ID A0A429Z8Y1_9ENTE Unreviewed; 625 AA.
AC A0A429Z8Y1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
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:RST90167.1};
GN ORFNames=C7P63_03570 {ECO:0000313|EMBL:RST90167.1};
OS Vagococcus humatus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Vagococcus.
OX NCBI_TaxID=1889241 {ECO:0000313|EMBL:RST90167.1, ECO:0000313|Proteomes:UP000277864};
RN [1] {ECO:0000313|EMBL:RST90167.1, ECO:0000313|Proteomes:UP000277864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 31581 {ECO:0000313|EMBL:RST90167.1,
RC ECO:0000313|Proteomes:UP000277864};
RA Gulvik C.A.;
RL Submitted (MAR-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:RST90167.1}.
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DR EMBL; PXZH01000001; RST90167.1; -; Genomic_DNA.
DR RefSeq; WP_125942780.1; NZ_PXZH01000001.1.
DR AlphaFoldDB; A0A429Z8Y1; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000277864; 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; 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; 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; PF03144; GTP_EFTU_D2; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:RST90167.1};
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:UP000277864}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 625 AA; 70263 MW; 7C79947E7196B8A7 CRC64;
MKHIVIGTAG HIDHGKTTLI KRLTGIETDT TREEKERGMS INLGFAYVDL PNGERIGIVD
VPGHEKFIKN MLAGVAGINL VLLVIDANEG IMPQTKEHMD ILTLLGIEDF IVVLTKVGAV
DEELREIVYE DIQESLKGTP LEQAPIIETD AVENIGIDKL KEVIMLKVEQ LSTDIVEAAP
RLNVDRSFSV KGFGTVVTGT LLDGSLKIGD ELIAYPGEIK TKVRNIQVHE TNQELAYPGQ
RTALNLTKIG VDEVGRGSVL TTKANVEPTW MLDTKITCLN LPQNQLELWD RVHLHIGTKE
VRGRIVPLGV DKILAGEEGF VQLRLEEQVA VKSGDHFIIR SYSPVVTIGG GVVLEANPVK
HRRFNEETLA SLKIKEEGNF EDLILDYLNN KIKQFKTAKE IAEYLNANLD LVRDTLDDLI
VKGQVFPVSH TFLGMEEVNR SLVEMEQVLE NYHKKYRLRQ GMSLEEFRSK FGQFKGKELE
AMLKYLKEEQ LVQVTGSLIK LTDFEVSYNS YQLKEKERIE KVLKQSGLTP PSVEEILADS
PNAKEVLEAL NGVSIYYLNP ETIIHMDTFN HGVNFVKQHI TENGSLTLGE FRDEMDTSRK
YAMMFLEHLD ELGITKRVEN NRVLA
//