ID A0A1M7Y3V1_9BACT Unreviewed; 643 AA.
AC A0A1M7Y3V1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN02745220_01666 {ECO:0000313|EMBL:SHO46855.1};
OS Desulfopila aestuarii DSM 18488.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
OC Desulfobulbales; Desulfocapsaceae; Desulfopila.
OX NCBI_TaxID=1121416 {ECO:0000313|EMBL:SHO46855.1, ECO:0000313|Proteomes:UP000184603};
RN [1] {ECO:0000313|EMBL:SHO46855.1, ECO:0000313|Proteomes:UP000184603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18488 {ECO:0000313|EMBL:SHO46855.1,
RC ECO:0000313|Proteomes:UP000184603};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; FRFE01000006; SHO46855.1; -; Genomic_DNA.
DR RefSeq; WP_073612981.1; NZ_FRFE01000006.1.
DR AlphaFoldDB; A0A1M7Y3V1; -.
DR STRING; 1121416.SAMN02745220_01666; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000184603; 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 FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 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; 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; 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.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:SHO46855.1};
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:UP000184603}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 643 AA; 71988 MW; DEE5F730B3211D9E CRC64;
MREIVLGTAG HVDHGKTSLI RALTGIETDR LKEEKKRGIT IELGFAHLDL PCGHRLGIVD
VPGHEKFVKN MVAGVTGMDM VAFIIAADEG IMPQTVEHFE ICRLLGVKQG MVVLTKKDMV
DEDWLEMVQD EIHEFCEGSF LEEAPIIPVS SITGEGIDEV RKTLDEFVRQ HNFQEAFGPF
RLPVDRVFAM KGFGAVVTGT SISGRTTIGE ELQFYPGDTV AKVRGIQVHS QSVETVEAGH
RTAINMQGVD THDIERGMVL ATPNSLQPNY MLDCQLLYLG SNAKALAHRK RVRVHLGTAE
IIGRVSLLDR DELEPGQEAG VQLLLESPVA VWPDDHFVIR SYSPVATIGG GRVLGNVSPR
KRKRLTESDR AYNSKIFQVF LEGSIEERTL AFLKESGARG LTFDDLAIRL GLFGKHLKKA
LNDPLSTKKM VVVDSASQRY VDVEIAEKTK KEMLNYLAKY HKSNPLLTGL VREELRLSIG
KVIDQKVFAY CLNELLRKGE VVQEESMLRL ASHEVALKAD EEELQRELLS WYESKGLSTP
TVRETMDHFS EYSEKMLKGV LDLLLREAKL VKISETLYYE RKLIDDLVAK VVAEMQSKGE
IDAPGFKNLT GLTRKFSIPI LEYLDRIKLT IRVGDARVLR KKG
//
