ID A0AA35W7J5_GEOBA Unreviewed; 622 AA.
AC A0AA35W7J5;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=GBAR_LOCUS3889 {ECO:0000313|EMBL:CAI8004333.1};
OS Geodia barretti (Barrett's horny sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX NCBI_TaxID=519541 {ECO:0000313|EMBL:CAI8004333.1, ECO:0000313|Proteomes:UP001174909};
RN [1] {ECO:0000313|EMBL:CAI8004333.1}
RP NUCLEOTIDE SEQUENCE.
RA Steffen K., Cardenas P.;
RL Submitted (MAR-2023) 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 -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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:CAI8004333.1}.
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DR EMBL; CASHTH010000556; CAI8004333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA35W7J5; -.
DR Proteomes; UP001174909; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:CAI8004333.1};
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:UP001174909}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 622 AA; 68436 MW; F02809EEB41079A4 CRC64;
MYVIGTAGHV DHGKSTLVKA LTSIDPDRLP EEKEREMTVD LGFAWMTLPS GREVSIVDVP
GHERFIKNML AGVGGIDLAL LIVAADESVM PQTREHLAIL DILQVTRGLV VVTKTDLVDD
EELVELVKAE VEDTLQGTSF EGCPMVGVSA QTGDGLDELR GMIDSILDET EMRRDLGRPR
LPIDRCFTIS GFGTVVTGTL IDGSLAVGQQ IELAGSQQRA RIRGLQSHKT KVSSAEPGVR
LAVNLSGISR DDIERGEILT SPGWLRPARR LDARIRMVND APHPLKHNEG VTFHLFTSES
HARVRLLDAE QLDAGSEGWV QLLLSEALPV VKGDYFVVRS ADSTLGGGQV VDPNPRRRHR
RFDVDVSEQL MLLDEGADED VIVSVAEQWG PCNLTDLSRR ANLPREEALE RAVALAEEGD
LITLGDLSTD GDAVVYSALG WGALKGRLAG VLRSYHDQYP LRRGAPAQEV RSRVGLSQPV
YLRALARMGD EGFVAEDGQA VRLPGHEVEF TPKMEQQVAR YLQSLDREPY SPPTDQPLEG
ELLSALVDQG KVVRVGDSVV FAATAYQEMT VRVVEYLREN GSITVAEART LFDTSRKYIL
PLLERMDQEQ ITRRNGDERV LR
//
