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Database: UniProt
Entry: F1Q5Z6_DANRE
LinkDB: F1Q5Z6_DANRE
Original site: F1Q5Z6_DANRE 
ID   F1Q5Z6_DANRE            Unreviewed;       682 AA.
AC   F1Q5Z6; A0A8M1P708;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=HBS1-like protein {ECO:0000256|ARBA:ARBA00015186};
GN   Name=hbs1l {ECO:0000313|Ensembl:ENSDARP00000118572,
GN   ECO:0000313|RefSeq:NP_001295477.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-2987};
GN   Synonyms=wu:fc23c07 {ECO:0000313|RefSeq:NP_001295477.1}, zgc:55400
GN   {ECO:0000313|RefSeq:NP_001295477.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000118572};
RN   [1] {ECO:0000313|RefSeq:NP_001295477.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295477.1};
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.D., Sun X.J., Deng M., Zhang G.W., Zhou Y., Wu X.Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.L., Fan H.Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000118572}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118572};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000118572, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118572};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|RefSeq:NP_001295477.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295477.1};
RX   PubMed=25326603; DOI=10.1530/JOE-14-0539;
RA   Jimenez-Amilburu V., Jong-Raadsen S., Bakkers J., Spaink H.P.,
RA   Marin-Juez R.;
RT   "GLUT12 deficiency during early development results in heart failure and a
RT   diabetic phenotype in zebrafish.";
RL   J. Endocrinol. 224:1-15(2015).
RN   [5] {ECO:0000313|RefSeq:NP_001295477.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295477.1};
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [6] {ECO:0000313|RefSeq:NP_001295477.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295477.1};
RG   RefSeq;
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; BX927365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001295477.1; NM_001308548.1.
DR   STRING; 7955.ENSDARP00000118572; -.
DR   PaxDb; 7955-ENSDARP00000118572; -.
DR   Ensembl; ENSDART00000139076; ENSDARP00000118572; ENSDARG00000036778.
DR   Ensembl; ENSDART00000139076.3; ENSDARP00000118572.1; ENSDARG00000036778.8.
DR   GeneID; 324267; -.
DR   KEGG; dre:324267; -.
DR   AGR; ZFIN:ZDB-GENE-030131-2987; -.
DR   CTD; 10767; -.
DR   ZFIN; ZDB-GENE-030131-2987; hbs1l.
DR   eggNOG; KOG0458; Eukaryota.
DR   HOGENOM; CLU_007265_3_6_1; -.
DR   OMA; CFETEHR; -.
DR   OrthoDB; 5477300at2759; -.
DR   PhylomeDB; F1Q5Z6; -.
DR   TreeFam; TF105833; -.
DR   Proteomes; UP000000437; Alternate scaffold 23.
DR   Proteomes; UP000000437; Chromosome 23.
DR   Bgee; ENSDARG00000036778; Expressed in early embryo and 28 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IMP:ZFIN.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd01883; EF1_alpha; 1.
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   PRINTS; PR00315; ELONGATNFCT.
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   1: Evidence at protein level;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1Q5Z6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT   DOMAIN          256..480
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          56..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  75134 MW;  F426D4A70E17D45C CRC64;
     MSRHRNVRGY NYDEDFEDDD MYGQSVEDDY CISPATAAQF IYSRQDSRQA RHVETVEEAE
     YEEEEEEMPT SPTMTSTLDS LQQGRLYSCL DQMRTVLGDS IPDSTLTQAA LKYDCDPHRA
     LDFILSENTN TQAPSARTNP QLEPNTTAAP QKAKVREAPE SRVESEVVPK VARMTVSGKK
     QTMGFDVRSA EENGGVAPSL RRGPSPEATA VPTTETPSKQ STVTEDSAAP TPTRPSGKSK
     QQLNIRAELE KRQGGKPLLN LVVIGHVDAG KSTLMGHLLY LLGNVNKRTM HKYEQEAKKA
     GKASFAYAWV LDETGEERDR GVTMDVGMTK FETDSKVVTL MDAPGHKDFI PNMITGAAQA
     DVAVLVVDAS RGEFEAGFEA GGQTREHALL VRSLGVTQLA VAVNKMDQVN WQQERFQEII
     SKLGHFLKQA GFKDSDVFYV PTSGLSGENL TTKSKVADLT AWYTGPCLVE QIDAFKPPQR
     SVEKPFRLCV SDVFKDQGSG FCVTGKIEAG YIQTGDKVLA MPPNETCTVK GISLHDEALD
     WAAAGDHVSL TVTGMDIIKI NVGCVFCDPK EPIRACTRFR ARILLFNIEL PITQGFPVLL
     HYQTVSEPAT IRKLVSVLHK SSGEVLKKKP KCLSKGQNAV VEIQTQRPVA MELYKDYKEL
     GRFMLRYVGS TIAAGVVTEI KE
//
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