ID A0A1Q6CM44_9GAMM Unreviewed; 362 AA.
AC A0A1Q6CM44;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093};
GN ORFNames=BI291_09415 {ECO:0000313|EMBL:OKY27507.1};
OS Thalassotalea sp. PP2-459.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1742724 {ECO:0000313|EMBL:OKY27507.1, ECO:0000313|Proteomes:UP000186791};
RN [1] {ECO:0000313|EMBL:OKY27507.1, ECO:0000313|Proteomes:UP000186791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP2-459 {ECO:0000313|EMBL:OKY27507.1,
RC ECO:0000313|Proteomes:UP000186791};
RA Barja J.L., Dubert J.;
RT "Draft genome of the tyrosinase inhibitors producing Thalassotalea sp. PP2-
RT 459.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC translation in response to the peptide chain termination codons UAG and
CC UAA. {ECO:0000256|ARBA:ARBA00002986, ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00093}.
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:OKY27507.1}.
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DR EMBL; MKQD01000018; OKY27507.1; -; Genomic_DNA.
DR RefSeq; WP_074496364.1; NZ_MKQD01000018.1.
DR AlphaFoldDB; A0A1Q6CM44; -.
DR STRING; 1742724.BI291_09415; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000186791; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
DR HAMAP; MF_00093; Rel_fac_1; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004373; RF-1.
DR NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW Reference proteome {ECO:0000313|Proteomes:UP000186791}.
FT DOMAIN 230..246
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 362 AA; 41077 MW; 92A4166002D147F4 CRC64;
MKKSVYEKLE GLVERFEEVQ ALLSDPQTIA DQEKFQALSK EFKQLDEVTE VFNRYKSAQD
DFAAAEEMLK DEDPDLREMA QDEFKDAKKA VEALTDELQI LLLPRDPNDD NNCFVEIRAG
AGGDEAAIFA GDLYRMYTRY CESKGWRIEV MNMNESEQGG FKEVIFKIAG EGVYGQMKFE
SGGHRVQRVP ETESQGRVHT SACTVVVLPE IPESEAIEIN KADLRIDTFR ASGAGGQHVN
KTDSAIRITH IPTGLVVECQ DQRSQHKNRA QAMSVLQARL QAAEDEKRRS EEEDSRRNLV
ASGDRSERIR TYNYPQSRMT DHRINLTLYR LAEVMEGSLD LVLEPILQEY QADMLAALSE
SH
//
