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Database: UniProt
Entry: B4UB41_ANASK
LinkDB: B4UB41_ANASK
Original site: B4UB41_ANASK 
ID   B4UB41_ANASK            Unreviewed;       649 AA.
AC   B4UB41;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   OrderedLocusNames=AnaeK_0447 {ECO:0000313|EMBL:ACG71689.1};
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG71689.1, ECO:0000313|Proteomes:UP000001871};
RN   [1] {ECO:0000313|EMBL:ACG71689.1, ECO:0000313|Proteomes:UP000001871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|EMBL:ACG71689.1,
RC   ECO:0000313|Proteomes:UP000001871};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA   Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) 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}.
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DR   EMBL; CP001131; ACG71689.1; -; Genomic_DNA.
DR   RefSeq; WP_012524522.1; NC_011145.1.
DR   AlphaFoldDB; B4UB41; -.
DR   KEGG; ank:AnaeK_0447; -.
DR   HOGENOM; CLU_023030_3_0_7; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000001871; Chromosome.
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; 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; IPR004161; EFTu-like_2.
DR   InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 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; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09106; SelB-wing_2; 1.
DR   Pfam; PF09107; SelB-wing_3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:ACG71689.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ACG71689.1}.
FT   DOMAIN          1..176
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   649 AA;  67786 MW;  DCAA9C7E7203864F CRC64;
     MKRVVIGTAG HIDHGKTSLV RALTGIDTDR LRDEKRRGIT IELGFAHLAL PDGSVAGVVD
     VPGHERFVRS MAAGAGGIDL VVLVIAADEG VMPQTREHLD ICRLLGVPRG LVAVTKADLL
     PELGADWLPL LEQDVREVTR GTFLEGAPIV PVSSATGEGL DALRAALAAL AAEVPERPTD
     GPLFLPIDRA FSMKGFGTVV TGTLLSGQIA EGDAAALLPA SPGGDGLRVR SVQVHGKPTP
     RALAGQRTAV NLPGIEPAAI RRGQVLVHPG VVPPSSILDA ELTLLAAAPK PLRHRAKLLL
     HVGTAQVPAV ISLLDRAELA PGATAHAQLR LAEPAAALPG QRFILRGFAV LEGRGKTVGG
     GRVLAVAAPK RRRGRPESLA QLAVLAGADP EARLATVLAM AGPAGLDLPA LVGRTALSPK
     AAQATLDRLG ARGGAVLFDR ERRAYVAGTV AQELTRRMAA AVAAFHRDHP LAAGMGREAL
     RGKLPPVTDP RLFQRLLAHA AERGELVVEG DAVREKGHAA ASGESAGGAL KEKVAAALAK
     GGLTPPWLAE LPGAVGASAP DVQAVLKLLA AEGRALRVSS ELYFDAAAVK TLEAKLVAWL
     RERRQITTQE FKDLVGATRK HVIPLAEFFD REKVTLRVGE KRVLRGEGR
//
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