ID H3A486_LATCH Unreviewed; 377 AA.
AC H3A486;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00015364};
GN Name=GTPBP1 {ECO:0000313|Ensembl:ENSLACP00000004457.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004457.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004457.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AFYH01055767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01055768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01055769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01055770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A486; -.
DR STRING; 7897.ENSLACP00000004457; -.
DR Ensembl; ENSLACT00000004496.1; ENSLACP00000004457.1; ENSLACG00000003966.1.
DR eggNOG; KOG0463; Eukaryota.
DR GeneTree; ENSGT00940000156054; -.
DR HOGENOM; CLU_012821_1_0_1; -.
DR InParanoid; H3A486; -.
DR OMA; DCNDHEN; -.
DR TreeFam; TF350446; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000003966; Expressed in chordate pharynx and 6 other cell types or tissues.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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; 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:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..377
FT /note="GTP-binding protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003578973"
FT DOMAIN 1..102
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 290..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 41271 MW; 447AC1F8BEC3746B CRC64;
MTKEHLGLAL ALNVPVFVVV TKIDMCPANI LQETLKLLQR LLKSPGCRKI PVLVQNKDDV
IVTASNFSSE RMCPIFQISN VTGENLELLK MFLNLLSPRT SYNEEEPAEF QIDDTYSVPG
VGTVVSGTTL RGLIRLNDIL LLGPDPLGSF SPIAVKSIHR KRMPVKEVRG GQTASFALKK
IKRSSIRKGM VMVSPRLNPQ ASWEFEAEIL VLHHPTTISP RYQAMVHCGS IRQTATILTM
NKDCLRTGDK ATVHFRFIKT PEYLHTDQRL VFREGRTKAV GTIMKLLQTT NNLPSNSKPQ
QIKMQPMKKA SLPRRDEGAS GSALEETSGT VAQGSISAPG VNPQQSQTKS GGGGRRRGGQ
RHKVKSHGAV APPPGGS
//
