ID S9VTP1_SCHCR Unreviewed; 446 AA.
AC S9VTP1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN ORFNames=SPOG_01414 {ECO:0000313|EMBL:EPY49529.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY49529.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY49529.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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:0000256|ARBA:ARBA00001874};
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DR EMBL; KE546995; EPY49529.1; -; Genomic_DNA.
DR RefSeq; XP_013025556.1; XM_013170102.1.
DR AlphaFoldDB; S9VTP1; -.
DR STRING; 653667.S9VTP1; -.
DR EnsemblFungi; EPY49529; EPY49529; SPOG_01414.
DR GeneID; 25035743; -.
DR eggNOG; KOG0466; Eukaryota.
DR HOGENOM; CLU_027154_0_1_1; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 1512042at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:EnsemblFungi.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:EnsemblFungi.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR GO; GO:0005840; C:ribosome; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:1990856; F:methionyl-initiator methionine tRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:EnsemblFungi.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:EnsemblFungi.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IEA:EnsemblFungi.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EPY49529.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT DOMAIN 21..227
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 446 AA; 48508 MW; 3561E510A06318D5 CRC64;
MAENLDISEL SPIHPAIISR QATINIGTIG HVAHGKSTVV KAISGVHTVR FKNELERNIT
IKLGYANAKI YKCSNTECAR PGCFRSYPSG KEDNPPCEIC GTPMNLVRHV SFVDCPGHDI
LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM QLKHIIILQN KVDLIREAAA
EEHYQSILKF IKGTVAENSP IVPISAQLKY NIDAILEYIV KKIPIPVRDY TTAPRLIVIR
SFDVNKPGAE VEDLKGGVAG GSILSGVLRL GDEIEIRPGI VTKDEEGHIK CQPIFSRIVS
LFAEHNDLKI AVPGGLIGVG TTVDPTLCRA DRLVGQVLGS KGNLPEVYTE LEINYFLLRR
LLGVKSGDKN TTKVQKLAKN EVLMVNIGST STGGRVMMVK ADMAKILLTA PACTEIGEKV
ALSRRIEKHW RLIGWAKVVE GKTLQV
//
