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Database: UniProt
Entry: I3IQR0_9BACT
LinkDB: I3IQR0_9BACT
Original site: I3IQR0_9BACT 
ID   I3IQR0_9BACT            Unreviewed;       641 AA.
AC   I3IQR0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   28-JAN-2026, entry version 54.
DE   SubName: Full=Selenocysteine-specific translation elongation factor {ECO:0000313|EMBL:GAB64055.1};
GN   ORFNames=KSU1_D0746 {ECO:0000313|EMBL:GAB64055.1};
OS   Candidatus Jettenia caeni.
OC   Bacteria; Pseudomonadati; Planctomycetota; Candidatus Brocadiia;
OC   Candidatus Brocadiales; Candidatus Brocadiaceae; Candidatus Jettenia.
OX   NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB64055.1, ECO:0000313|Proteomes:UP000002985};
RN   [1] {ECO:0000313|EMBL:GAB64055.1, ECO:0000313|Proteomes:UP000002985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA   Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA   Furukawa K., Fujii T.;
RT   "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT   reductase instead of a NirS-type with cytochrome cd1.";
RL   FEBS Lett. 586:1658-1663(2012).
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:GAB64055.1}.
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DR   EMBL; BAFH01000004; GAB64055.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3IQR0; -.
DR   STRING; 247490.KSU1_D0746; -.
DR   eggNOG; COG3276; Bacteria.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000002985; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   CDD; cd15491; selB_III; 1.
DR   Gene3D; 1.10.10.2770; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR057335; Beta-barrel_SelB.
DR   InterPro; IPR050055; EF-Tu_GTPase.
DR   InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015191; SelB_WHD4.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
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; PF25461; Beta-barrel_SelB; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF09106; WHD_2nd_SelB; 1.
DR   Pfam; PF09107; WHD_3rd_SelB; 1.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 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; 3.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:GAB64055.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002985}.
FT   DOMAIN          10..181
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   641 AA;  71354 MW;  53509B6085325EB6 CRC64;
     MEQSTHTLHT EHLIIGTAGH IDHGKTSLVK ALTGIDADRL PEEKQRGLTI DIGFAYLDLN
     SDYRISIVDV PGHERFVKNM LAGATSINLV LFVIAADGGV MPQTVEHLEI INLLGIQHGI
     VVVTKKDLVT DEWLEVVQDD IKRILAGTTL EHAPILPVST ITGEGIESCK AMIKKLITQV
     KVRGSDRVFR LPIDRSFTIS GYGCVVTGPI LGGQISVDNE VEILPLKKTL RVRGIEVTGE
     QVHTAFAGQR AAINLTGIKS GEVKRGYELS IPGYLEPTNL IDATLKLIKS IKNPLKNRTR
     IRFHSNTSEV MGRVILLDRD SLKPGEESCI QIFLENLITT ERNDRFIIRS YSPAYTIGGG
     VVLRSNTTRL KRFKGETLKI LKTLASGNLA DIIEQIYLNN SHAVLTSDDI SRQANIHPSI
     AADITAELVK KGSLLKFDID GKGVVFHRNI IAALREEILH ILRTFHKENP LKAGIEETYL
     KTLLRKDTHP LSIAASLSTL KREKTIKVID GKLSLKDFEI ELSAQDKSKA NKIEEFFLHA
     GFTPPSIEEV YTKFGTSSKS TISLLVEQKK IIALENDLYF HTTTLDTLKG IIKEYIRKHG
     SINVAQFRDL TKTSRKFAVP LMEYFDAIRF TRRTGDVRIL L
//
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