SELB_MOOTH
ID SELB_MOOTH Reviewed; 634 AA.
AC Q46455;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=SelB translation factor;
GN Name=selB;
OS Moorella thermoacetica (Clostridium thermoaceticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=1525;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35608 / DSM 521 / JCM 9319;
RX PubMed=8893853; DOI=10.1006/jmbi.1996.0525;
RA Kromayer M., Wilting R., Tormay P., Boeck A.;
RT "Domain structure of the prokaryotic selenocysteine-specific elongation
RT factor SelB.";
RL J. Mol. Biol. 262:413-420(1996).
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.
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}.
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DR EMBL; X99830; CAA68147.1; -; Genomic_DNA.
DR EMBL; Y14814; CAA75097.1; -; Genomic_DNA.
DR RefSeq; WP_011393980.1; NZ_VCDY01000003.1.
DR PDB; 1LVA; X-ray; 2.12 A; A=377-634.
DR PDB; 1WSU; X-ray; 2.30 A; A/B/C/D=512-634.
DR PDB; 2PLY; X-ray; 2.60 A; A/B=377-634.
DR PDB; 2UWM; X-ray; 2.31 A; A/B=377-634.
DR PDB; 2V9V; X-ray; 1.10 A; A=377-511.
DR PDBsum; 1LVA; -.
DR PDBsum; 1WSU; -.
DR PDBsum; 2PLY; -.
DR PDBsum; 2UWM; -.
DR PDBsum; 2V9V; -.
DR AlphaFoldDB; Q46455; -.
DR SMR; Q46455; -.
DR DIP; DIP-29313N; -.
DR PATRIC; fig|1525.11.peg.1494; -.
DR OMA; YAIDRVF; -.
DR OrthoDB; 244339at2; -.
DR EvolutionaryTrace; Q46455; -.
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:InterPro.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015189; Elong_fac_SelB-wing-hlx_typ-1.
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; PF09105; SelB-wing_1; 1.
DR Pfam; PF09106; SelB-wing_2; 1.
DR Pfam; PF09107; SelB-wing_3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF46785; SSF46785; 4.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..634
FT /note="Selenocysteine-specific elongation factor"
FT /id="PRO_0000091476"
FT DOMAIN 1..173
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 10..17
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 38..42
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 60..63
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 115..118
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 150..152
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:2V9V"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:2V9V"
FT HELIX 407..419
FT /evidence="ECO:0007829|PDB:2V9V"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:2V9V"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:2V9V"
FT HELIX 437..457
FT /evidence="ECO:0007829|PDB:2V9V"
FT HELIX 466..473
FT /evidence="ECO:0007829|PDB:2V9V"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2PLY"
FT HELIX 479..491
FT /evidence="ECO:0007829|PDB:2V9V"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:2V9V"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:2V9V"
FT HELIX 513..529
FT /evidence="ECO:0007829|PDB:1LVA"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:1LVA"
FT HELIX 547..559
FT /evidence="ECO:0007829|PDB:1LVA"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:1LVA"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:1LVA"
FT HELIX 574..588
FT /evidence="ECO:0007829|PDB:1LVA"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:1LVA"
FT HELIX 606..618
FT /evidence="ECO:0007829|PDB:1LVA"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:1LVA"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:1LVA"
SQ SEQUENCE 634 AA; 70666 MW; 626F9E8A693A8296 CRC64;
MDYIVVGTAG HVDHGKTVLV KALTGVDTDR LKEEKERGIS IELGFAPLTL PSGRQLGLVD
VPGHERFIRQ MLAGVGGMDL VMLVVAADEG VMPQTREHLA IIDLLQIKKG IIVITKIDLV
EADWLELVRE EVRQAVKGTV LEDAPLVEVS ALTGEGIAEL REQLDALAAV TPPRPAAGRV
RLPIDRVFSV TGFGTVVTGT LWSGTIKVGD ELEVQPEGLK TRARNLQVHG RTVKEARAGQ
RVAVNLAGIE TEAVHRGSSL LTPGFLTPTY RLDASFKLLN GARPLANRDR VHFYLGTSEA
LGRVVLLDRD ELNGGEEALI QLLMEKPVVA SREDRFILRS YSPMETIGGG IIIDPVPPKH
RRFQPEVLVS LQRRLEGSPE KILAQIIQEH REGLDWQEAA TRASLSLEET RKLLQSMAAA
GQVTLLRVEN DLYAISTERY QAWWQAVTRA LEEFHSRYPL RPGLAREELR SRYFSRLPAR
VYQALLEEWS REGRLQLAAN TVALAGFTPS FSETQKKLLK DLEDKYRVSR WQPPSFKEVA
GSFNLDPSEL EELLHYLVRE GVLVKINDEF YWHRQALGEA REVIKNLAST GPFGLAEARD
ALGSSRKYVL PLLEYLDQVK FTRRVGDKRV VVGN
