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Database: UniProt
Entry: A0A414SY41_9FIRM
LinkDB: A0A414SY41_9FIRM
Original site: A0A414SY41_9FIRM 
ID   A0A414SY41_9FIRM        Unreviewed;       637 AA.
AC   A0A414SY41;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JAN-2026, entry version 27.
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:RHG26784.1};
GN   ORFNames=DW265_05780 {ECO:0000313|EMBL:RHG26784.1};
OS   Dorea longicatena.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC   Lachnospiraceae; Dorea.
OX   NCBI_TaxID=88431 {ECO:0000313|EMBL:RHG26784.1, ECO:0000313|Proteomes:UP000284095};
RN   [1] {ECO:0000313|EMBL:RHG26784.1, ECO:0000313|Proteomes:UP000284095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM22-22 {ECO:0000313|EMBL:RHG26784.1,
RC   ECO:0000313|Proteomes:UP000284095};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-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:RHG26784.1}.
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DR   EMBL; QRIC01000009; RHG26784.1; -; Genomic_DNA.
DR   RefSeq; WP_118224689.1; NZ_QRIC01000009.1.
DR   AlphaFoldDB; A0A414SY41; -.
DR   Proteomes; UP000284095; 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; 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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:RHG26784.1};
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:UP000284095}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   637 AA;  72357 MW;  C575AB8430CC555E CRC64;
     MKNIIIGTAG HIDHGKTTLI KALTGRNTDR WEEEQRRGIT IDLGFTYFDL PGGDRAGIID
     VPGHEKFINN MVAGVVGMDL VLLVIAADEG IMPQTREHMD ILNLLGIEKS IIVLNKCDLV
     DEEWLEMMEE DVREELSGTF LEHAPLIRVS AATGEGLGDL VKEIEHQTRD EVVQKDIHTI
     PRLPIDRVFS LSGFGTIITG TLVSGTITKE DTLQMYPVGT ECKIRSIQVH GEDKKECYAG
     QRVAINLSNV KKKEIKRGCV LAPLNSMKNT DLLDVKLNVL DSSVRILTNH TRLHFFTGTS
     EVLCRAVLLD KEEIGPGESG YVQLRMEEEV AVRRGDKFVV RFYSPMETIG GGVVLEPNPK
     IKRRFQPEVI EELKRKEEGS SADVIEMHVK SHADTLITVS ELAKLTALSL EEVEQDVKEL
     EGQGSVYVFP MRKDTYVWHC DSAREAEHIL LKALTEYEEK YPYRYGIKKA QVQTTYFKKL
     KPNVYDRILT LLEEQGSLKR VDEFLSTPGY EVRKDKIYDR VSEFLLDTFK KAGFDFARYS
     EITCKDVPQE IMDDILNILL EEKQIVKIND EMYTLTSYME TAKEKIREHL KEDPLITIAQ
     VRDMFATSRK SAKPILEYMD SIKVTKKTGA ESERVAY
//
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