ID H6BNL2_EXODN Unreviewed; 1096 AA.
AC H6BNL2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Elongation factor EF-2 {ECO:0000313|EMBL:EHY53197.1};
GN ORFNames=HMPREF1120_01395 {ECO:0000313|EMBL:EHY53197.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53197.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53197.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53197.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH226130; EHY53197.1; -; Genomic_DNA.
DR RefSeq; XP_009153658.1; XM_009155410.1.
DR AlphaFoldDB; H6BNL2; -.
DR STRING; 858893.H6BNL2; -.
DR GeneID; 20306034; -.
DR VEuPathDB; FungiDB:HMPREF1120_01395; -.
DR eggNOG; KOG0467; Eukaryota.
DR HOGENOM; CLU_002794_3_1_1; -.
DR InParanoid; H6BNL2; -.
DR OMA; FARCDIQ; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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 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 Elongation factor {ECO:0000313|EMBL:EHY53197.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EHY53197.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 17..295
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 469..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 121478 MW; 10C384E9D612A962 CRC64;
MPAIAPSQLI ALQSNAQNIR NICILAHVDH GKTSLSDSLI ATNGIISPKM AGKIRYLDSR
PDEQIRGITM ESSAISLYFS MMRRQKENEE LKKEEYLINL IDSPGHIDFS SEVSTASRLC
DAAVVLVDAV EGVCSQTVTV LRQVWIEKLK PLLVINKIDR LITELKMSPA EAYSHLERVL
EGVNAVIGGF FHGERMEEDL QWREKLDQKR AAREQQKQDV LSENASEGDF SQTFEEKDDE
DLYFAPEKNN VIFASAIDGW AFTVRQFSGI YEKKLGIKRS VLEKVLWGDF YLDPKTKKVL
GQKHLKGRNL KPLFVQLVLE PIWQAYDATV GINGGRGDSA LLEKITKSLA INLPAHILRS
RDPKAVLQAL FAAWLPLSTA VLVSVIEYLP SPPNAQATRL PEMIDDLVSS KSIDPALKDA
MINFDTSENA PVVAYVSKMV AIPESELPSK RRKLGTTLTA DEARELARKK RAEIAKTQAE
AEGSANVDSI TNGLNTTRIG EEADEDESPE QPEDPEHLIG FARLFSGSLS VGDEVYVLPP
KFNPAFPHAS PEPKKVPITA LYLLMGRSLE PLDKVPAGVV FGIEGLEGHI LKTGTLCSQL
EGGINLAGIS TLSEPIVRVA LEPTNPMDLN KMIKGLKLLE RSDPCAVYEQ MASGEHVILT
AGELHLERCL KDLRERFARC DIQPGEPIVP YRETIVKAEE MEPPKNPELP RGTVIAVTAS
KTVSVRLRVR PLPKTVTEFL IKNSSTIRRL YAEKQAQEDV TKTSDEAAET AKDEAVDLGN
ETGNERGNLS LQEFRKQLQA AFDEVKEDKE AWQKIIPRIC AFGPRRVGPN LFIDSTGTNA
CKRFLMEQPE ARKNPETDTN NDQGEEGQGE DDKSTRPAGQ DFSDTVVYAF QLATSQGPLC
REPMQGVAVF LEDISQQLPS ESSDPAVESG RLTGELISAV REAIRSAFLD WSPRILLAMY
SCTIQATPDV LGRVYSVLTR RRGAILSEAL LEGTPYFTIE AKLPVAESFG FSEEIRKRTS
GLAQPMLRFI GFEMLDDVDP FWVPRSEEEL EDLGVHGERE NVAKKYVDAV RKRKGLLVKG
ARGGRDAEKQ KTLKTN
//
