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Database: UniProt
Entry: A0A0L6UA43_9BASI
LinkDB: A0A0L6UA43_9BASI
Original site: A0A0L6UA43_9BASI 
ID   A0A0L6UA43_9BASI        Unreviewed;      1127 AA.
AC   A0A0L6UA43;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-OCT-2025, entry version 35.
DE   RecName: Full=Ribosome assembly protein 1 {ECO:0000256|ARBA:ARBA00068031};
DE   AltName: Full=Elongation factor-like 1 {ECO:0000256|ARBA:ARBA00081809};
GN   ORFNames=VP01_815g6 {ECO:0000313|EMBL:KNZ45403.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ45403.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ45403.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ45403.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); 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:ARBA00048548};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNZ45403.1}.
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DR   EMBL; LAVV01013671; KNZ45403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6UA43; -.
DR   STRING; 27349.A0A0L6UA43; -.
DR   VEuPathDB; FungiDB:VP01_815g6; -.
DR   OrthoDB; 364892at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:TreeGrafter.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR   GO; GO:0042256; P:cytosolic ribosome assembly; IEA:TreeGrafter.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd04096; eEF2_snRNP_like_C; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16268; EF2_II; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   FunFam; 3.30.70.240:FF:000006; Elongation factor like GTPase 1; 1.
DR   FunFam; 3.90.1430.10:FF:000002; Elongation factor like GTPase 1; 1.
DR   FunFam; 3.40.50.300:FF:000746; Ribosome assembly protein 1; 1.
DR   FunFam; 3.30.70.870:FF:000002; Translation elongation factor 2; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR056752; EFL1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF25118; EFL1; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT   DOMAIN          8..301
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          197..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1127 AA;  125155 MW;  C3096C1004FAA0AF CRC64;
     MSSATSPHQI RNVCILAHVD HGKSSYADSL LAANNIITPK MAGKLRYLDS RPDEQERGIT
     MKSSAVSLAY ATLRPDPNGI EQLQQFRINL IDTPGHVDFT TEVSTASRLC DGALVLVDVV
     EGVCTQTISV LRQVWNEQLK PILVINKVDR LIVELRLSPT EAYYHLVRLV EQVNAIMGSF
     FFTDRIEQDL RWREAAEQSQ LESKPTPEKP FTETDDQDIY FDPTKGDVIF SSAIDNWSFN
     IASFAHIWSK KLGIEKAKLE SCLWGDFFFD PKSKKVLSKK QASLKGSSLK PMFVQFVLDN
     LWAVYDSVVL NPDTTKTEKI IQSLGLKIRL QDLKSKDSKN LLLAICSQWL PISNTTFRTI
     VAKVPDPITS QSRRLPKMLY PDLPDTTQAT PHNNIERDLY AGRSDDSSHV VIYVSKMFAV
     PISELPQFQR KQLTAEEMRE RGRAVRVPTQ AASATNGAIP IHQAPASAEI GAIVNPASSE
     LPSTTPAPIP QAESTLPEDP TKNGTEQSSP DEGEALIGFA RIYSGTVRVN QKLTCVLPKY
     NSNNPDQLNS THLKTVTIEN LYIIMGRSLV ETTEVRAGHV FGIGGLAGKV LRNATLCAPP
     ISKANNCERD ENFDELINLA GVQLASAPIV RVSLEPKQPS DMPKLVEGLK LLNQSDPCVE
     TLIQDTGEHR CLRDLRERFA KIQIQASKPI VPFRETAVRA AEMTPPKTQD QPRGTICGSV
     LGGLVSFTVR AIPMPGPITN YLSMNSELMR RISLREARKL NPTNSDLDTT ATAEPSSTNK
     EDPAAASLTE EAHYKQKQQQ RSDISQASPN DSDSFFWAGL VTACKACADI STPEIDWLES
     VDSIWAFGPK RSGANLLLDK LPGSVRSLRS PNRKNSRSVV VEEQAQEKEG GSKLDSTQEN
     QSISPLMSMR EFDDSIETAF QLATFKGPLC AEPMSGLCFS IERLEIHGDD LAASVKTIRS
     KWSQLTGELI SALQDAFKSA FLDWSPRLML AMYTCEIQAT TEVLGKVYGV IARRKGTIKS
     EEIKEGTTFY TIVAQMPMIE SFGFNDELMK KTSGVALPQF VFDGFQVAFD LDPFWLPTTE
     AELEDFGSLA DKENLPRKYI DQVRKRKGMF VEKKIVQHAE KQRTMKR
//
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