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Database: UniProt
Entry: A0A3P9MTT5_POERE
LinkDB: A0A3P9MTT5_POERE
Original site: A0A3P9MTT5_POERE 
ID   A0A3P9MTT5_POERE        Unreviewed;       710 AA.
AC   A0A3P9MTT5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00015364};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000000767.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000000767.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000000767.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Promotes degradation of target mRNA species. Plays a role in
CC       the regulation of circadian mRNA stability. Binds GTP and has GTPase
CC       activity. {ECO:0000256|ARBA:ARBA00025630}.
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DR   AlphaFoldDB; A0A3P9MTT5; -.
DR   STRING; 8081.ENSPREP00000000767; -.
DR   Ensembl; ENSPRET00000000802.1; ENSPREP00000000767.1; ENSPREG00000000559.1.
DR   GeneTree; ENSGT00940000156054; -.
DR   OMA; RECTISN; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000000559; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   CDD; cd04165; GTPBP1_like; 1.
DR   CDD; cd03694; GTPBP_II; 1.
DR   CDD; cd03708; GTPBP_III; 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; IPR035531; GTPBP1-like.
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   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal 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   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        661..679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          159..390
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          31..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  78170 MW;  8D3D44CF72D212A9 CRC64;
     MASLAAEHEP GITPGSGALA DALVPASIFA PDRGGCGEED GDECFEDEDM TNGKPEDRRI
     DCSSKLALVS PNGEQYDSLL RQLRDRMEDG CGETIYVVGM GSDGGDWGLD EKDMEASVAT
     IHSMCEQLDT DLIPLRERTE AAGMVVDYLI RRRVGELDFL EVRVAVVGNV DAGKSTLLGV
     LTHGELDNGR GFARQKLFRH KHEMESGRTS SVGNDILGFD QEGQVVNKPD SHGGSLDWTK
     ICEKSSKVIT FIDLAGHEKY LKTTVFGMTG HLPDFCMLMV GSNAGIVGMT KEHLGLALAL
     NVPVFVVVTK IDMCPANILQ ETLKLLQRLL KSPGCRKIPV LVQNKDDVIV AASNFSSERM
     CPIFQISNVT GENMDLLKMF LNLLSSRTSY RDDQPAEFQI DDTYSVPGVG TVVSGTTLRG
     LIRLNDTMLL GPDPLGSFIP IAVKSIHRKR MPVKEVRGGQ TASFALKKIK RSSIRKGMVM
     VSPKLNPQAT WEFEAEILVL HHPTTISPRY QAMVHCGSIR QTATILSMNR DCLRTGDKAS
     VHFRFIKTPE YLHCDQRLVF REGRTKAVGT ITKLLHSTNN MPSNSKPPQI KMQSTKKVPL
     RKEDGTMATS DDAATIAQPA GSSTSQPVSQ RRSIDTPNCS NLPEVTVFSS TSWRSVINSN
     IFVFLFFLLS PIHLFINLIN VKSLFCFIPN SNFATLHHFF ILYTLLCLRG
//
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