ID Q5A6S3_CANAL Unreviewed; 480 AA.
AC Q5A6S3;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Translation initiation factor eIF2B subunit gamma {ECO:0000256|ARBA:ARBA00044196};
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit gamma {ECO:0000256|ARBA:ARBA00044229};
GN Name=GCD1 {ECO:0000313|CGD:CAL0000190232,
GN ECO:0000313|EMBL:AOW31137.1};
GN OrderedLocusNames=CAALFM_CR03990CA {ECO:0000313|EMBL:AOW31137.1},
GN orf19.8111 {ECO:0000313|CGD:CAL0000190232};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW31137.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW31137.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW31137.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW31137.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000256|ARBA:ARBA00007878}.
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DR EMBL; CP017630; AOW31137.1; -; Genomic_DNA.
DR RefSeq; XP_717344.1; XM_712251.1.
DR AlphaFoldDB; Q5A6S3; -.
DR SMR; Q5A6S3; -.
DR STRING; 237561.Q5A6S3; -.
DR EnsemblFungi; CR_03990C_A-T; CR_03990C_A-T-p1; CR_03990C_A.
DR GeneID; 3640965; -.
DR KEGG; cal:CAALFM_CR03990CA; -.
DR CGD; CAL0000190232; GCD1.
DR VEuPathDB; FungiDB:CR_03990C_A; -.
DR eggNOG; KOG1462; Eukaryota.
DR HOGENOM; CLU_016743_3_0_1; -.
DR InParanoid; Q5A6S3; -.
DR OMA; CDFITDI; -.
DR OrthoDB; 161736at2759; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IBA:GO_Central.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:1903574; P:negative regulation of cellular response to amino acid starvation; IEA:EnsemblFungi.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblFungi.
DR CDD; cd04652; LbH_eIF2B_gamma_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR45989; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR PANTHER; PTHR45989:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:AOW31137.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559}.
FT DOMAIN 7..160
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT REGION 318..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..472
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 54321 MW; 3D9E8643CC94FB41 CRC64;
MEFTAVIVCG KGKALTPFSQ ARSTGIPKPL LPIANKPMVQ YVLDWCLQAN FSRIIVLFEK
EDESSGVLEQ TIKRYQEEKE KTNTNKNESH VSIDVIPYNC ENNGLILYKL YELYSENKVS
NNNFIILPCD LITNLPPQVI IEAYRNKNDS DLGLVIAYKN QLDIEDKKAK IFPQSYTIYS
DTDENGNESP MFLDTYSQAD IEFHQALSIR TQMCWRYPAA TVSNKLLNSG IFLGSCSQIF
SVFDEQKDKF TESYFEKRSL MKIVRDLARR SWKHALHQAS VGFFIVPKQA TFFRCNNLPV
LMEANRYFMK KQAIAKSASQ NTQAPNKQDK QSGAHVGNDS LVGENTELGE KTNVKRSVIG
SNCKIGKKNK ITGCLILDNV EIHDDVTLEN CIIGHDVIIQ GKCKLTNCNV ESTNEVAHNT
QAKNSNLLCL TLEGLVNEDD QYGDDSDDEE DSEEYDSTDD EDESEFEDEY TGNEDGLFAY
//
