ID B2AW53_PODAN Unreviewed; 1078 AA.
AC B2AW53;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 10-JUN-2026, entry version 90.
DE RecName: Full=Ribosome assembly protein 1 {ECO:0000256|ARBA:ARBA00068031};
DE AltName: Full=Elongation factor-like 1 {ECO:0000256|ARBA:ARBA00081809};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP32100.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP32100.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; FO904942; CDP32100.1; -; Genomic_DNA.
DR RefSeq; XP_001907954.1; XM_001907919.1.
DR STRING; 515849.B2AW53; -.
DR GeneID; 6191997; -.
DR KEGG; pan:PODANSg4989; -.
DR VEuPathDB; FungiDB:PODANS_7_5980; -.
DR eggNOG; KOG0467; Eukaryota.
DR HOGENOM; CLU_002794_3_1_1; -.
DR OrthoDB; 364892at2759; -.
DR Proteomes; UP000001197; Chromosome 7.
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; 3.90.1430.10: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; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR056752; EFL1.
DR InterPro; IPR004161; EFTu-like_2.
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; PF14492; EFG_III; 1.
DR Pfam; PF25118; EFL1; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 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:UP000001197};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT DOMAIN 17..280
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 444..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..776
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 119452 MW; 25188F1EA063E786 CRC64;
MPVVSPEKLA KLQQNADDVR NICILAHVDH GKTSLTDALL ATNGIISPRL AGKIRYLDSR
PDEQLRGITM ESSAISLYFS MLRRSSPEAT PEPKEYLINL IDSPGHIDFS SEVSTASRLC
DGAVVLVDAV EGVCSQTVTV LRQTWIEKLK PLLVINKIDR LITELKMTPN EAYIHLSKLL
EQVNAVLGSF FQGERMEEDL NWRERMEERR AQAVANKEAQ LVDQQSDAGD LQFQEKDDEE
IYFAPEKNNV IFGSAIDGWA FTVRQFAGLY EKKLGIKRSL LEKVLWGNFY LDPKTRKVLG
PKHLKGRNLK PIFVQLVLET IWAVYGATVG GDHGKGDPAM LEKITKSLNI TMPPHILRSR
DPKLLLTTVF ASWLPLSVAL LVSVVESLPS PRTAQAERLP ELLQEVPGAD QIDPAIKEAM
VSFKKEKSDP MVAYVSKMVS VKESELPENR RKGPMNGEEA RDLARKKRAE ALRAQKEARG
DREDDDVQFI TDGLASASLE TQTPEEEEKP AETEHLIGFS RIYSGTLSVG DEVYVLPPKF
SPANPLAEPV PKKVKVEALY MMMGRNLELL DTVPAGVVFG IRGLEGSGLL KSGTICSQLE
GSVNLAGIAN LHGKPIVRVA LEPENPSDLD KMIKGLQLLV QSDPCAEYEQ FSTGEHVLLT
AGELHLERCL TDLRERFARC EIQASAPIVP YRETIVRAEE MRPPVNKDLG RGVVVGVTSS
KQVTITLRVR PLPAEVTDFL GKNTASIKTL YSGQKNGDDE GSVAQDDSSE ADAVEDNDLT
ITKALTAEEL SKELQSTLDK SEKARDASIW KDAVDRIISF GPRRTGPNIL IDATKDQFFP
KAFAADKEAV ARAVKISGDE SLDARHFSDK IAYAFQLATH HGPLCHEPVQ GIAVFIEDVS
VNIEGNVTAR DHINRLTGEV IKTVQQSIHK GFLDWSPRLM LAMYSVEIQA GTEVLGRVYD
VLTRRRGKVQ SEAMNEGTPF FTIVATLPVA ESFGFADDMR KRTSGAAQPQ LIFTGFEILD
EDPFWVPFTE DDLEDLGEFG DKEIVAKRYM DGVRRRKGLL VEGRNVATDA SKQRTLKR
//
