ID A0A8J2YPK7_9PROT Unreviewed; 689 AA.
AC A0A8J2YPK7;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
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:GGF04994.1};
GN ORFNames=GCM10011611_08030 {ECO:0000313|EMBL:GGF04994.1};
OS Aliidongia dinghuensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Dongiaceae; Aliidongia.
OX NCBI_TaxID=1867774 {ECO:0000313|EMBL:GGF04994.1, ECO:0000313|Proteomes:UP000646365};
RN [1] {ECO:0000313|EMBL:GGF04994.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15725 {ECO:0000313|EMBL:GGF04994.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGF04994.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15725 {ECO:0000313|EMBL:GGF04994.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) 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:GGF04994.1}.
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DR EMBL; BMJQ01000002; GGF04994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J2YPK7; -.
DR Proteomes; UP000646365; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000646365}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 661..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 73278 MW; 24AF852542145D4C CRC64;
MIIGTAGHID HGKTALVKAL TGIDCDRLKE EKARGITIDL GFAYWPIEGG RVLGFVDVPG
HERFVHTMLA GAGGIDFALL VVAADDGIMP QTLEHLAILD LLGIEHGLVA LTKADLVTPE
RLEEVSQAVR SVLAATALAD IGILPVSALT GLGIEELGAR LAAAAAETAE RSAEGGFRLA
VDRVFTLAGI GVVATGTVLA GEVRVGDAVE LSPSGLSARV RSLHAQNRPA ETGRCGDRCA
LNLAGPGIGK EAIRRGDMVL APGLHAPTDR IDATLRVLTG EAKPISQWFP ARLHHATAEV
GARVVLLGDG SIEPGTTAEV QLVLDRPIAA AQRDRYVLRD VSAQRTIGGG RFIDLRGPAR
RRRTPERAAQ RAALALADAQ TAFTALLAAP PFAADLAAYA RDRGLSAMQT EKMAREAGLV
LLEAGTARIA IAPDRWQSFA ASVTEQLAAY HAENPDLQGM GREKLRLQLT PRLPAPVFVA
TLQRLARDGG LVLDGAFVRL ASHTVRLAPG DEAAWAVIAP LLGGAERFRP PRVRDIAGMT
GRVERDVRRL LKLAGRLGWA DEVAPDHFFL RPTVREMIGL LIEEAGRAPG GELTAAQFRD
RLDNGRKVAI QILEFFDRHG VTLRKGDLRR PNRHRLDLFG APVLSSDSFF GGDSSLVGRS
DFKSEWGSEP VPGGFDSHSL PPPSSRGVA
//
