ID Q7S829_NEUCR Unreviewed; 1102 AA.
AC Q7S829;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN ORFNames=NCU05270 {ECO:0000313|EMBL:EAA32491.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA32491.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA32491.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
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DR EMBL; CM002239; EAA32491.1; -; Genomic_DNA.
DR RefSeq; XP_961727.1; XM_956634.2.
DR AlphaFoldDB; Q7S829; -.
DR SMR; Q7S829; -.
DR STRING; 367110.Q7S829; -.
DR PaxDb; 5141-EFNCRP00000005078; -.
DR EnsemblFungi; EAA32491; EAA32491; NCU05270.
DR GeneID; 3877875; -.
DR KEGG; ncr:NCU05270; -.
DR VEuPathDB; FungiDB:NCU05270; -.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; Q7S829; -.
DR OMA; EFAVMLC; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 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 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EAA32491.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001805}.
FT DOMAIN 507..725
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 121478 MW; CCEE858A6E757EF6 CRC64;
MAPKKKGNKK ANDDWEAELG ESIAPVNNNG ADAAAASPAA ADDEAASGGG GLMERMRKAK
EKRKKKGLAD DWEAELGEDA PGAEKPAAAE PVPDLSAKVA EEANLDDEFA LPEKKGKGGK
GKQQQQQQKA APAAAAKKDE DAADEDGPRV LTKAEKEKLK KEREKQRKKE QAAAKKKGTT
PAAAAKAEPA KEEKKAETPS PVSTPASTPA PEAAAGGKKK KLPAHLLALQ KQQEELRRRQ
EEEARLLAEE KARIEEEERA AAEEAKRKEE ERARKKEKEK QRIEQLKKEG KFMTKAQKEE
KARNERKLQQ MLAAGIKVNA LEGEESKKKP VYDDKKKRAA NKKKDEEKAL AEAAERARLA
AEALVKEQEE KARIEREKAE KEAAAKAEAA KAAAEDSVDE DWEAAVASDK EDVKDSWDAD
SDEEEETKKE ETKKEASKPA AANGKTQAKK EESESESESE EESEEESSED EEATARELEE
ARRKKEAAER REKAHQAALA ARSADNLRSP ICCILGHVDT GKTKLLDKIR QTNVQEGEAG
GITQQIGATY FPVEAIKQKT HVVNRDGKFE FKVPGLLIID TPGHESFSNL RSRGSSLCNI
AILVVDIMHG LEPQTLESMR LLRERKTPFI VALNKIDRLY GWKKIENNGF QESLALQNKA
VQNEFKNRLE QTKLAFAEQG FNSELFYQNK SMAKYVSLVP TSAHTGEGIP DMLKLIVQLT
QERMVGSLMY LSEVQATVLE VKAIEGFGMT IDVILTNGIL REGDRIILCG TEGVIKTNIR
ALLTPAPLRE LRLKSQYVHN KEVKAALGVK ISAPGLEGAI AGSRLLVVGP DDDEDDLEDE
VEADLASLFS RVEKSGRGVS VQASTLGSLE ALLDFLKECK IPVANVGIGP VYKRDVMQCG
IMLEKAPDYA VMLCFDVKVD KEAQEYADQQ GVKIFTADII YHLFDSFTKH MDELLEKKKE
ESKLLAVFPC VLAPVAVFNK SGPIVIGVDV VEGQLKINTP ISAVKTNPVT GAREVIDLGR
VTSIERDHKQ IPVCKKGQPS VAIKIEMGGN QPTYGRHLEE KDMLYSKISR ASINCLKEFY
RKDVTNDEWQ LIIKLKPMFD IA
//
