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Database: UniProt
Entry: H0V949_CAVPO
LinkDB: H0V949_CAVPO
Original site: H0V949_CAVPO 
ID   H0V949_CAVPO            Unreviewed;       623 AA.
AC   H0V949;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=HBS1-like protein {ECO:0000256|ARBA:ARBA00015186};
GN   Name=HBS1L {ECO:0000313|Ensembl:ENSCPOP00000006327.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000006327.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000006327.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000006327.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR   EMBL; AAKN02038382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02038383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02038384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02038385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02038386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0V949; -.
DR   STRING; 10141.ENSCPOP00000006327; -.
DR   Ensembl; ENSCPOT00000007084.3; ENSCPOP00000006327.3; ENSCPOG00000007015.4.
DR   VEuPathDB; HostDB:ENSCPOG00000007015; -.
DR   GeneTree; ENSGT00940000156274; -.
DR   HOGENOM; CLU_007265_3_6_1; -.
DR   InParanoid; H0V949; -.
DR   OMA; CFETEHR; -.
DR   TreeFam; TF105833; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000007015; Expressed in adrenal gland and 12 other cell types or tissues.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
DR   GO; GO:1990533; C:Dom34-Hbs1 complex; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:Ensembl.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:Ensembl.
DR   CDD; cd16267; HBS1-like_II; 1.
DR   CDD; cd04093; HBS1_C_III; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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   PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF109732; HBS1-like domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          248..419
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          123..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  68675 MW;  8EB0479CEC558C8A CRC64;
     MARHRNVRGY NYDEDFEDDD FYGQSVEDDY CISPSTAAQF IYSQRDKPSV CYDDLKDSAN
     SVSDQQLSGL DQARLYSCLD HMREVLGDAV PDEILIEAVM KNKFDVQKAL SFVLERDNGQ
     NLKDKSGRVM STGKIPKGKS VESQSSRSES EIVPKVAKMT VSGKKQTMGF EVPGVAAEEN
     GHVIQTPLKG PVDEDTAIAS SDILETVTSS ALPSPLQSDR RADSGRRYVG KQLHQFVPIG
     MVLAPKLSLL SNHLMFRLRG VTMDVGMTKF ETTTKVITLM DAPGHKDFIP NMITGAAQAD
     VAVLVVDASR GEFEAGFETG GQTREHGLLV RSLGVTQLAV AVNKMDQVNW QQERFQEITG
     KLGHFLKQAG FKESDVAFIP TSGLSGENLI TRSQLNELTK WYKGLCLLEQ IDSFKPPQRS
     VDKPFRLCVS DVFKDQGSGF CVTGKIEAGY IQIGDRLLAM PPNETCTARG ITLHDEPVDW
     AAAGDHVSLN LVGMDIIKIN VGCIFCGPKE PIKACTRFRA RILIFNIEIP ITKGFPVLLH
     YQTVSEPAVI KRLISVLSKS SGEVTKKKPK LLTKGQNALV ELQTQRPVAL ELYKDFKELG
     RFMLRYSGST IAAGVVTEVF CND
//
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