ID A0AA35XJF4_GEOBA Unreviewed; 620 AA.
AC A0AA35XJF4;
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_LOCUS29481 {ECO:0000313|EMBL:CAI8053935.1};
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:CAI8053935.1, ECO:0000313|Proteomes:UP001174909};
RN [1] {ECO:0000313|EMBL:CAI8053935.1}
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:CAI8053935.1}.
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DR EMBL; CASHTH010004130; CAI8053935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA35XJF4; -.
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 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; 2.
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; 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; 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:CAI8053935.1};
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..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 620 AA; 67989 MW; BE9AA70E09C9E643 CRC64;
MYVIGTAGHV DHGKSTLVEA LTGIDPDRLR EEKERGMTID LGFAWLQLPS GNEISIVDVP
GHERFVNNML AGVGGIDLAL LVVAADESVM PQTREHLAII DLLRVQRGLV AITKRDLVDE
DWLELVTADV EETLEGTVLE GAGIYPVSAM TGEGLPELVA AIDSMLDDTP PKRDVGRPRL
PIDRAFTISG FGTVVTGTLI DGKIETGQDV ELVVAGRSTR IRGLQTHKKG QGEAQPGTRV
AANIINVSQD EVARGEVLTT EGWLRPTDAI DVRVRVIPDA PQALRHNMYV TVHTGSSEVV
GRLRLLEKDV LEPGETSWAQ VKLDAPLAVV KGDYYVIRSN SRTLGGGNIV ETHARRHRRN
DHSIIERLEV MELGSAQDIL LKTIEASEPS RLDELVTRAN MGADIVKAEL EAIAAENLIV
ALGGEGISRG SFVFSTAGWD AVMEKTQRSL EAYYRQFPLR RGAPKEELRS RLGMSAQVFN
LAFARLQHQA VVEEDGALVR LPGYEPTLSD AQNKQVDAYL RLLETEPFSP PTDAPLDGEV
LNLLDEQGKV VRVSESVVYS AEAYEQMVTI ISEHIRENGD ISVANVRDVL GTSRKYALAL
MDYLDHKRIT RRVGDTRVLR
//
