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Database: UniProt
Entry: A0A0N8H9F0_9BACT
LinkDB: A0A0N8H9F0_9BACT
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ID   A0A0N8H9F0_9BACT        Unreviewed;       530 AA.
AC   A0A0N8H9F0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-MAR-2018, entry version 19.
DE   RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072, ECO:0000256|SAAS:SAAS00669815};
DE            Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN   Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072,
GN   ECO:0000313|EMBL:KPM47188.1};
GN   ORFNames=AFM12_15380 {ECO:0000313|EMBL:KPM47188.1};
OS   Jiulongibacter sediminis.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Jiulongibacter.
OX   NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM47188.1, ECO:0000313|Proteomes:UP000050454};
RN   [1] {ECO:0000313|EMBL:KPM47188.1, ECO:0000313|Proteomes:UP000050454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN14-9 {ECO:0000313|EMBL:KPM47188.1,
RC   ECO:0000313|Proteomes:UP000050454};
RA   Liu Y., Du J., Shao Z.;
RT   "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Increases the formation of ribosomal termination
CC       complexes and stimulates activities of RF-1 and RF-2. It binds
CC       guanine nucleotides and has strong preference for UGA stop codons.
CC       It may interact directly with the ribosome. The stimulation of RF-
CC       1 and RF-2 is significantly reduced by GTP and GDP, but not by
CC       GMP. {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS00089114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS00336660}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. PrfC
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00072,
CC       ECO:0000256|SAAS:SAAS00534159}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00072}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPM47188.1}.
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DR   EMBL; LGTQ01000012; KPM47188.1; -; Genomic_DNA.
DR   RefSeq; WP_055149832.1; NZ_LGTQ01000012.1.
DR   EnsemblBacteria; KPM47188; KPM47188; AFM12_15380.
DR   PATRIC; fig|1605367.3.peg.503; -.
DR   Proteomes; UP000050454; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.3280; -; 1.
DR   HAMAP; MF_00072; Rel_fac_3; 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004548; PrfC.
DR   InterPro; IPR032090; RF3_C.
DR   InterPro; IPR038467; RF3_C_sf.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43556; PTHR43556; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF16658; RF3_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
DR   TIGRFAMs; TIGR00503; prfC; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050454};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00089100};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00089095};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00089120};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072,
KW   ECO:0000256|SAAS:SAAS00414956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050454}.
FT   DOMAIN        8    276       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      85     89       GTP. {ECO:0000256|HAMAP-Rule:MF_00072}.
FT   NP_BIND     139    142       GTP. {ECO:0000256|HAMAP-Rule:MF_00072}.
FT   COILED      220    240       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   530 AA;  60667 MW;  4B769BB21CC305EB CRC64;
     MSFQSELKRR RTFAIIAHPD AGKTTLTEKL LLFGGAIQTA GAVKSNKIKK STTSDFMEIE
     KQRGISVATS VMTFEYNNLK INILDTPGHK DFAEDTYRTL TAVDSVILVI DCVKGVEEQT
     EKLMEVCRMR DTPVIIFVNK MDREGKAPFD LLDELEQKLN IGVRPITWPV NGGRDFKGVY
     HLLEKKMNFF AVNKTKLEED IFEYDIDSEE LRSKIGNKDA EQLQEDVELI EGVYEEFDNK
     TYLRGEIAPV FFGSAVSNFG VMELLNTFCD VSPLPISRET NVRVVEPTEP KFSGFVFKIH
     ANIDPRHRDR IAFLRVCSGT FERSKFYEHV RLDKKLRFSN PYMFMADSKN VVEEAYPGDV
     VGLYDTGNFK IGDTLTEGEE LQFTGIPSFS PELFREVINA DPMKTKQLEK GVQQLSEEGV
     AQLFTMQPGN RKIIGTVGEL QFEVIQHRLL HEYGAKCRFE AKPYSKACWL TSENPEALAE
     FIRLKNNFIA YDKDENPVFL AETDWILRMN KENNPEITFH TTSEFKVKED
//
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