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Database: UniProt
Entry: A0A372G0Z1_9ACTN
LinkDB: A0A372G0Z1_9ACTN
Original site: A0A372G0Z1_9ACTN 
ID   A0A372G0Z1_9ACTN        Unreviewed;       600 AA.
AC   A0A372G0Z1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   28-JAN-2026, entry version 30.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   Name=selB {ECO:0000313|EMBL:RFS46653.1};
GN   ORFNames=D0Q02_09400 {ECO:0000313|EMBL:RFS46653.1};
OS   Micromonospora craniellae.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS46653.1, ECO:0000313|Proteomes:UP000262621};
RN   [1] {ECO:0000313|EMBL:RFS46653.1, ECO:0000313|Proteomes:UP000262621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW63014 {ECO:0000313|EMBL:RFS46653.1,
RC   ECO:0000313|Proteomes:UP000262621};
RA   Li L., Lin H.W.;
RT   "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT   South China Sea.";
RL   Submitted (AUG-2018) 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:RFS46653.1}.
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DR   EMBL; QVFU01000007; RFS46653.1; -; Genomic_DNA.
DR   RefSeq; WP_117227595.1; NZ_CP061725.1.
DR   AlphaFoldDB; A0A372G0Z1; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000262621; 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   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; 2.
DR   InterPro; IPR057335; Beta-barrel_SelB.
DR   InterPro; IPR050055; EF-Tu_GTPase.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015191; SelB_WHD4.
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   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; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09107; WHD_3rd_SelB; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:RFS46653.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262621}.
FT   DOMAIN          1..168
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   600 AA;  63090 MW;  E31DF813E473A420 CRC64;
     MLVVATAGHV DHGKSTLVRA LTGMEPDRWA EERRRGMTID LGFAWTTLAS GTTVAFVDVP
     GHERFVPNML AGVGPVPAAA VVVAADEGWM PQSAEHLAAL DALGVAYGLL VVTRADLADP
     GPALARARAE LAVTSLRGVE AVVVSGVTGV GLPDLRAALD RLAARVPSAD RTAPVRLWVD
     RSFTVRGSGT VVTGTLGAGR LRVGDELELA GTGEKVRVRG LHRLGEARDA VDPVARVAVN
     LRGVPRDRVA RGDALLTPGR FRASELVDVR LAGDAVTALP ATLTLHVGAA AVPARVRPLG
     GDTLRLRLGR PVPLLVGDRA LLRDPGRHHV AGGVTVLDVL PPLLRRRGAA AARAAVLATL
     DGRPDLAGEL RRRGLVRAGD LVRAGVPVPV APVAGDWLAD PDHWRRLADR LADAVARYTR
     EHPLEPGAPV EVLRRQLDLP DRVLVEALVR APLRLTAGRV GTAGADPLPE SVARAVALVR
     DDYAAYPFRA PDADRLAAVG LGVREIGAAV RAGALLRLTG NVLLLPGAPQ QAVRVLAGLP
     QPFTLSAARQ AWDTTRRVAV PLLELLDRQG RTRRLPDDAR VVVDADCVDP PAAGRPGRLP
//
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