ID A0A087Y7L8_POEFO Unreviewed; 666 AA.
AC A0A087Y7L8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00015364};
GN Name=GTPBP1 {ECO:0000313|Ensembl:ENSPFOP00000014021.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000014021.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000014021.2}
RP IDENTIFICATION.
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 EMBL; AYCK01003621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016525815.1; XM_016670329.1.
DR AlphaFoldDB; A0A087Y7L8; -.
DR STRING; 48698.ENSPFOP00000014021; -.
DR Ensembl; ENSPFOT00000014040.2; ENSPFOP00000014021.2; ENSPFOG00000013922.2.
DR GeneID; 103136460; -.
DR CTD; 402863; -.
DR eggNOG; KOG0463; Eukaryota.
DR GeneTree; ENSGT00940000156054; -.
DR OMA; DFCMLMX; -.
DR OrthoDB; 129286at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 151..381
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 578..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 72422 MW; CD27BD94C6A8178D CRC64;
MASAATCPGS TPPESIVPAC MFAPDRGCAD DPSCEEDFED GEGTNGQSVD YLDLSKKLIL
VSPTGEQYDS LLRQLRERIE EGCGETIYVV GMGSDGGDYG LDEKDMEASV ATVRSLCEQI
EADLILLRER MESGGKIRDY LIRRRVGEQD FLEVRVAVVG NVDAGKSTLL GVLTHGELDN
GRGFARQKLF RHKHEMESGR TSSVGNDILG FDQEGQVVNK PDSHGGGLDW TKICEKSSKV
ITFIDLAGHE KYLKTTVFGM TGHLPDFCML MVGSNAGIVG MTKEHLGLAL ALNVPVFVVV
TKIDMCPANI LQETLKLLQR LLKSPGCRKI PVLVQNKDDV VVTASNFSSE RMCPIFQISN
VTGENMDLLK MFLNLLSPRT TFNNDEPAEF QIDDTYSVPG VGTVVSGTTL RGLIRLNDTL
LLGPDPLGTF IPIAVKSIHR KRMPVREVHG GQTASFALKK IKRSSIRKGM VMVSPKLMPQ
ATWEFEAEIL VLHHPTTISP RYQAMVHCGS IRQTATILTM NKDCLRTGDK ASVHFRFIKT
PEYLHCDQKL VFREGRTKAV GTITKLLQSV STQAAKAQQA KCQVSRKSSR EGTSGSEDAG
STARPLSPTL ASTVAEEDAL CKDDNKENKL KSGGGGRRRG GQRHRGKGQN TAAMSSAMPT
GAAGLS
//