ID G3T620_LOXAF Unreviewed; 605 AA.
AC G3T620;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00015364};
GN Name=GTPBP1 {ECO:0000313|Ensembl:ENSLAFP00000008930.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000008930.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000008930.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008930.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000008930.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008930.3};
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 STRING; 9785.ENSLAFP00000008930; -.
DR Ensembl; ENSLAFT00000010668.3; ENSLAFP00000008930.3; ENSLAFG00000010667.3.
DR eggNOG; KOG0463; Eukaryota.
DR GeneTree; ENSGT00940000156054; -.
DR HOGENOM; CLU_012821_2_0_1; -.
DR InParanoid; G3T620; -.
DR OMA; CENDPAH; -.
DR TreeFam; TF350446; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 2.
DR Gene3D; 2.40.30.10; Translation factors; 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 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.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 210..320
FT /note="Tr-type G"
FT /evidence="ECO:0000259|Pfam:PF00009"
FT REGION 508..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 66704 MW; AB13CB8E188E116C CRC64;
LVLVSPTSEQ YDSLLRQMWE RMDEGCGETI YVIGQGSDGT EYGLSEADME ASYATVKSMA
EQIEADVILL RERQEAGGRV RDYLVRKRVG DNDFLEVRVA VVGNVDAGKS TLLGVLTHGE
LDNGRFARQK TLRHKHEIES EHCQGVITDL LGWATERGLH GRSIRHIRXL VGLERCQEQG
KIMIQLPLTM HFVFPDVWVF IFYCFHLSPD FVLRQVGSNA GIVGMTKEHL GLALALNVPV
FVVVTKIDMC PANILQETLK LLQRLLKSPG CRKIPVLVQS KDDVIVMASN FSSERMCPIF
QLSNVTGENL ELLKMFLNLL SPRTSYREEE PAEFQIDDTY SVPGVGTVVS GTTLRGLIKL
NDTLLLGPDP LGNFLSIAVK SIHRKRMPVK EVRGGQTSFA LKKIKRSSIR KGMVMVSPRL
NPQASWEFEA EILVLHHPTT ISPRYQAMVH CGSIRQTATI LSMDKDCLRT GDKATVHFRF
IKTPEYLHID QRLVFREGRT KAVGTITKLL QTTNNSPMNS KPQQIKMQST KKGPLSRREE
GGPAGGPSVG VPPPGDTATS LGAAQPSAAG SLQPQPKPSS GGRRRGGQRH KVKSQGACGT
PASGC
//