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Database: UniProt
Entry: A8UVI9_9AQUI
LinkDB: A8UVI9_9AQUI
Original site: A8UVI9_9AQUI 
ID   A8UVI9_9AQUI            Unreviewed;       583 AA.
AC   A8UVI9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=HG1285_00205 {ECO:0000313|EMBL:EDP75139.1};
OS   Hydrogenivirga sp. 128-5-R1-1.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX   NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP75139.1, ECO:0000313|Proteomes:UP000005981};
RN   [1] {ECO:0000313|EMBL:EDP75139.1, ECO:0000313|Proteomes:UP000005981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP75139.1,
RC   ECO:0000313|Proteomes:UP000005981};
RA   Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Translation factor necessary for the incorporation of
CC       selenocysteine into proteins. It probably replaces EF-Tu for the
CC       insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC       and GDP. {ECO:0000256|ARBA:ARBA00025526}.
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:EDP75139.1}.
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DR   EMBL; ABHJ01000006; EDP75139.1; -; Genomic_DNA.
DR   RefSeq; WP_008287209.1; NZ_ABHJ01000006.1.
DR   AlphaFoldDB; A8UVI9; -.
DR   PATRIC; fig|392423.7.peg.2286; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000005981; Unassembled WGS sequence.
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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR   CDD; cd04171; SelB; 1.
DR   CDD; cd03696; SelB_II; 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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR048638; SelB-like_WHD3.
DR   InterPro; IPR015191; SelB_WHD4.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004535; Transl_elong_SelB.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00475; selB; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09107; SelB-wing_3; 1.
DR   Pfam; PF21580; SelB_WHD3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:EDP75139.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Protein biosynthesis {ECO:0000313|EMBL:EDP75139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005981}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   583 AA;  65936 MW;  8E75A6CC38228FA0 CRC64;
     MKFVLFATAG HVDHGKTSLI RALTGIDTDR LPEEKRRGLT IDLGFAYLDF PEEGLRLELI
     DVPGHERFIR NSVAGLSSVS GILLVVDAGE GVMPQTREHL SVAKLLGIKH GVAVLTKIDK
     VEGEILELAE DELRNFLGEE DFELPVVKVS SLNGEGLELL RDRLREEALK ALENKEELPL
     RVLVDSAFVV KGYGTVIRGS CVEGKVREGD RVVVEPLGVV SKIRKIQNHG KFVREAQAGE
     RVALNLPDVN YDEVKRGFWV LKPGSYIKSG RMVVRSESLL KPGRLYSFFF GMREVRGRLS
     HVGEGIFILR LEEGVVARRG DRAVVLDPTG RLAGGVEVIH PYPRVLKKSF IKENAGLLLE
     SYEEYLLREM GPVGLSGELF RKLTGRAPNT GILERVSVKV GDRFYSKEFV EHLKKRLELF
     IKERIGEEGY GVPKAELTER FGLSNTLFEY IISSLKNFRL LGEHVVDERN SDLTQNADFI
     RLKELLREGI REEREILSAG VPKEVLSLSI KRRHVHRLGE FLIISEELLR HYEEKLRTLG
     EGFTVQEAKK ATGLTRKFLI PLLEHLDFLG MTERKGDRRV WRR
//
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