ID Q9M657_CHOCR Unreviewed; 765 AA.
AC Q9M657;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Elongation factor 2 {ECO:0000313|EMBL:AAF71704.1};
DE Flags: Fragment;
GN Name=EF2 {ECO:0000313|EMBL:AAF71704.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:AAF71704.1};
RN [1] {ECO:0000313|EMBL:AAF71704.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10811219; DOI=10.1038/35011054;
RA Moreira D., Le Guyader H., Philippe H.;
RT "The origin of red algae and the evolution of chloroplasts.";
RL Nature 405:69-72(2000).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AF213661; AAF71704.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9M657; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; IPR031157; G_TR_CS.
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; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 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 SMART; SM00889; EFG_IV; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:AAF71704.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 1..220
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAF71704.1"
FT NON_TER 765
FT /evidence="ECO:0000313|EMBL:AAF71704.1"
SQ SEQUENCE 765 AA; 84802 MW; 4BDBDB5C57FE043E CRC64;
HGKSTLHDSL VAAAGIIAMP TPRQELTDTR QDEQDRCITI KSTGISLFFE FPGRSPAPQG
TDGRNFLINL IDSPGHVDFS SEVTAALRVI DGALVVVDSV EGVCVQTETV LRQALAERIK
PVMTINKLDR SFLELQLEPE DMYQNFSRII ETANVIMSTY QDEELGDVQV YPDAGTVAFS
AGLHGWGFTL NRFARMYSKK FGVEPEKMTS RLWGDSFFNR KEKKWTKREG KEAFRAFCEF
IIKPIKKIIE LCMSDKIDDL EKLLSGLEIK LTTEDKELRQ KPLMKRVLQK WIPADEALLE
MMVLHLPSSA QAQKYRAELL YEGPPDDACC TGIRNCDDGP LMLYISKMVP TADKGRFYAF
GSVSSGTVRA GMKVGIMGPN YVPGTKKDLA VKSVQRTLLM MGRRTDAVDS VPCGNTVGLV
GLDQVIIKSG TISDVESAFP LKDMKYSVSP VVRVAVEPKN PSDLPELVEG LRRLAKSDPL
VQTITEESGE HVIAGAGELH LEICLKDLKD DFMNGAEIRV SNPVVTFRET IEGVENPENT
AICLSKSPNK HNRLYIYATP LPDNLPEAIE DGKVTPRDEA KARMKMLRDL VWSSEDAAKK
IWCFGPDTTG ANLLVDRAKA VQYLNDIKDS CVAAFQWATK EGVLCDENMR GILFNIHDCS
LHADTIHRGG GQFIPTCRRA LFGAQLLAGP KLVEPFFLVE IQCPETIVGP IYGVLTHKRG
HVFEEVQRPG TPMFNVKAYL PVQESFGFTP DLRSATGGQA FPQCV
//