(data stored in SCRATCH zone)

SWISSPROT: A4AVN5_MARSH

ID   A4AVN5_MARSH            Unreviewed;       358 AA.
AC   A4AVN5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   OrderedLocusNames=FB2170_01287 {ECO:0000313|EMBL:EAQ99965.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99965.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99965.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination
CC       of translation in response to the peptide chain termination codons
CC       UAG and UAA. {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
CC       factor family. {ECO:0000256|HAMAP-Rule:MF_00093}.
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DR   EMBL; CP002157; EAQ99965.1; -; Genomic_DNA.
DR   RefSeq; WP_013304951.1; NC_014472.1.
DR   STRING; 313603.FB2170_01287; -.
DR   EnsemblBacteria; EAQ99965; EAQ99965; FB2170_01287.
DR   KEGG; fbc:FB2170_01287; -.
DR   eggNOG; ENOG4105C8K; Bacteria.
DR   eggNOG; COG0216; LUCA.
DR   HOGENOM; HOG000074815; -.
DR   KO; K02835; -.
DR   OMA; DLFRMYQ; -.
DR   OrthoDB; 928964at2; -.
DR   BioCyc; MSP313603:G1GNS-520-MONOMER; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I_II.
DR   InterPro; IPR004373; PrfA.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AVN5.
DR   SWISS-2DPAGE; A4AVN5.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW   Methylation {ECO:0000256|HAMAP-Rule:MF_00093};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   DOMAIN       62    177       PCRF. {ECO:0000259|SMART:SM00937}.
FT   COILED       44     64       {ECO:0000256|SAM:Coils}.
FT   COILED       74     94       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     233    233       N5-methylglutamine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00093}.
SQ   SEQUENCE   358 AA;  40399 MW;  5BC5C5A42E85B52F CRC64;
     MIDKLNIVKQ RFDEVSDLII QPDVISDQKR YVQLTKEYKD LKDLMEKRDA YVELTNNIQE
     AEEIISDGSD AEMLEMAKMQ LDEAKTALPK LEEDIKLMLI PKDPEDAKDV VVEIRAGTGG
     DEASIFAGDL FRMYTKYCEG RGWKTNVIDL SEGTSGGYKE IQFEVSGADV YGTLKFEAGV
     HRVQRVPQTE TQGRVHTSAA TVMVLPEAED FDVQIDPKDV RIDFFCSSGP GGQSVNTTYS
     AVRLTHIPTG LVAQCQDQKS QHKNKDKAFR VLRSRLYDLE LARKQEEDAA KRNSQVSSGD
     RSAKIRTYNY AQGRVTDHRI GLTLYDLQNI INGDIQKIID ELSLVENTEK LKEASEIF
//

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