GTPB1_XENLA
ID GTPB1_XENLA Reviewed; 654 AA.
AC Q5XGS8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=GTP-binding protein 1;
GN Name=gtpbp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. GTPBP1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC084354; AAH84354.1; -; mRNA.
DR RefSeq; NP_001088313.1; NM_001094844.1.
DR AlphaFoldDB; Q5XGS8; -.
DR SMR; Q5XGS8; -.
DR DNASU; 495150; -.
DR GeneID; 495150; -.
DR KEGG; xla:495150; -.
DR CTD; 495150; -.
DR Xenbase; XB-GENE-951188; gtpbp1.S.
DR OrthoDB; 682656at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 495150; Expressed in egg cell and 19 other tissues.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR CDD; cd04165; GTPBP1_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR039263; GTPB1.
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:SF9; PTHR43721:SF9; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..654
FT /note="GTP-binding protein 1"
FT /id="PRO_0000293473"
FT DOMAIN 147..377
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..163
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 195..199
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 241..244
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 297..300
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 355..357
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 566..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 241..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 297..300
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 654 AA; 70910 MW; F1422829266F9C2E CRC64;
MASLASSQTE PNTSESPVPA SMFSPEPDGE DSDCSLDGEP LRNGEADIDV TSKFVLVSPS
AEQYDSLLHQ LRDRMDEGRG ETIYVIGQGS DGTEYGLNEA DMEASVATVT SMAEQIVADM
ILLREHQEAG GKVQDYLVRK SVGDNDFLEV RVAVVGNVDA GKSTLLGVLT HGELDNGRGF
ARQKLFRHKH EIESGRTSSV GNDILGFDNH GQVVNKPDNH GGSLEWTKIC EKSSKIITFI
DLAGHEKYLK TTVFGMTGHL PDFCMLMVGS NAGIVGMTKE HLGLALALNV PVFVVVTKID
MCPANILQET LKLLQRLLKS PGCRKIPVLV QNKDDVIVTA SNFSSERMCP IFQISNVTGE
NLDLLKMFLN LLSPRSSSRE EEPAEFQIDD TYSVPGVGTV VSGTTLRGLI KLNDLLLLGP
DPLGNFTSIA VKSIHRKRMP VKEVRGGQTA SFALKKIKRS TIRKGMVMVS PRLNPQASWE
FEAEILVLHH PTTISPRYQA MVHCGSIRQT ATILTMSRDC LRTGDKAIVH FRFIKTPEYL
HIDQRLVFRE GRTKAVGTIT KLLQSTNNLP MNSKPPQQVK MQSTKKSLHG KKDEQSPAAA
VTEEASPSAA AIGVTAGAGA MQAQPKTGGG GRRRGGQRHK VKAQGACTAS TGGC