGPKVE
EAKPAAPEKT EAPVAAPEKE DKSGKKRKIP AHLAAIQKQQ EALAKQREEQ AKLEAAERAA
EEERLRQEAE EEKKKAEARQ RKKEKEKEKK EQLKKEGKLL SEADRKRKQQ QELRLKQLLE
SGVKVAGLSE GVEEKKKPAV DKKRKGPKKE EIDLEAAAER ARQEAEAAEA ERQRLAKEAE
EAAAAAAAAE ADAAKQEESS ELDDWEKAAD EDLKESWDAE SSDEDAGSAK GASKSAANGS
ASKTTGTNGA VTKPTTSSSL PIRDSGRPPK ERPIESDTES EESSSDEEKT ATQRALAKKK
AEAAARRAKA HEEALAARSK DNLRSPICCI LGHVDTGKTK LLDKIRQTNV QEGEAGGITQ
QIGATYFPVD ALKQKTAVVN KDGKFEFKVP GLLVIDTPGH ESFSNLRSRG SSLCNIAILV
VDIMHGLEPQ TLESMKLLRD RKTPFIVALN KIDRLYGWKK IDNNGFQDSL AFQSKGVVAE
FESRLAETKL AFAKEGFNSE LFYENKDMRR YVSLVPTSAH TGEGIPDLLK LLVSLTQERM
TSSLMYLSEV ECTVLEVKVI EGLGTTIDVV LSNGVLHEGD RIVLCGTDGP IATNIRALLT
PAPLKELRLK SQYVHNKECK AALGVKIAAN DLEKAIAGSR LLVVGPEDDE DDLMDDVMAD
LQSLLSKISK DNRGVSVQAS TLGSLEALLE FLKQSKIPVA NIAIGPVYKR DVMMAGTMLE
KAREYAVMLC FDVKVDKEAQ QYAEENGIKI FTADIIYHLF DAFTKHMEEL REKKKEESKM
HAVFPCVLSP IQVFNKKDPI VVGVDVVEGA LRPLTPIAVV KTNPVTGVKE IITLGRVASI
EREHKAIPIC KKGQPSVAVK IEGPNQPMYG RQLEDKDTLY SLISRRSIDT LKEFYRDEVT
RDEWALLKKL KPIFDIP
//
