位置:首页 > 蛋白库 > GTPB1_XENLA
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024