HBS1L_BOVIN
ID HBS1L_BOVIN Reviewed; 686 AA.
AC Q2KHZ2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=HBS1-like protein;
GN Name=HBS1L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway. In the presence of ABCE1 and PELO, is required for
CC 48S complex formation from 80S ribosomes and dissociation of vacant 80S
CC ribosomes. Together with PELO and in presence of ABCE1, recognizes
CC stalled ribosomes and promotes dissociation of elongation complexes
CC assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of
CC the mRNA, a mechanism to release non-functional ribosomes and to
CC degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway.
CC {ECO:0000250|UniProtKB:Q9Y450}.
CC -!- SUBUNIT: Interacts with the SKI complex.
CC {ECO:0000250|UniProtKB:Q9Y450}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
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; BC112830; AAI12831.1; -; mRNA.
DR RefSeq; NP_001039963.1; NM_001046498.2.
DR AlphaFoldDB; Q2KHZ2; -.
DR SMR; Q2KHZ2; -.
DR STRING; 9913.ENSBTAP00000026869; -.
DR PaxDb; Q2KHZ2; -.
DR PRIDE; Q2KHZ2; -.
DR GeneID; 541083; -.
DR KEGG; bta:541083; -.
DR CTD; 10767; -.
DR eggNOG; KOG0458; Eukaryota.
DR InParanoid; Q2KHZ2; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR037189; HBS1-like_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF08938; HBS1_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF109732; SSF109732; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Translation regulation.
FT CHAIN 1..686
FT /note="HBS1-like protein"
FT /id="PRO_0000244874"
FT DOMAIN 260..484
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..276
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 325..329
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 346..349
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 408..411
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 447..449
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 197..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269..276
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 346..350
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 408..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS7"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 624
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS7"
SQ SEQUENCE 686 AA; 75850 MW; F031D705567250DD CRC64;
MARHRNVRGY NYDEDFEDDD LYGQSVEDDY CISPSTAAQF IYSRRDKPSA VEPVEEYDYE
DLKEFSSSFV NHQLSGIDQA RLYSCLDHMR EVLGDAVPDD ILIEAVLKNK FDVQKALSVV
LEQDKVQNLK VRSEGAISTG KIAKGKSIDS QSSQSESEIV PKVTKMTVSG KKQTMGFEVP
RVTAEENGHS FHTPQKGHSS EDTSLVSSDA LESASKSALP SHTIQASEEQ SSTPTPVKKS
GKLRQQIDIK AELEKRQGGK QLLNLVVIGH VDAGKSTLMG HLLYLLGDVN KRTMHKYEQE
SKKAGKASFA YAWVLDETGE ERERGVTMDV GMTKFETKTK VITLMDAPGH KDFIPNMITG
AAQADVAVLV VDASRGEFEA GFETGGQTRE HGLLVRSLGV TQLAVAVNKM DQVNWQQERF
QEITGKLGHF LKQAGFKESD VAFIPTSGLS GENLITRSQS SELTKWYKGL CLLEQIDSFK
PPQRSIDKPF RLCVSDVFKD QGSGFCVTGK IEAGYIQTGD RLLAMPPNET CTAKGITLHD
EPVDWAAAGD HVSLTLVGMD IIKINVGCIF CVPKEPIKVC TRFRARILIF NIEIPITKGF
PVLLHYQTVS EPAVIKRLIS VLNKSTGEVT KKKPKLLTKG QNALVELQTQ RPVALELYKD
FKELGRFMLR YSGSTIAAGV VTEIKD
