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Database: UniProt
Entry: A0A246RHS4_9ACTN
LinkDB: A0A246RHS4_9ACTN
Original site: A0A246RHS4_9ACTN 
ID   A0A246RHS4_9ACTN        Unreviewed;       585 AA.
AC   A0A246RHS4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   28-JAN-2026, entry version 27.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=B5D80_22335 {ECO:0000313|EMBL:OWV03689.1};
OS   Micromonospora wenchangensis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1185415 {ECO:0000313|EMBL:OWV03689.1, ECO:0000313|Proteomes:UP000197174};
RN   [1] {ECO:0000313|EMBL:OWV03689.1, ECO:0000313|Proteomes:UP000197174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AA 2012002 {ECO:0000313|EMBL:OWV03689.1,
RC   ECO:0000313|Proteomes:UP000197174};
RA   Yang H.;
RT   "Whole genome sequence of Micromonospora wenchangensis, isolated from
RT   mangrove soil.";
RL   Submitted (MAR-2017) 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:OWV03689.1}.
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DR   EMBL; MZMV01000041; OWV03689.1; -; Genomic_DNA.
DR   RefSeq; WP_088645871.1; NZ_MZMV01000041.1.
DR   AlphaFoldDB; A0A246RHS4; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000197174; 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   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; 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:OWV03689.1};
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:UP000197174}.
FT   DOMAIN          1..167
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   585 AA;  61587 MW;  A075406811AD665A CRC64;
     MHVVATAGHV DHGKSTLVRA LTGMEPDRWA EERRRGMTID LGFAWTTLPG GDPVAFVDVP
     GHERFVPNML AGVGPVPAVL VVVAADEGWM PQSAEHLAAL HALGVSHGLL VVTRADLADP
     GPATAQAHAQ LAATSLGAVE SVAVSAVTGA GLPELRAALG RLVARLPAPD PDRPVRLWID
     RAFTIRGSGT VVTGTLGGGE LRVGDRLTLA TTGEPVRVRG LHRLGTPTQR VAAVARVAVN
     LRGTPRERLG RGDALLTPDR FHRTDLVDVR LAGDPAGDLP ATLTLHVGSA AVAVRVRPLG
     GDTVRLRLAR PLPLLTGDRA LLRDPGRHHV CGGVTVLDVA PPPLSRRGAA AARAAVLADL
     DGRPDLAGEL RRRRLVRAAE LIRMGVSGDA TPVVGDWLAD PAHWRWLGAR LVEEVAAWAA
     AHPLEPDAPT EAVRQRLGLP DRALVEALVR PPLTLRAGRI GTGVPGLPEP VARAIDRVRG
     EYAAHPFRAP EADQLTALGL GPREVGAAVR AGALLRLAEN VVLLPDAADD AVRVLARLPQ
     PFTLSAARQA LDTTRRVAVP LLELLDRRGV TRRLPGDERM VVGSG
//
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