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Database: UniProt
Entry: B6K0P3_SCHJY
LinkDB: B6K0P3_SCHJY
Original site: B6K0P3_SCHJY 
ID   B6K0P3_SCHJY            Unreviewed;       573 AA.
AC   B6K0P3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Elongation factor 1 alpha like protein {ECO:0000313|EMBL:EEB07514.2};
GN   Name=hbs1 {ECO:0000313|JaponicusDB:SJAG_02601};
GN   ORFNames=SJAG_02601 {ECO:0000313|EMBL:EEB07514.2};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB07514.2, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB07514.2, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
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DR   EMBL; KE651166; EEB07514.2; -; Genomic_DNA.
DR   RefSeq; XP_002173807.2; XM_002173771.2.
DR   AlphaFoldDB; B6K0P3; -.
DR   STRING; 402676.B6K0P3; -.
DR   EnsemblFungi; EEB07514; EEB07514; SJAG_02601.
DR   GeneID; 7047708; -.
DR   JaponicusDB; SJAG_02601; hbs1.
DR   VEuPathDB; FungiDB:SJAG_02601; -.
DR   eggNOG; KOG0458; Eukaryota.
DR   HOGENOM; CLU_007265_3_2_1; -.
DR   OMA; CFETEHR; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:1990533; C:Dom34-Hbs1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IEA:UniProt.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:EnsemblFungi.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd16267; HBS1-like_II; 1.
DR   CDD; cd04093; HBS1_C_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; IPR015033; HBS1-like_N.
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; PTHR23115:SF288; ELONGATION FACTOR 1 ALPHA-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF08938; HBS1_N; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Elongation factor {ECO:0000313|EMBL:EEB07514.2};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:EEB07514.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          158..384
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          117..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          12..39
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        117..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  63962 MW;  7D11AADB95E82CC4 CRC64;
     MSRHKDLKNL DLNDYEDEFE AEEELTEDQE EAYREAIEQV QTALEGTNIP FQEIKDTVWY
     YYFDVNKSVN YLLSKAIKAK EKDAKKTPVA QSQTKENSTK DVTAAVKKVT ISQPSNALRK
     KQVIPQTTKT ESEHAQIPQK KEPKLLDIPS LYEKEHEKPS IHLVVSGHVD SGKSTMIGRL
     LYEVGMVDER SMQKLKQSAA NAGKGSFSYA WLLDSTDEER ARGVTMDVAD TTFESSKHIY
     QIGDAPGHKD FISGMIAGAY LSDYAILVVD ASPNNFERGF FSNGQTREHA YLLRALSVKG
     IAVCVNKLDT VDWSYERFIA IKENILDFLV SKVGFKETMV HIVPVSGLSG ENLIKRDEPK
     LLSWYNGPTL MNILDDFVPP TKPVKASLRI TVNDTYRSAK GVCVQGRVES GNVQNNQVLF
     NVSTNSDAYV KSIIRNGHPH DWSVAGDNIT MQLTDIDANE IRPGDILTTT SQPVKKTKSF
     IAEIQTFDLL RPILSGATLV LHRGRLSAPV VIKLQSVNGK KVRHITSRKT AIVKFTFLDG
     SYPICTVDDC KTLGKIILRR EGDTVAAGVI RKV
//
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