ID A0A0C9YBH5_9AGAR Unreviewed; 1212 AA.
AC A0A0C9YBH5;
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=K443DRAFT_673197 {ECO:0000313|EMBL:KIK07617.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK07617.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK07617.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK07617.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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; KN838546; KIK07617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YBH5; -.
DR STRING; 1095629.A0A0C9YBH5; -.
DR HOGENOM; CLU_002656_1_0_1; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000054477; 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:UP000054477}.
FT DOMAIN 613..831
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 132742 MW; ABC640999B8C00CE CRC64;
MPPKNKGKKA KKGDDDFWDK AGETVEPQKL ASPPDDVEET FEKQSSLSVS GFSALSMADN
TPAEVDDEDF GGLMSVLKAS TAKSKKDKKK NKTSEPVNGL VDTADADEAA PTISKQPQQV
TAEDMADEEW GPVKEKKKKD KKGKGKKGKA GPEEEEEEEE KPTAEAAATS EAPPAVSEKN
NDDENNDDAG DDIDEPGTKI LSKKEKEKLK KEREKAKKKA QVAAKKAAEG VEPAAPPPAA
AVEPAKADEK DEEEGEEVAG GKADAKKKKK KKGKKDDDPP APAPAPAPGK KKGGISALKA
IMEEKKRLEE EARRLAEEER KRIEEEERRL EAEERQKEEE KQRRKEKEKA KREIAKKEGR
LLTKKQREEK QMAEIRKQAL LASGVQIEGL QQQSGNGPPA TKKVVYGNRK KKGPGAKDAS
PAPESRPRSP ELASPTLPVA EEVKPNVDED LKSDWEASSD EETKAAAGVK DSWDASSDEE
EASPEPAKPS EKLDVKAPSS KPIQDKPKPP LTKPTPKVQP SVKGAPKPVI SKVEDAKPPS
KEEEETSSSG LESEDDSGDS EGSDSDDDSE DESSSDEELT SAQKMAAQRK AEAAERRAKA
HELALAARNK DDLRSPICCI LGHVDTGKTK LLDKIRQTNV QEGEAGGITQ QIGATYFPVD
AIKTKTAVLN KEGQQKYKIP GLLVIDTPGH ESFTNLRSRG SSLCNIAILV VDIMHGLEAQ
TLESLRLLRD KKTPFIVALN KIDRIYGWTP TPDGAFRESL EKQSRSVQRE FEDRVTKTIL
AFAEEGLNAC LYYENKSFAR NVSLVPTSAI TGEGVPDMIL LLVNLTQQRM SDRLMYLSEL
ECTVLEVKVI EGLGTTIDVV LSNGILREGD RIVVCGLNGP IVTQVRALLT PQPLREMRIK
SVYVHHKEVK AALGVKVTAP DLEKAIAGSR LLVVGPDDDE EDLKEEVMSD LTSLLNNIDK
SGRGVCVQAS TLGSLEALLD FLKSSKIPVS GINIGPVYKR DVMRAGTMLE KAKELACILC
FDVPIDKDAE RLAEEMGIRL FKADIIYHLF DSFKAYNQEI TEAKRRDAAP QAVWPCRLKI
IANFCKRDPI ILGVDILDGT LRVGTPLAVV KIDPVTGKKD IIDLGKITSL EINHKNQEIV
KKSQAGGGVA VKIEHAVYQS AKMFGRHFDE KDELLSHITR QSIDVLKTSF KADVPNEEWL
LIRALKPRFN IP
//
