ID A0A133VJ00_9EURY Unreviewed; 1258 AA.
AC A0A133VJ00;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
GN ORFNames=AKJ53_00370 {ECO:0000313|EMBL:KXB06425.1};
OS candidate division MSBL1 archaeon SCGC-AAA382F02.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698282 {ECO:0000313|EMBL:KXB06425.1, ECO:0000313|Proteomes:UP000070491};
RN [1] {ECO:0000313|EMBL:KXB06425.1, ECO:0000313|Proteomes:UP000070491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA382F02 {ECO:0000313|EMBL:KXB06425.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome.
CC {ECO:0000256|ARBA:ARBA00024731}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXB06425.1}.
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DR EMBL; LHYG01000003; KXB06425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VJ00; -.
DR PATRIC; fig|1698282.3.peg.249; -.
DR Proteomes; UP000070491; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd01514; Elongation_Factor_C; 1.
DR CDD; cd00081; Hint; 2.
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; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_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 InterPro; IPR004543; Transl_elong_EFG/EF2_arc.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00490; aEF-2; 1.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
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; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
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.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 4: Predicted;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Intron homing {ECO:0000256|ARBA:ARBA00022886};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000070491}.
FT DOMAIN 276..407
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 542..564
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 548..773
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1228..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 142221 MW; 8BF5A6D493788906 CRC64;
MRRYKHLSDV QELMWDHDHV RDIGIIAHID HGKCVSPRTR IALANRITRA ETLFEKKKEE
GEIEKESEDE ICVDVSDLDI EVNSFDKNSK EIVRGKITKM WKMKKTDPLV HIVTGSGNKI
KTTPEHQFLT LEEDGSLKFT RANQLEEGMN IVSARKLTHS TDEEDVKDYI LSKLSKDYGF
YVFVSGEFNE KIRKMDWDNL YKFSKSKLKK DSFEIGGREK RYRLRDIYNI CKELDLSLKE
LYEEIRTLNY RGKEWRGEHS SLPIKLPPNL SPLYYLAGLC MDDGDLYSNI TNSNPEIHEK
VRREASKLGL DVTVREFKNR TSRIELGGKT LTKILQSLFD YPIEEKSRKI KVSDLLFMSK
KEDISLFIQG YLDADGTIEK ERSAVSVNSN SIEMLEGIQL LLLKFDVASK INRVKSTLYI
SGRLSLEEFS EIGFSTTEKQ RKLKELLAKS QSSKLDYVPI KGSVLKNIRC ELDIPQTKMD
PGYSNYESTN IGLSKNSLKN ILTRFEEEGQ PTAEINELKT LAKADTSFTE VEKVERSSKE
EYVYDFTVED YHNFIAEGII VHNTTLTDSL VADSGIISEE HAGEQLFTDF MEEEQERGIT
IQTAAVSLAH EFEDEEYLIN LLDTPGHVDF SGDVTRALRA IDGAVVVVDA VEGVMVQTET
VLRQAIREHV HPILYINKVD RLIDELKLNP EEMQEKFIKI ITKFNKLLKK YAPDELAERW
KVSVEGGSVA FGSATEKWAL SATQMEKKNI TFKDIIDAHE KGEIEKLTEE SPLDEVILDM
VVHHLPNPDE AQAERIAKIW RGDPESKLGK SMIQSDKDGP LCMIVTDVEV DEQAGVVSTG
RVFSGTLEVG KEVHLVNANK GARVQQVGVY MGPDRVGVEK APAGNIAAVI GMEDAIVGET
IVEKGIEAQG FEDLQYVSEP VVTIAVEPKE YKDLPQLIEE MRRISREDPN VVVDIDEETG
EYLISGMGEL HLQIVQHELE DSGLEIQTSE PLVVYRESIK GKSGPVEGVS PNRHNRLKFA
VEPLEEEVVE ALDSGEIYEK QDQKEKAKKL RELGWETKPA KNVLGIEGQN ILVDTTKGIQ
YLREIEEYMA DAFSNAMEEG PLMNEPVRGV KVMLTNAKLH EDTIHRGPAQ IMPATRKAIH
AVMLSDEPTV LEPFLKVEAR TPQKFLGDVT QVIKGRRGQV NSIESEEDLA IVDSSIPVSE
SFGLSADMRS STEGRALWGS EFEKFDEVPQ SLQGEAIRET RERKGMKPKP PKPGELVE
//
