ID A0A7R7XDF6_9EURO Unreviewed; 1073 AA.
AC A0A7R7XDF6;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 10-JUN-2026, entry version 19.
DE RecName: Full=Ribosome assembly protein 1 {ECO:0000256|ARBA:ARBA00068031};
DE AltName: Full=Elongation factor-like 1 {ECO:0000256|ARBA:ARBA00081809};
GN Name=RIA1 {ECO:0000313|EMBL:BCS19397.1};
GN ORFNames=APUU_12225S {ECO:0000313|EMBL:BCS19397.1};
OS Aspergillus puulaauensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1220207 {ECO:0000313|EMBL:BCS19397.1, ECO:0000313|Proteomes:UP000654913};
RN [1] {ECO:0000313|EMBL:BCS19397.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MK2 {ECO:0000313|EMBL:BCS19397.1};
RG Aspergillus puulaauensis MK2 genome sequencing consortium;
RA Kazuki M., Futagami T.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BCS19397.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MK2 {ECO:0000313|EMBL:BCS19397.1};
RA Futagami T., Mori K., Kadooka C., Tanaka T.;
RT "Aspergillus puulaauensis MK2 genome sequence.";
RL Submitted (FEB-2021) 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}.
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DR EMBL; AP024443; BCS19397.1; -; Genomic_DNA.
DR RefSeq; XP_041551591.1; XM_041698403.1.
DR AlphaFoldDB; A0A7R7XDF6; -.
DR GeneID; 64969402; -.
DR KEGG; apuu:APUU_12225S; -.
DR OrthoDB; 364892at2759; -.
DR Proteomes; UP000654913; Chromosome 1.
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:UniProtKB-ARBA.
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; 3.40.50.300: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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000654913};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 17..281
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..487
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 212..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 118937 MW; 31F61F414520EB51 CRC64;
MPVVSVEDLV RLQQKPDDIR NICILAHVDH GKTSLTDSLI ATNGIISPKL AGKIRYLDSR
PDEQLRGITM ESSAISLFFS MMRRSAPDAQ PEAKEYLINL IDSPGHIDFS SEVSTASRLC
DGAVVLVDAV EGVCSQTVTV LRQTWVEQLK PILVINKMDR LVTELQMTPA EAYSHLSRLL
EQVNAVIGSF YQGERMEEDL QWRERMEERV NAATQQKQTQ DGESVDGSVD GAQFEERDDE
DLYFAPEKNN VIFCSAVDGW AFTVRQFAAI YEKKLGIKRS VLEKVLWGDY YLDSKTKRVL
GQKHLKGRAL KPMFVQLVLD SVWAAYEATT GGGKGKGDPA LLEKITKSLN INIPPYILRS
RDPKNIMTTL FSQWLPLSTA LLVSVIEYLP SPRAAQASRL PPMIEESPGS KFVDTKIKDA
MVQFKTGADE PVVAYVSKMA AIPESELLAS KKTSATTMSA DEAREIARRK REEIAKMQAE
AAGNNQDDDF SRVTSAFEKA TVDDAEEGEQ DQKEDPEHLI GFARLYSGTL SVGDSIYVLP
PKFSPENLHA SPEPQKVIVT DLYLLMGRSL EPLKSVPAGA VFGIGGLAGH ILKTGTLCSQ
LDGSINLAGV SLDTPPIVRV ALEPVNPSDL SKMVTGLRLL EQSDPCALYE VLPNGEHVIL
TAGELHLERC LKDLRERFAK CEIQTGQTIV PYRETIVNAP EMAAPKNPEL GRGGILTVSG
SKQLTVRLRV VPLPEVVTEF FTKHVGTIKR LQSEKRTPKA DGEPDSTQQD EATDAAGEAR
DVTLLSLEDF KKELNKTFEE VKEDKELWKD VVERVIAFGP RRIGPNILVD ATAVNTCEKF
LLDDHKQQPS ILPETASRDA LTVRDFSDKI TYAFQLAMGQ GPLCQEPIQG TAVFLEEIQI
DASENEIDMG RLTGETIRLV RESISQGFLD WSPRIMLAMY SCEIQASTEV LGRVYGVITR
RRGRILSETM KEGTPFFTIV SLLPVAESFG FAEEIRKRTS GAAQPQLIFA GFEALDQDPF
WVPATEEELE DLGELADREN VAKMYVDAVR ARKGLFVQGR KLIDAEKQKT LKK
//
