ID Q2CCK0_OCEGH Unreviewed; 531 AA.
AC Q2CCK0;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Peptide chain release factor 3 {ECO:0000256|HAMAP-Rule:MF_00072};
DE Short=RF-3 {ECO:0000256|HAMAP-Rule:MF_00072};
GN Name=prfC {ECO:0000256|HAMAP-Rule:MF_00072};
GN ORFNames=OG2516_02818 {ECO:0000313|EMBL:EAR50413.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR50413.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR50413.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
CC -!- FUNCTION: Increases the formation of ribosomal termination complexes
CC and stimulates activities of RF-1 and RF-2. It binds guanine
CC nucleotides and has strong preference for UGA stop codons. It may
CC interact directly with the ribosome. The stimulation of RF-1 and RF-2
CC is significantly reduced by GTP and GDP, but not by GMP.
CC {ECO:0000256|HAMAP-Rule:MF_00072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00072}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. PrfC subfamily.
CC {ECO:0000256|ARBA:ARBA00009978, ECO:0000256|HAMAP-Rule:MF_00072}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAR50413.1}.
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DR EMBL; AAOT01000029; EAR50413.1; -; Genomic_DNA.
DR RefSeq; WP_007254093.1; NZ_CH724107.1.
DR AlphaFoldDB; Q2CCK0; -.
DR STRING; 314256.OG2516_02818; -.
DR eggNOG; COG4108; Bacteria.
DR HOGENOM; CLU_002794_2_1_5; -.
DR OrthoDB; 9802948at2; -.
DR Proteomes; UP000003635; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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 CDD; cd04169; RF3; 1.
DR CDD; cd16259; RF3_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.70.3280; Peptide chain release factor 3, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00072; Rel_fac_3; 1.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR004161; EFTu-like_2.
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_dom_3_sf.
DR InterPro; IPR041732; RF3_GTP-bd.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00503; prfC; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43556; PEPTIDE CHAIN RELEASE FACTOR RF3; 1.
DR PANTHER; PTHR43556:SF2; PEPTIDE CHAIN RELEASE FACTOR RF3; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF16658; RF3_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00072};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00072};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00072};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00072}; Reference proteome {ECO:0000313|Proteomes:UP000003635}.
FT DOMAIN 12..281
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 89..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 531 AA; 59377 MW; 627F224D9548D263 CRC64;
MSNRPALPAE IARRRTFAII SHPDAGKTTL TEKFLLFGGA IQMAGQVRAK GEARRTRSDF
MQMEKDRGIS VSASAMSFDY GKFRYNLVDT PGHSDFSEDT YRTLTAVDAA IMVIDGAKGV
ESQTRKLFEV CRLRDLPILT FCNKMDRESR DTFEIIDEIQ ENLAIDVTPA SWPIGVGRDF
LGCYDLLRDR LELMDRADRN RVAESIEING LDDPKLAQHV PAELLDKLRE EVEMARELLP
PLDPKAFLEG TMTPIWFGSA INSFGVKELM DGLGNYGPEP QPTPAEPRQI APEEPKVTGF
VFKVQANMDP KHRDRVAFVR MASGHFERGM KLTHVRSKKP MAISNPVLFL ASDRELAEEA
WAGDIIGIPN HGQLRIGDTL TEGEALQVKG IPSFAPELLQ GVRAGDPMKA KHLEKALMQF
AEEGAAKVFK PSFGSGFIVG VVGALQFEVL ASRIEMEYGL PVRFDGSQFT SARWVSGKRE
EVDRFAAANK QHIAHDHDGD IVYLTRLQWD IDRVERDWPD IRLTATKEMM A
//
