ID F8MM16_NEUT8 Unreviewed; 1083 AA.
AC F8MM16;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=NEUTE1DRAFT_62805 {ECO:0000313|EMBL:EGO57690.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO57690.1};
RN [1] {ECO:0000313|EMBL:EGO57690.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO57690.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL891304; EGO57690.1; -; Genomic_DNA.
DR RefSeq; XP_009850789.1; XM_009852487.1.
DR AlphaFoldDB; F8MM16; -.
DR GeneID; 20828964; -.
DR KEGG; nte:NEUTE1DRAFT62805; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_62805; -.
DR HOGENOM; CLU_002794_3_1_1; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 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; 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_dom.
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; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 17..279
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 755..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 119216 MW; 3D36715E8BBA72E0 CRC64;
MPVVQPEKLA KLQQNADDVR NICILAHVDH GKTSLTDALL ATNGIISPKL AGKIRYLDSR
PDEQQRGITM ESSAISLYFS MLRRSAPDAT PEAKEYLINL IDSPGHIDFS SEVSTASRLC
DGAVVLVDAV EGVCSQTVTV LRQAWTEKLK PLLVINKIDR LVTELKMTPG EAYIHLSKIL
EQVNAVLGSF FQGERMEEDL NWRDRMEERV AAAAAKEAQI AAGQPDSGEL QFQEKDDEEI
YFAPEKNNVI FGSAIDGWAF TVRQFAGMYE KKLGIKRGLL EKVLWGNFYM DPKTKKVLGP
KHLKGRPLKP IFVQLVLEPI WAVYQATVGG DSGKGDPALL EKITKSLNLS VPPHILRSRD
PKLLLTTVFA SWLPLSTALL VSVVESLPSP KAAQADRLPD LLASVPGADH IDPKVKDAMV
SFKKDPSEPM VAYVSKMISV PESELPENRR RGPLSPEEAR ELARKKRAEA IRAQGGADAD
ADMNDLANAF TSTSLTDNAV PELEEKPVEA EHLIGFTRIY SGTLSVGDEI YVLPPKFSPA
DPHAQPVPKK VTVTALYMLM GRNLEALPSV PAGVVFGIRG LEGSGLLKSG TLCSQLEGSV
NLAGIANLAG RPIVRVALEP VNPYDLDKMI QGLHLLVQSD PCAEYEHFSS GEHVLSTAGE
LHLERCLTDL RERFARCEIQ AGAPIVPYRE TIVRAEEMRP PVNKELGRGV VVGVTSSKQV
TVTLRVRPLP APVTEFLQKN SAGIKRLYTD RKAAGVEDGA ESPSVEEATL ENGTPSDVKI
EEDEEVSQAA TTLTPEELKK QLQAQLDGVK DKEAWKDVID RIASFGPRRT GANILVDATK
DQLFSKAFSA DKIRNQAPTG DEKLHPAHFS DKIMYGFQLA TQQGPLCNEP VQGIAVFVED
VLVAQTEDDE TSSARDRIGR LTGEVIKTVQ QSIHKGFLDW SPRLMLAMYS CEIQASTEVL
GRVYDVLTRR RGRVQLEAMN EGTPFFTIQA LLPVAESFGF ADDMRKRTSG AAQPQLIFTG
YEILDEDPFW VPFTEDDLED LGEFGDRENV AKRYMDSVRR RKGLLVEGRN VATNAEKQKT
LKR
//
