SELB_HAEIN
ID SELB_HAEIN Reviewed; 619 AA.
AC P43927;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=SelB translation factor;
GN Name=selB; OrderedLocusNames=HI_0709;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. SelB subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC22366.1; -; Genomic_DNA.
DR PIR; I64087; I64087.
DR RefSeq; NP_438867.1; NC_000907.1.
DR RefSeq; WP_005694594.1; NC_000907.1.
DR AlphaFoldDB; P43927; -.
DR SMR; P43927; -.
DR STRING; 71421.HI_0709; -.
DR EnsemblBacteria; AAC22366; AAC22366; HI_0709.
DR KEGG; hin:HI_0709; -.
DR PATRIC; fig|71421.8.peg.739; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_2_0_6; -.
DR OMA; YAIDRVF; -.
DR PhylomeDB; P43927; -.
DR BioCyc; HINF71421:G1GJ1-743-MON; -.
DR Proteomes; UP000000579; Chromosome.
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:0035368; F:selenocysteine insertion sequence binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0016259; P:selenocysteine metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR015191; Elong_fac_SelB-wing-hlx_typ-3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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 Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; SelB-wing_2; 1.
DR Pfam; PF09107; SelB-wing_3; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00475; selB; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..619
FT /note="Selenocysteine-specific elongation factor"
FT /id="PRO_0000091475"
FT DOMAIN 1..169
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 7..14
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 35..39
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 56..59
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 111..114
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 144..146
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 7..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 56..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 111..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 619 AA; 69975 MW; 5960BACDE578D404 CRC64;
MIIVTSGHVD HGKTALLKAL TGTSTAHLPE EKKRGMTIDL GYAYLPLENK VLGFIDVPGH
EKFLSNMLAG LGGVHYAMLI VAADEGVAVQ TKEHLAILRQ LQFHEIIVVI TKADRTNSAQ
IESLIQTIKQ DYSFLRNANY FVTSAETGQG ISELRHYLAN LAELADTQKP FRYAIDRVFS
VKGAGTVVTG TAFSGTVKVN DEIYLSTGQK IRIKAIHAQN TSSEQGIAGQ RLALNLNADL
DRTPMKRGDW LLQNEPLPPT DRISVQILAE VPLNESQPVH IYHGASRTTG KLTLLQGKNA
AKNDRTLAEI ILDSPLFLAF GDKLILRSGD TKTLIAGARV LEINSPKRHK RTEVRLNFLA
NLALAENASQ RIALTLQHNA TTARQLMWTE QLTSLQLDKA LAERDAVRYQ DWCFNPNYVQ
EKTQQILTAL NIYHEQHNDQ LGVSKARLYR MATLNQPENL IHHFIDEMLD DGRLQQTRGW
IHLPEHKIQF NTEEKSRWTD VLNEFEKANG QAIWVRDMAN ALAIDESIMR NFMYKAGKLG
YLTPIVKDRF FLTETLYAYA RLIKQIAEEK GKVSVNEVRD KLNFGRKLTV QLMEYFDRMG
FLRRKGNDHI LRDKNVFDL
