HBS1L_PONAB
ID HBS1L_PONAB Reviewed; 684 AA.
AC Q5R6Y0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=HBS1-like protein;
GN Name=HBS1L;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
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DR EMBL; CR860346; CAH92480.1; -; mRNA.
DR RefSeq; NP_001126462.1; NM_001132990.1.
DR AlphaFoldDB; Q5R6Y0; -.
DR SMR; Q5R6Y0; -.
DR STRING; 9601.ENSPPYP00000019066; -.
DR Ensembl; ENSPPYT00000019817; ENSPPYP00000019066; ENSPPYG00000017027.
DR GeneID; 100173449; -.
DR KEGG; pon:100173449; -.
DR CTD; 10767; -.
DR eggNOG; KOG0458; Eukaryota.
DR GeneTree; ENSGT00940000156274; -.
DR HOGENOM; CLU_007265_3_6_1; -.
DR InParanoid; Q5R6Y0; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000001595; Chromosome 6.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..684
FT /note="HBS1-like protein"
FT /id="PRO_0000091493"
FT DOMAIN 258..482
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 130..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..274
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 323..327
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 344..347
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 406..409
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 445..447
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 208..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 344..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 406..409
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 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS7"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 622
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZS7"
SQ SEQUENCE 684 AA; 75533 MW; F05ED94E925750D1 CRC64;
MARHRNVRGY NYDEDFEDDD LYGQSVEDDY CISPSTAAQF IYSRRDKPSV EPVEEYDYED
LKESSNSVSN HQLSGFDQAR LYSCLDHMRE ILGDAVPDEI LIEAVLKNKF DVQKALSGVL
EQDRVQSLKD KNEGTVSTGK IAKGKPVDSQ TSRSESEIVP KVAKMTVSGK KQTMGFEVPG
VSSEENGHSF HTPQKGPPIE DAIASSDVLE TASKSANPPH TIQASEEQSS TPAPVKKSGK
LRQQIDVKAE LEKRQGGKQL LNLVVIGHVD AGKSTLMGHM LYLLGNINKR TMHKYEQESK
KAGKASFAYA WVLDETGEER ERGVTMDVGM TKFETTTKVI TLMDAPGHKD FIPNMITGAA
QADVAVLVVD ASRGEFEAGF ETGGQTREHG LLVRSLGVTQ LAVAVNKMDQ VNWQQERFQE
ITGKLGHFLK QAGFKESDVA FIPTSGLSGE NLITRSRSSE LTKWYKGLCL LEQIDSFKPP
QRSIDKPFRL CVSDVFKDQG SGFCITGKIE AGYIQTGDRL LAMPPNETCT VKGITLHDEP
VDWAAAGDHV SLTLVGMDII KINVGCIFCG PKVPIKACTR FRARILIFNI EIPITKGFPV
LLHYQTVSEP AVIKRLISVL NKSTGEVTKK KPKFLTKGQN ALVELQTQRP IALELYKDFK
ELGRFMLRYG GSTIAAGVVT EMKE
