ID A0A844H7Z9_9RHOB Unreviewed; 631 AA.
AC A0A844H7Z9;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
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:MTH35411.1};
GN ORFNames=GL279_12450 {ECO:0000313|EMBL:MTH35411.1};
OS Paracoccus limosus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=913252 {ECO:0000313|EMBL:MTH35411.1, ECO:0000313|Proteomes:UP000442533};
RN [1] {ECO:0000313|EMBL:MTH35411.1, ECO:0000313|Proteomes:UP000442533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17370 {ECO:0000313|EMBL:MTH35411.1,
RC ECO:0000313|Proteomes:UP000442533};
RA Dong K.;
RL Submitted (NOV-2019) 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:MTH35411.1}.
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DR EMBL; WMIF01000017; MTH35411.1; -; Genomic_DNA.
DR RefSeq; WP_155064964.1; NZ_WMIF01000017.1.
DR AlphaFoldDB; A0A844H7Z9; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000442533; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
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; 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; 3.
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; 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 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 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; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:MTH35411.1};
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:UP000442533}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 631 AA; 67371 MW; 0FB85BF5B24A43B8 CRC64;
MIVGTAGHID HGKTALVKAL TGVDADRLAE EKARGITIDL GFAYADLGAG SITGFVDVPG
HEKFVHTMLA GAGGIDLALL VVACDDGIMP QTREHLAILD LLGISRGIVA LTKADLATAP
RIATLQAEVE NLLANTSLCE STILPVSSLT GAGVENLRAE LVRAECHTSQ RAADARFRMA
LDRSFSLSGA GTVVTGTVLS GRVAVGDQIQ ISPSGLPARV RGIHAQNRKA ETGLAGQRCA
LNLAGDQITR EAIHRGDVAL DPALHAPTER IDVSLRVLDS EPKPLTTWFP ARLHLGAAEA
GARVVPLQGP IAPGETGLAQ IVLDRPLAAS VGERFILRDV SARRSIGGGR LIDLRPPARR
RARPERLAAL DAMALPDPAL ALQALATLAP VALDAFARDH ALPPEAFDTP LIPGTRLAAS
PDTLASLRAQ MQDQLAAFHA ENPDLQGMGR ERLRLALTLR LPKADFTGFI RHEANAGSIA
LDGACLRLPG HLPRLSPADE AAYALIAPRL TGADRFRPPR VRDFATELGH DEGDLRRILL
MAARQGRVDR IAHDHFFARA TTVEMVGILR DLSAAAEDGW FTAPAFRDRV NNGRKVAIQI
LDFFDRLGLT LRRGDLRRIN PHRIDLFTPD G
//
