ID A0A0A1CU66_9MICC Unreviewed; 536 AA.
AC A0A0A1CU66;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=ART_1121 {ECO:0000313|EMBL:AIY00720.1};
OS Arthrobacter sp. PAMC 25486.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY00720.1, ECO:0000313|Proteomes:UP000030301};
RN [1] {ECO:0000313|EMBL:AIY00720.1, ECO:0000313|Proteomes:UP000030301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY00720.1,
RC ECO:0000313|Proteomes:UP000030301};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT Arctic.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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|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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00072}.
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DR EMBL; CP007595; AIY00720.1; -; Genomic_DNA.
DR RefSeq; WP_038462956.1; NZ_CP007595.1.
DR AlphaFoldDB; A0A0A1CU66; -.
DR STRING; 1494608.ART_1121; -.
DR KEGG; arm:ART_1121; -.
DR HOGENOM; CLU_002794_2_1_11; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000030301; Chromosome.
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; 3.40.50.300; 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; 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; 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; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00072};
KW Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT DOMAIN 19..287
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00072"
SQ SEQUENCE 536 AA; 58934 MW; B5C09B6384BA1EFB CRC64;
MSSPAQSPAR ATEISGQAER RRTFAVISHP DAGKSTLTEA LALHAKVIGT AGATNGKSNR
KDTISDWQQM EKDRGISISS AALQFSYRDT VINLLDTPGH ADFSEDTYRV LAAVDCAVML
IDAGKGLETQ TMKLFEVCRQ RNLPIITVIN KWDRPGLDPL ELMDEITERT GLTPMPLTWA
IGIAGDFRGV WDVRRNEFAK FARNSSGAQI ALTEYLTPEQ AAESEGDAWT DSTDEASLVV
DEANPLDLDA FYAGKATPLL FSSAALNFGV KQILDTLVDF APPAAPRADI EGNDRPVDAP
FSGFVFKVQA GMNQAHRDHV AFVRVCSGMF ERGMVVTQTR TGKSFATKYA QQVFGRDREV
IDTAFPGDVV GLVNASALRV GDSLFVEESV EYPAIPLFAP EHFQVARSKD PSKYKQFRRG
IEQLEHEGVI QVLRSDLRGD QAPVLAAVGP MQFEVVEDRM HHDFNAPMRL ERLPYSLARL
TTADATAVLA NLHGAEVLER SDGEFLALFN DIWAMRRVEK NNPDLPLTEI GTSMQK
//
