IF2G_CRYNH
ID IF2G_CRYNH Reviewed; 473 AA.
AC J9VR81;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE Short=eIF-2-gamma;
DE EC=3.6.5.3;
GN ORFNames=CNAG_01018;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2]
RP INDUCTION.
RX PubMed=29581526; DOI=10.1038/s41598-018-21965-y;
RA Brandao F., Esher S.K., Ost K.S., Pianalto K., Nichols C.B., Fernandes L.,
RA Bocca A.L., Pocas-Fonseca M.J., Alspaugh J.A.;
RT "HDAC genes play distinct and redundant roles in Cryptococcus neoformans
RT virulence.";
RL Sci. Rep. 8:5209-5209(2018).
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC involved in the early steps of protein synthesis. In the presence of
CC GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC step that determines the rate of protein translation. The 43S PIC binds
CC to mRNA and scans downstream to the initiation codon, where it forms a
CC 48S initiation complex by codon-anticodon base pairing. This leads to
CC the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B. {ECO:0000250|UniProtKB:P32481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC heterotrimeric G-protein composed of an alpha, a beta and a gamma
CC subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. {ECO:0000250|UniProtKB:P32481}.
CC -!- INDUCTION: Transcriptionally up-regulated in an HDA1-dependent manner.
CC {ECO:0000269|PubMed:29581526}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; CP003824; AFR95129.1; -; Genomic_DNA.
DR RefSeq; XP_012049258.1; XM_012193868.1.
DR AlphaFoldDB; J9VR81; -.
DR SMR; J9VR81; -.
DR SwissPalm; J9VR81; -.
DR EnsemblFungi; AFR95129; AFR95129; CNAG_01018.
DR GeneID; 23884764; -.
DR VEuPathDB; FungiDB:CNAG_01018; -.
DR HOGENOM; CLU_027154_0_1_1; -.
DR Proteomes; UP000010091; Chromosome 5.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Hydrolase; Initiation factor; Methyltransferase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Transferase.
FT CHAIN 1..473
FT /note="Eukaryotic translation initiation factor 2 subunit
FT gamma"
FT /id="PRO_0000449277"
FT DOMAIN 40..250
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 49..56
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 77..81
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 135..138
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 193..196
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 228..230
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 52..57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 193..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 228..230
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
SQ SEQUENCE 473 AA; 50373 MW; 3ED5F30E20682D63 CRC64;
MSAINDPIAA ASSGPSEPVQ EVQVDVTKLT ALSPEVISKQ ATINIGTIGH VAHGKSSTVR
AISGVQTVRF KNELERNITI KLGYANAKIY KCQNPDCPPP SCFKSYPSSK EAHPKCERPG
CDGRMDLQRH VSFVDCPGHD ILMATMLTGA AVMNGALLLI AGNESCPQPQ TGEHLAALEI
IGVDPKNIVI LQNKMDLVRE SEAMEHCESI KKFVEGTTAR LAPIIPVSAQ LKFNIDAVVA
AICNIAPPNY DFSADPRMVV IRSFDVNKPG AGVDELKGGV AGGSILQGVF KVGQEVEIRP
GLITRDANGV CTCRPLRSRI VSLHAEQNHL QFAVPGGLIG VGTLVDPALC RADRLLGMVM
SSVGKGPSIY VEIRAEVFLL RRLLGVKTDD SKKAKVGKLV VGETLFVNIG ASQTGGRITA
VKGGDVSIAL TTPACCEKGE KIALSRRIDK HWRLIGWGKV RSGGTLCEVV DPE
